PDCD6
entrez
10016
canonical
uniprot
O75340
canonical
ensembl
ENSG00000249915
resolver
ensp
ENSP00000264933
resolver
ensp
ENSP00000422085
resolver
ensp
ENSP00000423815
resolver
ensp
ENSP00000482332
resolver
ensp
ENSP00000485024
resolver
enst
ENST00000614778
resolver
enst
ENST00000618970
resolver
genesymbol
PDCD6
resolver
genesymbol_syn
ALG2
resolver
hgnc
HGNC:8765
resolver
uniprot
A0A024QZ42
resolver
uniprot
A0A087WZ38
resolver
uniprot
B2RD16
resolver
uniprot
E7ESR3
resolver
uniprot
Q2YDC2
resolver
uniprot
Q53FC3
resolver
uniprot
Q5TZS0
resolver
uniprot_entry
A0A024QZ42_HUMAN
resolver
uniprot_entry
A0A087WZ38_HUMAN
resolver
uniprot_entry
PDCD6_HUMAN
resolver
uniprot_entry
Q53FC3_HUMAN
resolver
uniprot_sec
B2RD16
resolver
uniprot_sec
E7ESR3
resolver
uniprot_sec
Q2YDC2
resolver
uniprot_sec
Q5TZS0
resolver
amino_acid_sequence
MAAYSYRPGPGAGPGPAAGAALPDQSFLWNVFQRVDKDRSGVISDTELQQALSNGTWTPFNPVTVRSIISMFDRENKAGVNFSEFTGVWKYITDWQNVFRTYDRDNSGMIDKNELKQALSGFGYRLSDQFHDILIRKFDRQGRGQIAFDDFIQGCIVLQRLTDIFRRYDTDQDGWIQVSYEQYLSMVFSIV
uniprot
proteins
function
FUNCTION: Calcium sensor that plays a key role in processes such as endoplasmic reticulum (ER)-Golgi vesicular transport, endosomal biogenesis or membrane repair. Acts as an adapter that bridges unrelated proteins or stabilizes weak protein-protein complexes in response to calcium: calcium-binding triggers exposure of apolar surface, promoting interaction with different sets of proteins thanks to 3 different hydrophobic pockets, leading to translocation to membranes (PubMed:20691033, PubMed:25667979). Involved in ER-Golgi transport by promoting the association between PDCD6IP and TSG101, thereby bridging together the ESCRT-III and ESCRT-I complexes (PubMed:19520058). Together with PEF1, acts as a calcium-dependent adapter for the BCR(KLHL12) complex, a complex involved in ER-Golgi transport by regulating the size of COPII coats (PubMed:27716508). In response to cytosolic calcium increase, the heterodimer formed with PEF1 interacts with, and bridges together the BCR(KLHL12) complex and SEC31 (SEC31A or SEC31B), promoting monoubiquitination of SEC31 and subsequent collagen export, which is required for neural crest specification (PubMed:27716508). Involved in the regulation of the distribution and function of MCOLN1 in the endosomal pathway (PubMed:19864416). Promotes localization and polymerization of TFG at endoplasmic reticulum exit site (PubMed:27813252). Required for T-cell receptor-, Fas-, and glucocorticoid-induced apoptosis (By similarity). May mediate Ca(2+)-regulated signals along the death pathway: interaction with DAPK1 can accelerate apoptotic cell death by increasing caspase-3 activity (PubMed:16132846). Its role in apoptosis may however be indirect, as suggested by knockout experiments (By similarity). May inhibit KDR/VEGFR2-dependent angiogenesis; the function involves inhibition of VEGF-induced phosphorylation of the Akt signaling pathway (PubMed:21893193). In case of infection by HIV-1 virus, indirectly inhibits HIV-1 production by affecting viral Gag expression and distribution (PubMed:27784779). {ECO:0000250|UniProtKB:P12815, ECO:0000269|PubMed:16132846, ECO:0000269|PubMed:19520058, ECO:0000269|PubMed:19864416, ECO:0000269|PubMed:20691033, ECO:0000269|PubMed:21893193, ECO:0000269|PubMed:25667979, ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27784779, ECO:0000269|PubMed:27813252}.; FUNCTION: [Isoform 2]: Has a lower Ca(2+) affinity than isoform 1 (By similarity). {ECO:0000250|UniProtKB:P12815}.
uniprot
proteins
mass_dalton
21868
uniprot
proteins
mutagenesis
MUTAGEN 47; /note="E->A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-114."; /evidence="ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:18256029, ECO:0000269|PubMed:27716508"; MUTAGEN 52; /note="L->A: Strongly impaired interaction with SEC31A. Slightly reduced interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:25667979"; MUTAGEN 53; /note="S->G: Slightly reduced interaction with SEC31A. Does not affect interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:25667979"; MUTAGEN 57; /note="W->A: Does not affect interaction with SEC31A. Reduces the interaction with HEBP2, PDCD6IP and ANXA7."; /evidence="ECO:0000269|PubMed:18256029, ECO:0000269|PubMed:25667979, ECO:0000269|PubMed:27784779"; MUTAGEN 60; /note="F->A: Abolishes the interaction with SEC31A, PDCD6IP, ANXA7 and ANXA11."; /evidence="ECO:0000269|PubMed:18256029, ECO:0000269|PubMed:27716508"; MUTAGEN 85; /note="F->A: Strongly impaired interaction with SEC31A and TFG. Does not affect interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:25667979, ECO:0000269|PubMed:27813252"; MUTAGEN 89; /note="W->A: Does not affect interaction with SEC31A. Does not affect interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:25667979"; MUTAGEN 91; /note="Y->A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11."; /evidence="ECO:0000269|PubMed:18256029"; MUTAGEN 92; /note="I->A: Does not affect interaction with SEC31A. Does not affect interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:25667979"; MUTAGEN 95; /note="W->A: Abolishes the interaction with PDCD6IP, ANXA7 and ANXA11."; /evidence="ECO:0000269|PubMed:18256029"; MUTAGEN 114; /note="E->A: Loss of interaction with SEC31A and PLSCR3, and loss of localization to the endoplasmic reticulum; when associated with A-47."; /evidence="ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:18256029"; MUTAGEN 122; /note="F->A: Increases interaction with PDCD6IP and ANXA7. Impairs interaction with ANXA11. Augments stauroporine-induced cell death."; /evidence="ECO:0000269|PubMed:20691033"; MUTAGEN 122; /note="F->G: Increases interaction with PDCD6IP. Impairs interaction with ANXA11."; /evidence="ECO:0000269|PubMed:20691033"; MUTAGEN 122; /note="F->S: Increases interaction with PDCD6IP. Impairs interaction with ANAX7 and ANXA11."; /evidence="ECO:0000269|PubMed:20691033"; MUTAGEN 122; /note="F->W: Impairs interaction with ANXA11."; /evidence="ECO:0000269|PubMed:20691033"; MUTAGEN 148; /note="F->S: Slightly reduced interaction with SEC31A. Does not affect interaction with PDCD6IP."; /evidence="ECO:0000269|PubMed:25667979"; MUTAGEN 180; /note="Y->A: Abolishes the interaction with PDCD6IP, TSG101, ANXA7 and ANXA11. Does not affect interaction with TFG and SEC31A."; /evidence="ECO:0000269|PubMed:18256029, ECO:0000269|PubMed:27813252
uniprot
proteins
pubmed
11278427
uniprot
proteins
pubmed
11883899
uniprot
proteins
pubmed
11883939
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
15372022
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
16132846
uniprot
proteins
pubmed
16957052
uniprot
proteins
pubmed
16959974
uniprot
proteins
pubmed
17045351
uniprot
proteins
pubmed
17889823
uniprot
proteins
pubmed
18256029
uniprot
proteins
pubmed
18940611
uniprot
proteins
pubmed
18997320
uniprot
proteins
pubmed
19520058
uniprot
proteins
pubmed
19864416
uniprot
proteins
pubmed
20691033
uniprot
proteins
pubmed
21122810
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21893193
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
25667979
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
27716508
uniprot
proteins
pubmed
27784779
uniprot
proteins
pubmed
27813252
uniprot
proteins
sequence_length
191
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000269|PubMed:16957052, ECO:0000269|PubMed:27813252}; Peripheral membrane protein {ECO:0000269|PubMed:16957052}. Cytoplasmic vesicle, COPII-coated vesicle membrane {ECO:0000269|PubMed:27716508}. Cytoplasm {ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27784779}. Nucleus {ECO:0000269|PubMed:17045351, ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:27784779}. Endosome {ECO:0000269|PubMed:19864416}. Note=Interaction with RBM22 induces relocalization from the cytoplasm to the nucleus (PubMed:17045351). Translocated from the cytoplasm to the nucleus after heat shock cell treatment. Accumulates in cytoplasmic vesicle-like organelles after heat shock treatment, which may represent stress granules (PubMed:21122810). In response to calcium increase, relocates from cytoplasm to COPII vesicle coat (PubMed:27716508). Localizes to endoplasmic reticulum exit site (ERES) (PubMed:27813252). {ECO:0000269|PubMed:17045351, ECO:0000269|PubMed:21122810, ECO:0000269|PubMed:27716508, ECO:0000269|PubMed:27813252}.
uniprot
proteins