PDCD6IP
entrez
10015
canonical
uniprot
Q8WUM4
canonical
ensembl
ENSG00000170248
resolver
ensp
ENSP00000307387
resolver
ensp
ENSP00000411825
resolver
ensp
ENSP00000791540
resolver
genesymbol
PDCD6IP
resolver
genesymbol_syn
AIP1
resolver
genesymbol_syn
ALIX
resolver
genesymbol_syn
KIAA1375
resolver
hgnc
HGNC:8766
resolver
uniprot
C5MQH7
resolver
uniprot
E9PFU1
resolver
uniprot
Q6NUS1
resolver
uniprot
Q9BX86
resolver
uniprot
Q9NUN0
resolver
uniprot
Q9P2H2
resolver
uniprot
Q9UKL5
resolver
uniprot_entry
PDC6I_HUMAN
resolver
uniprot_sec
C5MQH7
resolver
uniprot_sec
E9PFU1
resolver
uniprot_sec
Q6NUS1
resolver
uniprot_sec
Q9BX86
resolver
uniprot_sec
Q9NUN0
resolver
uniprot_sec
Q9P2H2
resolver
uniprot_sec
Q9UKL5
resolver
amino_acid_sequence
MATFISVQLKKTSEVDLAKPLVKFIQQTYPSGGEEQAQYCRAAEELSKLRRAAVGRPLDKHEGALETLLRYYDQICSIEPKFPFSENQICLTFTWKDAFDKGSLFGGSVKLALASLGYEKSCVLFNCAALASQIAAEQNLDNDEGLKIAAKHYQFASGAFLHIKETVLSALSREPTVDISPDTVGTLSLIMLAQAQEVFFLKATRDKMKDAIIAKLANQAADYFGDAFKQCQYKDTLPKEVFPVLAAKHCIMQANAEYHQSILAKQQKKFGEEIARLQHAAELIKTVASRYDEYVNVKDFSDKINRALAAAKKDNDFIYHDRVPDLKDLDPIGKATLVKSTPVNVPISQKFTDLFEKMVPVSVQQSLAAYNQRKADLVNRSIAQMREATTLANGVLASLNLPAAIEDVSGDTVPQSILTKSRSVIEQGGIQTVDQLIKELPELLQRNREILDESLRLLDEEEATDNDLRAKFKERWQRTPSNELYKPLRAEGTNFRTVLDKAVQADGQVKECYQSHRDTIVLLCKPEPELNAAIPSANPAKTMQGSEVVNVLKSLLSNLDEVKKEREGLENDLKSVNFDMTSKFLTALAQDGVINEEALSVTELDRVYGGLTTKVQESLKKQEGLLKNIQVSHQEFSKMKQSNNEANLREEVLKNLATAYDNFVELVANLKEGTKFYNELTEILVRFQNKCSDIVFARKTERDELLKDLQQSIAREPSAPSIPTPAYQSSPAGGHAPTPPTPAPRTMPPTKPQPPARPPPPVLPANRAPSATAPSPVGAGTAAPAPSQTPGSAPPPQAQGPPYPTYPGYPGYCQMPMPMGYNPYAYGQYNMPYPPVYHQSPGQAPYPGPQQPSYPFPQPPQQSYYPQQ
uniprot
proteins
disease_involvement
DISEASE: Microcephaly 29, primary, autosomal recessive (MCPH29) [MIM:620047]: A form of microcephaly, a disease defined as a head circumference more than 3 standard deviations below the age, sex and ethnically matched mean. Brain weight is markedly reduced and the cerebral cortex is disproportionately small. MCPH29 is characterized by small head circumference apparent at birth and associated with global developmental delay, impaired intellectual development, speech delay, and behavioral abnormalities. Affected individuals also have poor overall growth with short stature, mild dysmorphic facial features, and seizures. {ECO:0000269|PubMed:32286682}. Note=The disease may be caused by variants affecting the gene represented in this entry.
uniprot
proteins
function
FUNCTION: Multifunctional protein involved in endocytosis, multivesicular body biogenesis, membrane repair, cytokinesis, apoptosis and maintenance of tight junction integrity. Class E VPS protein involved in concentration and sorting of cargo proteins of the multivesicular body (MVB) for incorporation into intralumenal vesicles (ILVs) that are generated by invagination and scission from the limiting membrane of the endosome. Binds to the phospholipid lysobisphosphatidic acid (LBPA) which is abundant in MVBs internal membranes. The MVB pathway requires the sequential function of ESCRT-O, -I,-II and -III complexes (PubMed:14739459). The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis (PubMed:17556548, PubMed:17853893). Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis (PubMed:17556548, PubMed:17853893, PubMed:18641129). May play a role in the regulation of both apoptosis and cell proliferation. Regulates exosome biogenesis in concert with SDC1/4 and SDCBP (PubMed:22660413). By interacting with F-actin, PARD3 and TJP1 secures the proper assembly and positioning of actomyosin-tight junction complex at the apical sides of adjacent epithelial cells that defines a spatial membrane domain essential for the maintenance of epithelial cell polarity and barrier (By similarity). {ECO:0000250|UniProtKB:Q9WU78, ECO:0000269|PubMed:14739459, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129, ECO:0000269|PubMed:22660413}.; FUNCTION: (Microbial infection) Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function requires the interaction with CHMP4B. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as enveloped virus budding (HIV-1 and other lentiviruses). {ECO:0000269|PubMed:14505569, ECO:0000269|PubMed:14505570, ECO:0000269|PubMed:14519844, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:18641129}.
uniprot
proteins
mass_dalton
96023
uniprot
proteins
mutagenesis
MUTAGEN 199; /note="F->D: Does not support cytokinesis; loss of normal midbody formation; loss of CHMP4A-, CHMP4B- and CHMP4C-binding in a yeast two-hybrid assay; no effect on localization to the midbody; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17428861, ECO:0000269|PubMed:18641129"; MUTAGEN 212; /note="I->D: Does not support cytokinesis; loss of normal midbody formation; loss of CHMP4A-, CHMP4B- and CHMP4C-binding in a yeast two-hybrid assay; impairs rescue of PTAP-type L domain-deficient HIV-1 p6; no effect on localization to the midbody."; /evidence="ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129"; MUTAGEN 216; /note="L->D: Abolishes interaction with CHMP4B and abolishes rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17428861"; MUTAGEN 317; /note="F->A: Diminishes rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17428861"; MUTAGEN 318; /note="I->A: Greatly diminishes rescue of PTAP-type L domain--deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17428861"; MUTAGEN 319; /note="Y->A: Greatly diminishes rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:17428861"; MUTAGEN 319; /note="Y->F: No effect on rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:17428861"; MUTAGEN 495; /note="F->D: Impairs rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17350572"; MUTAGEN 498; /note="V->D: Reduces interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17277784, ECO:0000269|PubMed:17350572"; MUTAGEN 509; /note="V->D: Abolishes interaction with HIV-1 p6; impairs rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17277784, ECO:0000269|PubMed:17350572"; MUTAGEN 512; /note="C->A: No effect on interaction with HIV-1 p6; impairs rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17277784"; MUTAGEN 676; /note="F->A: Loss of interaction with SDCBP."; /evidence="ECO:0000269|PubMed:22660413"; MUTAGEN 676; /note="F->D: Abolishes interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6; no effect on cytokinesis, nor on midbody formation."; /evidence="ECO:0000269|PubMed:17277784, ECO:0000269|PubMed:17350572, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129"; MUTAGEN 680; /note="L->D: Impairs rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17350572"; MUTAGEN 683; /note="I->A: No effect on interaction with HIV-1 p6."; /evidence="ECO:0000269|PubMed:17277784, ECO:0000269|PubMed:17350572"; MUTAGEN 683; /note="I->D: Reduces interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17277784, ECO:0000269|PubMed:17350572"; MUTAGEN 717..720; /note="PSAP->AAAA: No effect on midbody formation, nor on cytokinesis; reduced TSG101-binding; no effect on HIV-1 release. Almost complete loss of TSG101-binding and impaired cytokinesis; when associated with 852-A--A-855."; /evidence="ECO:0000269|PubMed:18641129"; MUTAGEN 720; /note="P->L: Abolishes interaction with TSG101; no effect on rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17350572"; MUTAGEN 744..745; /note="PR->VD: No effect on midbody formation; loss of CD2AP- and SH3KBP1-binding in a yeast two-hybrid assay; no effect on HIV-1 release."; /evidence="ECO:0000269|PubMed:18641129"; MUTAGEN 757..759; /note="RPP->GAA: No effect on midbody formation; loss of SH3GL2-binding in a yeast two-hybrid assay."; /evidence="ECO:0000269|PubMed:18641129"; MUTAGEN 757..758; /note="RP->AA: Abolishes interaction with SH3GL1 and SH3GL2; no effect on rescue of PTAP-type L domain-deficient HIV-1 p6."; /evidence="ECO:0000269|PubMed:17350572"; MUTAGEN 794..813; /note="Missing: Does not support the formation of normal midbodies; loss of localization to the midbody; loss of CD2AP-, CEP55-, SH3GL2-, SH3KBP1-, TSG101-binding in a yeast two-hybrid assay."; /evidence="ECO:0000269|PubMed:18641129"; MUTAGEN 800..802; /note="GPP->AAA: Abolishes interaction with CEP55; inhibits support of cytokinesis."; /evidence="ECO:0000269|PubMed:17853893"; MUTAGEN 801..802; /note="PP->VD: Loss of midbody localization; does not support cytokinesis; loss of CEP55-binding in a yeast two-hybrid assay; no effect on HIV-1 release."; /evidence="ECO:0000269|PubMed:18641129"; MUTAGEN 801; /note="P->A: Decreased interaction with CEP55."; /evidence="ECO:0000269|PubMed:18948538"; MUTAGEN 802; /note="P->A: Decreased interaction with CEP55."; /evidence="ECO:0000269|PubMed:18948538"; MUTAGEN 803..804; /note="YP->VD: No effect on CEP55-binding in a yeast two-hybrid assay."; /evidence="ECO:0000269|PubMed:18641129"; MUTAGEN 805..806; /note="TY->VD: Loss of CEP55-binding in a yeast two-hybrid assay."; /evidence="ECO:0000269|PubMed:18641129"; MUTAGEN 806; /note="Y->A: Abolishes interaction with CEP55."; /evidence="ECO:0000269|PubMed:18948538"; MUTAGEN 852..855; /note="PSYP->ASAA: Loss of homoologimerization and reduced TSG101-binding; decreased HIV-1 release; no effect on cytokinesis. Almost complete loss of TSG101-binding and impaired cytokinesis; when associated with 717-A--A-720."; /evidence="ECO:0000269|PubMed:18641129"; MUTAGEN 864..865; /note="YY->AA: Loss of homooligomerization; reduced TSG101-binding; impaired HIV-1 release."; /evidence="ECO:0000269|PubMed:18641129
uniprot
proteins
post_translational_modification
PTM: May be phosphorylated on tyrosine residues by activated PDGFRB. {ECO:0000269|PubMed:20494825}.
uniprot
proteins
pubmed
10718198
uniprot
proteins
pubmed
11683497
uniprot
proteins
pubmed
12860994
uniprot
proteins
pubmed
14505569
uniprot
proteins
pubmed
14505570
uniprot
proteins
pubmed
14519844
uniprot
proteins
pubmed
14583093
uniprot
proteins
pubmed
14678797
uniprot
proteins
pubmed
14702039
uniprot
proteins
pubmed
14739459
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15849434
uniprot
proteins
pubmed
15908698
uniprot
proteins
pubmed
16641997
uniprot
proteins
pubmed
16957052
uniprot
proteins
pubmed
17081065
uniprot
proteins
pubmed
17277784
uniprot
proteins
pubmed
17350572
uniprot
proteins
pubmed
17428861
uniprot
proteins
pubmed
17556548
uniprot
proteins
pubmed
17853893
uniprot
proteins
pubmed
18066081
uniprot
proteins
pubmed
18256029
uniprot
proteins
pubmed
18511562
uniprot
proteins
pubmed
18641129
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18940611
uniprot
proteins
pubmed
18948538
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19520058
uniprot
proteins
pubmed
19608861
uniprot
proteins
pubmed
19906316
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
20494825
uniprot
proteins
pubmed
21191027
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
22073189
uniprot
proteins
pubmed
22223895
uniprot
proteins
pubmed
22660413
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24129315
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
25686249
uniprot
proteins
pubmed
25786915
uniprot
proteins
pubmed
25944712
uniprot
proteins
pubmed
32286682
uniprot
proteins
sequence_length
868
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000250|UniProtKB:Q9QZA2}. Melanosome {ECO:0000269|PubMed:17081065}. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome {ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893}. Secreted, extracellular exosome {ECO:0000269|PubMed:22660413}. Cell junction, tight junction {ECO:0000250|UniProtKB:Q9WU78}. Midbody, Midbody ring {ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129}. Note=Identified by mass spectrometry in melanosome fractions from stage I to stage IV. Colocalized with CEP55 at centrosomes of non-dividing cells. Component of the actomyosin-tight junction complex (By similarity). PDCD6IP targeting to the midbody requires the interaction with CEP55 (PubMed:18641129). {ECO:0000250|UniProtKB:Q9QZA2, ECO:0000250|UniProtKB:Q9WU78, ECO:0000269|PubMed:17081065, ECO:0000269|PubMed:17556548, ECO:0000269|PubMed:17853893, ECO:0000269|PubMed:18641129}.
uniprot
proteins