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A0FGR8

- ESYT2_HUMAN

UniProt

A0FGR8 - ESYT2_HUMAN

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Protein

Extended synaptotagmin-2

Gene

ESYT2

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

Functioni

Tethers the endoplasmic reticulum to the cell membrane and promotes the formation of appositions between the endoplasmic reticulum and the cell membrane. Binds glycerophospholipids in a barrel-like domain and may play a role in cellular lipid transport. Plays a role in FGF signaling via its role in the rapid internalization of FGFR1 that has been activated by FGF1 binding; this occurs most likely via the AP-2 complex.4 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi400 – 4001Calcium 1; via carbonyl oxygen1 Publication
Metal bindingi401 – 4011Calcium 11 Publication
Metal bindingi401 – 4011Calcium 21 Publication
Metal bindingi413 – 4131Calcium 21 Publication
Metal bindingi460 – 4601Calcium 11 Publication
Metal bindingi460 – 4601Calcium 21 Publication
Metal bindingi461 – 4611Calcium 2; via carbonyl oxygen1 Publication
Metal bindingi462 – 4621Calcium 11 Publication
Metal bindingi462 – 4621Calcium 21 Publication
Metal bindingi462 – 4621Calcium 3; via carbonyl oxygen1 Publication
Metal bindingi464 – 4641Calcium 3; via carbonyl oxygen1 Publication
Metal bindingi466 – 4661Calcium 31 Publication
Metal bindingi467 – 4671Calcium 11 Publication

GO - Molecular functioni

  1. calcium-dependent phospholipid binding Source: FlyBase
  2. calcium ion binding Source: UniProtKB
  3. identical protein binding Source: IntAct
  4. phosphatidylcholine binding Source: UniProtKB
  5. phosphatidylethanolamine binding Source: UniProtKB
  6. phosphatidylinositol binding Source: UniProtKB

GO - Biological processi

  1. endocytosis Source: UniProtKB-KW
  2. lipid transport Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

Endocytosis, Lipid transport, Transport

Keywords - Ligandi

Calcium, Lipid-binding, Metal-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Extended synaptotagmin-2
Short name:
E-Syt2
Alternative name(s):
Chr2Syt
Gene namesi
Name:ESYT2
Synonyms:FAM62B, KIAA1228
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:22211. ESYT2.

Subcellular locationi

Cell membrane; Peripheral membrane protein. Endoplasmic reticulum membrane; Multi-pass membrane protein
Note: Detected at sites of contact between the endoplasmic reticulum membrane and the cell membrane. Recruited to the cell membrane via the third C2 domain.

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini1 – 103103CytoplasmicSequence AnalysisAdd
BLAST
Transmembranei104 – 12421HelicalSequence AnalysisAdd
BLAST
Topological domaini125 – 1273LumenalSequence Analysis
Transmembranei128 – 14821HelicalSequence AnalysisAdd
BLAST
Topological domaini149 – 921773CytoplasmicSequence AnalysisAdd
BLAST

GO - Cellular componenti

  1. extrinsic component of cytoplasmic side of plasma membrane Source: UniProtKB
  2. integral component of plasma membrane Source: FlyBase
  3. intrinsic component of endoplasmic reticulum membrane Source: UniProtKB
  4. membrane Source: UniProtKB
  5. organelle membrane contact site Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cell membrane, Endoplasmic reticulum, Membrane

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi401 – 4011D → A: Abolishes calcium binding; when associated with A-413. 1 Publication
Mutagenesisi413 – 4131D → A: Abolishes calcium binding; when associated with A-401. 1 Publication
Mutagenesisi413 – 4131D → N: Strongly reduces calcium binding. 1 Publication
Mutagenesisi466 – 4661D → A: Impairs binding of the third calcium ion, but has no effect on the binding of the other two calcium ions. 1 Publication
Mutagenesisi833 – 8408KRRSGRRK → AAASGAAA: Abolishes location at the cell membrane. 1 Publication

Organism-specific databases

PharmGKBiPA165617947.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 921921Extended synaptotagmin-2PRO_0000278258Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei691 – 6911Phosphoserine1 Publication
Modified residuei738 – 7381PhosphoserineBy similarity
Modified residuei739 – 7391Phosphoserine1 Publication
Modified residuei743 – 7431Phosphoserine4 Publications
Modified residuei748 – 7481Phosphoserine1 Publication
Modified residuei755 – 7551Phosphoserine2 Publications
Modified residuei758 – 7581Phosphoserine5 Publications
Modified residuei761 – 7611Phosphoserine5 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiA0FGR8.
PaxDbiA0FGR8.
PRIDEiA0FGR8.

PTM databases

PhosphoSiteiA0FGR8.

Expressioni

Tissue specificityi

Widely expressed with high level in cerebellum.1 Publication

Gene expression databases

BgeeiA0FGR8.
CleanExiHS_FAM62B.
ExpressionAtlasiA0FGR8. baseline and differential.
GenevestigatoriA0FGR8.

Organism-specific databases

HPAiHPA002132.

Interactioni

Subunit structurei

Homodimer. Interacts with ESYT1 and ESYT3. Interacts with FGFR1 that has been activated by FGF1 binding. Interacts with the AP-2 complex; identified in a complex with the AP-2 complex and FGFR1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself3EBI-3184170,EBI-3184170
ESYT1Q9BSJ84EBI-3184170,EBI-355956
ESYT3A0FGR93EBI-3184170,EBI-8771391

Protein-protein interaction databases

BioGridi121556. 9 interactions.
IntActiA0FGR8. 8 interactions.
MINTiMINT-4541681.

Structurei

Secondary structure

1
921
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi196 – 21924Combined sources
Helixi221 – 2266Combined sources
Helixi230 – 2323Combined sources
Beta strandi235 – 2417Combined sources
Beta strandi248 – 2558Combined sources
Beta strandi264 – 28219Combined sources
Turni283 – 2864Combined sources
Beta strandi287 – 30418Combined sources
Beta strandi316 – 3238Combined sources
Beta strandi326 – 3338Combined sources
Helixi334 – 3374Combined sources
Turni341 – 3455Combined sources
Helixi348 – 35811Combined sources
Beta strandi365 – 3706Combined sources
Helixi372 – 3798Combined sources
Beta strandi384 – 39613Combined sources
Turni405 – 4073Combined sources
Beta strandi414 – 4207Combined sources
Beta strandi423 – 4264Combined sources
Beta strandi437 – 44610Combined sources
Beta strandi453 – 4608Combined sources
Beta strandi463 – 4653Combined sources
Beta strandi467 – 4759Combined sources
Helixi476 – 4827Combined sources
Beta strandi483 – 4908Combined sources
Beta strandi494 – 4963Combined sources
Beta strandi498 – 51215Combined sources
Helixi515 – 52410Combined sources
Beta strandi535 – 54713Combined sources
Beta strandi560 – 5667Combined sources
Beta strandi569 – 5724Combined sources
Beta strandi583 – 59311Combined sources
Turni595 – 5973Combined sources
Beta strandi599 – 6068Combined sources
Turni607 – 6093Combined sources
Beta strandi612 – 6198Combined sources
Helixi621 – 6244Combined sources
Helixi627 – 6293Combined sources
Beta strandi630 – 6367Combined sources
Beta strandi638 – 6403Combined sources
Beta strandi645 – 65612Combined sources
Beta strandi789 – 7979Combined sources
Turni798 – 8014Combined sources
Beta strandi802 – 81110Combined sources
Beta strandi823 – 8319Combined sources
Beta strandi835 – 8373Combined sources
Beta strandi851 – 8588Combined sources
Helixi862 – 8676Combined sources
Beta strandi869 – 8768Combined sources
Beta strandi889 – 8946Combined sources
Turni899 – 9024Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DMGNMR-A785-913[»]
4NPJX-ray2.10A/B363-660[»]
4NPKX-ray2.55A363-660[»]
4P42X-ray2.44A/B191-662[»]
ProteinModelPortaliA0FGR8.
SMRiA0FGR8. Positions 191-659, 756-919.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiA0FGR8.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini372 – 473102C2 1PROSITE-ProRule annotationAdd
BLAST
Domaini523 – 61795C2 2PROSITE-ProRule annotationAdd
BLAST
Domaini788 – 892105C2 3PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni195 – 370176Glycerophospholipid-binding barrel-like domainAdd
BLAST
Regioni833 – 8408Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi736 – 7394Poly-Ser

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 (PubMed:24373768). The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for location at the cell membrane (PubMed:23791178).2 Publications
Contains a barrel-like domain that binds glycerophospholipids in its interior; can bind two lipid molecules simultaneously. Binds a variety of lipids, including phosphatidylethanolamine, phosphatidylcholine and phosphatidylinositol (PubMed:24847877).1 Publication

Sequence similaritiesi

Belongs to the extended synaptotagmin family.Curated
Contains 3 C2 domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, Transmembrane, Transmembrane helix

Phylogenomic databases

eggNOGiCOG5038.
GeneTreeiENSGT00550000074417.
HOVERGENiHBG055795.
InParanoidiA0FGR8.
OMAiVDVGQQP.
OrthoDBiEOG7RNJZK.
PhylomeDBiA0FGR8.
TreeFamiTF324255.

Family and domain databases

Gene3Di2.60.40.150. 3 hits.
InterProiIPR000008. C2_dom.
[Graphical view]
PfamiPF00168. C2. 3 hits.
[Graphical view]
SMARTiSM00239. C2. 3 hits.
[Graphical view]
SUPFAMiSSF49562. SSF49562. 3 hits.
PROSITEiPS50004. C2. 3 hits.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: A0FGR8-1) [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
MTANRDAALS SHRHPGCAQR PRTPTFASSS QRRSAFGFDD GNFPGLGERS
60 70 80 90 100
HAPGSRLGAR RRAKTARGLR GHRQRGAGAG LSRPGSARAP SPPRPGGPEN
110 120 130 140 150
PGGVLSVELP GLLAQLARSF ALLLPVYALG YLGLSFSWVL LALALLAWCR
160 170 180 190 200
RSRGLKALRL CRALALLEDE ERVVRLGVRA CDLPAWVHFP DTERAEWLNK
210 220 230 240 250
TVKHMWPFIC QFIEKLFRET IEPAVRGANT HLSTFSFTKV DVGQQPLRIN
260 270 280 290 300
GVKVYTENVD KRQIILDLQI SFVGNCEIDL EIKRYFCRAG VKSIQIHGTM
310 320 330 340 350
RVILEPLIGD MPLVGALSIF FLRKPLLEIN WTGLTNLLDV PGLNGLSDTI
360 370 380 390 400
ILDIISNYLV LPNRITVPLV SEVQIAQLRF PVPKGVLRIH FIEAQDLQGK
410 420 430 440 450
DTYLKGLVKG KSDPYGIIRV GNQIFQSRVI KENLSPKWNE VYEALVYEHP
460 470 480 490 500
GQELEIELFD EDPDKDDFLG SLMIDLIEVE KERLLDEWFT LDEVPKGKLH
510 520 530 540 550
LRLEWLTLMP NASNLDKVLT DIKADKDQAN DGLSSALLIL YLDSARNLPS
560 570 580 590 600
GKKISSNPNP VVQMSVGHKA QESKIRYKTN EPVWEENFTF FIHNPKRQDL
610 620 630 640 650
EVEVRDEQHQ CSLGNLKVPL SQLLTSEDMT VSQRFQLSNS GPNSTIKMKI
660 670 680 690 700
ALRVLHLEKR ERPPDHQHSA QVKRPSVSKE GRKTSIKSHM SGSPGPGGSN
710 720 730 740 750
TAPSTPVIGG SDKPGMEEKA QPPEAGPQGL HDLGRSSSSL LASPGHISVK
760 770 780 790 800
EPTPSIASDI SLPIATQELR QRLRQLENGT TLGQSPLGQI QLTIRHSSQR
810 820 830 840 850
NKLIVVVHAC RNLIAFSEDG SDPYVRMYLL PDKRRSGRRK THVSKKTLNP
860 870 880 890 900
VFDQSFDFSV SLPEVQRRTL DVAVKNSGGF LSKDKGLLGK VLVALASEEL
910 920
AKGWTQWYDL TEDGTRPQAM T
Length:921
Mass (Da):102,357
Last modified:November 28, 2006 - v1
Checksum:iD57F1BD9BB0A0C8A
GO
Isoform 2 (identifier: A0FGR8-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: MTANRDAALS...RAPSPPRPGG → MTPPSRAEAG...GAGGAGGRAA

Note: No experimental confirmation available.

Show »
Length:893
Mass (Da):98,902
Checksum:i9C059B137A2F1EFB
GO
Isoform 4 (identifier: A0FGR8-4) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-204: Missing.
     706-731: PVIGGSDKPGMEEKAQPPEAGPQGLH → SQSRSRPPASPRTSRCPSPPRSCGKG
     732-921: Missing.

Note: No experimental confirmation available.

Show »
Length:527
Mass (Da):59,403
Checksum:iE4257349511C9C28
GO
Isoform 5 (identifier: A0FGR8-5) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-593: Missing.
     594-603: NPKRQDLEVE → MPVLPPCVLQ

Note: No experimental confirmation available.

Show »
Length:328
Mass (Da):35,846
Checksum:iEF531CFF2A35D17C
GO
Isoform 6 (identifier: A0FGR8-6) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     550-550: S → SNPLEFNPDVLKKTAVQRALKS

Note: No experimental confirmation available.

Show »
Length:942
Mass (Da):104,708
Checksum:i207D6C010DB58248
GO

Sequence cautioni

The sequence BAA91539.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAC85769.1 differs from that shown. Reason: Frameshift at position 800. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti141 – 1411L → V in CAH10642. (PubMed:17974005)Curated
Sequence conflicti612 – 6121S → P in BAC85769. (PubMed:14702039)Curated
Sequence conflicti615 – 6151N → S in BAC86489. (PubMed:14702039)Curated
Sequence conflicti795 – 7951R → Q in BAC85769. (PubMed:14702039)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti210 – 2101C → S.
Corresponds to variant rs13233513 [ dbSNP | Ensembl ].
VAR_030725
Natural varianti638 – 6381S → G.1 Publication
Corresponds to variant rs2305473 [ dbSNP | Ensembl ].
VAR_030726

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 593593Missing in isoform 5. 1 PublicationVSP_023236Add
BLAST
Alternative sequencei1 – 204204Missing in isoform 4. 1 PublicationVSP_023238Add
BLAST
Alternative sequencei1 – 9797MTANR…PRPGG → MTPPSRAEAGVRRSRVPSEG RWRGAEPPGISASTQPASAG RAARHCGAMSGARGEGPEAG AGGAGGRAA in isoform 2. 1 PublicationVSP_023239Add
BLAST
Alternative sequencei550 – 5501S → SNPLEFNPDVLKKTAVQRAL KS in isoform 6. 1 PublicationVSP_038324
Alternative sequencei594 – 60310NPKRQDLEVE → MPVLPPCVLQ in isoform 5. 1 PublicationVSP_023240
Alternative sequencei706 – 73126PVIGG…PQGLH → SQSRSRPPASPRTSRCPSPP RSCGKG in isoform 4. 1 PublicationVSP_023241Add
BLAST
Alternative sequencei732 – 921190Missing in isoform 4. 1 PublicationVSP_023242Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ993201 mRNA. Translation: ABJ97706.1.
AY368150 mRNA. Translation: AAR89381.1.
AK001181 mRNA. Translation: BAA91539.1. Different initiation.
AK124091 mRNA. Translation: BAC85769.1. Frameshift.
AK126214 mRNA. Translation: BAC86489.1.
CH236954 Genomic DNA. Translation: EAL23931.1.
AB033054 mRNA. Translation: BAA86542.2.
AL833233 mRNA. Translation: CAH10642.1.
BC013957 mRNA. Translation: AAH13957.2.
AJ303365 mRNA. Translation: CAC33887.1.
CCDSiCCDS34791.1. [A0FGR8-2]
RefSeqiNP_065779.1. NM_020728.2. [A0FGR8-2]
UniGeneiHs.490795.

Genome annotation databases

EnsembliENST00000251527; ENSP00000251527; ENSG00000117868. [A0FGR8-2]
GeneIDi57488.
KEGGihsa:57488.
UCSCiuc003wob.1. human. [A0FGR8-2]
uc003woc.1. human. [A0FGR8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
DQ993201 mRNA. Translation: ABJ97706.1 .
AY368150 mRNA. Translation: AAR89381.1 .
AK001181 mRNA. Translation: BAA91539.1 . Different initiation.
AK124091 mRNA. Translation: BAC85769.1 . Frameshift.
AK126214 mRNA. Translation: BAC86489.1 .
CH236954 Genomic DNA. Translation: EAL23931.1 .
AB033054 mRNA. Translation: BAA86542.2 .
AL833233 mRNA. Translation: CAH10642.1 .
BC013957 mRNA. Translation: AAH13957.2 .
AJ303365 mRNA. Translation: CAC33887.1 .
CCDSi CCDS34791.1. [A0FGR8-2 ]
RefSeqi NP_065779.1. NM_020728.2. [A0FGR8-2 ]
UniGenei Hs.490795.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2DMG NMR - A 785-913 [» ]
4NPJ X-ray 2.10 A/B 363-660 [» ]
4NPK X-ray 2.55 A 363-660 [» ]
4P42 X-ray 2.44 A/B 191-662 [» ]
ProteinModelPortali A0FGR8.
SMRi A0FGR8. Positions 191-659, 756-919.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 121556. 9 interactions.
IntActi A0FGR8. 8 interactions.
MINTi MINT-4541681.

PTM databases

PhosphoSitei A0FGR8.

Proteomic databases

MaxQBi A0FGR8.
PaxDbi A0FGR8.
PRIDEi A0FGR8.

Protocols and materials databases

DNASUi 57488.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000251527 ; ENSP00000251527 ; ENSG00000117868 . [A0FGR8-2 ]
GeneIDi 57488.
KEGGi hsa:57488.
UCSCi uc003wob.1. human. [A0FGR8-2 ]
uc003woc.1. human. [A0FGR8-1 ]

Organism-specific databases

CTDi 57488.
GeneCardsi GC07M158523.
H-InvDB HIX0007266.
HGNCi HGNC:22211. ESYT2.
HPAi HPA002132.
neXtProti NX_A0FGR8.
PharmGKBi PA165617947.
HUGEi Search...
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG5038.
GeneTreei ENSGT00550000074417.
HOVERGENi HBG055795.
InParanoidi A0FGR8.
OMAi VDVGQQP.
OrthoDBi EOG7RNJZK.
PhylomeDBi A0FGR8.
TreeFami TF324255.

Miscellaneous databases

ChiTaRSi ESYT2. human.
EvolutionaryTracei A0FGR8.
GeneWikii FAM62B.
GenomeRNAii 57488.
NextBioi 63768.
PROi A0FGR8.

Gene expression databases

Bgeei A0FGR8.
CleanExi HS_FAM62B.
ExpressionAtlasi A0FGR8. baseline and differential.
Genevestigatori A0FGR8.

Family and domain databases

Gene3Di 2.60.40.150. 3 hits.
InterProi IPR000008. C2_dom.
[Graphical view ]
Pfami PF00168. C2. 3 hits.
[Graphical view ]
SMARTi SM00239. C2. 3 hits.
[Graphical view ]
SUPFAMi SSF49562. SSF49562. 3 hits.
PROSITEi PS50004. C2. 3 hits.
[Graphical view ]
ProtoNeti Search...

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), FUNCTION, SUBCELLULAR LOCATION, CALCIUM-DEPENDENT LIPID-BINDING, TISSUE SPECIFICITY.
  2. Shan Y.X., Yu L.
    Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  3. "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] (ISOFORMS 4 AND 5), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 511-921 (ISOFORMS 1/2), VARIANT GLY-638.
    Tissue: Esophageal carcinoma and Thymus.
  4. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "Prediction of the coding sequences of unidentified human genes. XV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.
    DNA Res. 6:337-345(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 79-921 (ISOFORM 1).
    Tissue: Brain.
  6. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 141-921.
    Tissue: Melanoma.
  8. "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] OF 454-921 (ISOFORM 6).
    Tissue: Colon.
  9. "Genomic analysis of synaptotagmin genes."
    Craxton M.A.
    Genomics 77:43-49(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 747-904.
    Tissue: Brain.
  10. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  11. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-758 AND SER-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-743; SER-755; SER-758 AND SER-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-691; SER-739; SER-748; SER-755; SER-758 AND SER-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  15. "Extended-synaptotagmin-2 mediates FGF receptor endocytosis and ERK activation in vivo."
    Jean S., Mikryukov A., Tremblay M.G., Baril J., Guillou F., Bellenfant S., Moss T.
    Dev. Cell 19:426-439(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH FGFR1 AND AP2B1, SUBCELLULAR LOCATION, FUNCTION.
  16. "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-743; SER-758 AND SER-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-758 AND SER-761, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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, DOMAIN, MUTAGENESIS OF 833-LYS--LYS-840, INTERACTION WITH ESYT1 AND ESYT3.
  20. "Solution structure of the third C2 domain of KIAA1228 protein."
    RIKEN structural genomics initiative (RSGI)
    Submitted (OCT-2006) to the PDB data bank
    Cited for: STRUCTURE BY NMR OF 222-350.
  21. "Structure of a lipid-bound extended synaptotagmin indicates a role in lipid transfer."
    Schauder C.M., Wu X., Saheki Y., Narayanaswamy P., Torta F., Wenk M.R., De Camilli P., Reinisch K.M.
    Nature 510:552-555(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.44 ANGSTROMS) OF 191-662 IN COMPLEX WITH PHOSPHATIDYLETHANOLAMINE, LIPID-BINDING, FUNCTION, DOMAIN, SUBUNIT.
  22. "Structure and Ca(2+)-binding properties of the tandem C(2) domains of E-Syt2."
    Xu J., Bacaj T., Zhou A., Tomchick D.R., Sudhof T.C., Rizo J.
    Structure 22:269-280(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 363-660 IN COMPLEX WITH CALCIUM, DOMAIN, CALCIUM BINDING, MUTAGENESIS OF ASP-401; ASP-413 AND ASP-466.

Entry informationi

Entry nameiESYT2_HUMAN
AccessioniPrimary (citable) accession number: A0FGR8
Secondary accession number(s): A4D229
, Q69YJ2, Q6UKI4, Q6ZTU0, Q6ZVU1, Q9BQS0, Q9NW47, Q9ULJ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: November 28, 2006
Last modified: October 29, 2014
This is version 83 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

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