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Protein

Programmed cell death 6-interacting protein

Gene

PDCD6IP

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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:17853893, PubMed:17556548). Adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis (PubMed:17853893, PubMed:17556548, 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).By similarity5 Publications
(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).5 Publications

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • proteinase activated receptor binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

GO - Biological processi

  • actomyosin contractile ring assembly Source: UniProtKB
  • apoptotic process Source: UniProtKB-KW
  • bicellular tight junction assembly Source: UniProtKB
  • cell separation after cytokinesis Source: UniProtKB
  • maintenance of epithelial cell apical/basal polarity Source: UniProtKB
  • mitotic cytokinesis Source: UniProtKB
  • multivesicular body assembly Source: ParkinsonsUK-UCL
  • positive regulation of exosomal secretion Source: UniProtKB
  • positive regulation of extracellular exosome assembly Source: UniProtKB
  • protein homooligomerization Source: UniProtKB
  • protein transport Source: UniProtKB-KW
  • regulation of centrosome duplication Source: UniProtKB
  • regulation of extracellular exosome assembly Source: UniProtKB
  • regulation of membrane permeability Source: UniProtKB
  • ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
  • viral budding Source: UniProtKB
  • viral budding via host ESCRT complex Source: UniProtKB
  • viral life cycle Source: Reactome

Keywordsi

Biological processApoptosis, Cell cycle, Cell division, Host-virus interaction, Protein transport, Transport

Enzyme and pathway databases

ReactomeiR-HSA-162588. Budding and maturation of HIV virion.
R-HSA-5210891. Uptake and function of anthrax toxins.

Names & Taxonomyi

Protein namesi
Recommended name:
Programmed cell death 6-interacting protein
Short name:
PDCD6-interacting protein
Alternative name(s):
ALG-2-interacting protein 1
ALG-2-interacting protein X
Hp95
Gene namesi
Name:PDCD6IP
Synonyms:AIP1, ALIX, KIAA1375
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 3

Organism-specific databases

EuPathDBiHostDB:ENSG00000170248.13.
HGNCiHGNC:8766. PDCD6IP.

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cell junction, Cytoplasm, Cytoskeleton, Secreted, Tight junction

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi199F → 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. 2 Publications1
Mutagenesisi212I → 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. 3 Publications1
Mutagenesisi216L → D: Abolishes interaction with CHMP4B and abolishes rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication1
Mutagenesisi317F → A: Diminishes rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication1
Mutagenesisi318I → A: Greatly diminishes rescue of PTAP-type L domain--deficient HIV-1 p6. 1 Publication1
Mutagenesisi319Y → A: Greatly diminishes rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications1
Mutagenesisi319Y → F: No effect on rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications1
Mutagenesisi495F → D: Impairs rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication1
Mutagenesisi498V → D: Reduces interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications1
Mutagenesisi509V → D: Abolishes interaction with HIV-1 p6; impairs rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications1
Mutagenesisi512C → A: No effect on interaction with HIV-1 p6; impairs rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication1
Mutagenesisi676F → A: Loss of interaction with SDCBP. 1 Publication1
Mutagenesisi676F → 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. 4 Publications1
Mutagenesisi680L → D: Impairs rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication1
Mutagenesisi683I → A: No effect on interaction with HIV-1 p6. 2 Publications1
Mutagenesisi683I → D: Reduces interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications1
Mutagenesisi717 – 720PSAP → 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. 1 Publication4
Mutagenesisi720P → L: Abolishes interaction with TSG101; no effect on rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication1
Mutagenesisi744 – 745PR → VD: No effect on midbody formation; loss of CD2AP- and SH3KBP1-binding in a yeast two-hybrid assay; no effect on HIV-1 release. 1 Publication2
Mutagenesisi757 – 759RPP → GAA: No effect on midbody formation; loss of SH3GL2-binding in a yeast two-hybrid assay. 1 Publication3
Mutagenesisi757 – 758RP → AA: Abolishes interaction with SH3GL1 and SH3GL2; no effect on rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication2
Mutagenesisi794 – 813Missing : 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. 1 PublicationAdd BLAST20
Mutagenesisi800 – 802GPP → AAA: Abolishes interaction with CEP55; inhibits support of cytokinesis. 1 Publication3
Mutagenesisi801 – 802PP → 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. 1 Publication2
Mutagenesisi801P → A: Decreased interaction with CEP55. 1 Publication1
Mutagenesisi802P → A: Decreased interaction with CEP55. 1 Publication1
Mutagenesisi803 – 804YP → VD: No effect on CEP55-binding in a yeast two-hybrid assay. 1 Publication2
Mutagenesisi805 – 806TY → VD: Loss of CEP55-binding in a yeast two-hybrid assay. 1 Publication2
Mutagenesisi806Y → A: Abolishes interaction with CEP55. 1 Publication1
Mutagenesisi852 – 855PSYP → 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. 1 Publication4
Mutagenesisi864 – 865YY → AA: Loss of homooligomerization; reduced TSG101-binding; impaired HIV-1 release. 1 Publication2

Organism-specific databases

DisGeNETi10015.
OpenTargetsiENSG00000170248.
PharmGKBiPA33116.

Polymorphism and mutation databases

BioMutaiPDCD6IP.
DMDMi31076831.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedCombined sources1 Publication
ChainiPRO_00002188912 – 868Programmed cell death 6-interacting proteinAdd BLAST867

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei2N-acetylalanineCombined sources1 Publication1
Modified residuei215N6-acetyllysineCombined sources1
Modified residuei479PhosphothreonineCombined sources1
Modified residuei481PhosphoserineCombined sources1
Modified residuei730PhosphoserineCombined sources1
Modified residuei738PhosphothreonineCombined sources1
Modified residuei741PhosphothreonineCombined sources1
Modified residuei745Omega-N-methylarginineCombined sources1

Post-translational modificationi

May be phosphorylated on tyrosine residues by activated PDGFRB.1 Publication

Keywords - PTMi

Acetylation, Methylation, Phosphoprotein

Proteomic databases

EPDiQ8WUM4.
MaxQBiQ8WUM4.
PaxDbiQ8WUM4.
PeptideAtlasiQ8WUM4.
PRIDEiQ8WUM4.

2D gel databases

UCD-2DPAGEiQ8WUM4.

PTM databases

iPTMnetiQ8WUM4.
PhosphoSitePlusiQ8WUM4.
SwissPalmiQ8WUM4.

Expressioni

Gene expression databases

BgeeiENSG00000170248.
CleanExiHS_PDCD6IP.
ExpressionAtlasiQ8WUM4. baseline and differential.
GenevisibleiQ8WUM4. HS.

Organism-specific databases

HPAiCAB016212.
HPA011905.

Interactioni

Subunit structurei

Self-associates (PubMed:14505570, PubMed:14519844). Interacts with SH3KBP1/CIN85 (By similarity). Interacts with PDCD6 in a calcium -dependent manner (PubMed:16957052, PubMed:18256029, PubMed:18940611). Interacts with TSG101 in a calcium-dependent manner; PDCD6IP homooligomerization may be required for TSG101-binding (PubMed:14505570, PubMed:14519844, PubMed:18641129, PubMed:19520058, PubMed:17350572). Interacts with SGSM3 (PubMed:15849434). Directly interacts with CHMP4A, CHMP4B and CHMP4C (PubMed:12860994, PubMed:14505569, PubMed:14505570, PubMed:14519844, PubMed:14678797, PubMed:14583093, PubMed:17428861, PubMed:17350572, PubMed:18511562). Directly interacts with CEP55 in a 1:2 stoechiometry (PubMed:17853893, PubMed:17556548, PubMed:18641129, PubMed:18948538). The interaction with CEP55 is required for PDCD6IP targeting to the midbody (PubMed:18641129). May interact with PDGFRB (PubMed:20494825). Interacts with SH3GL1 and SH3GL2/endophilin-1 (PubMed:17350572). Forms a complex with SDCBP and SDC2 (PubMed:22660413). Found in a complex with F-actin, TJP1/ZO-1 and PARD3 (By similarity). Interacts with CD2AP (PubMed:17853893). Interacts with ARRDC1 (PubMed:21191027).By similarity21 Publications
(Microbial infection) Interacts with HIV-1 p6 (PubMed:14505569, PubMed:17350572, PubMed:17277784, PubMed:18066081). Interacts with HIV-1 p9 (PubMed:18066081). Interacts with EIAV p9 (PubMed:14505569, PubMed:14519844, PubMed:17350572, PubMed:18066081). Interacts with murine leukemia virus Gag polyprotein (via LYPX(n)L motif) (PubMed:15908698).6 Publications

Binary interactionsi

Show more details

GO - Molecular functioni

  • calcium-dependent protein binding Source: UniProtKB
  • proteinase activated receptor binding Source: UniProtKB
  • protein homodimerization activity Source: UniProtKB

Protein-protein interaction databases

BioGridi115332. 112 interactors.
DIPiDIP-29327N.
IntActiQ8WUM4. 62 interactors.
MINTiMINT-4999333.
STRINGi9606.ENSP00000411825.

Structurei

Secondary structure

1868
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi18 – 28Combined sources11
Beta strandi33 – 35Combined sources3
Helixi39 – 55Combined sources17
Helixi62 – 78Combined sources17
Turni79 – 83Combined sources5
Turni84 – 86Combined sources3
Beta strandi93 – 96Combined sources4
Beta strandi98 – 100Combined sources3
Beta strandi104 – 106Combined sources3
Beta strandi110 – 114Combined sources5
Helixi116 – 136Combined sources21
Beta strandi140 – 142Combined sources3
Helixi143 – 170Combined sources28
Beta strandi171 – 173Combined sources3
Turni177 – 179Combined sources3
Helixi181 – 205Combined sources25
Helixi210 – 231Combined sources22
Helixi241 – 266Combined sources26
Helixi270 – 290Combined sources21
Turni292 – 294Combined sources3
Helixi298 – 317Combined sources20
Helixi326 – 328Combined sources3
Beta strandi348 – 350Combined sources3
Turni354 – 357Combined sources4
Helixi361 – 398Combined sources38
Turni399 – 402Combined sources4
Helixi403 – 406Combined sources4
Beta strandi408 – 412Combined sources5
Helixi415 – 426Combined sources12
Turni427 – 429Combined sources3
Helixi430 – 471Combined sources42
Turni473 – 475Combined sources3
Helixi481 – 514Combined sources34
Helixi517 – 523Combined sources7
Helixi527 – 532Combined sources6
Helixi541 – 543Combined sources3
Helixi547 – 575Combined sources29
Helixi581 – 590Combined sources10
Beta strandi591 – 593Combined sources3
Helixi596 – 639Combined sources44
Helixi644 – 697Combined sources54
Beta strandi802 – 805Combined sources4
Turni810 – 813Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2OEVX-ray3.30A1-698[»]
2OEWX-ray2.55A1-359[»]
2OEXX-ray2.58A/B360-702[»]
2OJQX-ray2.87A360-702[»]
2R02X-ray2.60A2-698[»]
2R03X-ray2.59A2-698[»]
2R05X-ray2.55A2-698[»]
2XS1X-ray2.30A1-698[»]
2XS8X-ray2.50A1-698[»]
2ZNEX-ray2.20C/D799-812[»]
3C3OX-ray2.15A1-359[»]
3C3QX-ray2.10A1-359[»]
3C3RX-ray2.02A1-359[»]
3E1RX-ray2.00C797-809[»]
3WUVX-ray2.79C/F/I/L/O/R796-810[»]
4JJYX-ray6.50A/B355-708[»]
ProteinModelPortaliQ8WUM4.
SMRiQ8WUM4.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WUM4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini3 – 392BRO1PROSITE-ProRule annotationAdd BLAST390

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni176 – 868Interaction with EIAV p9Add BLAST693
Regioni176 – 503Interaction with CHMP4A, CHMP4B and CHMP4CAdd BLAST328
Regioni418 – 868Interaction with SDCBP1 PublicationAdd BLAST451
Regioni503 – 868Self-associationAdd BLAST366
Regioni717 – 720Interaction with TSG1014
Regioni801 – 806Interaction with CEP551 Publication6
Regioni864 – 868Essential to promote virus budding5

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi717 – 860Pro-richAdd BLAST144

Phylogenomic databases

eggNOGiKOG2220. Eukaryota.
ENOG410XQX6. LUCA.
GeneTreeiENSGT00780000121909.
HOGENOMiHOG000006938.
HOVERGENiHBG053533.
InParanoidiQ8WUM4.
KOiK12200.
OMAiSDFCFAR.
OrthoDBiEOG091G04NC.
PhylomeDBiQ8WUM4.
TreeFamiTF323502.

Family and domain databases

InterProiView protein in InterPro
IPR025304. ALIX_V_dom.
IPR004328. BRO1_dom.
PfamiView protein in Pfam
PF13949. ALIX_LYPXL_bnd. 1 hit.
PF03097. BRO1. 1 hit.
SMARTiView protein in SMART
SM01041. BRO1. 1 hit.
PROSITEiView protein in PROSITE
PS51180. BRO1. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8WUM4-1) [UniParc]FASTAAdd 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
MATFISVQLK KTSEVDLAKP LVKFIQQTYP SGGEEQAQYC RAAEELSKLR
60 70 80 90 100
RAAVGRPLDK HEGALETLLR YYDQICSIEP KFPFSENQIC LTFTWKDAFD
110 120 130 140 150
KGSLFGGSVK LALASLGYEK SCVLFNCAAL ASQIAAEQNL DNDEGLKIAA
160 170 180 190 200
KHYQFASGAF LHIKETVLSA LSREPTVDIS PDTVGTLSLI MLAQAQEVFF
210 220 230 240 250
LKATRDKMKD AIIAKLANQA ADYFGDAFKQ CQYKDTLPKE VFPVLAAKHC
260 270 280 290 300
IMQANAEYHQ SILAKQQKKF GEEIARLQHA AELIKTVASR YDEYVNVKDF
310 320 330 340 350
SDKINRALAA AKKDNDFIYH DRVPDLKDLD PIGKATLVKS TPVNVPISQK
360 370 380 390 400
FTDLFEKMVP VSVQQSLAAY NQRKADLVNR SIAQMREATT LANGVLASLN
410 420 430 440 450
LPAAIEDVSG DTVPQSILTK SRSVIEQGGI QTVDQLIKEL PELLQRNREI
460 470 480 490 500
LDESLRLLDE EEATDNDLRA KFKERWQRTP SNELYKPLRA EGTNFRTVLD
510 520 530 540 550
KAVQADGQVK ECYQSHRDTI VLLCKPEPEL NAAIPSANPA KTMQGSEVVN
560 570 580 590 600
VLKSLLSNLD EVKKEREGLE NDLKSVNFDM TSKFLTALAQ DGVINEEALS
610 620 630 640 650
VTELDRVYGG LTTKVQESLK KQEGLLKNIQ VSHQEFSKMK QSNNEANLRE
660 670 680 690 700
EVLKNLATAY DNFVELVANL KEGTKFYNEL TEILVRFQNK CSDIVFARKT
710 720 730 740 750
ERDELLKDLQ QSIAREPSAP SIPTPAYQSS PAGGHAPTPP TPAPRTMPPT
760 770 780 790 800
KPQPPARPPP PVLPANRAPS ATAPSPVGAG TAAPAPSQTP GSAPPPQAQG
810 820 830 840 850
PPYPTYPGYP GYCQMPMPMG YNPYAYGQYN MPYPPVYHQS PGQAPYPGPQ
860
QPSYPFPQPP QQSYYPQQ
Length:868
Mass (Da):96,023
Last modified:March 1, 2002 - v1
Checksum:i573588D1F612EC93
GO
Isoform 2 (identifier: Q8WUM4-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     239-239: K → KYFYFQ

Note: No experimental confirmation available.
Show »
Length:873
Mass (Da):96,772
Checksum:iFAC77FBE20C69D70
GO
Isoform 3 (identifier: Q8WUM4-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     240-271: EVFPVLAAKHCIMQANAEYHQSILAKQQKKFG → VSYCFYKHLLTLHVKYLDFFVYKKQVETYKEI
     272-868: Missing.

Show »
Length:271
Mass (Da):30,453
Checksum:iEDE1855B7AFA2275
GO

Sequence cautioni

The sequence BAA92092 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti580M → T in BAA92092 (PubMed:14702039).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_0689757V → M1 PublicationCorresponds to variant dbSNP:rs11554560Ensembl.1
Natural variantiVAR_053017309A → T1 PublicationCorresponds to variant dbSNP:rs3792594Ensembl.1
Natural variantiVAR_053018378V → I2 PublicationsCorresponds to variant dbSNP:rs3203777Ensembl.1
Natural variantiVAR_069765429G → S1 PublicationCorresponds to variant dbSNP:rs148256302Ensembl.1
Natural variantiVAR_053019550N → S2 PublicationsCorresponds to variant dbSNP:rs9813017Ensembl.1
Natural variantiVAR_053020638K → E. Corresponds to variant dbSNP:rs3183982Ensembl.1
Natural variantiVAR_024381730S → L1 PublicationCorresponds to variant dbSNP:rs1127732Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_044860239K → KYFYFQ in isoform 2. 1 Publication1
Alternative sequenceiVSP_057190240 – 271EVFPV…QKKFG → VSYCFYKHLLTLHVKYLDFF VYKKQVETYKEI in isoform 3. 1 PublicationAdd BLAST32
Alternative sequenceiVSP_057191272 – 868Missing in isoform 3. 1 PublicationAdd BLAST597

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF349951 mRNA. Translation: AAK20398.1.
GQ131806 mRNA. Translation: ACS12984.1.
AF151793 mRNA. Translation: AAF08220.1.
BT007367 mRNA. Translation: AAP36031.1.
AC112220 Genomic DNA. No translation available.
AC123901 Genomic DNA. No translation available.
BC020066 mRNA. Translation: AAH20066.1.
BC068454 mRNA. Translation: AAH68454.1.
AK002122 mRNA. Translation: BAA92092.1. Different initiation.
AB037796 mRNA. Translation: BAA92613.1.
CCDSiCCDS2660.1. [Q8WUM4-1]
CCDS54561.1. [Q8WUM4-2]
RefSeqiNP_001155901.1. NM_001162429.2. [Q8WUM4-2]
NP_001243121.1. NM_001256192.1. [Q8WUM4-3]
NP_037506.2. NM_013374.5. [Q8WUM4-1]
UniGeneiHs.475896.

Genome annotation databases

EnsembliENST00000307296; ENSP00000307387; ENSG00000170248. [Q8WUM4-1]
ENST00000457054; ENSP00000411825; ENSG00000170248. [Q8WUM4-2]
GeneIDi10015.
KEGGihsa:10015.
UCSCiuc003cfx.5. human. [Q8WUM4-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPDC6I_HUMAN
AccessioniPrimary (citable) accession number: Q8WUM4
Secondary accession number(s): C5MQH7
, E9PFU1, Q6NUS1, Q9BX86, Q9NUN0, Q9P2H2, Q9UKL5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: March 1, 2002
Last modified: November 22, 2017
This is version 168 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references