C2CD5

Functionⁱ

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.1 Publication

Cofactorⁱ

Ca²⁺Note: Binds 2 calcium ions per subunit. The ions are bound to the C2 domains.

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Calcium bindingⁱ	13 – 27	15	1; low affinity			Add BLAST
Calcium bindingⁱ	75 – 86	12	2; high affinity			Add BLAST

GO - Molecular functionⁱ

calcium-dependent phospholipid binding
Source: UniProtKB
Inferred from direct assayⁱ
- 21907143
calcium ion binding
Source: UniProtKB
Inferred from direct assayⁱ
- 21907143

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.

Reactomeⁱ

R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: C2 domain-containing protein 5 Alternative name(s): C2 domain-containing phosphoprotein of 138 kDa
Gene namesⁱ	Name:C2CD5 Synonyms:CDP138, KIAA0528
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 12

Organism-specific databases

HGNCⁱ	HGNC:29062. C2CD5.

HGNCⁱ

HGNC:29062. C2CD5.

Subcellular locationⁱ

Cytoplasmic vesicle membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.
Cytoplasm › cell cortex
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.
Cell membrane
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.
Cell projection › ruffle
1 Publication
Manual assertion based on experiment inⁱ
- Ref.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.

Note:

Dynamically associated with GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in response to insulin stimulation.

GO - Cellular componentⁱ

cell cortex
Source: UniProtKB
Inferred from direct assayⁱ
- 21907143
cytoplasm Source: HPA
cytoplasmic vesicle membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 21907143
microtubule organizing center Source: HPA
plasma membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 21907143
ruffle membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 21907143

Complete GO annotation...

Keywords - Cellular componentⁱ

Cell membrane, Cell projection, Cytoplasm, Cytoplasmic vesicle, Membrane

Pathology & Biotechⁱ

Mutagenesis

Feature key	Position(s)	Length	Description
Mutagenesisⁱ	19 – 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. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Mutagenesisⁱ	26 – 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. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Mutagenesisⁱ	76 – 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. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Mutagenesisⁱ	78 – 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. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Mutagenesisⁱ	84 – 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. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Mutagenesisⁱ	197 – 197	1	S → A: Inhibits insulin-stimulated AKT2-induced phosphorylation, SLC2A4/GLUT4 translocation to the cell surface and GSV-PM fusion. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Mutagenesisⁱ	200 – 200	1	S → A: Does not inhibit insulin-stimulated SLC2A4/GLUT4 translocation. 1 Publication Manual assertion based on experiment inⁱ Ref.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.

Organism-specific databases

PharmGKBⁱ	PA143485515.

PharmGKBⁱ

PA143485515.

Polymorphism and mutation databases

DMDMⁱ	74750574.

DMDMⁱ

74750574.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 1000	1000	C2 domain-containing protein 5		PRO_0000247450	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	197 – 197	1	Phosphoserine; by PKB/AKT21 Publication Manual assertion based on experiment inⁱ Ref.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.
Modified residueⁱ	200 – 200	1	Phosphoserine1 Publication Manual assertion based on experiment inⁱ Ref.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.
Modified residueⁱ	260 – 260	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.18 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-295; SER-305; SER-323; SER-659; SER-662; THR-807 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	293 – 293	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	295 – 295	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.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]. Ref.18 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-295; SER-305; SER-323; SER-659; SER-662; THR-807 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	304 – 304	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q7TPS5 (C2CD5_MOUSE)
Modified residueⁱ	305 – 305	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.18 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-295; SER-305; SER-323; SER-659; SER-662; THR-807 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	306 – 306	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q7TPS5 (C2CD5_MOUSE)
Modified residueⁱ	317 – 317	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	323 – 323	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.18 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-295; SER-305; SER-323; SER-659; SER-662; THR-807 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	601 – 601	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	643 – 643	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.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]. Ref.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]. Ref.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]. Ref.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].
Modified residueⁱ	657 – 657	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q7TPS5 (C2CD5_MOUSE)
Modified residueⁱ	659 – 659	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.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]. Ref.18 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-295; SER-305; SER-323; SER-659; SER-662; THR-807 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	661 – 661	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q7TPS5 (C2CD5_MOUSE)
Modified residueⁱ	662 – 662	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.18 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-295; SER-305; SER-323; SER-659; SER-662; THR-807 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	666 – 666	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.19 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome." Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H. J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-666 AND SER-671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	671 – 671	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.19 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome." Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H. J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-666 AND SER-671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	807 – 807	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.18 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-295; SER-305; SER-323; SER-659; SER-662; THR-807 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	817 – 817	1	PhosphoserineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q7TPS5 (C2CD5_MOUSE)
Modified residueⁱ	852 – 852	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.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]. Ref.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]. Ref.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]. Ref.18 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-260; SER-295; SER-305; SER-323; SER-659; SER-662; THR-807 AND SER-852, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Post-translational modificationⁱ

Phosphorylated on Ser-197 by active myristoylated kinase AKT2; insulin-stimulated phosphorylation by AKT2 regulates SLC2A4/GLUT4 translocation into the plasma membrane.1 Publication

Keywords - PTMⁱ

Phosphoprotein

Proteomic databases

EPDⁱ	Q86YS7.
MaxQBⁱ	Q86YS7.
PaxDbⁱ	Q86YS7.
PeptideAtlasⁱ	Q86YS7.
PRIDEⁱ	Q86YS7.

PTM databases

iPTMnetⁱ	Q86YS7.
PhosphoSiteⁱ	Q86YS7.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000111731.
CleanExⁱ	HS_KIAA0528.
ExpressionAtlasⁱ	Q86YS7. baseline and differential.
Genevisibleⁱ	Q86YS7. HS.

Organism-specific databases

HPAⁱ	HPA046194.

Interactionⁱ

Protein-protein interaction databases

BioGridⁱ	115182. 32 interactions.
IntActⁱ	Q86YS7. 19 interactions.
STRINGⁱ	9606.ENSP00000334229.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q86YS7.
SMRⁱ	Q86YS7. Positions 3-143.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Domainⁱ	1 – 90	90	C2PROSITE-ProRule annotation Manual assertion according to rulesⁱ PROSITE-ProRule:PRU00041			Add BLAST

Domainⁱ

The C2 domain binds to calcium and membrane lipids.

Sequence similaritiesⁱ

Contains 1 C2 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGⁱ	KOG1031. Eukaryota. ENOG410XQDE. LUCA.
GeneTreeⁱ	ENSGT00390000000212.
HOGENOMⁱ	HOG000006746.
HOVERGENⁱ	HBG081824.
InParanoidⁱ	Q86YS7.
OMAⁱ	IGERMIA.
OrthoDBⁱ	EOG091G0FX6.
PhylomeDBⁱ	Q86YS7.
TreeFamⁱ	TF323431.

Family and domain databases

Gene3Dⁱ	2.60.40.150. 1 hit.
InterProⁱ	IPR000008. C2_dom. [Graphical view]
Pfamⁱ	PF00168. C2. 1 hit. [Graphical view]
SMARTⁱ	SM00239. C2. 1 hit. [Graphical view]
SUPFAMⁱ	SSF49562. SSF49562. 1 hit.
PROSITEⁱ	PS50004. C2. 1 hit. [Graphical view]

Sequences (5)ⁱ

Sequence statusⁱ: Complete.

This entry describes 5 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q86YS7-1) [UniParc]FASTA Add to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ 
        60         70         80         90        100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE 
       110        120        130        140        150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT 
       160        170        180        190        200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS 
       210        220        230        240        250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS 
       260        270        280        290        300
PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY 
       310        320        330        340        350
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF 
       360        370        380        390        400
FTLTAFPPGF LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK 
       410        420        430        440        450
SHAKALGCHA VVGYSESTSI CEEVCILSAS GTAAVLNPRF LQDGTVEGCL 
       460        470        480        490        500
EQRLEENLPT RCGFCHIPYD ELNMPFPAHL TYCYNCRKQK VPDVLFTTID 
       510        520        530        540        550
LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF MEYEVHTQLM 
       560        570        580        590        600
NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK 
       610        620        630        640        650
TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ 
       660        670        680        690        700
RSRLLRSQSE SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP 
       710        720        730        740        750
PSGFYSCNTE IMPGINNWTS EIQMFTSVRV IRLSSLNLTN QALNKNFNDL 
       760        770        780        790        800
CENLLKSLYF KLRSMIPCCL CHVNFTVSLP EDELIQVTVT AVAITFDKNQ 
       810        820        830        840        850
ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF PPAKAMTVEK 
       860        870        880        890        900
ASPVGDGNFR NRSAPPCANS TVGVVKMTPL SFIPGAKITK YLGIINMFFI 
       910        920        930        940        950
RETTSLREEG GVSGFLHAFI AEVFAMVRAH VAALGGNAVV SYIMKQCVFM 
       960        970        980        990       1000
ENPNKNQAQC LINVSGDAVV FVRESDLEVV SSQQPTTNCQ SSCTEGEVTT

Length:1,000

Mass (Da):110,447

Last modified:June 1, 2003 - v1

Checksum:ⁱ7C51961F54CBBACD

GO

Isoform 2 (identifier: Q86YS7-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT

« Hide

        10         20         30         40         50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ 
        60         70         80         90        100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE 
       110        120        130        140        150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT 
       160        170        180        190        200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS 
       210        220        230        240        250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS 
       260        270        280        290        300
PAAFLPACNS PSKEMKESPL VHPPSHGCRS THNSPIHTAT GSRLTQNFSV 
       310        320        330        340        350
SVPTLIYTGM GSGSAGKEGG PFKALLRQQT QSALEQREFP FFTLTAFPPG 
       360        370        380        390        400
FLVHVGGVVS ARSVKLLDRI HNPDEPETRD AWWAEIRQEI KSHAKALGCH 
       410        420        430        440        450
AVVGYSESTS ICEEVCILSA SGTAAVLNPR FLQDGTVEGC LEQRLEENLP 
       460        470        480        490        500
TRCGFCHIPY DELNMPFPAH LTYCYNCRKQ KVPDVLFTTI DLPTDATVIG 
       510        520        530        540        550
KGCLIQARLC RLKKKAQAEA NATAISNLLP FMEYEVHTQL MNKLKLKGMN 
       560        570        580        590        600
ALFGLRIQIT VGENMLMGLA SATGVYLAAL PTPGGIQIAG KTPNDGSYEQ 
       610        620        630        640        650
HISHMQKKIN DTIAKNKELY EINPPEISEE IIGSPIPEPR QRSRLLRSQS 
       660        670        680        690        700
ESSDEVTELD LSHGKKDAFV LEIDDTDAME DVHSLLTDVP PPSGFYSCNT 
       710        720        730        740        750
EIMPGINNWT SEIQMFTSVR VIRLSSLNLT NQALNKNFND LCENLLKSLY 
       760        770        780        790        800
FKLRSMIPCC LCHVNFTVSL PEDELIQVTV TAVAITFDKN QALQTTKTPV 
       810        820        830        840        850
EKSLQRASTD NEELLQFPLE LCSDSLPSHP FPPAKEHLES ASSNSGIPAA 
       860        870        880        890        900
QRATSVDYSS FADRCSSWIE LIKLKAQTIR RGSIKTTMTV EKASPVGDGN 
       910        920        930        940        950
FRNRSAPPCA NSTVGVVKMT PLSFIPGAKI TKYLGIINMF FIRETTSLRE 
       960        970        980        990       1000
EGGVSGFLHA FIAEVFAMVR AHVAALGGNA VVSYIMKQCV FMENPNKNQA 
      1010       1020       1030       1040 
QCLINVSGDA VVFVRESDLE VVSSQQPTTN CQSSCTEGEV TT

Note: No experimental confirmation available.

Show »

Length:1,042

Mass (Da):114,994

Checksum:ⁱ23C91754C1A61236

GO

Isoform 3 (identifier: Q86YS7-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT

« Hide

        10         20         30         40         50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ 
        60         70         80         90        100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE 
       110        120        130        140        150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT 
       160        170        180        190        200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS 
       210        220        230        240        250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS 
       260        270        280        290        300
PAAFLPACNS PSKEMKEIPF NEDPNPNTHS SGPSTPLKNQ TYSFSPSKSY 
       310        320        330        340        350
SRQSSSSDTD LSLTPKTGMG SGSAGKEGGP FKALLRQQTQ SALEQREFPF 
       360        370        380        390        400
FTLTAFPPGF LVHVGGVVSA RSVKLLDRIH NPDEPETRDA WWAEIRQEIK 
       410        420        430        440        450
SHAKALGCHA VVGYSESTSI CEEVCILSAS GTAAVLNPRF LQDGTVEGCL 
       460        470        480        490        500
EQRLEENLPT RCGFCHIPYD ELNMPFPAHL TYCYNCRKQK VPDVLFTTID 
       510        520        530        540        550
LPTDATVIGK GCLIQARLCR LKKKAQAEAN ATAISNLLPF MEYEVHTQLM 
       560        570        580        590        600
NKLKLKGMNA LFGLRIQITV GENMLMGLAS ATGVYLAALP TPGGIQIAGK 
       610        620        630        640        650
TPNDGSYEQH ISHMQKKIND TIAKNKELYE INPPEISEEI IGSPIPEPRQ 
       660        670        680        690        700
RSRLLRSQSE SSDEVTELDL SHGKKDAFVL EIDDTDAMED VHSLLTDVPP 
       710        720        730        740        750
PSGFYSCNTE IMPGINNWTS EIQMFTSVRV IRLSSLNLTN QALNKNFNDL 
       760        770        780        790        800
CENLLKSLYF KLRSMIPCCL CHVNFTVSLP EDELIQVTVT AVAITFDKNQ 
       810        820        830        840        850
ALQTTKTPVE KSLQRASTDN EELLQFPLEL CSDSLPSHPF PPAKEHLESA 
       860        870        880        890        900
SSNSGIPAAQ RATSVDYSSF ADRCSSWIEL IKLKAQTIRR GSIKTTMTVE 
       910        920        930        940        950
KASPVGDGNF RNRSAPPCAN STVGVVKMTP LSFIPGAKIT KYLGIINMFF 
       960        970        980        990       1000
IRETTSLREE GGVSGFLHAF IAEVFAMVRA HVAALGGNAV VSYIMKQCVF 
      1010       1020       1030       1040       1050
MENPNKNQAQ CLINVSGDAV VFVRESDLEV VSSQQPTTNC QSSCTEGEVT 

T

Note: No experimental confirmation available.

Show »

Length:1,051

Mass (Da):116,027

Checksum:ⁱ2C4D059D41F01BE8

GO

Isoform 4 (identifier: Q86YS7-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
     268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
     345-345: Q → QRGGSPHRFCRR
     845-845: A → EHLESASSNSGIPAAQRATSVDYSSFADRCSSWIELIKLKAQTIRRGSIKTT

« Hide

        10         20         30         40         50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ 
        60         70         80         90        100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE 
       110        120        130        140        150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT 
       160        170        180        190        200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS 
       210        220        230        240        250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS 
       260        270        280        290        300
PAAFLPACNS PSKEMKESPL VHPPSHGCRS THNSPIHTAT GSRLTQNFSV 
       310        320        330        340        350
SVPTLIYTGM GSGSAGKEGG PFKALLRQQT QSALEQRGGS PHRFCRRREF 
       360        370        380        390        400
PFFTLTAFPP GFLVHVGGVV SARSVKLLDR IHNPDEPETR DAWWAEIRQE 
       410        420        430        440        450
IKSHAKALGC HAVVGYSEST SICEEVCILS ASGTAAVLNP RFLQDGTVEG 
       460        470        480        490        500
CLEQRLEENL PTRCGFCHIP YDELNMPFPA HLTYCYNCRK QKVPDVLFTT 
       510        520        530        540        550
IDLPTDATVI GKGCLIQARL CRLKKKAQAE ANATAISNLL PFMEYEVHTQ 
       560        570        580        590        600
LMNKLKLKGM NALFGLRIQI TVGENMLMGL ASATGVYLAA LPTPGGIQIA 
       610        620        630        640        650
GKTPNDGSYE QHISHMQKKI NDTIAKNKEL YEINPPEISE EIIGSPIPEP 
       660        670        680        690        700
RQRSRLLRSQ SESSDEVTEL DLSHGKKDAF VLEIDDTDAM EDVHSLLTDV 
       710        720        730        740        750
PPPSGFYSCN TEIMPGINNW TSEIQMFTSV RVIRLSSLNL TNQALNKNFN 
       760        770        780        790        800
DLCENLLKSL YFKLRSMIPC CLCHVNFTVS LPEDELIQVT VTAVAITFDK 
       810        820        830        840        850
NQALQTTKTP VEKSLQRAST DNEELLQFPL ELCSDSLPSH PFPPAKEHLE 
       860        870        880        890        900
SASSNSGIPA AQRATSVDYS SFADRCSSWI ELIKLKAQTI RRGSIKTTMT 
       910        920        930        940        950
VEKASPVGDG NFRNRSAPPC ANSTVGVVKM TPLSFIPGAK ITKYLGIINM 
       960        970        980        990       1000
FFIRETTSLR EEGGVSGFLH AFIAEVFAMV RAHVAALGGN AVVSYIMKQC 
      1010       1020       1030       1040       1050
VFMENPNKNQ AQCLINVSGD AVVFVRESDL EVVSSQQPTT NCQSSCTEGE 

VTT

Note: No experimental confirmation available.Curated

Show »

Length:1,053

Mass (Da):116,305

Checksum:ⁱF27416DC231838AA

GO

Isoform 5 (identifier: Q86YS7-5) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
     268-316: IPFNEDPNPN...SDTDLSLTPK → SPLVHPPSHG...FSVSVPTLIY
     382-382: P → PAFVGIMGNTRSYKLLDWNSFNS
     845-845: A → EHLESASSNSGIPAAQRDRCSSWIELIKLKAQTIRRGSIKTT

« Hide

        10         20         30         40         50
MPGKLKVKIV AGRHLPVMDR ASDLTDAFVE VKFGNTTFKT DVYLKSLNPQ 
        60         70         80         90        100
WNSEWFKFEV DDEDLQDEPL QITVLDHDTY SANDAIGKVY IDIDPLLYSE 
       110        120        130        140        150
AATVISGWFP IYDTIHGIRG EINVVVKVDL FNDLNRFRQS SCGVKFFCTT 
       160        170        180        190        200
SIPKCYRAVI IHGFVEELVV NEDPEYQWID RIRTPRASNE ARQRLISLMS 
       210        220        230        240        250
GELQRKIGLK VLEMRGNAVV GYLQCFDLEG ESGLVVRAIG TACTLDKLSS 
       260        270        280        290        300
PAAFLPACNS PSKEMKESPL VHPPSHGCRS THNSPIHTAT GSRLTQNFSV 
       310        320        330        340        350
SVPTLIYTGM GSGSAGKEGG PFKALLRQQT QSALEQREFP FFTLTAFPPG 
       360        370        380        390        400
FLVHVGGVVS ARSVKLLDRI HNPAFVGIMG NTRSYKLLDW NSFNSDEPET 
       410        420        430        440        450
RDAWWAEIRQ EIKSHAKALG CHAVVGYSES TSICEEVCIL SASGTAAVLN 
       460        470        480        490        500
PRFLQDGTVE GCLEQRLEEN LPTRCGFCHI PYDELNMPFP AHLTYCYNCR 
       510        520        530        540        550
KQKVPDVLFT TIDLPTDATV IGKGCLIQAR LCRLKKKAQA EANATAISNL 
       560        570        580        590        600
LPFMEYEVHT QLMNKLKLKG MNALFGLRIQ ITVGENMLMG LASATGVYLA 
       610        620        630        640        650
ALPTPGGIQI AGKTPNDGSY EQHISHMQKK INDTIAKNKE LYEINPPEIS 
       660        670        680        690        700
EEIIGSPIPE PRQRSRLLRS QSESSDEVTE LDLSHGKKDA FVLEIDDTDA 
       710        720        730        740        750
MEDVHSLLTD VPPPSGFYSC NTEIMPGINN WTSEIQMFTS VRVIRLSSLN 
       760        770        780        790        800
LTNQALNKNF NDLCENLLKS LYFKLRSMIP CCLCHVNFTV SLPEDELIQV 
       810        820        830        840        850
TVTAVAITFD KNQALQTTKT PVEKSLQRAS TDNEELLQFP LELCSDSLPS 
       860        870        880        890        900
HPFPPAKEHL ESASSNSGIP AAQRDRCSSW IELIKLKAQT IRRGSIKTTM 
       910        920        930        940        950
TVEKASPVGD GNFRNRSAPP CANSTVGVVK MTPLSFIPGA KITKYLGIIN 
       960        970        980        990       1000
MFFIRETTSL REEGGVSGFL HAFIAEVFAM VRAHVAALGG NAVVSYIMKQ 
      1010       1020       1030       1040       1050
CVFMENPNKN QAQCLINVSG DAVVFVRESD LEVVSSQQPT TNCQSSCTEG 

EVTT

Note: No experimental confirmation available.Curated

Show »

Length:1,054

Mass (Da):116,468

Checksum:ⁱ2514DE8DDDBDB3A7

GO

Sequence cautionⁱ

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

The sequence BAG58665 differs from that shown. Reason: Frameshift at position 33. Curated

Experimental Info

Feature key	Position(s)	Length	Description
Sequence conflictⁱ	997 – 997	1	E → G in BAG58665 (PubMed:14702039).Curated
Isoform 4 (identifier: Q86YS7-4)
Sequence conflictⁱ	895 – 895	1	I → F in AAI43879 (PubMed:15489334).Curated
Isoform 5 (identifier: Q86YS7-5)
Sequence conflictⁱ	895 – 895	1	S → P in BAG58665 (PubMed:14702039).Curated

Alternative sequence

Feature key	Position(s)	Length	Description	Feature identifier	Actions
Alternative sequenceⁱ	268 – 316	49	IPFNE…SLTPK → SPLVHPPSHGCRSTHNSPIH TATGSRLTQNFSVSVPTLIY in isoform 2, isoform 4 and isoform 5. 2 Publications Manual assertion based on opinion inⁱ Ref.4 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). Ref.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; 2 AND 4).	VSP_028255	Add BLAST
Alternative sequenceⁱ	345 – 345	1	Q → QRGGSPHRFCRR in isoform 4. 1 Publication Manual assertion based on opinion inⁱ Ref.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; 2 AND 4).	VSP_055638
Alternative sequenceⁱ	382 – 382	1	P → PAFVGIMGNTRSYKLLDWNS FNS in isoform 5. 1 Publication Manual assertion based on opinion inⁱ Ref.4 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).	VSP_055639
Alternative sequenceⁱ	845 – 845	1	A → EHLESASSNSGIPAAQRATS VDYSSFADRCSSWIELIKLK AQTIRRGSIKTT in isoform 2, isoform 3 and isoform 4. 2 Publications Manual assertion based on opinion inⁱ Ref.4 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5). Ref.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; 2 AND 4).	VSP_028256
Alternative sequenceⁱ	845 – 845	1	A → EHLESASSNSGIPAAQRDRC SSWIELIKLKAQTIRRGSIK TT in isoform 5. 1 Publication Manual assertion based on opinion inⁱ Ref.4 "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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3 AND 5).	VSP_055640

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB011100 mRNA. Translation: BAA25454.3. Different initiation. AY166851 mRNA. Translation: AAO17290.1. AK295862 mRNA. Translation: BAG58665.1. Frameshift. AK299353 mRNA. Translation: BAG61349.1. AC053513 Genomic DNA. No translation available. BC042498 mRNA. Translation: AAH42498.2. BC053885 mRNA. Translation: AAH53885.1. BC117143 mRNA. Translation: AAI17144.1. BC143878 mRNA. Translation: AAI43879.1.
CCDSⁱ	CCDS31758.1. [Q86YS7-1] CCDS66337.1. [Q86YS7-3] CCDS66338.1. [Q86YS7-2] CCDS66339.1. [Q86YS7-5] CCDS66340.1. [Q86YS7-4]
PIRⁱ	T00072.
RefSeqⁱ	NP_001273102.1. NM_001286173.1. [Q86YS7-4] NP_001273103.1. NM_001286174.1. [Q86YS7-3] NP_001273104.1. NM_001286175.1. [Q86YS7-5] NP_001273105.1. NM_001286176.1. [Q86YS7-3] NP_001273106.1. NM_001286177.1. [Q86YS7-2] NP_055617.1. NM_014802.2. [Q86YS7-1]
UniGeneⁱ	Hs.271014.

Genome annotation databases

Ensemblⁱ	ENST00000333957; ENSP00000334229; ENSG00000111731. [Q86YS7-1] ENST00000396028; ENSP00000379345; ENSG00000111731. [Q86YS7-2] ENST00000446597; ENSP00000388756; ENSG00000111731. [Q86YS7-3] ENST00000536386; ENSP00000439392; ENSG00000111731. [Q86YS7-4] ENST00000542676; ENSP00000441951; ENSG00000111731. [Q86YS7-3] ENST00000545552; ENSP00000443204; ENSG00000111731. [Q86YS7-5]
GeneIDⁱ	9847.
KEGGⁱ	hsa:9847.
UCSCⁱ	uc001rfq.5. human. [Q86YS7-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AB011100 mRNA. Translation: BAA25454.3. Different initiation. AY166851 mRNA. Translation: AAO17290.1. AK295862 mRNA. Translation: BAG58665.1. Frameshift. AK299353 mRNA. Translation: BAG61349.1. AC053513 Genomic DNA. No translation available. BC042498 mRNA. Translation: AAH42498.2. BC053885 mRNA. Translation: AAH53885.1. BC117143 mRNA. Translation: AAI17144.1. BC143878 mRNA. Translation: AAI43879.1.
CCDSⁱ	CCDS31758.1. [Q86YS7-1] CCDS66337.1. [Q86YS7-3] CCDS66338.1. [Q86YS7-2] CCDS66339.1. [Q86YS7-5] CCDS66340.1. [Q86YS7-4]
PIRⁱ	T00072.
RefSeqⁱ	NP_001273102.1. NM_001286173.1. [Q86YS7-4] NP_001273103.1. NM_001286174.1. [Q86YS7-3] NP_001273104.1. NM_001286175.1. [Q86YS7-5] NP_001273105.1. NM_001286176.1. [Q86YS7-3] NP_001273106.1. NM_001286177.1. [Q86YS7-2] NP_055617.1. NM_014802.2. [Q86YS7-1]
UniGeneⁱ	Hs.271014.

3D structure databases

ProteinModelPortalⁱ	Q86YS7.
SMRⁱ	Q86YS7. Positions 3-143.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	115182. 32 interactions.
IntActⁱ	Q86YS7. 19 interactions.
STRINGⁱ	9606.ENSP00000334229.

PTM databases

iPTMnetⁱ	Q86YS7.
PhosphoSiteⁱ	Q86YS7.

Polymorphism and mutation databases

DMDMⁱ	74750574.

DMDMⁱ

74750574.

Proteomic databases

EPDⁱ	Q86YS7.
MaxQBⁱ	Q86YS7.
PaxDbⁱ	Q86YS7.
PeptideAtlasⁱ	Q86YS7.
PRIDEⁱ	Q86YS7.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000333957; ENSP00000334229; ENSG00000111731. [Q86YS7-1] ENST00000396028; ENSP00000379345; ENSG00000111731. [Q86YS7-2] ENST00000446597; ENSP00000388756; ENSG00000111731. [Q86YS7-3] ENST00000536386; ENSP00000439392; ENSG00000111731. [Q86YS7-4] ENST00000542676; ENSP00000441951; ENSG00000111731. [Q86YS7-3] ENST00000545552; ENSP00000443204; ENSG00000111731. [Q86YS7-5]
GeneIDⁱ	9847.
KEGGⁱ	hsa:9847.
UCSCⁱ	uc001rfq.5. human. [Q86YS7-1]

Organism-specific databases

CTDⁱ	9847.
GeneCardsⁱ	C2CD5.
HGNCⁱ	HGNC:29062. C2CD5.
HPAⁱ	HPA046194.
neXtProtⁱ	NX_Q86YS7.
PharmGKBⁱ	PA143485515.
HUGEⁱ	Search...
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	KOG1031. Eukaryota. ENOG410XQDE. LUCA.
GeneTreeⁱ	ENSGT00390000000212.
HOGENOMⁱ	HOG000006746.
HOVERGENⁱ	HBG081824.
InParanoidⁱ	Q86YS7.
OMAⁱ	IGERMIA.
OrthoDBⁱ	EOG091G0FX6.
PhylomeDBⁱ	Q86YS7.
TreeFamⁱ	TF323431.

Enzyme and pathway databases

Reactomeⁱ	R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.

Reactomeⁱ

R-HSA-1445148. Translocation of GLUT4 to the plasma membrane.

Miscellaneous databases

GenomeRNAiⁱ	9847.
PROⁱ	Q86YS7.

Gene expression databases

Bgeeⁱ	ENSG00000111731.
CleanExⁱ	HS_KIAA0528.
ExpressionAtlasⁱ	Q86YS7. baseline and differential.
Genevisibleⁱ	Q86YS7. HS.

Family and domain databases

Gene3Dⁱ	2.60.40.150. 1 hit.
InterProⁱ	IPR000008. C2_dom. [Graphical view]
Pfamⁱ	PF00168. C2. 1 hit. [Graphical view]
SMARTⁱ	SM00239. C2. 1 hit. [Graphical view]
SUPFAMⁱ	SSF49562. SSF49562. 1 hit.
PROSITEⁱ	PS50004. C2. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

C2CD5_HUMAN

Accessionⁱ

Primary (citable) accession number: Q86YS7
Secondary accession number(s): B4DJ03

Q86SU3

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	July 25, 2006
Last sequence update:	June 1, 2003
Last modified:	September 7, 2016
This is version 116 of the entry and version 1 of the sequence. [Complete history]

Entry statusⁱ

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.

Miscellaneousⁱ

Keywords - Technical termⁱ

Complete proteome, Reference proteome

Documents

Human chromosome 12
Human chromosome 12: entries, gene names and cross-references to MIM
SIMILARITY comments
Index of protein domains and families

Similar proteinsⁱ

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:

100%	UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%	UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%	UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q86YS7 (C2CD5_HUMAN)

UniProt

Q86YS7 - C2CD5_HUMAN

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C2 domain-containing protein 5

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Organism-specific databases

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (5)i

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (5)ⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ