Q86YS7 (C2CD5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
C2 domain-containing protein 5

Alternative name(s):
C2 domain-containing phosphoprotein of 138 kDa

Gene names

Name:	C2CD5
Synonyms:	CDP138, KIAA0528

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1000 AA.
Sequence status	Complete.
Protein existence	Evidence 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.15
Cofactor	Binds 2 calcium ions per subunit. The ions are bound to the C2 domains.
Subcellular location	Cytoplasmic vesicle membrane. Cytoplasm › cell cortex. Cell membrane. Cell projection › ruffle. Note: Dynamically associated with GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in response to insulin stimulation. Ref.15
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.15
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 process	Protein transport Transport
Cellular component	Cell membrane Cell projection Cytoplasm Cytoplasmic vesicle Membrane
Coding sequence diversity	Alternative splicing
Ligand	Calcium Lipid-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	insulin receptor signaling pathway via phosphatidylinositol 3-kinase cascade Inferred from sequence or structural similarity. Source: UniProtKB intracellular protein transmembrane transport Inferred from mutant phenotype Ref.15. 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.15. Source: UniProtKB positive regulation of vesicle fusion Inferred from mutant phenotype Ref.15. Source: UniProtKB protein localization to plasma membrane Inferred from electronic annotation. Source: Ensembl vesicle fusion Inferred from electronic annotation. Source: Ensembl
Cellular_component	cell cortex Inferred from direct assay Ref.15. Source: UniProtKB cytoplasmic vesicle membrane Inferred from direct assay Ref.15. Source: UniProtKB ruffle membrane Inferred from direct assay Ref.15. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from direct assay Ref.15. Source: UniProtKB calcium-dependent phospholipid binding Inferred from direct assay Ref.15. Source: UniProtKB
Complete GO annotation...

Alternative products

This entry describes 2 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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1000	1000	C2 domain-containing protein 5		PRO_0000247450
Regions
	Domain	1 – 90	90	C2
	Calcium binding	13 – 27	15	1; low affinity Ref.15
	Calcium binding	75 – 86	12	2; high affinity Ref.15
Amino acid modifications
	Modified residue	197	1	Phosphoserine; by PKB/AKT2 Ref.15
	Modified residue	200	1	Phosphoserine Ref.15
	Modified residue	293	1	Phosphoserine Ref.16
	Modified residue	295	1	Phosphoserine Ref.13 Ref.16
	Modified residue	317	1	Phosphothreonine Ref.11
	Modified residue	601	1	Phosphothreonine Ref.8
	Modified residue	643	1	Phosphoserine Ref.7 Ref.8 Ref.9 Ref.11 Ref.12
	Modified residue	659	1	Phosphoserine Ref.9 Ref.12
	Modified residue	852	1	Phosphoserine Ref.8 Ref.9 Ref.11 Ref.16
Natural variations
	Alternative sequence	268 – 316	49	IPFNE…SLTPK → SPLVHPPSHGCRSTHNSPIH TATGSRLTQNFSVSVPTLIY in isoform 2.		VSP_028255
	Alternative sequence	844 – 845	2	KA → KEHLESASSNSGIPAAQRAT SVDYSSFADRCSSWIELIKL KAQTIRRGSIKTT in isoform 2.		VSP_028256
Experimental info
	Mutagenesis	19	1	D → 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.15
	Mutagenesis	26	1	D → 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.15
	Mutagenesis	76	1	D → 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.15
	Mutagenesis	78	1	D → 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.15
	Mutagenesis	84	1	D → 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.15
	Mutagenesis	197	1	S → A: Inhibits insulin-stimulated AKT2-induced phosphorylation, SLC2A4/GLUT4 translocation to the cell surface and GSV-PM fusion. Ref.15
	Mutagenesis	200	1	S → A: Does not inhibit insulin-stimulated SLC2A4/GLUT4 translocation. Ref.15

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 1, 2003. Version 1. Checksum: 7C51961F54CBBACD	FASTA	1,000	110,447
	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
	Isoform 2 [UniParc]. Checksum: 23C91754C1A61236	FASTA	1,042	114,994
	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 PSKEMKESPL VHPPSHGCRS THNSPIHTAT GSRLTQNFSV 310 320 330 340 350 360 SVPTLIYTGM GSGSAGKEGG PFKALLRQQT QSALEQREFP FFTLTAFPPG FLVHVGGVVS 370 380 390 400 410 420 ARSVKLLDRI HNPDEPETRD AWWAEIRQEI KSHAKALGCH AVVGYSESTS ICEEVCILSA 430 440 450 460 470 480 SGTAAVLNPR FLQDGTVEGC LEQRLEENLP TRCGFCHIPY DELNMPFPAH LTYCYNCRKQ 490 500 510 520 530 540 KVPDVLFTTI DLPTDATVIG KGCLIQARLC RLKKKAQAEA NATAISNLLP FMEYEVHTQL 550 560 570 580 590 600 MNKLKLKGMN ALFGLRIQIT VGENMLMGLA SATGVYLAAL PTPGGIQIAG KTPNDGSYEQ 610 620 630 640 650 660 HISHMQKKIN DTIAKNKELY EINPPEISEE IIGSPIPEPR QRSRLLRSQS ESSDEVTELD 670 680 690 700 710 720 LSHGKKDAFV LEIDDTDAME DVHSLLTDVP PPSGFYSCNT EIMPGINNWT SEIQMFTSVR 730 740 750 760 770 780 VIRLSSLNLT NQALNKNFND LCENLLKSLY FKLRSMIPCC LCHVNFTVSL PEDELIQVTV 790 800 810 820 830 840 TAVAITFDKN QALQTTKTPV EKSLQRASTD NEELLQFPLE LCSDSLPSHP FPPAKEHLES 850 860 870 880 890 900 ASSNSGIPAA QRATSVDYSS FADRCSSWIE LIKLKAQTIR RGSIKTTMTV EKASPVGDGN 910 920 930 940 950 960 FRNRSAPPCA NSTVGVVKMT PLSFIPGAKI TKYLGIINMF FIRETTSLRE EGGVSGFLHA 970 980 990 1000 1010 1020 FIAEVFAMVR AHVAALGGNA VVSYIMKQCV FMENPNKNQA QCLINVSGDA VVFVRESDLE 1030 1040 VVSSQQPTTN CQSSCTEGEV TT

References

	« Hide 'large scale' referencesShow '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]	"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. , 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].
[4]	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.
[5]	"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.
[6]	"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.
[7]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[10]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]	"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, MASS SPECTROMETRY.
[12]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-295, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[14]	"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].
[15]	"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, MASS SEPCTROMETRY.
[16]	"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, MASS SPECTROMETRY.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AB011100 mRNA. Translation: BAA25454.3. Different initiation. 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.
IPI	IPI00465142. IPI00783895.
PIR	T00072.
RefSeq	NP_055617.1. NM_014802.1. XP_005253594.1. XM_005253537.1.
UniGene	Hs.271014.
3D structure databases
ProteinModelPortal	Q86YS7.
SMR	Q86YS7. Positions 3-125.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q86YS7. 2 interactions.
STRING	9606.ENSP00000334229.
PTM databases
PhosphoSite	Q86YS7.
Polymorphism databases
DMDM	74750574.
Proteomic databases
PaxDb	Q86YS7.
PRIDE	Q86YS7.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000333957; ENSP00000334229; ENSG00000111731. ENST00000396028; ENSP00000379345; ENSG00000111731.
GeneID	9847.
KEGG	hsa:9847.
UCSC	uc001rfq.3. human.
Organism-specific databases
CTD	9847.
GeneCards	GC12M022602.
HGNC	HGNC:29062. C2CD5.
HPA	HPA046194.
neXtProt	NX_Q86YS7.
PharmGKB	PA143485515.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG235531.
HOGENOM	HOG000006746.
HOVERGEN	HBG081824.
OrthoDB	EOG715Q38.
Gene expression databases
ArrayExpress	Q86YS7.
Bgee	Q86YS7.
CleanEx	HS_KIAA0528.
Genevestigator	Q86YS7.
Family and domain databases
InterPro	IPR000008. C2_dom. [Graphical view]
Pfam	PF00168. C2. 1 hit. [Graphical view]
SMART	SM00239. C2. 1 hit. [Graphical view]
SUPFAM	SSF49562. SSF49562. 1 hit.
PROSITE	PS50004. C2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	9847.
NextBio	37112.

Entry information

Entry name

C2CD5_HUMAN

Accession

Primary (citable) accession number: Q86YS7
Secondary accession number(s): O60280 , Q17RY7, Q7Z619, Q86SU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	June 1, 2003
Last modified:	December 11, 2013
This is version 87 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.