ID ESYT1_HUMAN Reviewed; 1104 AA. AC Q9BSJ8; A0FGR7; A8K2S2; O94848; Q6PJN4; Q9H6J1; Q9H6W2; Q9Y416; DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 13-JUL-2010, entry version 77. DE RecName: Full=Extended synaptotagmin-1; DE Short=E-Syt1; DE AltName: Full=Membrane-bound C2 domain-containing protein; GN Name=ESYT1; Synonyms=FAM62A, KIAA0747, MBC2; 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), SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=17360437; DOI=10.1073/pnas.0611725104; RA Min S.-W., Chang W.-P., Suedhof T.C.; RT "E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 RT domains."; RL Proc. Natl. Acad. Sci. U.S.A. 104:3823-3828(2007). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Hepatoma, Kidney, and Tongue; 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]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., RA Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RC TISSUE=Kidney; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA RT project: the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-1104 (ISOFORM 2). RC TISSUE=Brain; RX MEDLINE=99087487; PubMed=9872452; DOI=10.1093/dnares/5.5.277; RA Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., RA Kotani H., Nomura N., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XI. RT The complete sequences of 100 new cDNA clones from brain which code RT for large proteins in vitro."; RL DNA Res. 5:277-286(1998). RN [6] RP PROTEIN SEQUENCE OF 308-323; 446-457 AND 551-586, AND MASS RP SPECTROMETRY. RC TISSUE=B-cell lymphoma, and Platelet; RA Bienvenut W.V., Claeys D.; RL Submitted (NOV-2005) to UniProtKB. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 379-1104 (ISOFORM 1). RC TISSUE=Uterus; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822 AND TYR-1009, AND RP MASS SPECTROMETRY. RX PubMed=15592455; DOI=10.1038/nbt1046; RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., RA Zha X.-M., Polakiewicz R.D., Comb M.J.; RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer RT cells."; RL Nat. Biotechnol. 23:94-101(2005). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822 AND TYR-1009, AND RP MASS SPECTROMETRY. RC TISSUE=Lung carcinoma; RX PubMed=18083107; DOI=10.1016/j.cell.2007.11.025; RA Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., RA Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., RA Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., RA Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., RA Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.; RT "Global survey of phosphotyrosine signaling identifies oncogenic RT kinases in lung cancer."; RL Cell 131:1190-1203(2007). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-963, AND MASS RP SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=17924679; DOI=10.1021/pr070152u; RA Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.; RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa RT cells and high confident phosphopeptide identification by cross- RT validation of MS/MS and MS/MS/MS spectra."; RL J. Proteome Res. 6:4150-4162(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-963 AND SER-1034, AND RP MASS SPECTROMETRY. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RA Colinge J., Superti-Furga G., Bennett K.L.; RL Submitted (OCT-2008) to UniProtKB. RN [13] RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY. RC TISSUE=Embryonic kidney; RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., RA Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in RT a refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-822, AND MASS RP SPECTROMETRY. RC TISSUE=Mammary epithelium; RX PubMed=19534553; DOI=10.1021/pr900044c; RA Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., RA Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., RA Wiley H.S., Qian W.-J.; RT "An extensive survey of tyrosine phosphorylation revealing new sites RT in human mammary epithelial cells."; RL J. Proteome Res. 8:3852-3861(2009). RN [15] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1034, AND MASS RP SPECTROMETRY. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [16] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-817, AND MASS SPECTROMETRY. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). CC -!- FUNCTION: May play a role as calcium-regulated intrinsic membrane CC protein (By similarity). CC -!- SUBCELLULAR LOCATION: Membrane; Multi-pass membrane protein. CC Note=Localizes to intracellular membranes. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q9BSJ8-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BSJ8-2; Sequence=VSP_018277; CC Note=No experimental confirmation available; CC -!- TISSUE SPECIFICITY: Widely expressed. CC -!- SIMILARITY: Belongs to the extended synaptotagmin family. CC -!- SIMILARITY: Contains 5 C2 domains. CC -!- SEQUENCE CAUTION: CC Sequence=BAB15139.1; Type=Erroneous initiation; CC Sequence=BAB15268.1; Type=Erroneous initiation; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; DQ993200; ABJ97705.1; -; mRNA. DR EMBL; AK025463; BAB15139.1; ALT_INIT; mRNA. DR EMBL; AK025878; BAB15268.1; ALT_INIT; mRNA. DR EMBL; AK290337; BAF83026.1; -; mRNA. DR EMBL; CH471054; EAW96891.1; -; Genomic_DNA. DR EMBL; BC004998; AAH04998.1; -; mRNA. DR EMBL; AB018290; BAA34467.1; -; mRNA. DR EMBL; AL050134; CAB43284.1; -; mRNA. DR IPI; IPI00022143; -. DR IPI; IPI00746655; -. DR PIR; T08769; T08769. DR PIR; T13156; T13156. DR RefSeq; NP_001171725.1; -. DR RefSeq; NP_056107.1; -. DR UniGene; Hs.632729; -. DR SMR; Q9BSJ8; 326-758, 967-1103. DR IntAct; Q9BSJ8; 1. DR MINT; MINT-1144538; -. DR STRING; Q9BSJ8; -. DR PhosphoSite; Q9BSJ8; -. DR OGP; Q9Y416; -. DR PRIDE; Q9BSJ8; -. DR Ensembl; ENST00000267113; ENSP00000267113; ENSG00000139641; Homo sapiens. DR GeneID; 23344; -. DR KEGG; hsa:23344; -. DR UCSC; uc001sjq.1; human. DR UCSC; uc001sjr.1; human. DR CTD; 23344; -. DR GeneCards; GC12P054810; -. DR H-InvDB; HIX0010718; -. DR HGNC; HGNC:29534; ESYT1. DR HPA; HPA016858; -. DR PharmGKB; PA142671869; -. DR eggNOG; prNOG06718; -. DR HOVERGEN; HBG055795; -. DR OMA; SFLIRKP; -. DR OrthoDB; EOG983GQ3; -. DR PhylomeDB; Q9BSJ8; -. DR NextBio; 45301; -. DR ArrayExpress; Q9BSJ8; -. DR Bgee; Q9BSJ8; -. DR CleanEx; HS_FAM62A; -. DR Genevestigator; Q9BSJ8; -. DR GermOnline; ENSG00000139641; Homo sapiens. DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW. DR InterPro; IPR000008; C2_Ca-dep. DR InterPro; IPR008973; C2_Ca/lipid-bd_dom_CaLB. DR InterPro; IPR018029; C2_membr_targeting. DR InterPro; IPR020477; C2_region. DR Pfam; PF00168; C2; 5. DR PRINTS; PR00360; C2DOMAIN. DR SMART; SM00239; C2; 5. DR SUPFAM; SSF49562; C2_CaLB; 5. DR PROSITE; PS50004; C2; 5. PE 1: Evidence at protein level; KW Acetylation; Alternative splicing; Coiled coil; Complete proteome; KW Direct protein sequencing; Membrane; Phosphoprotein; Polymorphism; KW Repeat; Transmembrane. FT CHAIN 1 1104 Extended synaptotagmin-1. FT /FTId=PRO_0000234344. FT TRANSMEM 63 83 Helical; (Potential). FT TRANSMEM 245 265 Helical; (Potential). FT DOMAIN 316 417 C2 1. FT DOMAIN 465 558 C2 2. FT DOMAIN 634 735 C2 3. FT DOMAIN 785 877 C2 4. FT DOMAIN 972 1077 C2 5. FT COILED 91 116 Potential. FT COMPBIAS 924 935 Poly-Ser. FT COMPBIAS 1012 1015 Poly-Leu. FT MOD_RES 1 1 N-acetylmethionine. FT MOD_RES 817 817 N6-acetyllysine. FT MOD_RES 822 822 Phosphotyrosine. FT MOD_RES 963 963 Phosphoserine. FT MOD_RES 1009 1009 Phosphotyrosine. FT MOD_RES 1034 1034 Phosphoserine. FT VAR_SEQ 491 491 P -> PMVTSELYPPQ (in isoform 2). FT /FTId=VSP_018277. FT VARIANT 764 764 R -> C (in dbSNP:rs35075600). FT /FTId=VAR_038190. FT CONFLICT 133 133 F -> L (in Ref. 2; BAF83026). FT CONFLICT 489 489 D -> N (in Ref. 2; BAB15139). FT CONFLICT 738 738 L -> F (in Ref. 2; BAB15139). FT CONFLICT 785 785 S -> R (in Ref. 2; BAF83026). FT CONFLICT 998 998 L -> P (in Ref. 2; BAB15139). SQ SEQUENCE 1104 AA; 122856 MW; E72B20C458B96F19 CRC64; MERSPGEGPS PSPMDQPSAP SDPTDQPPAA HAKPDPGSGG QPAGPGAAGE ALAVLTSFGR RLLVLIPVYL AGAVGLSVGF VLFGLALYLG WRRVRDEKER SLRAARQLLD DEEQLTAKTL YMSHRELPAW VSFPDVEKAE WLNKIVAQVW PFLGQYMEKL LAETVAPAVR GSNPHLQTFT FTRVELGEKP LRIIGVKVHP GQRKEQILLD LNISYVGDVQ IDVEVKKYFC KAGVKGMQLH GVLRVILEPL IGDLPFVGAV SMFFIRRPTL DINWTGMTNL LDIPGLSSLS DTMIMDSIAA FLVLPNRLLV PLVPDLQDVA QLRSPLPRGI IRIHLLAARG LSSKDKYVKG LIEGKSDPYA LVRLGTQTFC SRVIDEELNP QWGETYEVMV HEVPGQEIEV EVFDKDPDKD DFLGRMKLDV GKVLQASVLD DWFPLQGGQG QVHLRLEWLS LLSDAEKLEQ VLQWNWGVSS RPDPPSAAIL VVYLDRAQDL PLKKGNKEPN PMVQLSIQDV TQESKAVYST NCPVWEEAFR FFLQDPQSQE LDVQVKDDSR ALTLGALTLP LARLLTAPEL ILDQWFQLSS SGPNSRLYMK LVMRILYLDS SEICFPTVPG CPGAWDVDSE NPQRGSSVDA PPRPCHTTPD SQFGTEHVLR IHVLEAQDLI AKDRFLGGLV KGKSDPYVKL KLAGRSFRSH VVREDLNPRW NEVFEVIVTS VPGQELEVEV FDKDLDKDDF LGRCKVRLTT VLNSGFLDEW LTLEDVPSGR LHLRLERLTP RPTAAELEEV LQVNSLIQTQ KSAELAAALL SIYMERAEDL PLRKGTKHLS PYATLTVGDS SHKTKTISQT SAPVWDESAS FLIRKPHTES LELQVRGEGT GVLGSLSLPL SELLVADQLC LDRWFTLSSG QGQVLLRAQL GILVSQHSGV EAHSHSYSHS SSSLSEEPEL SGGPPHITSS APELRQRLTH VDSPLEAPAG PLGQVKLTLW YYSEERKLVS IVHGCRSLRQ NGRDPPDPYV SLLLLPDKNR GTKRRTSQKK RTLSPEFNER FEWELPLDEA QRRKLDVSVK SNSSFMSRER ELLGKVQLDL AETDLSQGVA RWYDLMDNKD KGSS //