C2CD5
entrez
9847
canonical
uniprot
Q86YS7
canonical
ensembl
ENSG00000111731
resolver
ensp
ENSP00000334229
resolver
ensp
ENSP00000379345
resolver
ensp
ENSP00000388756
resolver
ensp
ENSP00000439392
resolver
ensp
ENSP00000441951
resolver
ensp
ENSP00000443204
resolver
ensp
ENSP00000576411
resolver
ensp
ENSP00000576412
resolver
ensp
ENSP00000576413
resolver
ensp
ENSP00000576414
resolver
ensp
ENSP00000576416
resolver
ensp
ENSP00000576417
resolver
ensp
ENSP00000592673
resolver
ensp
ENSP00000630624
resolver
ensp
ENSP00000630633
resolver
ensp
ENSP00000630634
resolver
genesymbol
C2CD5
resolver
genesymbol
KIAA0528
resolver
genesymbol_syn
CDP138
resolver
genesymbol_syn
KIAA0528
resolver
hgnc
HGNC:29062
resolver
uniprot
B4DJ03
resolver
uniprot
B4DRN7
resolver
uniprot
B7ZLK1
resolver
uniprot
B7ZLL0
resolver
uniprot
F5H2A1
resolver
uniprot
F5H5R1
resolver
uniprot
O60280
resolver
uniprot
Q17RY7
resolver
uniprot
Q7Z619
resolver
uniprot
Q86SU3
resolver
uniprot_entry
B7ZLK1_HUMAN
resolver
uniprot_entry
C2CD5_HUMAN
resolver
uniprot_sec
B4DJ03
resolver
uniprot_sec
B4DRN7
resolver
uniprot_sec
B7ZLL0
resolver
uniprot_sec
F5H2A1
resolver
uniprot_sec
F5H5R1
resolver
uniprot_sec
O60280
resolver
uniprot_sec
Q17RY7
resolver
uniprot_sec
Q7Z619
resolver
uniprot_sec
Q86SU3
resolver
amino_acid_sequence
MPGKLKVKIVAGRHLPVMDRASDLTDAFVEVKFGNTTFKTDVYLKSLNPQWNSEWFKFEVDDEDLQDEPLQITVLDHDTYSANDAIGKVYIDIDPLLYSEAATVISGWFPIYDTIHGIRGEINVVVKVDLFNDLNRFRQSSCGVKFFCTTSIPKCYRAVIIHGFVEELVVNEDPEYQWIDRIRTPRASNEARQRLISLMSGELQRKIGLKVLEMRGNAVVGYLQCFDLEGESGLVVRAIGTACTLDKLSSPAAFLPACNSPSKEMKEIPFNEDPNPNTHSSGPSTPLKNQTYSFSPSKSYSRQSSSSDTDLSLTPKTGMGSGSAGKEGGPFKALLRQQTQSALEQREFPFFTLTAFPPGFLVHVGGVVSARSVKLLDRIHNPDEPETRDAWWAEIRQEIKSHAKALGCHAVVGYSESTSICEEVCILSASGTAAVLNPRFLQDGTVEGCLEQRLEENLPTRCGFCHIPYDELNMPFPAHLTYCYNCRKQKVPDVLFTTIDLPTDATVIGKGCLIQARLCRLKKKAQAEANATAISNLLPFMEYEVHTQLMNKLKLKGMNALFGLRIQITVGENMLMGLASATGVYLAALPTPGGIQIAGKTPNDGSYEQHISHMQKKINDTIAKNKELYEINPPEISEEIIGSPIPEPRQRSRLLRSQSESSDEVTELDLSHGKKDAFVLEIDDTDAMEDVHSLLTDVPPPSGFYSCNTEIMPGINNWTSEIQMFTSVRVIRLSSLNLTNQALNKNFNDLCENLLKSLYFKLRSMIPCCLCHVNFTVSLPEDELIQVTVTAVAITFDKNQALQTTKTPVEKSLQRASTDNEELLQFPLELCSDSLPSHPFPPAKAMTVEKASPVGDGNFRNRSAPPCANSTVGVVKMTPLSFIPGAKITKYLGIINMFFIRETTSLREEGGVSGFLHAFIAEVFAMVRAHVAALGGNAVVSYIMKQCVFMENPNKNQAQCLINVSGDAVVFVRESDLEVVSSQQPTTNCQSSCTEGEVTT
uniprot
proteins
function
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. {ECO:0000269|PubMed:21907143}.
uniprot
proteins
mass_dalton
110447
uniprot
proteins
mutagenesis
MUTAGEN 19; /note="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."; /evidence="ECO:0000269|PubMed:21907143"; MUTAGEN 26; /note="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."; /evidence="ECO:0000269|PubMed:21907143"; MUTAGEN 76; /note="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."; /evidence="ECO:0000269|PubMed:21907143"; MUTAGEN 78; /note="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."; /evidence="ECO:0000269|PubMed:21907143"; MUTAGEN 84; /note="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."; /evidence="ECO:0000269|PubMed:21907143"; MUTAGEN 197; /note="S->A: Inhibits insulin-stimulated AKT2-induced phosphorylation, SLC2A4/GLUT4 translocation to the cell surface and GSV-PM fusion."; /evidence="ECO:0000269|PubMed:21907143"; MUTAGEN 200; /note="S->A: Does not inhibit insulin-stimulated SLC2A4/GLUT4 translocation."; /evidence="ECO:0000269|PubMed:21907143
uniprot
proteins
post_translational_modification
PTM: Phosphorylated on Ser-197 by active myristoylated kinase AKT2; insulin-stimulated phosphorylation by AKT2 regulates SLC2A4/GLUT4 translocation into the plasma membrane. {ECO:0000269|PubMed:21907143}.
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16541075
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18691976
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21907143
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
9628581
uniprot
proteins
sequence_length
1000
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasmic vesicle membrane {ECO:0000269|PubMed:21907143}. Cytoplasm, cell cortex {ECO:0000269|PubMed:21907143}. Cell membrane {ECO:0000269|PubMed:21907143}. Cell projection, ruffle {ECO:0000269|PubMed:21907143}. Note=Dynamically associated with GLUT4-containing glucose storage vesicles (GSV) and plasma membrane in response to insulin stimulation.
uniprot
proteins