ID 3BP1_HUMAN STANDARD; PRT; 701 AA. AC Q9Y3L3; Q6IBZ2; Q6ZVL9; Q96HQ5; Q9NSQ9; DT 23-JAN-2002, integrated into UniProtKB/Swiss-Prot. DT 16-AUG-2004, sequence version 3. DT 30-MAY-2006, entry version 51. DE SH3 domain-binding protein 1 (3BP-1). GN Name=SH3BP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RX PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84; RA Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A., RA Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J., RA Beare D.M., Dunham I.; RT "A genome annotation-driven approach to cloning the human ORFeome."; RL Genome Biol. 5:RESEARCH84.1-RESEARCH84.11(2004). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Uterus; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=20057165; PubMed=10591208; DOI=10.1038/990031; RA Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., RA Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., RA Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., RA Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J., RA Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., RA Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., RA Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., RA Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., RA Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., RA Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., RA Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., RA Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., RA Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., RA Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., RA Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., RA Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., RA Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., RA Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., RA Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., RA Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., RA Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., RA Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., RA Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., RA Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., RA Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., RA Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., RA Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., RA Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., RA Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., RA Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., RA Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., RA Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., RA Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., RA Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., RA Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., RA Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., RA Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., RA Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., RA Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., RA O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., RA Khan A.S., Lane L., Tilahun Y., Wright H.; RT "The DNA sequence of human chromosome 22."; RL Nature 402:489-495(1999). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 33-701 (ISOFORM 1). RC TISSUE=Pancreas; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 360-701 (ISOFORM 1). RC TISSUE=Melanoma; RG The German cDNA consortium; RL Submitted (JUN-2005) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Binds differentially to the SH3 domains of certain CC proteins of signal transduction pathways. This protein binds CC preferentially to the ABL1 proto-oncogene, SRC and GRB2. Shows GAP CC activity for Rac-related proteins but not for Rho- or Ras-related CC proteins. It inhibits PDGF-induced membrane ruffling mediated by CC Rac (By similarity). CC -!- INTERACTION: CC P08631:HCK; NbExp=1; IntAct=EBI-346869, EBI-346340; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9Y3L3-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9Y3L3-2; Sequence=VSP_011373, VSP_011374; CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 Rho-GAP domain. CC -!- CAUTION: Ref.2 (BAC85842) sequence differs from that shown due to CC a stop codon in position 56 which was translated as Cys to extend CC the sequence. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; CR456576; CAG30462.1; -; mRNA. DR EMBL; AK124370; BAC85842.1; ALT_INIT; mRNA. DR EMBL; Z83844; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC008282; AAH08282.1; ALT_INIT; mRNA. DR EMBL; AL157480; CAB75671.2; -; mRNA. DR PIR; T46916; T46916. DR UniGene; Hs.445351; -. DR HSSP; Q98935; 1F7C. DR IntAct; Q9Y3L3; -. DR Ensembl; ENSG00000100092; Homo sapiens. DR HGNC; HGNC:10824; SH3BP1. DR GO; GO:0005515; F:protein binding; IPI. DR InterPro; IPR004148; BAR. DR InterPro; IPR008936; Rho_GAP. DR InterPro; IPR000198; RhoGAP. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00324; RhoGAP; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50238; RHOGAP; 1. KW Alternative splicing; GTPase activation; Polymorphism; SH3-binding. FT CHAIN 1 701 SH3 domain-binding protein 1. FT /FTId=PRO_0000056723. FT DOMAIN 17 262 BAR. FT DOMAIN 276 469 Rho-GAP. FT MOTIF 617 625 SH3-binding (By similarity). FT VAR_SEQ 440 452 DQAQLDAASVSSI -> TEPARELGSQTLC (in FT isoform 2). FT /FTId=VSP_011373. FT VAR_SEQ 453 701 Missing (in isoform 2). FT /FTId=VSP_011374. FT VARIANT 431 431 L -> P (in dbSNP:929038). FT /FTId=VAR_019642. SQ SEQUENCE 701 AA; 75713 MW; 877D144E81F0F974 CRC64; MMKRQLHRMR QLAQTGSLGR TPETAEFLGE DLLQVEQRLE PAKRAAHNIH KRLQACLQGQ SGADMDKRVK KLPLMALSTT MAESFKELDP DSSMGKALEM SCAIQNQLAR ILAEFEMTLE RDVLQPLSRL SEEELPAILK HKKSLQKLVS DWNTLKSRLS QATKNSGSSQ GLGGSPGSHS HTTMANKVET LKEEEEELKR KVEQCRDEYL ADLYHFVTKE DSYANYFIRL LEIQADYHRR SLSSLDTALA ELRENHGQAD HSPSMTATHF PRVYGVSLAT HLQELGREIA LPIEACVMML LSEGMKEEGL FRLAAGASVL KRLKQTMASD PHSLEEFCSD PHAVAGALKS YLRELPEPLM TFDLYDDWMR AASLKEPGAR LQALQEVCSR LPPENLSNLR YLMKFLARLA EEQEVNKMTP SNIAIVLGPN LLWPPEKEGD QAQLDAASVS SIQVVGVVEA LIQSADTLFP GDINFNVSGL FSAVTLQDTV SDRLASEELP STAVPTPATT PAPAPAPAPA PAPALASAAT KERTESEVPP RPASPKVTRS PPETAAPVED MARRTKRPAP ARPTMPPPQV SGSRSSPPAP PLPPGSGSPG TPQALPRRLV GSSLRAPTVP PPLPPTPPQP ARRQSRRSPA SPSPASPGPA SPSPVSLSNP AQVDLGAATA EGGAPEAISG VPTPPAIPPQ PRPRSLASET N // ID 3BP1_MOUSE STANDARD; PRT; 601 AA. AC P55194; Q99KK8; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 04-APR-2006, entry version 50. DE SH3 domain-binding protein 1 (3BP-1). GN Name=Sh3bp1; Synonyms=3bp1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=95347339; PubMed=7621827; RA Cicchetti P., Ridley A.J., Zheng Y., Cerione R.A., Baltimore D.; RT "3BP-1, an SH3 domain binding protein, has GAP activity for Rac and RT inhibits growth factor-induced membrane ruffling in fibroblasts."; RL EMBO J. 14:3127-3135(1995). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] OF 263-601. RX MEDLINE=92358242; PubMed=1379745; RA Cicchetti P., Mayer B.J., Thiel G., Baltimore D.; RT "Identification of a protein that binds to the SH3 region of Abl and RT is similar to Bcr and GAP-rho."; RL Science 257:803-806(1992). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 528-537. RX MEDLINE=93174278; PubMed=8438166; RA Ren R., Mayer B.J., Cicchetti P., Baltimore D.; RT "Identification of a ten-amino acid proline-rich SH3 binding site."; RL Science 259:1157-1161(1993). CC -!- FUNCTION: Binds differentially to the SH3 domains of certain CC proteins of signal transduction pathways. This protein binds CC preferentially to the ABL1 proto-oncogene, SRC and GRB2. Shows GAP CC activity for Rac-related proteins but not for Rho- or Ras-related CC proteins. It inhibits PDGF-induced membrane ruffling mediated by CC Rac. CC -!- TISSUE SPECIFICITY: Expressed in all tissues examined. Highest CC levels found in spleen and brain, lowest in heart and liver. CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 Rho-GAP domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X87671; CAA61011.1; -; mRNA. DR EMBL; BC004598; AAH04598.1; -; mRNA. DR PIR; S56144; S56144. DR UniGene; Mm.4462; -. DR PDB; 1ABO; X-ray; C/D=528-537. DR MGI; MGI:104603; Sh3bp1. DR LinkHub; P55194; -. DR InterPro; IPR004148; BAR. DR InterPro; IPR008936; Rho_GAP. DR InterPro; IPR000198; RhoGAP. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00620; RhoGAP; 1. DR SMART; SM00324; RhoGAP; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50238; RHOGAP; 1. KW 3D-structure; GTPase activation; SH3-binding. FT CHAIN 1 601 SH3 domain-binding protein 1. FT /FTId=PRO_0000056724. FT DOMAIN 1 182 BAR. FT DOMAIN 196 390 Rho-GAP. FT MOTIF 529 537 SH3-binding. FT CONFLICT 46 48 RSG -> PLS (in Ref. 2). FT CONFLICT 229 229 Missing (in Ref. 2). FT CONFLICT 261 261 G -> D (in Ref. 2). FT CONFLICT 592 593 PA -> RP (in Ref. 2). FT STRAND 530 531 SQ SEQUENCE 601 AA; 65260 MW; 0FBBF357EEB02ECE CRC64; MAESFKELDP DSSMGKALEM TCAIQNQLAR ILAEFEMTLE RDVLQRSGRL SEEELPAILK HKKSLQKLVS DWNTLKSRLS QAAKNSGSNQ GLGGASGSHT HTTTANKVEM LKEEEEELKK KVEQCKDEYL ADLYHFSTKE DSYANYFIHL LEIQADYHRK SLTSLDTALA ELRDNHNQAD HSPLTTAAPF SRVYGVSLRT HLQDLGRDIA LPIEACVLLL LSEGMQEEEG LFRLAAGASV LKRLKQTMAS DPHSLEEFCS GPHAVAGALK SYLRELPEPL MTSDLYDDWM RAASLKEPGA RLEALHDVCS RLPQENFNNL RYLMKFLALL AEEQDVNKMT PSNIAIVLGP NLLWPPEKEG DQAQLDAASV SSIQVVGVVE ALIQNADTLF PGDINFNVSG IFPGLAPQEK VSSQQVSEEL PPVTVPAPAT TPAPTLAPAS MAVRERTEAD LPKPTSPKVS RNPTETAASA EDMTRKTKRP APARPTMPPP QPSSTRSSPP APSLPPGSVS PGTPQALPRR LVGTSLRAPT MPPPLPPVPP QPARRQSRRL PASPVISNMP AQVDQGVATE DREGPEAVGG HPPPPALPPQ PPARGLISET E // ID AMPH_CHICK STANDARD; PRT; 682 AA. AC P50478; DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-1996, sequence version 1. DT 30-MAY-2006, entry version 42. DE Amphiphysin. GN Name=AMPH; OS Gallus gallus (Chicken). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Archosauria; Aves; Neognathae; Galliformes; Phasianidae; Phasianinae; OC Gallus. OX NCBI_TaxID=9031; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Tetra-hybrid; TISSUE=Forebrain; RX MEDLINE=92331604; PubMed=1628617; RA Lichte B., Veh R.W., Meyer H.E., Kilimann M.W.; RT "Amphiphysin, a novel protein associated with synaptic vesicles."; RL EMBO J. 11:2521-2530(1992). CC -!- FUNCTION: May participate in mechanisms of regulated exocytosis in CC synapses and certain endocrine cell types. May control the CC properties of the membrane associated cytoskeleton. CC -!- SUBUNIT: Heterodimer with BIN1. Binds SH3GLB1 (By similarity). CC -!- SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; CC peripheral membrane protein; cytoplasmic side. CC -!- TISSUE SPECIFICITY: Is abundant in the forebrain and cerebellum. CC It is also found in the adrenal gland, anterior and posterior CC pituitary. CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X60422; CAA42953.1; -; mRNA. DR PIR; S22700; S22700. DR UniGene; Gga.2709; -. DR HSSP; O08839; 1BB9. DR Ensembl; ENSGALG00000012286; Gallus gallus. DR GO; GO:0005625; C:soluble fraction; IDA. DR GO; GO:0019717; C:synaptosome; IDA. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR003017; Amphiphysin_1. DR InterPro; IPR004148; BAR. DR InterPro; IPR001452; SH3. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01252; AMPHIPHYSIN1. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD003208; Amphiphysin_1; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. KW Coiled coil; Cytoskeleton; SH3 domain. FT CHAIN 1 682 Amphiphysin. FT /FTId=PRO_0000192950. FT DOMAIN 24 240 BAR. FT DOMAIN 609 682 SH3. FT COILED 10 84 Potential. FT COILED 144 191 Potential. SQ SEQUENCE 682 AA; 75205 MW; 61617F494F38EB20 CRC64; MADMKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGSRLQREL RAYLAAIKGM QDASKKLTES LHEVYEPDWY GREDVKMIGE KCDELWEDFH QKLVDGSLLT LDTYLGQFPD IKTRIAKRSR KLVDYDSARH HLEALQSSKR KDEGRITKAE EEFQKAQKVF EEFNTDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI ALLCHKLYEV MTKLGDQHAD KAFTIQGAPS DSGPLRIAKT PSPPEEVSPL PSPTASPNHM LAPASPAPAR PKSPTQLRKG PPVPPLPKLT PTKELQQENI INLFDDNFVP EINVTTPSQN EIPETKKVES LLDLDFDPFK PEVVSTGVTH SPMSQTLPWD LWTTTSELVQ PASSTAFNGF AQDTTAFAVQ SNENVTETLT EAEEAPLGEL KVEETPTAAV VEKEAILAEP DEPTEQAAES IEAGDKETTG IAEKESEVVS AAGGAVAVED SVVVAAGAGE GAVRTEQEAA AEGDKPQGEE KDVDVSQEKV SSIPSVVIEP ASNNEGEGEE HHVIMNESKD AAAEMGTQGT DSETSQIGSE QKATEEIQTT PSQDQPASAG DTASDMPPGF LFKVEVLHDF EAANSDELNL KRGDIVLVIP SETTADQEAG WLTGIKESEW LQYRDANSYK GLFPENFTRH LE // ID AMPH_HUMAN STANDARD; PRT; 695 AA. AC P49418; O43538; Q75MJ8; Q75MK5; Q75MM3; Q8N4G0; DT 01-FEB-1996, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1996, sequence version 1. DT 30-MAY-2006, entry version 61. DE Amphiphysin. GN Name=AMPH; Synonyms=AMPH1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Cerebellum; RX MEDLINE=94357284; PubMed=8076697; DOI=10.1016/0014-5793(94)00826-4; RA David C., Solimena M., de Camilli P.; RT "Autoimmunity in stiff-man syndrome with breast cancer is targeted to RT the C-terminal region of human amphiphysin, a protein similar to the RT yeast proteins, Rvs167 and Rvs161."; RL FEBS Lett. 351:73-79(1994). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC TISSUE=Brain; RX MEDLINE=95276740; PubMed=7757077; RA Yamamoto R., Li X., Winter S., Francke U., Kilimann M.W.; RT "Primary structure of human amphiphysin, the dominant autoantigen of RT paraneoplastic stiff-man syndrome, and mapping of its gene (AMPH) to RT chromosome 7p13-p14."; RL Hum. Mol. Genet. 4:265-268(1995). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Mammary gland; RX MEDLINE=98174372; PubMed=9513187; RA Floyd S.R., Butler M.H., Cremona O., David C., Freyberg Z., Zhang X., RA Solimena M., Tokunaga A., Ishizu H., Tsutsui K., De Camilli P.V.; RT "Expression of amphiphysin I, an autoantigen of paraneoplastic RT neurological syndromes, in breast cancer."; RL Mol. Med. 4:29-39(1998). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX MEDLINE=22737999; PubMed=12853948; DOI=10.1038/nature01782; RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., RA Waterston R.H., Wilson R.K.; RT "The DNA sequence of human chromosome 7."; RL Nature 424:157-164(2003). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Brain; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [6] RP X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 322-330 IN COMPLEX WITH RP AP2A2. RX PubMed=12057195; DOI=10.1016/S0969-2126(02)00784-0; RA Brett T.J., Traub L.M., Fremont D.H.; RT "Accessory protein recruitment motifs in clathrin-mediated RT endocytosis."; RL Structure 10:797-809(2002). CC -!- FUNCTION: May participate in mechanisms of regulated exocytosis in CC synapses and certain endocrine cell types. May control the CC properties of the membrane associated cytoskeleton. CC -!- SUBUNIT: Heterodimer with BIN1. Binds SH3GLB1 and AP2A2 (By CC similarity). CC -!- SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; CC peripheral membrane protein; cytoplasmic side. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=128 kDa; CC IsoId=P49418-1; Sequence=Displayed; CC Name=2; Synonyms=108 kDa; CC IsoId=P49418-2; Sequence=VSP_000245; CC -!- TISSUE SPECIFICITY: Neurons, certain endocrine cell types and CC spermatocytes. CC -!- DISEASE: Antibodies against AMPH are detected in patients with CC stiff-man syndrome, a rare disease of the central nervous system CC characterized by progressive rigidity of the body musculature with CC superimposed painful spasms. CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U07616; AAA21865.1; -; mRNA. DR EMBL; X81438; CAA57197.1; -; mRNA. DR EMBL; AF034996; AAC02977.1; -; mRNA. DR EMBL; AC011309; AAS07391.1; -; Genomic_DNA. DR EMBL; AC012490; AAS07563.1; -; Genomic_DNA. DR EMBL; AC007245; AAS07541.1; -; Genomic_DNA. DR EMBL; BC034376; AAH34376.1; -; mRNA. DR PIR; S62400; S62400. DR UniGene; Hs.592182; -. DR PDB; 1KY7; X-ray; P=322-331. DR PDB; 1UTC; X-ray; P/Q=379-387. DR Ensembl; ENSG00000078053; Homo sapiens. DR H-InvDB; HIX0006613; -. DR HGNC; HGNC:471; AMPH. DR MIM; 600418; gene. DR LinkHub; P49418; -. DR GO; GO:0015629; C:actin cytoskeleton; TAS. DR GO; GO:0008021; C:synaptic vesicle; TAS. DR GO; GO:0006897; P:endocytosis; TAS. DR GO; GO:0007268; P:synaptic transmission; TAS. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR003017; Amphiphysin_1. DR InterPro; IPR004148; BAR. DR InterPro; IPR001452; SH3. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01252; AMPHIPHYSIN1. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD003208; Amphiphysin_1; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. KW 3D-structure; Alternative splicing; Coiled coil; Cytoskeleton; KW SH3 domain. FT CHAIN 1 695 Amphiphysin. FT /FTId=PRO_0000192947. FT DOMAIN 24 240 BAR. FT DOMAIN 622 695 SH3. FT COILED 10 83 Potential. FT COILED 144 191 Potential. FT VAR_SEQ 425 466 Missing (in isoform 2). FT /FTId=VSP_000245. FT CONFLICT 496 496 K -> T (in Ref. 5; AAH34376). FT STRAND 325 325 FT STRAND 328 328 FT HELIX 382 384 SQ SEQUENCE 695 AA; 76257 MW; 78B4F75AB75BA357 CRC64; MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFTIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPAR PRSPSQTRKG PPVPPLPKVT PTKELQQENI ISFFEDNFVP EISVTTPSQN EVPEVKKEET LLDLDFDPFK PEVTPAGSAG VTHSPMSQTL PWDLWTTSTD LVQPASGGSF NGFTQPQDTS LFTMQTDQSM ICNLAESEQA PPTEPKAEEP LAAVTPAVGL DLGMDTRAEE PVEEAVIIPG ADADAAVGTL VSAAEGAPGE EAEAEKATVP AGEGVSLEEA KIGTETTEGA ESAQPEAEEL EATVPQEKVI PSVVIEPASN HEEEGENEIT IGAEPKETTE DAAPPGPTSE TPELATEQKP IQDPQPTPSA PAMGAADQLA SAREASQELP PGFLYKVETL HDFEAANSDE LTLQRGDVVL VVPSDSEADQ DAGWLVGVKE SDWLQYRDLA TYKGLFPENF TRRLD // ID AMPH_MOUSE STANDARD; PRT; 686 AA. AC Q7TQF7; Q8R1C4; DT 16-JAN-2004, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2003, sequence version 1. DT 30-MAY-2006, entry version 25. DE Amphiphysin. GN Name=Amph; Synonyms=Amph1; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6; TISSUE=Brain, and Eye; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: May participate in mechanisms of regulated exocytosis in CC synapses and certain endocrine cell types. May control the CC properties of the membrane associated cytoskeleton (By CC similarity). CC -!- SUBUNIT: Heterodimer with BIN1. Binds SH3GLB1 (By similarity). CC -!- SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; CC peripheral membrane protein; cytoplasmic side (By similarity). CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC024817; AAH24817.1; -; mRNA. DR EMBL; BC054718; AAH54718.1; -; mRNA. DR UniGene; Mm.101650; -. DR IntAct; Q7TQF7; -. DR Ensembl; ENSMUSG00000021314; Mus musculus. DR MGI; MGI:103574; Amph. DR GO; GO:0008021; C:synaptic vesicle; IDA. DR GO; GO:0007612; P:learning; IMP. DR GO; GO:0048488; P:synaptic vesicle endocytosis; IMP. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR003017; Amphiphysin_1. DR InterPro; IPR004148; BAR. DR InterPro; IPR001452; SH3. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01252; AMPHIPHYSIN1. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD003208; Amphiphysin_1; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. KW Coiled coil; Cytoskeleton; SH3 domain. FT CHAIN 1 686 Amphiphysin. FT /FTId=PRO_0000192948. FT DOMAIN 24 240 BAR. FT DOMAIN 613 686 SH3. FT COILED 10 83 Potential. FT COILED 144 191 Potential. FT COMPBIAS 261 311 Pro-rich. SQ SEQUENCE 686 AA; 75013 MW; D292E24653A442A5 CRC64; MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSSRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFSIQGAPS DSGPLRIAKT PSPPEEPSPL PSPTASPNHT LAPASPAPVR PRSPSQTRKG PPVPPLPKVT PTKELKQENI INFFEDNFVP EINVTTPSQN EVLEVKKEET LLDLDFDPFK PDVAPAGSAA ATHSPMSQTL PWDLWTTSTD LVQPASGGSF NDFTQAQDTS LFTMQTDQNM AETEQALPTE PQAEEPPATA AAPTAGLDLG LEMEEPKEEA VIPPATDTGE TVETAVPTEG APVEEAEAEK AALPAGEGGS PEGAKIDGES TELAISESPQ PVEPEAGAPQ VIPSVVIEPA SNHEGEGEHQ ETATGTEPRE AAEDVAAQGS AGEKQEVATE PTPLDSQATL PASAGAVDAS LSAGDATQEL PPGFLYKVET LHDFEAANSD ELNLQRGDVV LVVPSDSEAD QDAGWLVGVK ESDWLQYRDL ATYKGLFPEN FTRRLE // ID AMPH_RAT STANDARD; PRT; 683 AA. AC O08838; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 30-MAY-2006, entry version 51. DE Amphiphysin. GN Name=Amph; Synonyms=Amph1; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex; RX MEDLINE=98009145; PubMed=9348539; RA Wigge P., Koehler K., Vallis Y., Doyle C., Owen D., Hunt S.P., RA McMahon H.T.; RT "Amphiphysin heterodimers: potential role in clathrin-mediated RT endocytosis."; RL Mol. Biol. Cell 8:2003-2015(1997). RN [2] RP INTERACTION WITH AP2A2. RX PubMed=10430869; DOI=10.1073/pnas.96.16.8907; RA Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.; RT "Crystal structure of the alpha appendage of AP-2 reveals a RT recruitment platform for clathrin-coat assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999). CC -!- FUNCTION: May participate in mechanisms of regulated exocytosis in CC synapses and certain endocrine cell types. May control the CC properties of the membrane associated cytoskeleton (By CC similarity). CC -!- SUBUNIT: Heterodimer with BIN1. Binds SH3GLB1 (By similarity). CC Binds AP2A2. CC -!- INTERACTION: CC O08839:Bin1; NbExp=1; IntAct=EBI-80080, EBI-80095; CC P21575:Dnm1; NbExp=1; IntAct=EBI-80080, EBI-80070; CC -!- SUBCELLULAR LOCATION: Synaptic vesicle; synaptic vesicle membrane; CC peripheral membrane protein; cytoplasmic side (By similarity). CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y13381; CAA73808.1; -; mRNA. DR UniGene; Rn.44463; -. DR HSSP; O08839; 1BB9. DR IntAct; O08838; -. DR Ensembl; ENSRNOG00000012490; Rattus norvegicus. DR RGD; 620274; Amph1. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0046982; F:protein heterodimerization activity; IMP. DR GO; GO:0043087; P:regulation of GTPase activity; IMP. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR003017; Amphiphysin_1. DR InterPro; IPR004148; BAR. DR InterPro; IPR000108; Neu_cyt_fact_2. DR InterPro; IPR001452; SH3. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01252; AMPHIPHYSIN1. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD003208; Amphiphysin_1; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. KW Coiled coil; Cytoskeleton; SH3 domain. FT CHAIN 1 683 Amphiphysin. FT /FTId=PRO_0000192949. FT DOMAIN 24 240 BAR. FT DOMAIN 610 683 SH3. FT COILED 10 83 Potential. FT COILED 144 191 Potential. SQ SEQUENCE 683 AA; 74878 MW; 7FEA4A9E5A1F6631 CRC64; MADIKTGIFA KNVQKRLNRA QEKVLQKLGK ADETKDEQFE EYVQNFKRQE AEGTRLQREL RGYLAAIKGM QEASMKLTES LHEVYEPDWY GREDVKMVGE KCDVLWEDFH QKLVDGSLLT LDTYLGQFPD IKNRIAKRSR KLVDYDSARH HLEALQSSKR KDESRISKAE EEFQKAQKVF EEFNVDLQEE LPSLWSRRVG FYVNTFKNVS SLEAKFHKEI AVLCHKLYEV MTKLGDQHAD KAFSIQGAPS DSGPLRIAKT PSPPEEASPL PSPTASPNHT LAPASPAPVR PRSPSQTRKG PPVPPLPKVT PTKELQQENI INFFEDNFVP EINVTTPSQN EVLEVKKEET LLDLDFDPFK PDVTPAGSAA ATHSPMSQTL PWDLWTTSTD LVQPASGGSF NDFTQPQDTS LFTMQTDQNM AETEQALPTE PQAEEPPTTA AAPTAGLDLG LEMEEPKEEA AIPPGTDAGE TVGTEGSTGE EAEAEKAALP AGEGESPEGA KIDVESTELA SSESPQAAEL EAGAPQEKVI PSVVIEPASN HEGEEHQETT TGTETREATE DVAPQGPAGE KQELATEPTP LDSQAATPAP AGAVDASLSA GDAAQELPPG FLYKVETLHD FEAANSDELT LQRGDVVLVV PSDSEADQDA GWLVGVKESD WLQYRDLATY KGLFPENFTR HLE // ID BIN1_HUMAN STANDARD; PRT; 593 AA. AC O00499; O00297; O00545; O43867; O60552; O60553; O60554; O60555; AC O75514; O75515; O75516; O75517; O75518; Q92944; Q99688; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 30-MAY-2006, entry version 63. DE Myc box-dependent-interacting protein 1 (Bridging integrator 1) DE (Amphiphysin-like protein) (Amphiphysin II) (Box-dependent myc- DE interacting protein 1). GN Name=BIN1; Synonyms=AMPHL; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE (ISOFORM IIA). RC TISSUE=Brain; RX MEDLINE=97341217; PubMed=9195986; DOI=10.1074/jbc.272.26.16700; RA Ramjaun A.R., Micheva K.D., Bouchelet I., McPherson P.S.; RT "Identification and characterization of a nerve terminal-enriched RT amphiphysin isoform."; RL J. Biol. Chem. 272:16700-16706(1997). RN [2] RP NUCLEOTIDE SEQUENCE (ISOFORMS IIA AND BIN1). RC TISSUE=Brain, and Skeletal muscle; RX MEDLINE=97327761; PubMed=9182667; DOI=10.1083/jcb.137.6.1355; RA Butler M.H., David C., Ochoa G.-C., Freyberg Z., Daniell L., Grabs D., RA Cremona O., De Camilli P.; RT "Amphiphysin II (SH3P9; BIN1), a member of the amphiphysin/Rvs family, RT is concentrated in the cortical cytomatrix of axon initial segments RT and nodes of Ranvier in brain and around T tubules in skeletal RT muscle."; RL J. Cell Biol. 137:1355-1367(1997). RN [3] RP NUCLEOTIDE SEQUENCE (ISOFORM BIN1). RC TISSUE=Skeletal muscle; RX MEDLINE=96376973; PubMed=8782822; DOI=10.1038/ng0996-69; RA Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.; RT "BIN1 is a novel Myc-interacting protein with features of a tumour RT suppressor."; RL Nat. Genet. 14:69-76(1996). RN [4] RP SEQUENCE REVISION TO N-TERMINUS. RA Sakamuro D., Elliott K.J., Wechsler-Reya R., Prendergast G.C.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE (ISOFORMS IIB; IIC1; IIC2 AND IID). RC TISSUE=Brain; RX MEDLINE=98264340; PubMed=9603201; RA Ramjaun A.R., McPherson P.S.; RT "Multiple amphiphysin II splice variants display differential clathrin RT binding: identification of two distinct clathrin-binding sites."; RL J. Neurochem. 70:2369-2376(1998). RN [6] RP NUCLEOTIDE SEQUENCE (ISOFORMS II2 AND II3). RC TISSUE=Brain; RX MEDLINE=97366618; PubMed=9223448; DOI=10.1006/bbrc.1997.6927; RA Tsutsui K., Maeda Y., Tsutsui K., Seki S., Tokunaga A.; RT "cDNA cloning of a novel amphiphysin isoform and tissue-specific RT expression of its multiple splice variants."; RL Biochem. Biophys. Res. Commun. 236:178-183(1997). RN [7] RP NUCLEOTIDE SEQUENCE (ISOFORMS II3; II3; BIN1-10-13; BIN1-13 AND RP BIN1+12A). RC TISSUE=Fibroblast; RX MEDLINE=98058932; PubMed=9395479; DOI=10.1074/jbc.272.50.31453; RA Wechsler-Reya R.J., Sakamuro D., Zhang J., Duhadaway J., RA Prendergast G.C.; RT "Structural analysis of the human BIN1 gene. Evidence for tissue- RT specific transcriptional regulation and alternate RNA splicing."; RL J. Biol. Chem. 272:31453-31458(1997). RN [8] RP NUCLEOTIDE SEQUENCE (ISOFORM II2). RA Zhang J., Du W., Wechsler-Reya R.J., Duhadaway J., Sakamuro D., RA Prendergast G.C.; RL Submitted (MAY-1998) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 133-593. RC TISSUE=Brain; RA Yu W., Gibbs R.A.; RL Submitted (JUN-1998) to the EMBL/GenBank/DDBJ databases. RN [10] RP CHARACTERIZATION. RC TISSUE=Skeletal muscle; RX MEDLINE=98078712; PubMed=9418903; RA Wechsler-Reya R.J., Elliott K.J., Prendergast G.C.; RT "A role for the putative tumor suppressor Bin1 in muscle cell RT differentiation."; RL Mol. Cell. Biol. 18:566-575(1998). RN [11] RP PHOSPHORYLATION AT SER-296; SER-298 AND SER-303. RX PubMed=15302935; DOI=10.1073/pnas.0404720101; RA Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., RA Li J., Cohn M.A., Cantley L.C., Gygi S.P.; RT "Large-scale characterization of HeLa cell nuclear phosphoproteins."; RL Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). CC -!- FUNCTION: May be involved in regulation of synaptic vesicle CC endocytosis. May act as a tumor suppressor and inhibits malignant CC cell transformation. CC -!- SUBUNIT: Heterodimer with AMPH. Binds SH3GLB1 (By similarity). CC Binds to SYNJ1 and DNM1 through its SH3 domain, and to clathrin CC through a region outside of the SH3 domain. Also binds AP2A2. CC Interacts with the N-terminal transactivation domain of MYC in a CC manner requiring the integrity of the conserved MYC box regions 1 CC and 2. CC -!- SUBCELLULAR LOCATION: Isoform BIN1: Nucleus. Isoform IIa: CC Cytoplasm. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=11; CC Comment=Additional isoforms seem to exist; CC Name=IIA; CC IsoId=O00499-1; Sequence=Displayed; CC Name=IIB; CC IsoId=O00499-2; Sequence=VSP_000246, VSP_000252; CC Name=IIC1; CC IsoId=O00499-3; Sequence=VSP_000249; CC Name=IIC2; CC IsoId=O00499-4; Sequence=VSP_000246, VSP_000249; CC Name=IID; CC IsoId=O00499-5; Sequence=VSP_000248; CC Name=II2; CC IsoId=O00499-6; Sequence=VSP_000246, VSP_000253; CC Name=II3; CC IsoId=O00499-7; Sequence=VSP_000246, VSP_000250; CC Name=BIN1; CC IsoId=O00499-8; Sequence=VSP_000246, VSP_000247, VSP_000250; CC Name=BIN1-10-13; CC IsoId=O00499-9; Sequence=VSP_000246, VSP_000251; CC Name=BIN1-13; CC IsoId=O00499-10; Sequence=VSP_000246, VSP_000247, VSP_000251; CC Name=BIN1+12A; CC IsoId=O00499-11; Sequence=VSP_000246, VSP_000247, VSP_000253; CC -!- TISSUE SPECIFICITY: Isoform IIA is expressed only in the brain CC where it is concentrated in axon initial segments and nodes of CC Ranvier. Isoform BIN1 is widely expressed with highest expression CC in skeletal muscle. CC -!- PTM: Phosphorylated by protein kinase C (By similarity). CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF004015; AAC51345.1; -; mRNA. DR EMBL; AF070576; AAC28646.1; -; mRNA. DR EMBL; U68485; AAC17461.1; -; mRNA. DR EMBL; AF001383; AAB61363.1; -; mRNA. DR EMBL; AF043898; AAC39710.1; -; mRNA. DR EMBL; AF043899; AAC39711.1; -; mRNA. DR EMBL; AF043900; AAC39712.1; -; mRNA. DR EMBL; AF043901; AAC39713.1; -; mRNA. DR EMBL; U87558; AAB63263.1; -; mRNA. DR EMBL; AF068914; AAC24126.1; -; mRNA. DR EMBL; AF068915; AAC24127.1; -; mRNA. DR EMBL; AF068916; AAC24128.1; -; mRNA. DR EMBL; AF068917; AAC23750.1; -; mRNA. DR EMBL; AF068918; AAC23751.1; -; mRNA. DR EMBL; U84004; AAC23440.1; -; Genomic_DNA. DR EMBL; U83999; AAC23440.1; JOINED; Genomic_DNA. DR EMBL; U84001; AAC23440.1; JOINED; Genomic_DNA. DR EMBL; U84002; AAC23440.1; JOINED; Genomic_DNA. DR EMBL; U84003; AAC23440.1; JOINED; Genomic_DNA. DR EMBL; U84004; AAC23441.1; ALT_INIT; Genomic_DNA. DR EMBL; U83999; AAC23441.1; JOINED; Genomic_DNA. DR EMBL; U84001; AAC23441.1; JOINED; Genomic_DNA. DR EMBL; U84002; AAC23441.1; JOINED; Genomic_DNA. DR EMBL; U84003; AAC23441.1; JOINED; Genomic_DNA. DR PIR; JC5593; JC5593. DR UniGene; Hs.193163; -. DR PDB; 1MUZ; NMR; A=513-593. DR PDB; 1MV0; NMR; B=513-593. DR PDB; 1MV3; NMR; A=301-593. DR TRANSFAC; T03490; -. DR Ensembl; ENSG00000136717; Homo sapiens. DR H-InvDB; HIX0002430; -. DR HGNC; HGNC:1052; BIN1. DR MIM; 601248; gene. DR GO; GO:0015629; C:actin cytoskeleton; TAS. DR GO; GO:0008283; P:cell proliferation; TAS. DR GO; GO:0000074; P:regulation of progression through cell cycle; TAS. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR003023; Amphiphysin_2. DR InterPro; IPR004148; BAR. DR InterPro; IPR001452; SH3. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01253; AMPHIPHYSIN2. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. KW 3D-structure; Alternative splicing; Anti-oncogene; Cell cycle; KW Coiled coil; Developmental protein; Differentiation; Endocytosis; KW Nuclear protein; Phosphorylation; SH3 domain. FT CHAIN 1 593 Myc box-dependent-interacting protein 1. FT /FTId=PRO_0000192951. FT DOMAIN 29 276 BAR. FT DOMAIN 520 592 SH3. FT REGION 378 421 Clathrin-binding. FT COILED 15 42 Potential. FT COILED 193 267 Potential. FT MOD_RES 296 296 Phosphoserine. FT MOD_RES 298 298 Phosphoserine. FT MOD_RES 303 303 Phosphoserine. FT VAR_SEQ 174 204 Missing (in isoform IIB, isoform IIC2, FT isoform II2, isoform II3, isoform BIN1, FT isoform BIN1+12A, isoform BIN1-10-13 and FT isoform BIN1-13). FT /FTId=VSP_000246. FT VAR_SEQ 285 285 P -> PRKKSKLFSRLRRKKN (in isoform BIN1, FT isoform BIN1+12A and isoform BIN1-13). FT /FTId=VSP_000247. FT VAR_SEQ 335 487 Missing (in isoform BIN1-10-13 and FT isoform BIN1-13). FT /FTId=VSP_000251. FT VAR_SEQ 335 457 Missing (in isoform II3 and isoform FT BIN1). FT /FTId=VSP_000250. FT VAR_SEQ 335 421 Missing (in isoform IIC1 and isoform FT IIC2). FT /FTId=VSP_000249. FT VAR_SEQ 335 377 Missing (in isoform IID). FT /FTId=VSP_000248. FT VAR_SEQ 378 457 Missing (in isoform II2 and isoform FT BIN1+12A). FT /FTId=VSP_000253. FT VAR_SEQ 378 421 Missing (in isoform IIB). FT /FTId=VSP_000252. FT CONFLICT 474 474 A -> P (in Ref. 2). FT CONFLICT 481 481 A -> S (in Ref. 9). FT CONFLICT 510 510 S -> C (in Ref. 7). FT CONFLICT 528 528 Q -> H (in Ref. 7). FT CONFLICT 576 576 E -> K (in Ref. 7). FT STRAND 335 335 FT STRAND 345 345 FT STRAND 467 468 FT STRAND 515 516 FT TURN 519 520 FT STRAND 523 527 FT STRAND 529 529 FT STRAND 531 531 FT STRAND 535 537 FT STRAND 541 541 FT STRAND 543 544 FT STRAND 546 549 FT STRAND 553 553 FT HELIX 555 557 FT TURN 560 561 FT STRAND 562 567 FT HELIX 568 579 FT TURN 580 580 FT STRAND 582 585 FT HELIX 586 588 FT STRAND 589 591 SQ SEQUENCE 593 AA; 64699 MW; 0FF1956F0C7E3B50 CRC64; MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLNECLQEVY EPDWPGRDEA NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN TFQSIAGLEE NFHKEMSKLN QNLNDVLVGL EKQHGSNTFT VKAQPSDNAP AKGNKSPSPP DGSPAATPEI RVNHEPEPAG GATPGATLPK SPSQLRKGPP VPPPPKHTPS KEVKQEQILS LFEDTFVPEI SVTTPSQFEA PGPFSEQASL LDLDFDPLPP VTSPVKAPTP SGQSIPWDLW EPTESPAGSL PSGEPSAAEG TFAVSWPSQT AEPGPAQPAE ASEVAGGTQP AAGAQEPGET AASEAASSSL PAVVVETFPA TVNGTVEGGS GAGRLDLPPG FMFKVQAQHD YTATDTDELQ LKAGDVVLVI PFQNPEEQDE GWLMGVKESD WNQHKELEKC RGVFPENFTE RVP // ID BIN1_MOUSE STANDARD; PRT; 588 AA. AC O08539; Q62434; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 30-MAY-2006, entry version 66. DE Myc box-dependent-interacting protein 1 (Bridging integrator 1) DE (Amphiphysin-like protein) (Amphiphysin II) (SH3-domain-containing DE protein 9). GN Name=Bin1; Synonyms=Amphl, Sh3p9; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RC STRAIN=BALB/c; TISSUE=Brain; RX MEDLINE=97326078; PubMed=9182529; DOI=10.1074/jbc.272.24.15101; RA Leprince C., Romero F., Cussac D., Vayssiere B., Berger R., RA Tavitian A., Camonis J.H.; RT "A new member of the amphiphysin family connecting endocytosis and RT signal transduction pathways."; RL J. Biol. Chem. 272:15101-15105(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2). RC TISSUE=Embryo; RX MEDLINE=98294438; PubMed=9630982; DOI=10.1038/nbt0696-741; RA Sparks A.B., Hoffman N.G., McConnell S.J., Fowlkes D.M., Kay B.K.; RT "Cloning of ligand targets: systematic isolation of SH3 domain- RT containing proteins."; RL Nat. Biotechnol. 14:741-744(1996). RN [3] RP INTERACTION WITH SH3GLB1. RX PubMed=12456676; DOI=10.1074/jbc.M208568200; RA Modregger J., Schmidt A.A., Ritter B., Huttner W.B., Plomann M.; RT "Characterization of endophilin B1b, a brain-specific membrane- RT associated lysophosphatidic acid acyl transferase with properties RT distinct from endophilin A1."; RL J. Biol. Chem. 278:4160-4167(2003). CC -!- FUNCTION: May be involved in regulation of synaptic vesicle CC endocytosis. May act as a tumor suppressor and inhibits malignant CC cell transformation. CC -!- SUBUNIT: Heterodimer with AMPH (By similarity). Binds to SYNJ1 and CC DNM1 through its SH3 domain, and to clathrin through a region CC outside of the SH3 domain. Binds AP2A2. Interacts with the N- CC terminal transactivation domain of MYC in a manner requiring the CC integrity of the conserved MYC box regions 1 and 2. Binds SH3GLB1. CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; Synonyms=BRAMP2; CC IsoId=O08539-1; Sequence=Displayed; CC Name=2; Synonyms=SH3P9; CC IsoId=O08539-2; Sequence=VSP_000254, VSP_000255; CC -!- TISSUE SPECIFICITY: Isoform 1 is expressed mainly in the brain. CC Isoform 2 is widely expressed. CC -!- PTM: Phosphorylated by protein kinase C (By similarity). CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; U86405; AAC53318.1; -; mRNA. DR EMBL; U60884; AAC52661.1; -; mRNA. DR UniGene; Mm.4383; -. DR HSSP; O08839; 1BB9. DR SMR; O08539; 302-378, 507-588. DR IntAct; O08539; -. DR Ensembl; ENSMUSG00000024381; Mus musculus. DR MGI; MGI:108092; Bin1. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR003017; Amphiphysin_1. DR InterPro; IPR003023; Amphiphysin_2. DR InterPro; IPR004148; BAR. DR InterPro; IPR001452; SH3. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01253; AMPHIPHYSIN2. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD003208; Amphiphysin_1; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. KW Alternative splicing; Anti-oncogene; Cell cycle; Coiled coil; KW Developmental protein; Differentiation; Endocytosis; Nuclear protein; KW Phosphorylation; SH3 domain. FT CHAIN 1 588 Myc box-dependent-interacting protein 1. FT /FTId=PRO_0000192952. FT DOMAIN 29 276 BAR. FT DOMAIN 515 588 SH3. FT REGION 379 422 Clathrin-binding (By similarity). FT COILED 15 42 Potential. FT COILED 193 274 Potential. FT MOD_RES 296 296 Phosphoserine (By similarity). FT MOD_RES 298 298 Phosphoserine (By similarity). FT MOD_RES 304 304 Phosphoserine (By similarity). FT VAR_SEQ 174 204 Missing (in isoform 2). FT /FTId=VSP_000254. FT VAR_SEQ 335 457 Missing (in isoform 2). FT /FTId=VSP_000255. SQ SEQUENCE 588 AA; 64470 MW; 63CA362461500F38 CRC64; MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLSECLQEVY EPEWPGRDEA NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN TFQSIAGLEE NFHKEMSKLN QNLNDVLVSL EKQHGSNTFT VKAQPSDNAP EKGNKSPSPP PDGSPAATPE IRVNHEPEPA SGASPGATIP KSPSQLRKGP PVPPPPKHTP SKEMKQEQIL SLFDDAFVPE ISVTTPSQFE APGPFSEQAS LLDLDFEPLP PVASPVKAPT PSGQSIPWDL WEPTESQAGI LPSGEPSSAE GSFAVAWPSQ TAEPGPAQPA EASEVVGGAQ EPGETAASEA TSSSLPAVVV ETFSATVNGA VEGSAGTGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD VVLVIPFQNP EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVQ // ID BIN1_RAT STANDARD; PRT; 588 AA. AC O08839; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-JUL-1997, sequence version 1. DT 30-MAY-2006, entry version 67. DE Myc box-dependent-interacting protein 1 (Bridging integrator 1) DE (Amphiphysin-like protein) (Amphiphysin II). GN Name=Bin1; Synonyms=Amph2, Amphl; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], SUBUNIT, AND ALTERNATIVE SPLICING. RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex, and Kidney; RX MEDLINE=98009145; PubMed=9348539; RA Wigge P., Koehler K., Vallis Y., Doyle C., Owen D., Hunt S.P., RA McMahon H.T.; RT "Amphiphysin heterodimers: potential role in clathrin-mediated RT endocytosis."; RL Mol. Biol. Cell 8:2003-2015(1997). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM AMPH2-1). RC STRAIN=Sprague-Dawley; TISSUE=Brain cortex; RX MEDLINE=97424383; PubMed=9280305; DOI=10.1016/S0014-5793(97)00928-9; RA McMahon H.T., Wigge P., Smith C.; RT "Clathrin interacts specifically with amphiphysin and is displaced by RT dynamin."; RL FEBS Lett. 413:319-322(1997). RN [3] RP INTERACTION WITH AP2A2. RX PubMed=10430869; DOI=10.1073/pnas.96.16.8907; RA Traub L.M., Downs M.A., Westrich J.L., Fremont D.H.; RT "Crystal structure of the alpha appendage of AP-2 reveals a RT recruitment platform for clathrin-coat assembly."; RL Proc. Natl. Acad. Sci. U.S.A. 96:8907-8912(1999). RN [4] RP X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 506-588, FUNCTION, AND RP INTERACTION WITH DNM1. RX PubMed=9736607; DOI=10.1093/emboj/17.18.5273; RA Owen D.J., Wigge P., Vallis Y., Moore J.D.A., Evans P.R., RA McMahon H.T.; RT "Crystal structure of the amphiphysin-2 SH3 domain and its role in the RT prevention of dynamin ring formation."; RL EMBO J. 17:5273-5285(1998). CC -!- FUNCTION: May be involved in regulation of synaptic vesicle CC endocytosis. May act as a tumor suppressor and inhibits malignant CC cell transformation. CC -!- SUBUNIT: Heterodimer with AMPH. Binds SH3GLB1 (By similarity). CC Binds to SYNJ1 and DNM1 through its SH3 domain, and to clathrin CC through a region outside of the SH3 domain. Also binds AP2A2. CC Interacts with the N-terminal transactivation domain of MYC in a CC manner requiring the integrity of the conserved MYC box regions 1 CC and 2. CC -!- INTERACTION: CC O08838:Amph; NbExp=1; IntAct=EBI-80095, EBI-80080; CC P21575:Dnm1; NbExp=1; IntAct=EBI-80095, EBI-80070; CC -!- SUBCELLULAR LOCATION: Cytoplasm (By similarity). Nucleus (By CC similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=AMPH2-1; CC IsoId=O08839-1; Sequence=Displayed; CC Name=AMPH2-2; CC IsoId=O08839-2; Sequence=VSP_000260; CC Name=AMPH2-3; CC IsoId=O08839-3; Sequence=VSP_000258; CC Name=AMPH2-4; CC IsoId=O08839-4; Sequence=VSP_000256, VSP_000257; CC Name=AMPH2-5; CC IsoId=O08839-5; Sequence=VSP_000259; CC Name=AMPH2-6; CC IsoId=O08839-6; Sequence=VSP_000256, VSP_000259; CC -!- TISSUE SPECIFICITY: Isoform AMPH2-1 is expressed in brain, CC concentrated at nerve terminals. Isoform AMPH2-2 is widely CC expressed. CC -!- PTM: Phosphorylated by protein kinase C. CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; Y13380; CAA73807.1; -; mRNA. DR UniGene; Rn.17098; -. DR PDB; 1BB9; X-ray; @=495-588. DR SMR; O08839; 302-378. DR IntAct; O08839; -. DR Ensembl; ENSRNOG00000012852; Rattus norvegicus. DR RGD; 621786; Bin1. DR LinkHub; O08839; -. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0046982; F:protein heterodimerization activity; IPI. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR003017; Amphiphysin_1. DR InterPro; IPR003023; Amphiphysin_2. DR InterPro; IPR004148; BAR. DR InterPro; IPR001452; SH3. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR PRINTS; PR01253; AMPHIPHYSIN2. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD003208; Amphiphysin_1; 1. DR ProDom; PD000066; SH3; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. KW 3D-structure; Alternative splicing; Anti-oncogene; Cell cycle; KW Coiled coil; Developmental protein; Differentiation; Endocytosis; KW Nuclear protein; Phosphorylation; SH3 domain. FT CHAIN 1 588 Myc box-dependent-interacting protein 1. FT /FTId=PRO_0000192953. FT DOMAIN 29 276 BAR. FT DOMAIN 515 588 SH3. FT REGION 379 422 Clathrin-binding (By similarity). FT COILED 15 42 Potential. FT COILED 193 274 Potential. FT MOD_RES 296 296 Phosphoserine (By similarity). FT MOD_RES 298 298 Phosphoserine (By similarity). FT MOD_RES 304 304 Phosphoserine (By similarity). FT VAR_SEQ 173 205 Missing (in isoform AMPH2-4 and isoform FT AMPH2-6). FT /FTId=VSP_000256. FT VAR_SEQ 253 588 Missing (in isoform AMPH2-4). FT /FTId=VSP_000257. FT VAR_SEQ 335 588 Missing (in isoform AMPH2-3). FT /FTId=VSP_000258. FT VAR_SEQ 335 482 Missing (in isoform AMPH2-5 and isoform FT AMPH2-6). FT /FTId=VSP_000259. FT VAR_SEQ 423 460 Missing (in isoform AMPH2-2). FT /FTId=VSP_000260. FT STRAND 510 511 FT TURN 514 515 FT STRAND 518 524 FT STRAND 526 526 FT STRAND 529 530 FT TURN 531 532 FT STRAND 533 533 FT STRAND 536 536 FT TURN 538 539 FT STRAND 541 545 FT STRAND 548 548 FT HELIX 550 552 FT TURN 555 556 FT STRAND 557 562 FT HELIX 563 567 FT TURN 568 569 FT HELIX 572 575 FT STRAND 577 580 FT HELIX 581 583 FT STRAND 584 587 SQ SEQUENCE 588 AA; 64533 MW; 164AC90E09547F1A CRC64; MAEMGSKGVT AGKIASNVQK KLTRAQEKVL QKLGKADETK DEQFEQCVQN FNKQLTEGTR LQKDLRTYLA SVKAMHEASK KLSECLQEVY EPEWPGRDEA NKIAENNDLL WMDYHQKLVD QALLTMDTYL GQFPDIKSRI AKRGRKLVDY DSARHHYESL QTAKKKDEAK IAKPVSLLEK AAPQWCQGKL QAHLVAQTNL LRNQAEEELI KAQKVFEEMN VDLQEELPSL WNSRVGFYVN TFQSIAGLEE NFHKEMSKLN QNLNDVLVSL EKQHGSNTFT VKAQPSDSAP EKGNKSPSPP PDGSPAATPE IRVNHEPEPA SGASPGATIP KSPSQLRKGP PVPPPPKHTP SKEMKQEQIL SLFDDAFVPE ISVTTPSQFE APGPFSEQAS LLDLDFEPLP PVASPVKAPT PSGQSIPWDL WEPTESQAGV LPSGEPSSAE GSFAVAWPSQ TAEPGPAQPA EASEVVGGTQ EPGETAASEA TSSSLPAVVV ETFSATVNGA VEGSTTTGRL DLPPGFMFKV QAQHDYTATD TDELQLKAGD VVLVIPFQNP EEQDEGWLMG VKESDWNQHK ELEKCRGVFP ENFTERVQ // ID BIN3_HUMAN STANDARD; PRT; 253 AA. AC Q9NQY0; Q9BVG2; Q9NVY9; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 30-MAY-2006, entry version 29. DE Bridging integrator 3. GN Name=BIN3; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RX MEDLINE=21293007; PubMed=11274158; DOI=10.1074/jbc.M101096200; RA Routhier E.L., Burn T.C., Abbaszade I., Summers M., Albright C.F., RA Prendergast G.C.; RT "Human BIN3 complements the F-actin localization defects caused by RT loss of Hob3p, the fission yeast homolog of Rvs161p."; RL J. Biol. Chem. 276:21670-21677(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Lung, and Skin; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: Involved in cytokinesis and septation where it has a CC role in the localization of F-actin. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9NQY0-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9NQY0-2; Sequence=VSP_013465; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Ubiquitously expressed except in brain. CC -!- SIMILARITY: Contains 1 BAR domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF271732; AAF76218.1; -; mRNA. DR EMBL; AK001289; BAA91603.1; -; mRNA. DR EMBL; AK023980; BAB14751.1; -; mRNA. DR EMBL; BC001223; AAH01223.1; ALT_INIT; mRNA. DR EMBL; BC009824; AAH09824.1; -; mRNA. DR UniGene; Hs.232256; -. DR Ensembl; ENSG00000147439; Homo sapiens. DR H-InvDB; HIX0007372; -. DR HGNC; HGNC:1054; BIN3. DR MIM; 606396; gene. DR GO; GO:0008093; F:cytoskeletal adaptor activity; NAS. DR GO; GO:0007015; P:actin filament organization; NAS. DR GO; GO:0000910; P:cytokinesis; NAS. DR GO; GO:0008104; P:protein localization; IMP. DR GO; GO:0009826; P:unidimensional cell growth; IMP. DR InterPro; IPR004148; BAR. DR Pfam; PF03114; BAR; 1. DR SMART; SM00721; BAR; 1. DR PROSITE; PS51021; BAR; 1. KW Alternative splicing; Cell cycle; Cell division; Coiled coil; KW Cytoskeleton; Septation. FT CHAIN 1 253 Bridging integrator 3. FT /FTId=PRO_0000192955. FT DOMAIN 9 232 BAR. FT COILED 18 51 Potential. FT COILED 120 152 Potential. FT COILED 231 247 Potential. FT VAR_SEQ 1 54 Missing (in isoform 2). FT /FTId=VSP_013465. FT CONFLICT 122 122 N -> I (in Ref. 2; BAA91603). SQ SEQUENCE 253 AA; 29665 MW; 254CC7113749C584 CRC64; MSWIPFKIGQ PKKQIVPKTV ERDFEREYGK LQQLEEQTRR LQKDMKKSTD ADLAMSKSAV KISLDLLSNP LCEQDQDLLN MVTALDTAMK RMDAFNQEKV NQIQKTVIEP LKKFGSVFPS LNMAVKRREQ ALQDYRRLQA KVEKYEEKEK TGPVLAKLHQ AREELRPVRE DFEAKNRQLL EEMPRFYGSR LDYFQPSFES LIRAQVVYYS EMHKIFGDLS HQLDQPGHSD EQRERENEAK LSELRALSIV ADD // ID BIN3_MOUSE STANDARD; PRT; 253 AA. AC Q9JI08; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-OCT-2000, sequence version 1. DT 02-MAY-2006, entry version 29. DE Bridging integrator 3. GN Name=Bin3; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA]. RX MEDLINE=21293007; PubMed=11274158; DOI=10.1074/jbc.M101096200; RA Routhier E.L., Burn T.C., Abbaszade I., Summers M., Albright C.F., RA Prendergast G.C.; RT "Human BIN3 complements the F-actin localization defects caused by RT loss of Hob3p, the fission yeast homolog of Rvs161p."; RL J. Biol. Chem. 276:21670-21677(2001). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA]. RA Marcucci M.J., Slepnev V.I., De Camilli P.V.; RT "A mouse homolog of Saccharomyces cerevisiae RVS161 gene."; RL Submitted (MAR-2000) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=C57BL/6J; TISSUE=Aorta, Testis, and Vein; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=FVB/N; TISSUE=Kidney; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: Involved in cytokinesis and septation where it has a CC role in the localization of F-actin (By similarity). CC -!- SIMILARITY: Contains 1 BAR domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF271733; AAF76219.1; -; mRNA. DR EMBL; AF244361; AAK28356.1; -; mRNA. DR EMBL; AK005992; BAB24356.1; -; mRNA. DR EMBL; AK040685; BAC30666.1; -; mRNA. DR EMBL; BC026543; AAH26543.1; -; mRNA. DR UniGene; Mm.24186; -. DR Ensembl; ENSMUSG00000022089; Mus musculus. DR MGI; MGI:1929883; Bin3. DR GO; GO:0008093; F:cytoskeletal adaptor activity; ISS. DR GO; GO:0007015; P:actin filament organization; ISS. DR GO; GO:0000910; P:cytokinesis; ISS. DR GO; GO:0008104; P:protein localization; ISS. DR GO; GO:0009826; P:unidimensional cell growth; ISS. DR InterPro; IPR004148; BAR. DR Pfam; PF03114; BAR; 1. DR SMART; SM00721; BAR; 1. DR PROSITE; PS51021; BAR; 1. KW Cell cycle; Cell division; Coiled coil; Cytoskeleton; Septation. FT CHAIN 1 253 Bridging integrator 3. FT /FTId=PRO_0000192956. FT DOMAIN 9 232 BAR. FT COILED 16 57 Potential. FT COILED 120 151 Potential. SQ SEQUENCE 253 AA; 29651 MW; 051928DAB0CB7274 CRC64; MSWIPFKIGQ PKKQIVSKTV ERDFEREYGK LQQLEEQTKR LQKDMKKSTD ADLAMSKSAV KISQDLLSNP LCEQDQDFLH MVTALDTAMK RMDAFNQEKV NQIQKTVIEP LKKFSSIFPS LNMAVKRREQ ALQDYGRLQA KVEKYEEKEK TGPVLAKLHQ AREELRPVRE DFEAKNKQLL DEMPRFYGSR LDYFQPSFES LIRAQVIYYS EMHKIFGDLT QQLDQPGHSD EQRERENETK LSELRALSIV ADD // ID BIN3_RAT STANDARD; PRT; 253 AA. AC Q68FW8; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 11-OCT-2004, sequence version 1. DT 04-APR-2006, entry version 13. DE Bridging integrator 3. GN Name=Bin3; OS Rattus norvegicus (Rat). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Rattus. OX NCBI_TaxID=10116; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Kidney; RG NIH - Mammalian Gene Collection (MGC) project; RL Submitted (AUG-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in cytokinesis and septation where it has a CC role in the localization of F-actin (By similarity). CC -!- SIMILARITY: Contains 1 BAR domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC079146; AAH79146.1; -; mRNA. DR UniGene; Rn.153573; -. DR Ensembl; ENSRNOG00000018023; Rattus norvegicus. DR RGD; 1308253; Bin3. DR InterPro; IPR004148; BAR. DR Pfam; PF03114; BAR; 1. DR SMART; SM00721; BAR; 1. DR PROSITE; PS51021; BAR; 1. KW Cell cycle; Cell division; Coiled coil; Cytoskeleton; Septation. FT CHAIN 1 253 Bridging integrator 3. FT /FTId=PRO_0000192957. FT DOMAIN 9 232 BAR. FT COILED 16 57 Potential. FT COILED 120 151 Potential. SQ SEQUENCE 253 AA; 29691 MW; 5C4C6BF5AA8A8EDD CRC64; MSWIPFKIGQ PKKQIVSKTV ERDFEREYGK LQQLEEQTKR LQKDMKKSTD ADLAMSKSAV KISLDLLSNP LCEQDQDFLR MVTALDTAMK RMDAFNQEKV NQIQKTVIEP LKKFGSIFPS LNMAVKRREQ ALQDYGRLQA KVEKYEEKEK TGPVLAKLHQ AREELRPVRE DFEAKNKQLL DEMPRFYNSR LDYFQPSFES LIRAQVIYYS EMHKIFGDLT QQLDQPGHSD EHRERENETK LSELRALSIV ADD // ID BIN3_XENLA STANDARD; PRT; 252 AA. AC Q5PPZ5; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 04-JAN-2005, sequence version 1. DT 04-APR-2006, entry version 12. DE Bridging integrator 3 homolog. GN Name=bin3; OS Xenopus laevis (African clawed frog). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Amphibia; Batrachia; Anura; Mesobatrachia; Pipoidea; Pipidae; OC Xenopodinae; Xenopus; Xenopus. OX NCBI_TaxID=8355; RN [1] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Testis; RG NIH - Xenopus Gene Collection (XGC) project; RL Submitted (DEC-2004) to the EMBL/GenBank/DDBJ databases. CC -!- FUNCTION: Involved in cytokinesis and septation where it has a CC role in the localization of F-actin (By similarity). CC -!- SIMILARITY: Contains 1 BAR domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; BC087428; AAH87428.1; -; mRNA. DR UniGene; Xl.49879; -. DR InterPro; IPR004148; BAR. DR Pfam; PF03114; BAR; 1. DR SMART; SM00721; BAR; 1. DR PROSITE; PS51021; BAR; 1. KW Cell cycle; Cell division; Coiled coil; Cytoskeleton; Septation. FT CHAIN 1 252 Bridging integrator 3 homolog. FT /FTId=PRO_0000192958. FT DOMAIN 8 231 BAR. FT COILED 17 57 Potential. FT COILED 119 150 Potential. FT COILED 224 244 Potential. SQ SEQUENCE 252 AA; 29383 MW; 6ADB71846DF740A3 CRC64; MSWNLFKGGP KKQIVPKTVE RDFEREYGKL QQLEDQIKKL QKDMKKSIEA DLAMSKSAVR ISSDLLGNPL CEPDVDFLQM VTALDTAMKR MDAFNQEKVN QIQKTVMDPL KRYSSVFPSL NMAVKRREQA LQDYKRLQTK VEKYEEKDKT GAMIAKLHQA REELRPVRDD FEAKNHQLLD EMPKFYNSRT DFFKPSFQSL IRAQVVYYTE MSRVFGDLAQ QVDEVQLSDA EREQENEARL AELRSLSIVA DD // ID DNMBP_HUMAN STANDARD; PRT; 1577 AA. AC Q6XZF7; Q8IVY3; Q9Y2L3; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 05-JUL-2004, sequence version 1. DT 30-MAY-2006, entry version 27. DE Dynamin-binding protein (Scaffold protein Tuba). GN Name=DNMBP; Synonyms=KIAA1010; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; OC Catarrhini; Hominidae; Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING, AND RP TISSUE SPECIFICITY. RC TISSUE=Brain, and Skeletal muscle; RX PubMed=14506234; DOI=10.1074/jbc.M308104200; RA Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H., RA Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.; RT "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology RT domains, links dynamin to regulation of the actin cytoskeleton."; RL J. Biol. Chem. 278:49031-49043(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 263-1577 (ISOFORM 1). RC TISSUE=Brain; RX MEDLINE=99246063; PubMed=10231032; DOI=10.1093/dnares/6.1.63; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Hirosawa M., RA Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XIII. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 6:63-70(1999). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANT RP TRP-1413. RC TISSUE=Uterus; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). RN [4] RP STRUCTURE BY NMR OF 1278-1353 AND 1510-1575. RG RIKEN structural genomics initiative (RSGI); RT "NMR structure of SH3 domain of hypothetical protein BAA76854.1."; RL Submitted (DEC-2003) to the PDB data bank. CC -!- FUNCTION: Scaffold protein that links dynamin with actin- CC regulating proteins. May play a role in membrane trafficking CC between the cell surface and the Golgi (By similarity). CC -!- SUBUNIT: Binds DNM1 via its N-terminal SH3 domains. The C-terminal CC SH3 domain binds a complex containing actin, tubulin, Hsp70 and CC actin-regulatory proteins, such as ENAH, EVL, WASL, WIRE, CR16, CC WAVE1 and NAP1L1 (By similarity). CC -!- SUBCELLULAR LOCATION: Cytoplasmic. Localized to synapses and Golgi CC stacks (By similarity). CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q6XZF7-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6XZF7-2; Sequence=VSP_012079; CC -!- TISSUE SPECIFICITY: Detected in heart, brain, lung, liver, CC skeletal muscle, kidney and pancreas. CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain. CC -!- SIMILARITY: Contains 6 SH3 domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY196211; AAP34307.1; -; mRNA. DR EMBL; AB023227; BAA76854.1; -; mRNA. DR EMBL; BC041628; AAH41628.1; -; mRNA. DR UniGene; Hs.500771; -. DR PDB; 1UG1; NMR; A=1278-1358. DR PDB; 1UHC; NMR; A=1509-1575. DR Ensembl; ENSG00000107554; Homo sapiens. DR HGNC; HGNC:30373; DNMBP. DR LinkHub; Q6XZF7; -. DR InterPro; IPR004148; BAR. DR InterPro; IPR001331; GDS_CDC24. DR InterPro; IPR000108; Neu_cyt_fact_2. DR InterPro; IPR000219; RhoGEF. DR InterPro; IPR001452; SH3. DR InterPro; IPR011511; SH3_2. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00621; RhoGEF; 1. DR Pfam; PF00018; SH3_1; 4. DR Pfam; PF07653; SH3_2; 2. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 4. DR SMART; SM00721; BAR; 1. DR SMART; SM00325; RhoGEF; 1. DR SMART; SM00326; SH3; 6. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS00741; DH_1; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50002; SH3; 5. KW 3D-structure; Alternative splicing; Coiled coil; Cytoskeleton; KW Golgi apparatus; Polymorphism; Repeat; SH3 domain. FT CHAIN 1 1577 Dynamin-binding protein. FT /FTId=PRO_0000079959. FT DOMAIN 2 61 SH3 1. FT DOMAIN 66 126 SH3 2. FT DOMAIN 145 204 SH3 3. FT DOMAIN 243 302 SH3 4. FT DOMAIN 784 967 DH. FT DOMAIN 1008 1217 BAR. FT DOMAIN 1285 1348 SH3 5. FT DOMAIN 1513 1576 SH3 6. FT COILED 693 757 Potential. FT COILED 1136 1173 Potential. FT COMPBIAS 610 649 Pro-rich. FT COMPBIAS 1351 1449 Ser-rich. FT VAR_SEQ 1 754 Missing (in isoform 2). FT /FTId=VSP_012079. FT VARIANT 1413 1413 C -> W (in dbSNP:11190305). FT /FTId=VAR_024339. FT CONFLICT 831 831 M -> T (in Ref. 3). FT HELIX 1273 1283 FT STRAND 1284 1284 FT HELIX 1286 1288 FT STRAND 1289 1294 FT STRAND 1300 1302 FT TURN 1308 1309 FT STRAND 1311 1317 FT TURN 1320 1321 FT STRAND 1322 1322 FT STRAND 1324 1330 FT STRAND 1332 1339 FT HELIX 1340 1342 FT STRAND 1343 1345 FT STRAND 1350 1351 FT STRAND 1510 1511 FT STRAND 1514 1515 FT STRAND 1518 1522 FT STRAND 1524 1524 FT STRAND 1528 1531 FT STRAND 1534 1534 FT TURN 1536 1537 FT STRAND 1539 1545 FT TURN 1548 1549 FT STRAND 1550 1550 FT TURN 1552 1553 FT STRAND 1554 1561 FT STRAND 1563 1567 FT HELIX 1568 1570 FT STRAND 1571 1573 SQ SEQUENCE 1577 AA; 177347 MW; 5A1FDCB06124F627 CRC64; MEAGSVVRAI FDFCPSVSEE LPLFVGDIIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEIVT IPSLKEGERL FVCICEFTSQ ELDNLPLHRG DLVILDGIPT AGWLQGRSCW GARGFFPSSC VRELCLSSQS RQWHSQSALF QIPEYSMGQA RALMGLSAQL DEELDFREGD VITIIGVPEP GWFEGELEGR RGIFPEGFVE LLGPLRTVDE SVSSGNQDDC IVNGEVDTPV GEEEIGPDED EEEPGTYGVA LYRFQALEPN ELDFEVGDKI RILATLEDGW LEGSLKGRTG IFPYRFVKLC PDTRVEETMA LPQEGSLARI PETSLDCLEN TLGVEEQRHE TSDHEAEEPD CIISEAPTSP LGHLTSEYDT DRNSYQDEDT AGGPPRSPGV EWEMPLATDS PTSDPTEVVN GISSQPQVPF HPNLQKSQYY STVGGSHPHS EQYPDLLPLE ARTRDYASLP PKRMYSQLKT LQKPVLPLYR GSSVSASRVV KPRQSSPQLH NLASYTKKHH TSSVYSISER LEMKPGPQAQ GLVMEAATHS QGDGSTDLDS KLTQQLIEFE KSLAGPGTEP DKILRHFSIM DFNSEKDIVR GSSKLITEQE LPERRKALRP PPPRPCTPVS TSPHLLVDQN LKPAPPLVVR PSRPAPLPPS AQQRTNAVSP KLLSRHRPTC ETLEKEGPGH MGRSLDQTSP CPLVLVRIEE MERDLDMYSR AQEELNLMLE EKQDESSRAE TLEDLKFCES NIESLNMELQ QLREMTLLSS QSSSLVAPSG SVSAENPEQR MLEKRAKVIE ELLQTERDYI RDLEMCIERI MVPMQQAQVP NIDFEGLFGN MQMVIKVSKQ LLAALEISDA VGPVFLGHRD ELEGTYKIYC QNHDEAIALL EIYEKDEKIQ KHLQDSLADL KSLYNEWGCT NYINLGSFLI KPVQRVMRYP LLLMELLNST PESHPDKVPL TNAVLAVKEI NVNINEYKRR KDLVLKYRKG DEDSLMEKIS KLNIHSIIKK SNRVSSHLKH LTGFAPQIKD EVFEETEKNF RMQERLIKSF IRDLSLYLQH IRESACVKVV AAVSMWDVCM ERGHRDLEQF ERVHRYISDQ LFTNFKERTE RLVISPLNQL LSMFTGPHKL VQKRFDKLLD FYNCTERAEK LKDKKTLEEL QSARNNYEAL NAQLLDELPK FHQYAQGLFT NCVHGYAEAH CDFVHQALEQ LKPLLSLLKV AGREGNLIAI FHEEHSRVLQ QLQVFTFFPE SLPATKKPFE RKTIDRQSAR KPLLGLPSYM LQSEELRASL LARYPPEKLF QAERNFNAAQ DLDVSLLEGD LVGVIKKKDP MGSQNRWLID NGVTKGFVYS SFLKPYNPRR SHSDASVGSH SSTESEHGSS SPRFPRQNSG STLTFNPSSM AVSFTSGSCQ KQPQDASPPP KECDQGTLSA SLNPSNSESS PSRCPSDPDS TSQPRSGDSA DVARDVKQPT ATPRSYRNFR HPEIVGYSVP GRNGQSQDLV KGCARTAQAP EDRSTEPDGS EAEGNQVYFA VYTFKARNPN ELSVSANQKL KILEFKDVTG NTEWWLAEVN GKKGYVPSNY IRKTEYT // ID DNMBP_MOUSE STANDARD; PRT; 1580 AA. AC Q6TXD4; Q6ZQ05; Q8CEW8; Q8R0Y2; DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot. DT 07-DEC-2004, sequence version 2. DT 30-MAY-2006, entry version 23. DE Dynamin-binding protein (Scaffold protein Tuba). GN Name=Dnmbp; Synonyms=Kiaa1010; OS Mus musculus (Mouse). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; OC Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Sciurognathi; OC Muroidea; Muridae; Murinae; Mus. OX NCBI_TaxID=10090; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, ALTERNATIVE RP SPLICING, SUBCELLULAR LOCATION, AND INTERACTION WITH ACTIN; TUBULIN; RP HSP70 AND A COMPLEX OF ACTIN-REGULATORY PROTEINS. RC TISSUE=Embryo; RX PubMed=14506234; DOI=10.1074/jbc.M308104200; RA Salazar M.A., Kwiatkowski A.V., Pellegrini L., Cestra G., Butler M.H., RA Rossman K.L., Serna D.M., Sondek J., Gertler F.B., De Camilli P.; RT "Tuba, a novel protein containing bin/amphiphysin/Rvs and Dbl homology RT domains, links dynamin to regulation of the actin cytoskeleton."; RL J. Biol. Chem. 278:49031-49043(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Embryonic tail; RX MEDLINE=22977043; PubMed=14621295; DOI=10.1093/dnares/10.4.167; RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., RA Saga Y., Nagase T., Ohara O., Koga H.; RT "Prediction of the coding sequences of mouse homologues of KIAA gene: RT III. The complete nucleotide sequences of 500 mouse KIAA-homologous RT cDNAs identified by screening of terminal sequences of cDNA clones RT randomly sampled from size-fractionated libraries."; RL DNA Res. 10:167-180(2003). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC STRAIN=C57BL/6J; RX PubMed=16141072; DOI=10.1126/science.1112014; RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., RA Davis M.J., Wilming L.G., Aidinis V., Allen J.E., RA Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., RA Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., RA Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., RA Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., RA di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., RA Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., RA Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., RA Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., RA Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., RA Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., RA Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., RA Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., RA Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., RA Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., RA Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., RA Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., RA Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., RA Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., RA Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., RA Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., RA Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., RA Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., RA Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., RA Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., RA Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., RA Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., RA Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., RA Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., RA Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., RA Hayashizaki Y.; RT "The transcriptional landscape of the mammalian genome."; RL Science 309:1559-1563(2005). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 975-1580. RC STRAIN=FVB/N; TISSUE=Liver; RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899; RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G., RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D., RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K., RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F., RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L., RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E., RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C., RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J., RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H., RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W., RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A., RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A., RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G., RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C., RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M., RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E., RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.; RT "Generation and initial analysis of more than 15,000 full-length human RT and mouse cDNA sequences."; RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002). CC -!- FUNCTION: Scaffold protein that links dynamin with actin- CC regulating proteins. May play a role in membrane trafficking CC between the cell surface and the Golgi. CC -!- SUBUNIT: Interacts with DNM1 via its N-terminal SH3 domains. The CC C-terminal SH3 domain binds a complex containing actin, tubulin, CC Hsp70 and actin-regulatory proteins, such as ENAH, EVL, WASL, CC WIRE, CR16, WAVE1 and NAP1L1. CC -!- SUBCELLULAR LOCATION: Cytoplasmic. Localized to synapses and Golgi CC stacks. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; CC IsoId=Q6TXD4-1; Sequence=Displayed; CC Name=2; CC IsoId=Q6TXD4-2; Sequence=VSP_012081, VSP_012082, VSP_012083; CC Note=No experimental confirmation available; CC Name=3; CC IsoId=Q6TXD4-3; Sequence=VSP_012080, VSP_012084; CC Note=No experimental confirmation available; CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 DH (DBL-homology) domain. CC -!- SIMILARITY: Contains 6 SH3 domains. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AY383729; AAQ81299.1; -; mRNA. DR EMBL; AK129261; BAC98071.1; ALT_INIT; mRNA. DR EMBL; AK010367; BAC25293.1; -; mRNA. DR EMBL; BC025944; AAH25944.1; -; mRNA. DR UniGene; Mm.159024; -. DR HSSP; P29355; 1K76. DR SMR; Q6TXD4; 1286-1364, 1514-1578. DR MGI; MGI:1917352; Dnmbp. DR GO; GO:0005515; F:protein binding; IPI. DR InterPro; IPR004148; BAR. DR InterPro; IPR001331; GDS_CDC24. DR InterPro; IPR000108; Neu_cyt_fact_2. DR InterPro; IPR000219; RhoGEF. DR InterPro; IPR001452; SH3. DR InterPro; IPR011511; SH3_2. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00621; RhoGEF; 1. DR Pfam; PF00018; SH3_1; 4. DR Pfam; PF07653; SH3_2; 2. DR PRINTS; PR00499; P67PHOX. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 4. DR SMART; SM00721; BAR; 1. DR SMART; SM00325; RhoGEF; 1. DR SMART; SM00326; SH3; 6. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS00741; DH_1; 1. DR PROSITE; PS50010; DH_2; 1. DR PROSITE; PS50002; SH3; 5. KW Alternative splicing; Coiled coil; Cytoskeleton; Golgi apparatus; KW Repeat; SH3 domain. FT CHAIN 1 1580 Dynamin-binding protein. FT /FTId=PRO_0000079960. FT DOMAIN 2 61 SH3 1. FT DOMAIN 66 127 SH3 2. FT DOMAIN 146 205 SH3 3. FT DOMAIN 244 303 SH3 4. FT DOMAIN 783 970 DH. FT DOMAIN 1011 1220 BAR. FT DOMAIN 1288 1351 SH3 5. FT DOMAIN 1516 1579 SH3 6. FT COILED 694 755 Potential. FT COMPBIAS 609 672 Pro-rich. FT VAR_SEQ 1 1034 Missing (in isoform 3). FT /FTId=VSP_012080. FT VAR_SEQ 1 753 Missing (in isoform 2). FT /FTId=VSP_012081. FT VAR_SEQ 851 860 Missing (in isoform 2). FT /FTId=VSP_012082. FT VAR_SEQ 910 910 K -> KSLYHEW (in isoform 2). FT /FTId=VSP_012083. FT VAR_SEQ 1301 1580 AAQDLDVSLLEGDLVGVIKKKDPMGSQNRWLVDNGVTKGFV FT YSSFLKPYNPRCSHSDASVASHSSTESEHSGSSPGCHRQNS FT HSALTFNSNNMTVSFTSGLALTQPQDASPLKDCAHETLAVS FT WNTGHPETGPSTCSSDPGFSCQRRLGNPADGARDISQPAST FT LRGCQRSSPHSEVVGYSVPGRNDQGSDSIKGSARVCQAPED FT RDRGVGSSETEGNQVYFAIYTFKARNPNELSVLANQRLRIH FT EFKDVTGNTEWWLAEVNGRKGYVPSNYIRKTEYT -> LRR FT TWMSPFWKATWWA (in isoform 3). FT /FTId=VSP_012084. FT CONFLICT 1471 1471 S -> G (in Ref. 1). FT CONFLICT 1485 1485 R -> Q (in Ref. 1). SQ SEQUENCE 1580 AA; 177277 MW; CEB70B6459341C1F CRC64; MEPGSMVRAI FDFCPSVSEE LPLFVGDVIE VLAVVDEFWL LGKKEDVTGQ FPSSFVEIVT IPSLKEGERL FVCICEFVSR ELNSLSLHRG DLVILDDSAP TAGWLQGRSC WGAWGFFPSS CVQELCLSSR SRRWHAQSAL LQAPEYSLGQ ARALMGLSAQ LDEELDFREG DLITIIGVPE PGWFEGELEG RRGIFPEGFV ELLGPLRTVD ESVNSRSGDD SAVNGEVDVP PEEAESGGDE DDQQSGTYGI ALYRFQALET NELDFEVGDR IQILGTLEDG WLEGCLKGKT GVFPHRFVKL CPSNRTEETT AQPQESSFPK DSESSVGKSG DSVVEEARQE PWECEEERPD YDLPGQASVP QDHVAPEWTG DTISGQDKDA SGSSPDVDLE RPLAKDLSTP DPSEEVNGVS SQPQVPIHPK VQKSQHYLTA GGSHQTSDPF SELVPLEART RDYSSLPPRR TYAQGWSFQK PASHLQRASS LTASRLDRPS HFCHPAMASY AQKHQTSTEN TASLHDPPER PERRPGLQDR GPATDITTAS QGDSLDLDSK LTQQLIEFEK SLSGPSTEPE TIVRRFSIMD FYSEKDIVRG SSNSLPSQAF PERRKTLRPP PPRPRTPTPI SSHLLVDQSP KPVPTLVVRP SRPAPLPPPA QQRMNTASPK PTSCAHPGWE APEKEDSEHM EKSPAQTFPC PSMLARIRDV EQDLDTCTRA QEELNLLLEE KQDDPSRAET LETLRSYEST IQSLTLELQQ LRDMTLLSSQ SSSLAAPFGS VSTENPEQRM LEKRAKVVAE LLQTERDYIR DLEMCIERVM VPLQQAQVPN VDFEGLFGNM QTVIKVSKQL LAALEISDAV GMSSCDCLVP GPVFLDHRDE LEGTYRVYCQ NHDEAISLLE MYEKDEKTQK HLQDYLADLK GCTNYINLGS FLIKPVQRIM RYPLLLMELL NSTPESHPDK VPLTNAVLAV KEINVNINEY KRRKDLVLKY RKGDEDSLME KISKLNIHSI IKKSSRVSSH LKHLTGFAPQ LKDEVFEETE KNFRMQERLI KSFIRDLSLY LQHIRESACV KVVAAMSIWD LCMERGHHDL EQFEKVHRYI SDQLFTRFKE RTERLVINPL NQLLNMFTGP YKLVQKRFDK LLDFYNCTER AEKLKDKKTL EELQSARNNY EALNSQLLDE LPKFQQYAQS LFTNCIHGYA EAHCDFVQQA LEQLQPLLSL LKATDREGNL IAIFLEEHSR VLQQLQVFTF FPESLPAPRK PFERKTTDRQ SSRKTLLGMP SYMLQSEELR SSLLARYPPE KLFHVQRNFN AAQDLDVSLL EGDLVGVIKK KDPMGSQNRW LVDNGVTKGF VYSSFLKPYN PRCSHSDASV ASHSSTESEH SGSSPGCHRQ NSHSALTFNS NNMTVSFTSG LALTQPQDAS PLKDCAHETL AVSWNTGHPE TGPSTCSSDP GFSCQRRLGN PADGARDISQ PASTLRGCQR SSPHSEVVGY SVPGRNDQGS DSIKGSARVC QAPEDRDRGV GSSETEGNQV YFAIYTFKAR NPNELSVLAN QRLRIHEFKD VTGNTEWWLA EVNGRKGYVP SNYIRKTEYT // ID HOB1_SCHPO STANDARD; PRT; 466 AA. AC O74352; DT 16-MAY-2003, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 21-MAR-2006, entry version 29. DE Protein hob1 (Homolog of Bin1). GN Name=hob1; ORFNames=SPBC21D10.12; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE, AND FUNCTION. RX MEDLINE=22457105; PubMed=12569356; DOI=10.1038/sj.onc.1206162; RA Routhier E.L., Donover P.S., Prendergast G.C.; RT "hob1+, the fission yeast homolog of Bin1, is dispensable for RT endocytosis or actin organization, but required for the response to RT starvation or genotoxic stress."; RL Oncogene 22:637-648(2003). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). CC -!- FUNCTION: Has a role in DNA damage signaling as a part of stress CC response processes. CC -!- SIMILARITY: Contains 1 BAR domain. CC -!- SIMILARITY: Contains 1 SH3 domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF275637; AAF86458.1; -; mRNA. DR EMBL; AL031536; CAA20768.1; -; Genomic_DNA. DR PIR; T11684; T11684. DR HSSP; P08631; 1BU1. DR GeneDB_Spombe; SPBC21D10.12; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-004058-MONOMER; -. DR GO; GO:0051285; C:cell cortex of cell tip; TAS. DR GO; GO:0031097; C:medial ring; TAS. DR GO; GO:0005515; F:protein binding; IPI. DR GO; GO:0030467; P:establishment and/or maintenance of cell po...; IGI. DR GO; GO:0000074; P:regulation of progression through cell cycle; IMP. DR GO; GO:0006950; P:response to stress; IMP. DR InterPro; IPR004148; BAR. DR InterPro; IPR001452; SH3. DR Pfam; PF03114; BAR; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00452; SH3DOMAIN. DR ProDom; PD000066; SH3; 1. DR SMART; SM00721; BAR; 1. DR SMART; SM00326; SH3; 1. DR PROSITE; PS51021; BAR; 1. DR PROSITE; PS50002; SH3; 1. KW Coiled coil; Complete proteome; SH3 domain. FT CHAIN 1 466 Protein hob1. FT /FTId=PRO_0000192954. FT DOMAIN 17 269 BAR. FT DOMAIN 407 466 SH3. FT COILED 31 67 Potential. FT COILED 177 204 Potential. FT COMPBIAS 294 409 Ala/Pro/Ser-rich. SQ SEQUENCE 466 AA; 51392 MW; 441793950D6C2C7E CRC64; MSWKGFTKAL ARTPQTLRSK FNVGEITKDP IYEDAGRRFK SLETEAKKLA EDAKKYTDAI NGLLNHQIGF ADACIEIYKP ISGRASDPES YEQEGNAEGI EAAEAYKEIV YDLQKNLASE MDVINTRIVN PTGELLKIVK DVDKLLLKRD HKQLDYDRHR SSFKKLQEKK DKSLKDEKKL YEAETAFEQS SQEYEYYNEM LKEELPKLFA LAQSFIAPLF QGFYYMQLNV YYVLYEKMSH CEIQYFDFNT DILESYERRR GDVKDRAEAL TITKFKTAKP TYKRPGMGPG GKDATASSSS SFSSKREEAA AEPSSSTATD IPPPYSTPSV AGASDYSTPS AGYQTVQTTT TTTEAAAAQY PQAAFPPPPV MPQPAAAAVT TPVAAPVAAA AAAVPVPPPA PAPAAAPAAE HVVALYDYAA QAAGDLSFHA GDRIEVVSRT DNQNEWWIGR LNGAQGQFPG NYVQLE // ID HOB3_SCHPO STANDARD; PRT; 264 AA. AC Q9UUM7; P78850; DT 11-JUL-2001, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 07-FEB-2006, entry version 33. DE Protein hob3 (Homolog of Bin3). GN Name=hob3; ORFNames=SPBC725.09c; OS Schizosaccharomyces pombe (Fission yeast). OC Eukaryota; Fungi; Ascomycota; Schizosaccharomycetes; OC Schizosaccharomycetales; Schizosaccharomycetaceae; OC Schizosaccharomyces. OX NCBI_TaxID=4896; RN [1] RP NUCLEOTIDE SEQUENCE, AND FUNCTION. RX MEDLINE=21293007; PubMed=11274158; DOI=10.1074/jbc.M101096200; RA Routhier E.L., Burn T.C., Abbaszade I., Summers M., Albright C.F., RA Prendergast G.C.; RT "Human BIN3 complements the F-actin localization defects caused by RT loss of Hob3p, the fission yeast homolog of Rvs161p."; RL J. Biol. Chem. 276:21670-21677(2001). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=972; RX MEDLINE=21848401; PubMed=11859360; DOI=10.1038/nature724; RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A., RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S., RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., RA Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A., RA Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., RA Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., RA James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J., RA Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., RA Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., RA Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S., RA Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K., RA Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S., RA Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B., RA Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S., RA Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D., RA Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R., RA Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B., RA Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S., RA Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M., RA Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G., RA Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J., RA Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L., RA Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J., RA Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.; RT "The genome sequence of Schizosaccharomyces pombe."; RL Nature 415:871-880(2002). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC STRAIN=PR745; RX MEDLINE=98162722; PubMed=9501991; DOI=10.1093/dnares/4.6.363; RA Yoshioka S., Kato K., Nakai K., Okayama H., Nojima H.; RT "Identification of open reading frames in Schizosaccharomyces pombe RT cDNAs."; RL DNA Res. 4:363-369(1997). CC -!- FUNCTION: Involved in cytokinesis and septation where it has a CC role in the localization of F-actin. CC -!- SIMILARITY: Contains 1 BAR domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF275638; AAF86459.1; -; mRNA. DR EMBL; AL034352; CAA22181.1; -; Genomic_DNA. DR EMBL; D89200; BAA13861.1; ALT_INIT; mRNA. DR PIR; T40661; T40661. DR GeneDB_Spombe; SPBC725.09c; -. DR BioCyc; SPOM-XXX-01:SPOM-XXX-01-003552-MONOMER; -. DR GO; GO:0007015; P:actin filament organization; IGI. DR InterPro; IPR003005; Amphiphysin. DR InterPro; IPR004148; BAR. DR Pfam; PF03114; BAR; 1. DR PRINTS; PR01251; AMPHIPHYSIN. DR SMART; SM00721; BAR; 1. DR PROSITE; PS51021; BAR; 1. KW Cell cycle; Cell division; Coiled coil; Complete proteome; KW Cytoskeleton; Septation. FT CHAIN 1 264 Protein hob3. FT /FTId=PRO_0000192959. FT DOMAIN 17 237 BAR. FT COILED 25 65 Potential. FT COILED 165 187 Potential. FT CONFLICT 93 93 Q -> L (in Ref. 3). FT CONFLICT 96 96 E -> K (in Ref. 3). SQ SEQUENCE 264 AA; 30094 MW; 845388582305AD4D CRC64; MSWHGFKKAV NRAGTSVMMK TGHVERTVDR EFETEERRYR TMESAAKKLQ KEAKGYLDAL RAMTASQTRI ANTIDAFYGD AGSKDGVSAY YRQVVEDLDA DTVKELDGPF RTTVLDPISR FCSYFPDINA AITKRNHKLL DHDAMRAKVQ KLVDKPSNDT TKLPRTEKEA AMAKEVYETL NNQLVSELPQ LIALRVPYLD PSFEALVKIQ LRFCREGYEK MAQVQQYFDN SVREDYSNGL LDDKVEQVLQ SMRDLSIAGL NNSQ // ID P29_ECHGR STANDARD; PRT; 238 AA. AC Q9U8G7; DT 25-MAR-2003, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-2000, sequence version 1. DT 07-FEB-2006, entry version 19. DE Hydatid disease diagnostic antigen P-29. OS Echinococcus granulosus. OC Eukaryota; Metazoa; Platyhelminthes; Cestoda; Eucestoda; OC Cyclophyllidea; Taeniidae; Echinococcus. OX NCBI_TaxID=6210; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE. RX MEDLINE=20155408; PubMed=10693741; DOI=10.1016/S0166-6851(99)00166-8; RA Gonzalez G., Spinelli P., Lorenzo C., Hellman U., Nieto A., Willis A., RA Salinas G.; RT "Molecular characterization of P-29, a metacestode-specific component RT of Echinococcus granulosus which is immunologically related to, but RT distinct from, antigen 5."; RL Mol. Biochem. Parasitol. 105:177-185(2000). CC -!- DEVELOPMENTAL STAGE: Metacestode-specific. CC -!- SIMILARITY: Contains 1 BAR domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; AF078931; AAD53328.1; -; mRNA. DR InterPro; IPR004148; BAR. DR Pfam; PF03114; BAR; 1. DR SMART; SM00721; BAR; 1. DR PROSITE; PS51021; BAR; 1. KW Antigen; Direct protein sequencing. FT CHAIN 1 238 Hydatid disease diagnostic antigen P-29. FT /FTId=PRO_0000192962. FT DOMAIN 18 238 BAR. SQ SEQUENCE 238 AA; 27097 MW; 4F413D4ED19861CA CRC64; MSGFDVTKTF NRFTQRAGEL VNKNEKTSYP TRTSDLIHEI DQMKAWISKI ITATEEFVDI NIASKVADAF QKNKEKITTT DKLGTALEQV ASQSEKAAPQ LSKMLTEASD VHQRMATARK NFNSEVNTTF IEDLKNFLNT TLSEAQKAKT KLEEVRLDLD SDKTKLKNAK TAEQKAKWEA EVRKDESDFD RVHQESLTIF EKTCKEFDGL SVQLLDLIRA EKNYYEACAK ECSMMLGE // ID RV161_YEAST STANDARD; PRT; 265 AA. AC P25343; DT 01-MAY-1992, integrated into UniProtKB/Swiss-Prot. DT 01-MAY-1992, sequence version 1. DT 07-MAR-2006, entry version 45. DE Reduced viability upon starvation protein 161. GN Name=RVS161; Synonyms=END6, SPE161; OrderedLocusNames=YCR009C; GN ORFNames=YCR9C; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 44827 / SKQ2N; RX MEDLINE=90224366; PubMed=2183524; RA Urdaci M., Dulau L., Aigle M., Crouzet M.; RT "Sequence of the yeast gene RVS 161 located on chromosome III."; RL Yeast 6:173-176(1990). RN [2] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RX MEDLINE=92327849; PubMed=1626432; RA Skala J., Purnelle B., Goffeau A.; RT "The complete sequence of a 10.8 kb segment distal of SUF2 on the RT right arm of chromosome III from Saccharomyces cerevisiae reveals RT seven open reading frames including the RVS161, ADP1 and PGK genes."; RL Yeast 8:409-417(1992). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=92244356; PubMed=1574125; DOI=10.1038/357038a0; RA Oliver S.G., van der Aart Q.J.M., Agostoni-Carbone M.L., Aigle M., RA Alberghina L., Alexandraki D., Antoine G., Anwar R., Ballesta J.P.G., RA Benit P., Berben G., Bergantino E., Biteau N., Bolle P.-A., RA Bolotin-Fukuhara M., Brown A., Brown A.J.P., Buhler J.-M., Carcano C., RA Carignani G., Cederberg H., Chanet R., Contreras R., Crouzet M., RA Daignan-Fornier B., Defoor E., Delgado M.D., Demolder J., Doira C., RA Dubois E., Dujon B., Duesterhoeft A., Erdmann D., Esteban M., RA Fabre F., Fairhead C., Faye G., Feldmann H., Fiers W., RA Francingues-Gaillard M.-C., Franco L., Frontali L., Fukuhara H., RA Fuller L.J., Galland P., Gent M.E., Gigot D., Gilliquet V., RA Glansdorff N., Goffeau A., Grenson M., Grisanti P., Grivell L.A., RA de Haan M., Haasemann M., Hatat D., Hoenicka J., Hegemann J.H., RA Herbert C.J., Hilger F., Hohmann S., Hollenberg C.P., Huse K., RA Iborra F., Indge K.J., Isono K., Jacq C., Jacquet M., James C.M., RA Jauniaux J.-C., Jia Y., Jimenez A., Kelly A., Kleinhans U., Kreisl P., RA Lanfranchi G., Lewis C., van der Linden C.G., Lucchini G., RA Lutzenkirchen K., Maat M.J., Mallet L., Mannhaupt G., Martegani E., RA Mathieu A., Maurer C.T.C., McConnell D., McKee R.A., Messenguy F., RA Mewes H.-W., Molemans F., Montague M.A., Muzi Falconi M., Navas L., RA Newlon C.S., Noone D., Pallier C., Panzeri L., Pearson B.M., Perea J., RA Philippsen P., Pierard A., Planta R.J., Plevani P., Poetsch B., RA Pohl F.M., Purnelle B., Ramezani Rad M., Rasmussen S.W., Raynal A., RA Remacha M.A., Richterich P., Roberts A.B., Rodriguez F., Sanz E., RA Schaaff-Gerstenschlaeger I., Scherens B., Schweitzer B., Shu Y., RA Skala J., Slonimski P.P., Sor F., Soustelle C., Spiegelberg R., RA Stateva L.I., Steensma H.Y., Steiner S., Thierry A., Thireos G., RA Tzermia M., Urrestarazu L.A., Valle G., Vetter I., RA van Vliet-Reedijk J.C., Voet M., Volckaert G., Vreken P., Wang H., RA Warmington J.R., von Wettstein D., Wicksteed B.L., Wilson C., RA Wurst H., Xu G., Yoshikawa A., Zimmermann F.K., Sgouros J.G.; RT "The complete DNA sequence of yeast chromosome III."; RL Nature 357:38-46(1992). RN [4] RP CHARACTERIZATION. RC STRAIN=ATCC 44827 / SKQ2N; RX MEDLINE=92133163; PubMed=1776363; RA Crouzet M., Urdaci M., Dulau L., Aigle M.; RT "Yeast mutant affected for viability upon nutrient starvation: RT characterization and cloning of the RVS161 gene."; RL Yeast 7:727-743(1991). RN [5] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). CC -!- FUNCTION: Component of a cytoskeletal structure that is required CC for the formation of endocytic vesicles at the plasma membrane CC level. CC -!- INTERACTION: CC Q05670:FUS2; NbExp=1; IntAct=EBI-14490, EBI-7186; CC P39743:RVS167; NbExp=4; IntAct=EBI-14490, EBI-14500; CC -!- MISCELLANEOUS: Mutations in this gene results in sensitivity to CC carbon, nitrogen and sulfur starvation. CC -!- MISCELLANEOUS: Present with 7390 molecules/cell. CC -!- SIMILARITY: Contains 1 BAR domain. CC ----------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution-NoDerivs License CC ----------------------------------------------------------------------- DR EMBL; X63315; CAA44926.1; -; Genomic_DNA. DR EMBL; X59720; CAA42326.1; -; Genomic_DNA. DR PIR; S19516; S19516. DR IntAct; P25343; -. DR GermOnline; 138914; -. DR Ensembl; YCR009C; Saccharomyces cerevisiae. DR GenomeReviews; X59720_GR; YCR009C. DR SGD; S000000602; RVS161. DR BioCyc; SCER-S28-01:SCER-S28-01-000649-MONOMER; -. DR LinkHub; P25343; -. DR GO; GO:0030479; C:actin cortical patch; TAS. DR GO; GO:0045121; C:lipid raft; IDA. DR GO; GO:0005937; C:mating projection; IDA. DR GO; GO:0008092; F:cytoskeletal protein binding; IPI. DR GO; GO:0007121; P:bipolar bud site selection; IMP. DR GO; GO:0006897; P:endocytosis; IMP. DR GO; GO:0006970; P:response to osmotic stress; IMP. DR InterPro; IPR004148; BAR. DR Pfam; PF03114; BAR; 1. DR SMART; SM00721; BAR; 1. DR PROSITE; PS51021; BAR; 1. KW Coiled coil; Complete proteome; Cytoskeleton. FT CHAIN 1 265 Reduced viability upon starvation protein FT 161. FT /FTId=PRO_0000192960. FT DOMAIN 15 239 BAR. FT COILED 126 193 Potential. FT CONFLICT 95 95 Q -> E (in Ref. 1). SQ SEQUENCE 265 AA; 30250 MW; B35EA00E0C900E2D CRC64; MSWEGFKKAI NRAGHSVIIK NVDKTIDKEY DMEERRYKVL QRAGEALQKE AKGFLDSLRA VTASQTTIAE VISNLYDDSK YVAGGGYNVG NYYLQCVQDF DSETVKQLDG PLRETVLDPI TKFSTYFKEI EEAIKKRDHK KQDFDAAKAK VRRLVDKPAK DASKLPRAEK ELSLAKDIFE NLNNQLKTEL PQLVSLRVPY FDPSFEALIK IQLRFCTDGY TRLAQIQQYL DQQSRDDYAN GLLDTKIEEL LGQMTSLDIC ALGIK // ID RV167_YEAST STANDARD; PRT; 482 AA. AC P39743; DT 01-FEB-1995, integrated into UniProtKB/Swiss-Prot. DT 01-FEB-1995, sequence version 1. DT 16-MAY-2006, entry version 55. DE Reduced viability upon starvation protein 167. GN Name=RVS167; OrderedLocusNames=YDR388W; ORFNames=D9509.8; OS Saccharomyces cerevisiae (Baker's yeast). OC Eukaryota; Fungi; Ascomycota; Saccharomycotina; Saccharomycetes; OC Saccharomycetales; Saccharomycetaceae; Saccharomyces. OX NCBI_TaxID=4932; RN [1] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA]. RC STRAIN=ATCC 26109 / X2180; RX MEDLINE=93330299; PubMed=8336735; RA Bauer F., Urdaci M., Aigle M., Crouzet M.; RT "Alteration of a yeast SH3 protein leads to conditional viability with RT defects in cytoskeletal and budding patterns."; RL Mol. Cell. Biol. 13:5070-5084(1993). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RC STRAIN=S288c; RX MEDLINE=97313263; PubMed=9169867; RA Jacq C., Alt-Moerbe J., Andre B., Arnold W., Bahr A., Ballesta J.P.G., RA Bargues M., Baron L., Becker A., Biteau N., Bloecker H., Blugeon C., RA Boskovic J., Brandt P., Brueckner M., Buitrago M.J., Coster F., RA Delaveau T., del Rey F., Dujon B., Eide L.G., Garcia-Cantalejo J.M., RA Goffeau A., Gomez-Peris A., Granotier C., Hanemann V., Hankeln T., RA Hoheisel J.D., Jaeger W., Jimenez A., Jonniaux J.-L., Kraemer C., RA Kuester H., Laamanen P., Legros Y., Louis E.J., Moeller-Rieker S., RA Monnet A., Moro M., Mueller-Auer S., Nussbaumer B., Paricio N., RA Paulin L., Perea J., Perez-Alonso M., Perez-Ortin J.E., Pohl T.M., RA Prydz H., Purnelle B., Rasmussen S.W., Remacha M.A., Revuelta J.L., RA Rieger M., Salom D., Saluz H.P., Saiz J.E., Saren A.-M., Schaefer M., RA Scharfe M., Schmidt E.R., Schneider C., Scholler P., Schwarz S., RA Soler-Mira A., Urrestarazu L.A., Verhasselt P., Vissers S., Voet M., RA Volckaert G., Wagner G., Wambutt R., Wedler E., Wedler H., Woelfl S., RA Harris D.E., Bowman S., Brown D., Churcher C.M., Connor R., Dedman K., RA Gentles S., Hamlin N., Hunt S., Jones L., McDonald S., Murphy L.D., RA Niblett D., Odell C., Oliver K., Rajandream M.A., Richards C., RA Shore L., Walsh S.V., Barrell B.G., Dietrich F.S., Mulligan J.T., RA Allen E., Araujo R., Aviles E., Berno A., Carpenter J., Chen E., RA Cherry J.M., Chung E., Duncan M., Hunicke-Smith S., Hyman R.W., RA Komp C., Lashkari D., Lew H., Lin D., Mosedale D., Nakahara K., RA Namath A., Oefner P., Oh C., Petel F.X., Roberts D., Schramm S., RA Schroeder M., Shogren T., Shroff N., Winant A., Yelton M.A., RA Botstein D., Davis R.W., Johnston M., Andrews S., Brinkman R., RA Cooper J., Ding H., Du Z., Favello A., Fulton L., Gattung S., RA Greco T., Hallsworth K., Hawkins J., Hillier L.W., Jier M., RA Johnson D., Johnston L., Kirsten J., Kucaba T., Langston Y., RA Latreille P., Le T., Mardis E., Menezes S., Miller N., Nhan M., RA Pauley A., Peluso D., Rifkin L., Riles L., Taich A., Trevaskis E., RA Vignati D., Wilcox L., Wohldman P., Vaudin M., Wilson R., RA Waterston R., Albermann K., Hani J., Heumann K., Kleine K., RA Mewes H.-W., Zollner A., Zaccaria P.; RT "The nucleotide sequence of Saccharomyces cerevisiae chromosome IV."; RL Nature 387:75-78(1997). RN [3] RP INTERACTION WITH ACTIN. RX MEDLINE=95236199; PubMed=7719850; RA Amberg D.C., Basart E., Botstein D.; RT "Defining protein interactions with yeast actin in vivo."; RL Nat. Struct. Biol. 2:28-35(1995). RN [4] RP INTERACTION WITH ABP1. RX PubMed=10388809; RA Colwill K., Field D., Moore L., Friesen J., Andrews B.; RT "In vivo analysis of the domains of yeast Rvs167p suggests Rvs167p RT function is mediated through multiple protein interactions."; RL Genetics 152:881-893(1999). RN [5] RP LEVEL OF PROTEIN EXPRESSION. RX MEDLINE=22923965; PubMed=14562106; DOI=10.1038/nature02046; RA Ghaemmaghami S., Huh W.-K., Bower K., Howson R.W., Belle A., RA Dephoure N., O'Shea E.K., Weissman J.S.; RT "Global analysis of protein expression in yeast."; RL Nature 425:737-741(2003). RN [6] RP UBIQUITINATION AT LYS-481, AND MASS SPECTROMETRY. RX PubMed=12872131; DOI=10.1038/nbt849; RA Peng J., Schwartz D., Elias J.E., Thoreen C.C., Cheng D., RA Marsischky G., Roelofs J., Finley D., Gygi S.P.; RT "A proteomics approach to understanding protein ubiquitination."; RL Nat. Biotechnol. 21:921-926(2003). RN [7] RP INTERACTION WITH YBR108W. RX PubMed=15561700; DOI=10.1074/jbc.M412454200; RA Germann M., Swain E., Bergman L., Nickels J.T. Jr.; RT "Characterizing the sphingolipid signaling pathway that remediates RT defects associated with loss of the yeast amphiphysin-like orthologs, RT Rvs161p and Rvs167p."; RL J. Biol. Chem. 280:4270-4278(2005). CC -!- FUNCTION: Component of a cytoskeletal structure that is required CC for the formation of endocytic vesicles at the plasma membrane CC level. Could be implicated in cytoskeletal reorganization in CC response to environmental stresses and could act in the budding CC site selection mechanism. CC -!- SUBUNIT: Binds to actin. Interacts with ABP1 and YBR108W. CC -!- INTERACTION: CC P15891:ABP1; NbExp=1; IntAct=EBI-14500, EBI-2036; CC Q12168:ACF2; NbExp=4; IntAct=EBI-14500, EBI-32973; CC P60010:ACT1; NbExp=2; IntAct=EBI-14500, EBI-2169; CC Q12365:BBP1; NbExp=1; IntAct=EBI-14500, EBI-3448; CC Q06604:BSP1; NbExp=2; IntAct=EBI-14500, EBI-37047; CC Q08412:CUE5; NbExp=1; IntAct=EBI-14500, EBI-37580; CC P47128:EAF6; NbExp=1; IntAct=EBI-14500, EBI-25552; CC P40956:GTS1; NbExp=1; IntAct=EBI-14500, EBI-7968; CC Q12344:GYP5; NbExp=1; IntAct=EBI-14500, EBI-38508; CC Q12446:LAS17; NbExp=6; IntAct=EBI-14500, EBI-10022; CC P10566:MRS3; NbExp=1; IntAct=EBI-14500, EBI-11291; CC P33400:RIM101; NbExp=1; IntAct=EBI-14500, EBI-14422; CC P25343:RVS161; NbExp=4; IntAct=EBI-14500, EBI-14490; CC Q04964:SML1; NbExp=1; IntAct=EBI-14500, EBI-27834; CC Q00916:SNP1; NbExp=1; IntAct=EBI-14500, EBI-724; CC P31374:YAL017W; NbExp=1; IntAct=EBI-14500, EBI-9442; CC P38266:YBR108W; NbExp=3; IntAct=EBI-14500, EBI-21584; CC P38289:YBR163W; NbExp=1; IntAct=EBI-14500, EBI-20869; CC P38140:YBR239C; NbExp=2; IntAct=EBI-14500, EBI-21048; CC Q12510:YDL156W; NbExp=1; IntAct=EBI-14500, EBI-35343; CC Q03780:YDR239C; NbExp=1; IntAct=EBI-14500, EBI-30094; CC P53153:YGL085W; NbExp=1; IntAct=EBI-14500, EBI-23857; CC P40563:YIR003W; NbExp=1; IntAct=EBI-14500, EBI-25376; CC P47129:YJR083C; NbExp=1; IntAct=EBI-14500, EBI-25556; CC Q04322:YMR192W; NbExp=4; IntAct=EBI-14500, EBI-27427; CC P53933:YNL094W; NbExp=4; IntAct=EBI-14500, EBI-28798; CC P53901:YNL152W; NbExp=1; IntAct=EBI-14500, EBI-28955; CC Q12532:YPL009C; NbExp=1; IntAct=EBI-14500, EBI-33283; CC Q06833:YPR091C; NbExp=1; IntAct=EBI-14500, EBI-37290;