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A0FGR8 (ESYT2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Extended synaptotagmin-2

Short name=E-Syt2
Alternative name(s):
Chr2Syt
Gene names
Name:ESYT2
Synonyms:FAM62B, KIAA1228
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length921 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.1 Ref.15 Ref.19 Ref.21

Subunit structure

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. Ref.15 Ref.19 Ref.21

Subcellular location

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. Ref.1 Ref.15 Ref.19

Tissue specificity

Widely expressed with high level in cerebellum. Ref.1

Domain

Anchored to the endoplasmic reticulum membrane by a transmembrane hairpin structure; both N-terminus and C-terminus are cytoplasmic (Ref.19). Ref.19 Ref.21 Ref.22

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 (Ref.22). The third C2 domain mediates interaction with membranes enriched in phosphatidylinositol 4,5-bisphosphate and is required for location at the cell membrane (Ref.19). Ref.19 Ref.21 Ref.22

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 (Ref.21). Ref.19 Ref.21 Ref.22

Sequence similarities

Belongs to the extended synaptotagmin family.

Contains 3 C2 domains.

Sequence caution

The sequence BAA91539.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence BAC85769.1 differs from that shown. Reason: Frameshift at position 800.

Binary interactions

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: A0FGR8-1)

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.
Isoform 2 (identifier: A0FGR8-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-97: MTANRDAALS...RAPSPPRPGG → MTPPSRAEAG...GAGGAGGRAA
Note: No experimental confirmation available.
Isoform 4 (identifier: A0FGR8-4)

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.
Isoform 5 (identifier: A0FGR8-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-593: Missing.
     594-603: NPKRQDLEVE → MPVLPPCVLQ
Note: No experimental confirmation available.
Isoform 6 (identifier: A0FGR8-6)

The sequence of this isoform differs from the canonical sequence as follows:
     550-550: S → SNPLEFNPDVLKKTAVQRALKS
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 921921Extended synaptotagmin-2
PRO_0000278258

Regions

Topological domain1 – 103103Cytoplasmic Potential
Transmembrane104 – 12421Helical; Potential
Topological domain125 – 1273Lumenal Potential
Transmembrane128 – 14821Helical; Potential
Topological domain149 – 921773Cytoplasmic Potential
Domain372 – 473102C2 1
Domain523 – 61795C2 2
Domain788 – 892105C2 3
Region195 – 370176Glycerophospholipid-binding barrel-like domain
Region833 – 8408Required for phosphatidylinositol 4,5-bisphosphate-dependent location at the cell membrane
Compositional bias736 – 7394Poly-Ser

Sites

Metal binding4001Calcium 1; via carbonyl oxygen
Metal binding4011Calcium 1
Metal binding4011Calcium 2
Metal binding4131Calcium 2
Metal binding4601Calcium 1
Metal binding4601Calcium 2
Metal binding4611Calcium 2; via carbonyl oxygen
Metal binding4621Calcium 1
Metal binding4621Calcium 2
Metal binding4621Calcium 3; via carbonyl oxygen
Metal binding4641Calcium 3; via carbonyl oxygen
Metal binding4661Calcium 3
Metal binding4671Calcium 1

Amino acid modifications

Modified residue6911Phosphoserine Ref.14
Modified residue7381Phosphoserine By similarity
Modified residue7391Phosphoserine Ref.14
Modified residue7431Phosphoserine Ref.11 Ref.12 Ref.13 Ref.16
Modified residue7481Phosphoserine Ref.14
Modified residue7551Phosphoserine Ref.13 Ref.14
Modified residue7581Phosphoserine Ref.12 Ref.13 Ref.14 Ref.16 Ref.18
Modified residue7611Phosphoserine Ref.12 Ref.13 Ref.14 Ref.16 Ref.18

Natural variations

Alternative sequence1 – 593593Missing in isoform 5.
VSP_023236
Alternative sequence1 – 204204Missing in isoform 4.
VSP_023238
Alternative sequence1 – 9797MTANR…PRPGG → MTPPSRAEAGVRRSRVPSEG RWRGAEPPGISASTQPASAG RAARHCGAMSGARGEGPEAG AGGAGGRAA in isoform 2.
VSP_023239
Alternative sequence5501S → SNPLEFNPDVLKKTAVQRAL KS in isoform 6.
VSP_038324
Alternative sequence594 – 60310NPKRQDLEVE → MPVLPPCVLQ in isoform 5.
VSP_023240
Alternative sequence706 – 73126PVIGG…PQGLH → SQSRSRPPASPRTSRCPSPP RSCGKG in isoform 4.
VSP_023241
Alternative sequence732 – 921190Missing in isoform 4.
VSP_023242
Natural variant2101C → S.
Corresponds to variant rs13233513 [ dbSNP | Ensembl ].
VAR_030725
Natural variant6381S → G. Ref.3
Corresponds to variant rs2305473 [ dbSNP | Ensembl ].
VAR_030726

Experimental info

Mutagenesis4011D → A: Abolishes calcium binding; when associated with A-413. Ref.22
Mutagenesis4131D → A: Abolishes calcium binding; when associated with A-401. Ref.22
Mutagenesis4131D → N: Strongly reduces calcium binding. Ref.22
Mutagenesis4661D → A: Impairs binding of the third calcium ion, but has no effect on the binding of the other two calcium ions. Ref.22
Mutagenesis833 – 8408KRRSGRRK → AAASGAAA: Abolishes location at the cell membrane. Ref.19
Sequence conflict1411L → V in CAH10642. Ref.7
Sequence conflict6121S → P in BAC85769. Ref.3
Sequence conflict6151N → S in BAC86489. Ref.3
Sequence conflict7951R → Q in BAC85769. Ref.3

Secondary structure

................................................................... 921
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 28, 2006. Version 1.
Checksum: D57F1BD9BB0A0C8A

FASTA921102,357
        10         20         30         40         50         60 
MTANRDAALS SHRHPGCAQR PRTPTFASSS QRRSAFGFDD GNFPGLGERS HAPGSRLGAR 

        70         80         90        100        110        120 
RRAKTARGLR GHRQRGAGAG LSRPGSARAP SPPRPGGPEN PGGVLSVELP GLLAQLARSF 

       130        140        150        160        170        180 
ALLLPVYALG YLGLSFSWVL LALALLAWCR RSRGLKALRL CRALALLEDE ERVVRLGVRA 

       190        200        210        220        230        240 
CDLPAWVHFP DTERAEWLNK TVKHMWPFIC QFIEKLFRET IEPAVRGANT HLSTFSFTKV 

       250        260        270        280        290        300 
DVGQQPLRIN GVKVYTENVD KRQIILDLQI SFVGNCEIDL EIKRYFCRAG VKSIQIHGTM 

       310        320        330        340        350        360 
RVILEPLIGD MPLVGALSIF FLRKPLLEIN WTGLTNLLDV PGLNGLSDTI ILDIISNYLV 

       370        380        390        400        410        420 
LPNRITVPLV SEVQIAQLRF PVPKGVLRIH FIEAQDLQGK DTYLKGLVKG KSDPYGIIRV 

       430        440        450        460        470        480 
GNQIFQSRVI KENLSPKWNE VYEALVYEHP GQELEIELFD EDPDKDDFLG SLMIDLIEVE 

       490        500        510        520        530        540 
KERLLDEWFT LDEVPKGKLH LRLEWLTLMP NASNLDKVLT DIKADKDQAN DGLSSALLIL 

       550        560        570        580        590        600 
YLDSARNLPS GKKISSNPNP VVQMSVGHKA QESKIRYKTN EPVWEENFTF FIHNPKRQDL 

       610        620        630        640        650        660 
EVEVRDEQHQ CSLGNLKVPL SQLLTSEDMT VSQRFQLSNS GPNSTIKMKI ALRVLHLEKR 

       670        680        690        700        710        720 
ERPPDHQHSA QVKRPSVSKE GRKTSIKSHM SGSPGPGGSN TAPSTPVIGG SDKPGMEEKA 

       730        740        750        760        770        780 
QPPEAGPQGL HDLGRSSSSL LASPGHISVK EPTPSIASDI SLPIATQELR QRLRQLENGT 

       790        800        810        820        830        840 
TLGQSPLGQI QLTIRHSSQR NKLIVVVHAC RNLIAFSEDG SDPYVRMYLL PDKRRSGRRK 

       850        860        870        880        890        900 
THVSKKTLNP VFDQSFDFSV SLPEVQRRTL DVAVKNSGGF LSKDKGLLGK VLVALASEEL 

       910        920 
AKGWTQWYDL TEDGTRPQAM T 

« Hide

Isoform 2 [UniParc].

Checksum: 9C059B137A2F1EFB
Show »

FASTA89398,902
Isoform 4 [UniParc].

Checksum: E4257349511C9C28
Show »

FASTA52759,403
Isoform 5 [UniParc].

Checksum: EF531CFF2A35D17C
Show »

FASTA32835,846
Isoform 6 [UniParc].

Checksum: 207D6C010DB58248
Show »

FASTA942104,708

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS34791.1. [A0FGR8-2]
RefSeqNP_065779.1. NM_020728.2. [A0FGR8-2]
UniGeneHs.490795.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DMGNMR-A785-913[»]
4NPJX-ray2.10A/B363-660[»]
4NPKX-ray2.55A363-660[»]
4P42X-ray2.44A/B191-662[»]
ProteinModelPortalA0FGR8.
SMRA0FGR8. Positions 363-659, 756-919.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid121556. 9 interactions.
IntActA0FGR8. 8 interactions.
MINTMINT-4541681.

PTM databases

PhosphoSiteA0FGR8.

Proteomic databases

MaxQBA0FGR8.
PaxDbA0FGR8.
PRIDEA0FGR8.

Protocols and materials databases

DNASU57488.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000251527; ENSP00000251527; ENSG00000117868. [A0FGR8-2]
GeneID57488.
KEGGhsa:57488.
UCSCuc003wob.1. human. [A0FGR8-2]
uc003woc.1. human. [A0FGR8-1]

Organism-specific databases

CTD57488.
GeneCardsGC07M158523.
H-InvDBHIX0007266.
HGNCHGNC:22211. ESYT2.
HPAHPA002132.
neXtProtNX_A0FGR8.
PharmGKBPA165617947.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5038.
HOVERGENHBG055795.
InParanoidA0FGR8.
OMAVDVGQQP.
OrthoDBEOG7RNJZK.
PhylomeDBA0FGR8.
TreeFamTF324255.

Gene expression databases

ArrayExpressA0FGR8.
BgeeA0FGR8.
CleanExHS_FAM62B.
GenevestigatorA0FGR8.

Family and domain databases

Gene3D2.60.40.150. 3 hits.
InterProIPR000008. C2_dom.
[Graphical view]
PfamPF00168. C2. 3 hits.
[Graphical view]
SMARTSM00239. C2. 3 hits.
[Graphical view]
SUPFAMSSF49562. SSF49562. 3 hits.
PROSITEPS50004. C2. 3 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSESYT2. human.
EvolutionaryTraceA0FGR8.
GeneWikiFAM62B.
GenomeRNAi57488.
NextBio63768.
PROA0FGR8.

Entry information

Entry nameESYT2_HUMAN
AccessionPrimary (citable) accession number: A0FGR8
Secondary accession number(s): A4D229 expand/collapse secondary AC list , Q69YJ2, Q6UKI4, Q6ZTU0, Q6ZVU1, Q9BQS0, Q9NW47, Q9ULJ2
Entry history
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: November 28, 2006
Last modified: July 9, 2014
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM