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Protein

Extended synaptotagmin-1

Gene

ESYT1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport (By similarity). Binds calcium (via the C2 domains) and translocates to sites of contact between the endoplasmic reticulum and the cell membrane in response to increased cytosolic calcium levels. Helps tether the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane.By similarity2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi344 – 3441Calcium 1; via carbonyl oxygenBy similarity
Metal bindingi345 – 3451Calcium 1By similarity
Metal bindingi345 – 3451Calcium 2By similarity
Metal bindingi357 – 3571Calcium 2By similarity
Metal bindingi404 – 4041Calcium 1By similarity
Metal bindingi404 – 4041Calcium 2By similarity
Metal bindingi406 – 4061Calcium 1By similarity
Metal bindingi406 – 4061Calcium 2By similarity
Metal bindingi406 – 4061Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi408 – 4081Calcium 3; via carbonyl oxygenBy similarity
Metal bindingi410 – 4101Calcium 3By similarity
Metal bindingi411 – 4111Calcium 1By similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

Lipid transport, Transport

Keywords - Ligandi

Calcium, Lipid-binding, Metal-binding

Protein family/group databases

TCDBi9.A.57.1.1. the extended-synaptotagmin (e-syt) family.

Names & Taxonomyi

Protein namesi
Recommended name:
Extended synaptotagmin-1
Short name:
E-Syt1
Alternative name(s):
Membrane-bound C2 domain-containing protein
Gene namesi
Name:ESYT1
Synonyms:FAM62A, KIAA0747, MBC2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:29534. ESYT1.

Subcellular locationi

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 3838CytoplasmicSequence analysisAdd
BLAST
Transmembranei39 – 5921HelicalSequence analysisAdd
BLAST
Topological domaini60 – 623LumenalSequence analysis
Transmembranei63 – 8321HelicalSequence analysisAdd
BLAST
Topological domaini84 – 11041021CytoplasmicSequence analysisAdd
BLAST

GO - Cellular componenti

  • integral component of endoplasmic reticulum membrane Source: UniProtKB
  • membrane Source: UniProtKB
  • organelle membrane contact site Source: GO_Central
  • plasma membrane Source: UniProtKB-SubCell
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi406 – 4061D → A: No effect on translocation to sites of contact between the endoplasmic reticulum and the cell membrane. 1 Publication
Mutagenesisi663 – 6631D → A: Abolishes location at the cell membrane; when associated with A-675 and 722-A--A-729. 1 Publication
Mutagenesisi675 – 6751D → A: Abolishes location at the cell membrane; when associated with A-675 and 722-A--A-729. 1 Publication
Mutagenesisi722 – 7298DKDLDKDD → AKALAKAA: Abolishes location at the cell membrane; when associated with A-663 and A-675. 1 Publication
Mutagenesisi724 – 7241D → A: Loss of translocation to sites of contact between the endoplasmic reticulum and the cell membrane. 1 Publication

Organism-specific databases

PharmGKBiPA165512688.

Polymorphism and mutation databases

BioMutaiESYT1.
DMDMi74733019.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 11041104Extended synaptotagmin-1PRO_0000234344Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineCombined sources
Modified residuei324 – 3241Phosphoserine; by CDK5By similarity
Modified residuei817 – 8171N6-acetyllysineCombined sources
Modified residuei820 – 8201PhosphoserineCombined sources
Modified residuei941 – 9411PhosphoserineCombined sources
Modified residuei948 – 9481PhosphothreonineCombined sources
Modified residuei949 – 9491PhosphoserineCombined sources
Modified residuei963 – 9631PhosphoserineCombined sources
Modified residuei1009 – 10091PhosphotyrosineBy similarity
Modified residuei1034 – 10341PhosphoserineCombined sources

Post-translational modificationi

Phosphorylated on Ser residues in insulin-treated adipocytes (in vitro); this promotes interaction with SLC2A4.By similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ9BSJ8.
MaxQBiQ9BSJ8.
PaxDbiQ9BSJ8.
PRIDEiQ9BSJ8.

2D gel databases

OGPiQ9Y416.

PTM databases

iPTMnetiQ9BSJ8.
PhosphoSiteiQ9BSJ8.
SwissPalmiQ9BSJ8.

Expressioni

Tissue specificityi

Widely expressed.1 Publication

Gene expression databases

BgeeiQ9BSJ8.
CleanExiHS_FAM62A.
ExpressionAtlasiQ9BSJ8. baseline and differential.
GenevisibleiQ9BSJ8. HS.

Organism-specific databases

HPAiHPA016858.

Interactioni

Subunit structurei

Interacts (phosphorylated form) with SLC2A4 (By similarity). Interacts with ESYT2 and ESYT3.By similarity1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
ESYT2A0FGR84EBI-355956,EBI-3184170
ESYT3A0FGR93EBI-355956,EBI-8771391

Protein-protein interaction databases

BioGridi116927. 34 interactions.
IntActiQ9BSJ8. 15 interactions.
MINTiMINT-1144538.
STRINGi9606.ENSP00000267113.

Structurei

3D structure databases

ProteinModelPortaliQ9BSJ8.
SMRiQ9BSJ8. Positions 135-599, 648-914, 971-1103.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini316 – 417102C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini465 – 55894C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini634 – 735102C2 3PROSITE-ProRule annotationAdd
BLAST
Domaini785 – 87793C2 4PROSITE-ProRule annotationAdd
BLAST
Domaini972 – 1077106C2 5PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni139 – 313175Glycerophospholipid-binding barrel-like domainBy similarityAdd
BLAST
Regioni1018 – 10258Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membraneBy similarity

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili91 – 11626Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi924 – 93512Poly-SerAdd
BLAST
Compositional biasi1012 – 10154Poly-Leu

Domaini

Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic.1 Publication
The C2 domains mediate lipid and calcium binding. The N-terminal C2 domain binds calcium ions and is important for calcium-dependent lipid binding and interaction with membranes. Two calcium ions are bound at a high-affinity site and a third calcium ion is bound with lower affinity. May bind up to four calcium ions. In contrast, the second C2 domain apparently does not bind calcium (By similarity). The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for translocation to the cell membrane in response to increased cytosolic calcium levels (PubMed:24183667 and PubMed:23791178).By similarity
Contains a barrel-like domain that can bind various types of glycerophospholipids in its interior.By similarity

Sequence similaritiesi

Belongs to the extended synaptotagmin family.Curated
Contains 5 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Coiled coil, Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiENOG410ISCC. Eukaryota.
ENOG410XPR4. LUCA.
GeneTreeiENSGT00550000074417.
HOVERGENiHBG055795.
InParanoidiQ9BSJ8.
OMAiSQHSGVE.
OrthoDBiEOG7RNJZK.
PhylomeDBiQ9BSJ8.
TreeFamiTF324255.

Family and domain databases

Gene3Di2.60.40.150. 5 hits.
InterProiIPR000008. C2_dom.
IPR031468. SMP_LBD.
[Graphical view]
PfamiPF00168. C2. 5 hits.
PF17047. SMP_LBD. 1 hit.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 5 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 5 hits.
PROSITEiPS50004. C2. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9BSJ8-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERSPGEGPS PSPMDQPSAP SDPTDQPPAA HAKPDPGSGG QPAGPGAAGE
60 70 80 90 100
ALAVLTSFGR RLLVLIPVYL AGAVGLSVGF VLFGLALYLG WRRVRDEKER
110 120 130 140 150
SLRAARQLLD DEEQLTAKTL YMSHRELPAW VSFPDVEKAE WLNKIVAQVW
160 170 180 190 200
PFLGQYMEKL LAETVAPAVR GSNPHLQTFT FTRVELGEKP LRIIGVKVHP
210 220 230 240 250
GQRKEQILLD LNISYVGDVQ IDVEVKKYFC KAGVKGMQLH GVLRVILEPL
260 270 280 290 300
IGDLPFVGAV SMFFIRRPTL DINWTGMTNL LDIPGLSSLS DTMIMDSIAA
310 320 330 340 350
FLVLPNRLLV PLVPDLQDVA QLRSPLPRGI IRIHLLAARG LSSKDKYVKG
360 370 380 390 400
LIEGKSDPYA LVRLGTQTFC SRVIDEELNP QWGETYEVMV HEVPGQEIEV
410 420 430 440 450
EVFDKDPDKD DFLGRMKLDV GKVLQASVLD DWFPLQGGQG QVHLRLEWLS
460 470 480 490 500
LLSDAEKLEQ VLQWNWGVSS RPDPPSAAIL VVYLDRAQDL PLKKGNKEPN
510 520 530 540 550
PMVQLSIQDV TQESKAVYST NCPVWEEAFR FFLQDPQSQE LDVQVKDDSR
560 570 580 590 600
ALTLGALTLP LARLLTAPEL ILDQWFQLSS SGPNSRLYMK LVMRILYLDS
610 620 630 640 650
SEICFPTVPG CPGAWDVDSE NPQRGSSVDA PPRPCHTTPD SQFGTEHVLR
660 670 680 690 700
IHVLEAQDLI AKDRFLGGLV KGKSDPYVKL KLAGRSFRSH VVREDLNPRW
710 720 730 740 750
NEVFEVIVTS VPGQELEVEV FDKDLDKDDF LGRCKVRLTT VLNSGFLDEW
760 770 780 790 800
LTLEDVPSGR LHLRLERLTP RPTAAELEEV LQVNSLIQTQ KSAELAAALL
810 820 830 840 850
SIYMERAEDL PLRKGTKHLS PYATLTVGDS SHKTKTISQT SAPVWDESAS
860 870 880 890 900
FLIRKPHTES LELQVRGEGT GVLGSLSLPL SELLVADQLC LDRWFTLSSG
910 920 930 940 950
QGQVLLRAQL GILVSQHSGV EAHSHSYSHS SSSLSEEPEL SGGPPHITSS
960 970 980 990 1000
APELRQRLTH VDSPLEAPAG PLGQVKLTLW YYSEERKLVS IVHGCRSLRQ
1010 1020 1030 1040 1050
NGRDPPDPYV SLLLLPDKNR GTKRRTSQKK RTLSPEFNER FEWELPLDEA
1060 1070 1080 1090 1100
QRRKLDVSVK SNSSFMSRER ELLGKVQLDL AETDLSQGVA RWYDLMDNKD

KGSS
Length:1,104
Mass (Da):122,856
Last modified:June 1, 2001 - v1
Checksum:iE72B20C458B96F19
GO
Isoform 2 (identifier: Q9BSJ8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     491-491: P → PMVTSELYPPQ

Note: No experimental confirmation available.
Show »
Length:1,114
Mass (Da):124,003
Checksum:i3ECE7EC47B8A90A8
GO

Sequence cautioni

The sequence BAB15139.1 differs from that shown. Reason: Erroneous initiation. Curated
The sequence BAB15268.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti133 – 1331F → L in BAF83026 (PubMed:14702039).Curated
Sequence conflicti489 – 4891D → N in BAB15139 (PubMed:14702039).Curated
Sequence conflicti738 – 7381L → F in BAB15139 (PubMed:14702039).Curated
Sequence conflicti785 – 7851S → R in BAF83026 (PubMed:14702039).Curated
Sequence conflicti998 – 9981L → P in BAB15139 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti764 – 7641R → C.
Corresponds to variant rs35075600 [ dbSNP | Ensembl ].
VAR_038190

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei491 – 4911P → PMVTSELYPPQ in isoform 2. 1 PublicationVSP_018277

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ993200 mRNA. Translation: ABJ97705.1.
AK025463 mRNA. Translation: BAB15139.1. Different initiation.
AK025878 mRNA. Translation: BAB15268.1. Different initiation.
AK290337 mRNA. Translation: BAF83026.1.
CH471054 Genomic DNA. Translation: EAW96891.1.
BC004998 mRNA. Translation: AAH04998.1.
AB018290 mRNA. Translation: BAA34467.1.
AL050134 mRNA. Translation: CAB43284.1.
CCDSiCCDS53801.1. [Q9BSJ8-2]
CCDS8904.1. [Q9BSJ8-1]
PIRiT08769.
T13156.
RefSeqiNP_001171725.1. NM_001184796.1. [Q9BSJ8-2]
NP_056107.1. NM_015292.2. [Q9BSJ8-1]
UniGeneiHs.632729.

Genome annotation databases

EnsembliENST00000267113; ENSP00000267113; ENSG00000139641. [Q9BSJ8-2]
ENST00000394048; ENSP00000377612; ENSG00000139641. [Q9BSJ8-1]
GeneIDi23344.
KEGGihsa:23344.
UCSCiuc001sjq.4. human. [Q9BSJ8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ993200 mRNA. Translation: ABJ97705.1.
AK025463 mRNA. Translation: BAB15139.1. Different initiation.
AK025878 mRNA. Translation: BAB15268.1. Different initiation.
AK290337 mRNA. Translation: BAF83026.1.
CH471054 Genomic DNA. Translation: EAW96891.1.
BC004998 mRNA. Translation: AAH04998.1.
AB018290 mRNA. Translation: BAA34467.1.
AL050134 mRNA. Translation: CAB43284.1.
CCDSiCCDS53801.1. [Q9BSJ8-2]
CCDS8904.1. [Q9BSJ8-1]
PIRiT08769.
T13156.
RefSeqiNP_001171725.1. NM_001184796.1. [Q9BSJ8-2]
NP_056107.1. NM_015292.2. [Q9BSJ8-1]
UniGeneiHs.632729.

3D structure databases

ProteinModelPortaliQ9BSJ8.
SMRiQ9BSJ8. Positions 135-599, 648-914, 971-1103.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116927. 34 interactions.
IntActiQ9BSJ8. 15 interactions.
MINTiMINT-1144538.
STRINGi9606.ENSP00000267113.

Protein family/group databases

TCDBi9.A.57.1.1. the extended-synaptotagmin (e-syt) family.

PTM databases

iPTMnetiQ9BSJ8.
PhosphoSiteiQ9BSJ8.
SwissPalmiQ9BSJ8.

Polymorphism and mutation databases

BioMutaiESYT1.
DMDMi74733019.

2D gel databases

OGPiQ9Y416.

Proteomic databases

EPDiQ9BSJ8.
MaxQBiQ9BSJ8.
PaxDbiQ9BSJ8.
PRIDEiQ9BSJ8.

Protocols and materials databases

DNASUi23344.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000267113; ENSP00000267113; ENSG00000139641. [Q9BSJ8-2]
ENST00000394048; ENSP00000377612; ENSG00000139641. [Q9BSJ8-1]
GeneIDi23344.
KEGGihsa:23344.
UCSCiuc001sjq.4. human. [Q9BSJ8-1]

Organism-specific databases

CTDi23344.
GeneCardsiESYT1.
HGNCiHGNC:29534. ESYT1.
HPAiHPA016858.
neXtProtiNX_Q9BSJ8.
PharmGKBiPA165512688.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410ISCC. Eukaryota.
ENOG410XPR4. LUCA.
GeneTreeiENSGT00550000074417.
HOVERGENiHBG055795.
InParanoidiQ9BSJ8.
OMAiSQHSGVE.
OrthoDBiEOG7RNJZK.
PhylomeDBiQ9BSJ8.
TreeFamiTF324255.

Miscellaneous databases

ChiTaRSiESYT1. human.
GeneWikiiFAM62A.
GenomeRNAii23344.
PROiQ9BSJ8.

Gene expression databases

BgeeiQ9BSJ8.
CleanExiHS_FAM62A.
ExpressionAtlasiQ9BSJ8. baseline and differential.
GenevisibleiQ9BSJ8. HS.

Family and domain databases

Gene3Di2.60.40.150. 5 hits.
InterProiIPR000008. C2_dom.
IPR031468. SMP_LBD.
[Graphical view]
PfamiPF00168. C2. 5 hits.
PF17047. SMP_LBD. 1 hit.
[Graphical view]
PRINTSiPR00360. C2DOMAIN.
SMARTiSM00239. C2. 5 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 5 hits.
PROSITEiPS50004. C2. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "E-Syts, a family of membranous Ca2+-sensor proteins with multiple C2 domains."
    Min S.-W., Chang W.-P., Suedhof T.C.
    Proc. Natl. Acad. Sci. U.S.A. 104:3823-3828(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
  2. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Hepatoma, Kidney and Tongue.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Kidney.
  5. "Prediction of the coding sequences of unidentified human genes. XI. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Suyama M., Kikuno R., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 5:277-286(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 43-1104 (ISOFORM 2).
    Tissue: Brain.
  6. Bienvenut W.V., Claeys D.
    Submitted (NOV-2005) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 308-323; 446-457 AND 551-586, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: B-cell lymphoma and Platelet.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 379-1104 (ISOFORM 1).
    Tissue: Uterus.
  8. "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells."
    Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J.
    Nat. Biotechnol. 23:94-101(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-963 AND SER-1034, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  12. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-817, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820 AND SER-963, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  15. "PI(4,5)P(2)-dependent and Ca(2+)-regulated ER-PM interactions mediated by the extended synaptotagmins."
    Giordano F., Saheki Y., Idevall-Hagren O., Colombo S.F., Pirruccello M., Milosevic I., Gracheva E.O., Bagriantsev S.N., Borgese N., De Camilli P.
    Cell 153:1494-1509(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, TOPOLOGY, LIPID-BINDING, MUTAGENESIS OF ASP-663; ASP-675 AND 722-ASP--ASP-729, INTERACTION WITH ESYT2 AND ESYT3.
  16. "Feedback regulation of receptor-induced Ca2+ signaling mediated by E-Syt1 and Nir2 at endoplasmic reticulum-plasma membrane junctions."
    Chang C.L., Hsieh T.S., Yang T.T., Rothberg K.G., Azizoglu D.B., Volk E., Liao J.C., Liou J.
    Cell Rep. 5:813-825(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-406 AND ASP-724.
  17. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-820; SER-941; THR-948; SER-949 AND SER-963, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiESYT1_HUMAN
AccessioniPrimary (citable) accession number: Q9BSJ8
Secondary accession number(s): A0FGR7
, A8K2S2, O94848, Q6PJN4, Q9H6J1, Q9H6W2, Q9Y416
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 16, 2006
Last sequence update: June 1, 2001
Last modified: June 8, 2016
This is version 132 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.