Full text data of ESYT1
ESYT1
(FAM62A, KIAA0747, MBC2)
[Confidence: high (present in two of the MS resources)]
Extended synaptotagmin-1; E-Syt1 (Membrane-bound C2 domain-containing protein)
Extended synaptotagmin-1; E-Syt1 (Membrane-bound C2 domain-containing protein)
hRBCD
IPI00022143
IPI00022143 KIAA0747 protein ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
IPI00022143 KIAA0747 protein ATP + 1-phosphatidyl-1D-myo-inositol = ADP + 1-phosphatidyl-1D-myo-inositol 3-phosphate soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a not mentioned n/a found at its expected molecular weight found at molecular weight
UniProt
Q9BSJ8
ID ESYT1_HUMAN Reviewed; 1104 AA.
AC Q9BSJ8; A0FGR7; A8K2S2; O94848; Q6PJN4; Q9H6J1; Q9H6W2; Q9Y416;
read moreDT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 106.
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 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [12]
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.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-963, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role as calcium-regulated intrinsic membrane
CC protein (By similarity).
CC -!- INTERACTION:
CC A0FGR8:ESYT2; NbExp=4; IntAct=EBI-355956, EBI-3184170;
CC A0FGR9:ESYT3; NbExp=3; IntAct=EBI-355956, EBI-8771391;
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;
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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 PIR; T08769; T08769.
DR PIR; T13156; T13156.
DR RefSeq; NP_001171725.1; NM_001184796.1.
DR RefSeq; NP_056107.1; NM_015292.2.
DR UniGene; Hs.632729; -.
DR ProteinModelPortal; Q9BSJ8; -.
DR SMR; Q9BSJ8; 331-447, 648-741, 971-1103.
DR IntAct; Q9BSJ8; 8.
DR MINT; MINT-1144538; -.
DR STRING; 9606.ENSP00000267113; -.
DR PhosphoSite; Q9BSJ8; -.
DR DMDM; 74733019; -.
DR OGP; Q9Y416; -.
DR PaxDb; Q9BSJ8; -.
DR PRIDE; Q9BSJ8; -.
DR DNASU; 23344; -.
DR Ensembl; ENST00000267113; ENSP00000267113; ENSG00000139641.
DR Ensembl; ENST00000394048; ENSP00000377612; ENSG00000139641.
DR Ensembl; ENST00000541590; ENSP00000445952; ENSG00000139641.
DR GeneID; 23344; -.
DR KEGG; hsa:23344; -.
DR UCSC; uc001sjq.3; human.
DR CTD; 23344; -.
DR GeneCards; GC12P056536; -.
DR HGNC; HGNC:29534; ESYT1.
DR HPA; HPA016858; -.
DR neXtProt; NX_Q9BSJ8; -.
DR PharmGKB; PA165512688; -.
DR eggNOG; COG5038; -.
DR HOVERGEN; HBG055795; -.
DR OMA; SQHSGVE; -.
DR OrthoDB; EOG7RNJZK; -.
DR PhylomeDB; Q9BSJ8; -.
DR ChiTaRS; ESYT1; human.
DR GeneWiki; FAM62A; -.
DR GenomeRNAi; 23344; -.
DR NextBio; 45301; -.
DR PRO; PR:Q9BSJ8; -.
DR ArrayExpress; Q9BSJ8; -.
DR Bgee; Q9BSJ8; -.
DR CleanEx; HS_FAM62A; -.
DR Genevestigator; Q9BSJ8; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR InterPro; IPR000008; C2_dom.
DR Pfam; PF00168; C2; 5.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 5.
DR SUPFAM; SSF49562; SSF49562; 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 Reference proteome; Repeat; Transmembrane; Transmembrane helix.
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 820 820 Phosphoserine.
FT MOD_RES 963 963 Phosphoserine.
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
//
ID ESYT1_HUMAN Reviewed; 1104 AA.
AC Q9BSJ8; A0FGR7; A8K2S2; O94848; Q6PJN4; Q9H6J1; Q9H6W2; Q9Y416;
read moreDT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 106.
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 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 IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
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 [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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 [12]
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.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-963, AND
RP MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May play a role as calcium-regulated intrinsic membrane
CC protein (By similarity).
CC -!- INTERACTION:
CC A0FGR8:ESYT2; NbExp=4; IntAct=EBI-355956, EBI-3184170;
CC A0FGR9:ESYT3; NbExp=3; IntAct=EBI-355956, EBI-8771391;
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;
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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 PIR; T08769; T08769.
DR PIR; T13156; T13156.
DR RefSeq; NP_001171725.1; NM_001184796.1.
DR RefSeq; NP_056107.1; NM_015292.2.
DR UniGene; Hs.632729; -.
DR ProteinModelPortal; Q9BSJ8; -.
DR SMR; Q9BSJ8; 331-447, 648-741, 971-1103.
DR IntAct; Q9BSJ8; 8.
DR MINT; MINT-1144538; -.
DR STRING; 9606.ENSP00000267113; -.
DR PhosphoSite; Q9BSJ8; -.
DR DMDM; 74733019; -.
DR OGP; Q9Y416; -.
DR PaxDb; Q9BSJ8; -.
DR PRIDE; Q9BSJ8; -.
DR DNASU; 23344; -.
DR Ensembl; ENST00000267113; ENSP00000267113; ENSG00000139641.
DR Ensembl; ENST00000394048; ENSP00000377612; ENSG00000139641.
DR Ensembl; ENST00000541590; ENSP00000445952; ENSG00000139641.
DR GeneID; 23344; -.
DR KEGG; hsa:23344; -.
DR UCSC; uc001sjq.3; human.
DR CTD; 23344; -.
DR GeneCards; GC12P056536; -.
DR HGNC; HGNC:29534; ESYT1.
DR HPA; HPA016858; -.
DR neXtProt; NX_Q9BSJ8; -.
DR PharmGKB; PA165512688; -.
DR eggNOG; COG5038; -.
DR HOVERGEN; HBG055795; -.
DR OMA; SQHSGVE; -.
DR OrthoDB; EOG7RNJZK; -.
DR PhylomeDB; Q9BSJ8; -.
DR ChiTaRS; ESYT1; human.
DR GeneWiki; FAM62A; -.
DR GenomeRNAi; 23344; -.
DR NextBio; 45301; -.
DR PRO; PR:Q9BSJ8; -.
DR ArrayExpress; Q9BSJ8; -.
DR Bgee; Q9BSJ8; -.
DR CleanEx; HS_FAM62A; -.
DR Genevestigator; Q9BSJ8; -.
DR GO; GO:0016021; C:integral to membrane; IEA:UniProtKB-KW.
DR InterPro; IPR000008; C2_dom.
DR Pfam; PF00168; C2; 5.
DR PRINTS; PR00360; C2DOMAIN.
DR SMART; SM00239; C2; 5.
DR SUPFAM; SSF49562; SSF49562; 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 Reference proteome; Repeat; Transmembrane; Transmembrane helix.
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 820 820 Phosphoserine.
FT MOD_RES 963 963 Phosphoserine.
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
//