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Q86YS7 (C2CD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 94. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
C2 domain-containing protein 5
Alternative name(s):
C2 domain-containing phosphoprotein of 138 kDa
Gene names
Name:C2CD5
Synonyms:CDP138, KIAA0528
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1000 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Required for insulin-stimulated glucose transport and glucose transporter SLC2A4/GLUT4 translocation from intracellular glucose storage vesicle (GSV) to the plasma membrane (PM) in adipocytes. Binds phospholipid membranes in a calcium-dependent manner and is necessary for the optimal membrane fusion between SLC2A4/GLUT4 GSV and the PM. Ref.16

Cofactor

Binds 2 calcium ions per subunit. The ions are bound to the C2 domains.

Subcellular location

Cytoplasmic vesicle membrane. Cytoplasmcell cortex. Cell membrane. Cell projectionruffle. Note: Dynamically associated with GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in response to insulin stimulation. Ref.16

Domain

The C2 domain binds to calcium and membrane lipids.

Post-translational modification

Phosphorylated on Ser-197 by active myristoylated kinase AKT2; insulin-stimulated phosphorylation by AKT2 regulates SLC2A4/GLUT4 translocation into the plasma membrane. Ref.16

Sequence similarities

Contains 1 C2 domain.

Sequence caution

The sequence BAA25454.3 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
   Biological processProtein transport
Transport
   Cellular componentCell membrane
Cell projection
Cytoplasm
Cytoplasmic vesicle
Membrane
   Coding sequence diversityAlternative splicing
   LigandCalcium
Lipid-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to insulin stimulus

Inferred from direct assay Ref.16. Source: UniProtKB

insulin receptor signaling pathway via phosphatidylinositol 3-kinase

Inferred from sequence or structural similarity. Source: UniProtKB

intracellular protein transmembrane transport

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of glucose import in response to insulin stimulus

Inferred from electronic annotation. Source: Ensembl

positive regulation of glucose transport

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of protein targeting to membrane

Inferred from mutant phenotype Ref.16. Source: UniProtKB

positive regulation of vesicle fusion

Inferred from mutant phenotype Ref.16. Source: UniProtKB

protein localization to plasma membrane

Inferred from electronic annotation. Source: Ensembl

vesicle fusion

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentcell cortex

Inferred from direct assay Ref.16. Source: UniProtKB

cytoplasmic vesicle membrane

Inferred from direct assay Ref.16. Source: UniProtKB

plasma membrane

Inferred from direct assay Ref.16. Source: UniProtKB

ruffle membrane

Inferred from direct assay Ref.16. Source: UniProtKB

   Molecular_functioncalcium ion binding

Inferred from direct assay Ref.16. Source: UniProtKB

calcium-dependent phospholipid binding

Inferred from direct assay Ref.16. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q86YS7-1)

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: Q86YS7-2)

The sequence of this isoform differs from the canonical sequence as follows:
     268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
     844-845: KA → KEHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT
Note: No experimental confirmation available.
Isoform 3 (identifier: Q86YS7-3)

The sequence of this isoform differs from the canonical sequence as follows:
     844-845: KA → KEHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 10001000C2 domain-containing protein 5
PRO_0000247450

Regions

Domain1 – 9090C2
Calcium binding13 – 27151; low affinity Ref.16
Calcium binding75 – 86122; high affinity Ref.16

Amino acid modifications

Modified residue1971Phosphoserine; by PKB/AKT2 Ref.16
Modified residue2001Phosphoserine Ref.16
Modified residue2931Phosphoserine Ref.17
Modified residue2951Phosphoserine Ref.14 Ref.17
Modified residue3171Phosphothreonine Ref.12
Modified residue6011Phosphothreonine Ref.9
Modified residue6431Phosphoserine Ref.8 Ref.9 Ref.10 Ref.12 Ref.13
Modified residue6591Phosphoserine Ref.10 Ref.13
Modified residue8521Phosphoserine Ref.9 Ref.10 Ref.12 Ref.17

Natural variations

Alternative sequence268 – 31649IPFNE…SLTPK → SPLVHPPSHGCRSTHNSPIH TATGSRLTQNFSVSVPTLIY in isoform 2.
VSP_028255
Alternative sequence844 – 8452KA → KEHLESASSNSGIPAAQRAT SVDYSSFADRCSSWIELIKL KAQTIRRGSIKTT in isoform 2 and isoform 3.
VSP_028256

Experimental info

Mutagenesis191D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-26; A-76; A-78 and A-84. Ref.16
Mutagenesis261D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-76; A-78 and A-84. Ref.16
Mutagenesis761D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-78 and A-84. Ref.16
Mutagenesis781D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-76 and A-84. Ref.16
Mutagenesis841D → A: Reduces calcium-binding, phospholipid membrane-binding and insulin-stimulated SLC2A4/GLUT4 translocation; when associated with A-19; A-26; A-76 and A-78. Ref.16
Mutagenesis1971S → A: Inhibits insulin-stimulated AKT2-induced phosphorylation, SLC2A4/GLUT4 translocation to the cell surface and GSV-PM fusion. Ref.16
Mutagenesis2001S → A: Does not inhibit insulin-stimulated SLC2A4/GLUT4 translocation. Ref.16

Sequences

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

Last modified June 1, 2003. Version 1.
Checksum: 7C51961F54CBBACD

FASTA1,000110,447
        10         20         30         40         50         60 
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ WNSEWFKFEV 

        70         80         90        100        110        120 
DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE AATVISGWFP IYDTIHGIRG 

       130        140        150        160        170        180 
EINVVVKVDL FNDLNRFRQS SCGVKFFCTT SIPKCYRAVI IHGFVEELVV NEDPEYQWID 

       190        200        210        220        230        240 
RIRTPRASNE ARQRLISLMS GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG 

       250        260        270        280        290        300 
TACTLDKLSS PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY 

       310        320        330        340        350        360 
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF FTLTAFPPGF 

       370        380        390        400        410        420 
LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK SHAKALGCHA VVGYSESTSI 

       430        440        450        460        470        480 
CEEVCILSAS GTAAVLNPRF LQDGTVEGCL EQRLEENLPT RCGFCHIPYD ELNMPFPAHL 

       490        500        510        520        530        540 
TYCYNCRKQK VPDVLFTTID LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF 

       550        560        570        580        590        600 
MEYEVHTQLM NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK 

       610        620        630        640        650        660 
TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ RSRLLRSQSE 

       670        680        690        700        710        720 
SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP PSGFYSCNTE IMPGINNWTS 

       730        740        750        760        770        780 
EIQMFTSVRV IRLSSLNLTN QALNKNFNDL CENLLKSLYF KLRSMIPCCL CHVNFTVSLP 

       790        800        810        820        830        840 
EDELIQVTVT AVAITFDKNQ ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF 

       850        860        870        880        890        900 
PPAKAMTVEK ASPVGDGNFR NRSAPPCANS TVGVVKMTPL SFIPGAKITK YLGIINMFFI 

       910        920        930        940        950        960 
RETTSLREEG GVSGFLHAFI AEVFAMVRAH VAALGGNAVV SYIMKQCVFM ENPNKNQAQC 

       970        980        990       1000 
LINVSGDAVV FVRESDLEVV SSQQPTTNCQ SSCTEGEVTT 

« Hide

Isoform 2 [UniParc].

Checksum: 23C91754C1A61236
Show »

FASTA1,042114,994
Isoform 3 [UniParc].

Checksum: 2C4D059D41F01BE8
Show »

FASTA1,051116,027

References

« Hide 'large scale' references
[1]"Prediction of the coding sequences of unidentified human genes. IX. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
DNA Res. 5:31-39(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[2]Ohara O., Nagase T., Ishikawa K.
Submitted (JAN-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[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] (ISOFORM 3).
[4]"The finished DNA sequence of human chromosome 12."
Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R. expand/collapse author list , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Guo J.H., Yu L.
Submitted (OCT-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Tissue: Brain.
[6]"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] (ISOFORMS 1 AND 2).
Tissue: Cerebellum and Lung carcinoma.
[7]"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.
[8]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-643, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"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 THR-601; SER-643 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"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-643; SER-659 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-317; SER-643 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[13]"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-643 AND SER-659, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[14]"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-295, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[15]"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].
[16]"C2 domain-containing phosphoprotein CDP138 regulates GLUT4 insertion into the plasma membrane."
Xie X., Gong Z., Mansuy-Aubert V., Zhou Q.L., Tatulian S.A., Sehrt D., Gnad F., Brill L.M., Motamedchaboki K., Chen Y., Czech M.P., Mann M., Kruger M., Jiang Z.Y.
Cell Metab. 14:378-389(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, PHOSPHORYLATION AT SER-197 AND SER-200, INTERACTION WITH PHOSPHOLIPIDS, CALCIUM-BINDING, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-19; ASP-26; ASP-76; ASP-78; ASP-84; SER-197 AND SER-200, IDENTIFICATION BY MASS SPECTROMETRY.
[17]"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-293; SER-295 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB011100 mRNA. Translation: BAA25454.3. Different initiation.
AK299353 mRNA. Translation: BAG61349.1.
AC053513 Genomic DNA. No translation available.
AY166851 mRNA. Translation: AAO17290.1.
BC042498 mRNA. Translation: AAH42498.2.
BC053885 mRNA. Translation: AAH53885.1.
BC117143 mRNA. Translation: AAI17144.1.
CCDSCCDS31758.1. [Q86YS7-1]
CCDS66338.1. [Q86YS7-2]
PIRT00072.
RefSeqNP_001273102.1. NM_001286173.1.
NP_001273103.1. NM_001286174.1.
NP_001273104.1. NM_001286175.1.
NP_001273105.1. NM_001286176.1.
NP_001273106.1. NM_001286177.1. [Q86YS7-2]
NP_055617.1. NM_014802.2. [Q86YS7-1]
UniGeneHs.271014.

3D structure databases

ProteinModelPortalQ86YS7.
SMRQ86YS7. Positions 3-128.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115182. 6 interactions.
IntActQ86YS7. 2 interactions.
STRING9606.ENSP00000334229.

PTM databases

PhosphoSiteQ86YS7.

Polymorphism databases

DMDM74750574.

Proteomic databases

MaxQBQ86YS7.
PaxDbQ86YS7.
PRIDEQ86YS7.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000333957; ENSP00000334229; ENSG00000111731. [Q86YS7-1]
ENST00000396028; ENSP00000379345; ENSG00000111731. [Q86YS7-2]
ENST00000446597; ENSP00000388756; ENSG00000111731.
GeneID9847.
KEGGhsa:9847.
UCSCuc001rfq.3. human. [Q86YS7-1]
uc001rfr.3. human. [Q86YS7-2]

Organism-specific databases

CTD9847.
GeneCardsGC12M022602.
HGNCHGNC:29062. C2CD5.
HPAHPA046194.
neXtProtNX_Q86YS7.
PharmGKBPA143485515.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG235531.
HOGENOMHOG000006746.
HOVERGENHBG081824.
OrthoDBEOG715Q38.
PhylomeDBQ86YS7.
TreeFamTF323431.

Gene expression databases

ArrayExpressQ86YS7.
BgeeQ86YS7.
CleanExHS_KIAA0528.
GenevestigatorQ86YS7.

Family and domain databases

Gene3D2.60.40.150. 1 hit.
InterProIPR000008. C2_dom.
[Graphical view]
PfamPF00168. C2. 1 hit.
[Graphical view]
SMARTSM00239. C2. 1 hit.
[Graphical view]
SUPFAMSSF49562. SSF49562. 1 hit.
PROSITEPS50004. C2. 1 hit.
[Graphical view]
ProtoNetSearch...

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GenomeRNAi9847.
NextBio35474430.

Entry information

Entry nameC2CD5_HUMAN
AccessionPrimary (citable) accession number: Q86YS7
Secondary accession number(s): B4DRN7 expand/collapse secondary AC list , O60280, Q17RY7, Q7Z619, Q86SU3
Entry history
Integrated into UniProtKB/Swiss-Prot: July 25, 2006
Last sequence update: June 1, 2003
Last modified: July 9, 2014
This is version 94 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

Human chromosome 12

Human chromosome 12: entries, gene names and cross-references to MIM