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A0FGR8

- ESYT2_HUMAN

UniProt

A0FGR8 - ESYT2_HUMAN

Protein

Extended synaptotagmin-2

Gene

ESYT2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 82 (01 Oct 2014)
      Sequence version 1 (28 Nov 2006)
      Previous versions | rss
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    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. phosphatidylcholine binding Source: UniProtKB
    4. phosphatidylethanolamine binding Source: UniProtKB
    5. phosphatidylinositol binding Source: UniProtKB
    6. protein binding Source: IntAct

    GO - Biological processi

    1. endocytosis Source: UniProtKB-KW
    2. lipid transport Source: UniProtKB-KW

    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.

    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

    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. 2 Publications
    Mutagenesisi413 – 4131D → A: Abolishes calcium binding; when associated with A-401. 2 Publications
    Mutagenesisi413 – 4131D → N: Strongly reduces calcium binding. 2 Publications
    Mutagenesisi466 – 4661D → A: Impairs binding of the third calcium ion, but has no effect on the binding of the other two calcium ions. 2 Publications
    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

    ArrayExpressiA0FGR8.
    BgeeiA0FGR8.
    CleanExiHS_FAM62B.
    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. 8 interactions.
    IntActiA0FGR8. 8 interactions.
    MINTiMINT-4541681.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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 363-659, 756-919.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiA0FGR8.

    Topological domain

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

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei104 – 12421HelicalSequence AnalysisAdd
    BLAST
    Transmembranei128 – 14821HelicalSequence AnalysisAdd
    BLAST

    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.
    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

    MTANRDAALS SHRHPGCAQR PRTPTFASSS QRRSAFGFDD GNFPGLGERS    50
    HAPGSRLGAR RRAKTARGLR GHRQRGAGAG LSRPGSARAP SPPRPGGPEN 100
    PGGVLSVELP GLLAQLARSF ALLLPVYALG YLGLSFSWVL LALALLAWCR 150
    RSRGLKALRL CRALALLEDE ERVVRLGVRA CDLPAWVHFP DTERAEWLNK 200
    TVKHMWPFIC QFIEKLFRET IEPAVRGANT HLSTFSFTKV DVGQQPLRIN 250
    GVKVYTENVD KRQIILDLQI SFVGNCEIDL EIKRYFCRAG VKSIQIHGTM 300
    RVILEPLIGD MPLVGALSIF FLRKPLLEIN WTGLTNLLDV PGLNGLSDTI 350
    ILDIISNYLV LPNRITVPLV SEVQIAQLRF PVPKGVLRIH FIEAQDLQGK 400
    DTYLKGLVKG KSDPYGIIRV GNQIFQSRVI KENLSPKWNE VYEALVYEHP 450
    GQELEIELFD EDPDKDDFLG SLMIDLIEVE KERLLDEWFT LDEVPKGKLH 500
    LRLEWLTLMP NASNLDKVLT DIKADKDQAN DGLSSALLIL YLDSARNLPS 550
    GKKISSNPNP VVQMSVGHKA QESKIRYKTN EPVWEENFTF FIHNPKRQDL 600
    EVEVRDEQHQ CSLGNLKVPL SQLLTSEDMT VSQRFQLSNS GPNSTIKMKI 650
    ALRVLHLEKR ERPPDHQHSA QVKRPSVSKE GRKTSIKSHM SGSPGPGGSN 700
    TAPSTPVIGG SDKPGMEEKA QPPEAGPQGL HDLGRSSSSL LASPGHISVK 750
    EPTPSIASDI SLPIATQELR QRLRQLENGT TLGQSPLGQI QLTIRHSSQR 800
    NKLIVVVHAC RNLIAFSEDG SDPYVRMYLL PDKRRSGRRK THVSKKTLNP 850
    VFDQSFDFSV SLPEVQRRTL DVAVKNSGGF LSKDKGLLGK VLVALASEEL 900
    AKGWTQWYDL TEDGTRPQAM T 921
    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 BAC85769.1 differs from that shown. Reason: Frameshift at position 800.
    The sequence BAA91539.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    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:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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:
    PDBe
    RCSB PDB
    PDBj
    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 363-659, 756-919.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 121556. 8 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.
    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

    ArrayExpressi A0FGR8.
    Bgeei A0FGR8.
    CleanExi HS_FAM62B.
    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

    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 0:0-0(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 1, 2014
    This is version 82 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

    Dasty 3