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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

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 appears to require the sequential function of ESCRT-O, -I,-II and -III complexes. The ESCRT machinery also functions in topologically equivalent membrane fission events, such as the terminal stages of cytokinesis and enveloped virus budding (HIV-1 and other lentiviruses). Appears to be an adapter for a subset of ESCRT-III proteins, such as CHMP4, to function at distinct membranes. Required for completion of cytokinesis. Involved in HIV-1 virus budding. Can replace TSG101 it its role of supporting HIV-1 release; this function implies the interaction with CHMP4B. 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).7 Publications

GO - Molecular functioni

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

GO - Biological processi

  • apoptotic process Source: UniProtKB-KW
  • cell cycle Source: UniProtKB-KW
  • cell separation after 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 transport Source: UniProtKB-KW
  • regulation of centrosome duplication Source: UniProtKB
  • regulation of extracellular exosome assembly Source: UniProtKB
  • ubiquitin-independent protein catabolic process via the multivesicular body sorting pathway Source: UniProtKB
  • viral budding via host ESCRT complex Source: UniProtKB
  • viral life cycle Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Apoptosis, 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

HGNCiHGNC:8766. PDCD6IP.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • endoplasmic reticulum exit site Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular vesicle Source: UniProtKB
  • focal adhesion Source: UniProtKB
  • immunological synapse Source: BHF-UCL
  • melanosome Source: UniProtKB-SubCell
  • membrane Source: UniProtKB
  • microtubule organizing center Source: UniProtKB-SubCell
  • myelin sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Secreted

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi199 – 1991F → D: Abolishes interaction with CHMP4B and abolishes rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication
Mutagenesisi212 – 2121I → D: Abolishes interaction with CHMP4A; impairs rescue of PTAP-type L domain-deficient HIV-1 p6; inhibits support of cytokinesis. 2 Publications
Mutagenesisi216 – 2161L → D: Abolishes interaction with CHMP4B and abolishes rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication
Mutagenesisi317 – 3171F → A: Diminishes rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication
Mutagenesisi318 – 3181I → A: Greatly diminishes rescue of PTAP-type L domain--deficient HIV-1 p6. 1 Publication
Mutagenesisi319 – 3191Y → A: Greatly diminishes rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications
Mutagenesisi319 – 3191Y → F: No effect on rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications
Mutagenesisi495 – 4951F → D: Impairs rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication
Mutagenesisi498 – 4981V → D: Reduces interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications
Mutagenesisi509 – 5091V → D: Abolishes interaction with HIV-1 p6; impairs rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications
Mutagenesisi512 – 5121C → A: No effect on interaction with HIV-1 p6; impairs rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication
Mutagenesisi676 – 6761F → A: Loss of interaction with SDCBP. 1 Publication
Mutagenesisi676 – 6761F → 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. 3 Publications
Mutagenesisi680 – 6801L → D: Impairs rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication
Mutagenesisi683 – 6831I → A: No effect on interaction with HIV-1 p6. 2 Publications
Mutagenesisi683 – 6831I → D: Reduces interaction with HIV-1 p6 and EIAV p9; abolishes rescue of PTAP-type L domain-deficient HIV-1 p6. 2 Publications
Mutagenesisi720 – 7201P → L: Abolishes interaction with TSG101; no effect on rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication
Mutagenesisi757 – 7582RP → AA: Abolishes interaction with SH3GL1 and SH3GL2; no effect on rescue of PTAP-type L domain-deficient HIV-1 p6. 1 Publication
Mutagenesisi800 – 8023GPP → AAA: Abolishes interaction with CEP55; inhibits support of cytokinesis. 1 Publication
Mutagenesisi801 – 8011P → A: Diminishes interaction with CEP55. 1 Publication
Mutagenesisi802 – 8021P → A: Diminishes interaction with CEP55. 1 Publication
Mutagenesisi806 – 8061Y → A: Abolishes interaction with CEP55. 1 Publication

Organism-specific databases

PharmGKBiPA33116.

Polymorphism and mutation databases

BioMutaiPDCD6IP.
DMDMi31076831.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedCombined sources1 Publication
Chaini2 – 868867Programmed cell death 6-interacting proteinPRO_0000218891Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanineCombined sources1 Publication
Modified residuei215 – 2151N6-acetyllysineCombined sources
Modified residuei479 – 4791PhosphothreonineCombined sources
Modified residuei481 – 4811PhosphoserineCombined sources
Modified residuei730 – 7301PhosphoserineCombined sources
Modified residuei738 – 7381PhosphothreonineCombined sources
Modified residuei741 – 7411PhosphothreonineCombined sources

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiQ8WUM4.
MaxQBiQ8WUM4.
PaxDbiQ8WUM4.
PeptideAtlasiQ8WUM4.
PRIDEiQ8WUM4.

2D gel databases

UCD-2DPAGEQ8WUM4.

PTM databases

iPTMnetiQ8WUM4.
PhosphoSiteiQ8WUM4.
SwissPalmiQ8WUM4.

Expressioni

Gene expression databases

BgeeiQ8WUM4.
CleanExiHS_PDCD6IP.
ExpressionAtlasiQ8WUM4. baseline and differential.
GenevisibleiQ8WUM4. HS.

Organism-specific databases

HPAiCAB016212.
HPA011905.

Interactioni

Subunit structurei

Interacts with SH3KBP1. Interacts with PDCD6 and TSG101 in a calcium-dependent manner. Interacts with and SGSM3. Self-associates. Interacts with CHMP4A; the interaction is direct. Interacts with CHMP4B; the interaction is direct. Interacts with CHMP4C; the interaction is direct. Interacts with HIV-1 p6. Interacts with EIAV p9; the interaction has been shown in vitro. Interacts with CEP55; the interaction is direct; CEP55 binds PDCD6IP in a 2:1 stoechiometry. May interact with PDGFRB. Interacts with SH3GL1 and SH3GL2. Interacts with murine leukemia virus Gag polyprotein (via LYPX(n)L motif). Interacts with murine leukemia virus Gag polyprotein (via LYPX(n)L motif). Interacts with SDCBP (PubMed:22660413). Forms a complex with SDCBP and SDC2 (PubMed:22660413).22 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P299913EBI-310624,EBI-8826747From a different organism.
CD2APQ9Y5K62EBI-310624,EBI-298152
CEP55D3DR373EBI-310624,EBI-10173536
CEP55Q53EZ49EBI-310624,EBI-747776
FYNP062416EBI-310624,EBI-515315
gagP033472EBI-310624,EBI-1220741From a different organism.
gagP697302EBI-310624,EBI-1220941From a different organism.
HCKP086314EBI-310624,EBI-346340
Hoxa1P090223EBI-310624,EBI-3957603From a different organism.
PDCD6O753405EBI-310624,EBI-352915

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. 111 interactions.
DIPiDIP-29327N.
IntActiQ8WUM4. 54 interactions.
MINTiMINT-4999333.
STRINGi9606.ENSP00000411825.

Structurei

Secondary structure

1
868
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi18 – 2811Combined sources
Beta strandi33 – 353Combined sources
Helixi39 – 5517Combined sources
Helixi62 – 7817Combined sources
Turni79 – 835Combined sources
Turni84 – 863Combined sources
Beta strandi93 – 964Combined sources
Beta strandi98 – 1003Combined sources
Beta strandi104 – 1063Combined sources
Beta strandi110 – 1145Combined sources
Helixi116 – 13621Combined sources
Beta strandi140 – 1423Combined sources
Helixi143 – 17028Combined sources
Beta strandi171 – 1733Combined sources
Turni177 – 1793Combined sources
Helixi181 – 20525Combined sources
Helixi210 – 23122Combined sources
Helixi241 – 26626Combined sources
Helixi270 – 29021Combined sources
Turni292 – 2943Combined sources
Helixi298 – 31720Combined sources
Helixi326 – 3283Combined sources
Beta strandi348 – 3503Combined sources
Turni354 – 3574Combined sources
Helixi361 – 39838Combined sources
Turni399 – 4024Combined sources
Helixi403 – 4064Combined sources
Beta strandi408 – 4125Combined sources
Helixi415 – 42612Combined sources
Turni427 – 4293Combined sources
Helixi430 – 47142Combined sources
Turni473 – 4753Combined sources
Helixi481 – 51434Combined sources
Helixi517 – 5237Combined sources
Helixi527 – 5326Combined sources
Helixi541 – 5433Combined sources
Helixi547 – 57529Combined sources
Helixi581 – 59010Combined sources
Beta strandi591 – 5933Combined sources
Helixi596 – 63944Combined sources
Helixi644 – 69754Combined sources
Beta strandi802 – 8054Combined sources
Turni810 – 8123Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-702.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ8WUM4.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini3 – 392390BRO1PROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni176 – 868693Interaction with EIAV p9Add
BLAST
Regioni176 – 503328Interaction with CHMP4A, CHMP4B and CHMP4CAdd
BLAST
Regioni418 – 868451Interaction with SDCBP1 PublicationAdd
BLAST
Regioni503 – 868366Self-associationAdd
BLAST
Regioni717 – 7204Interaction with TSG101
Regioni797 – 80610Interaction with CEP55
Regioni864 – 8685Essential to promote virus budding

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi717 – 860144Pro-richAdd
BLAST

Sequence similaritiesi

Contains 1 BRO1 domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG2220. Eukaryota.
ENOG410XQX6. LUCA.
GeneTreeiENSGT00780000121909.
HOGENOMiHOG000006938.
HOVERGENiHBG053533.
InParanoidiQ8WUM4.
KOiK12200.
OMAiQVKECYQ.
OrthoDBiEOG7V49XV.
PhylomeDBiQ8WUM4.
TreeFamiTF323502.

Family and domain databases

Gene3Di1.25.40.280. 1 hit.
InterProiIPR025304. ALIX_V_dom.
IPR004328. BRO1_dom.
[Graphical view]
PfamiPF13949. ALIX_LYPXL_bnd. 1 hit.
PF03097. BRO1. 1 hit.
[Graphical view]
SMARTiSM01041. BRO1. 1 hit.
[Graphical view]
PROSITEiPS51180. BRO1. 1 hit.
[Graphical view]

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 BAA92092.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti580 – 5801M → T in BAA92092 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti7 – 71V → M.1 Publication
Corresponds to variant rs11554560 [ dbSNP | Ensembl ].
VAR_068975
Natural varianti309 – 3091A → T.1 Publication
Corresponds to variant rs3792594 [ dbSNP | Ensembl ].
VAR_053017
Natural varianti378 – 3781V → I.2 Publications
Corresponds to variant rs3203777 [ dbSNP | Ensembl ].
VAR_053018
Natural varianti429 – 4291G → S.1 Publication
Corresponds to variant rs148256302 [ dbSNP | Ensembl ].
VAR_069765
Natural varianti550 – 5501N → S.2 Publications
Corresponds to variant rs9813017 [ dbSNP | Ensembl ].
VAR_053019
Natural varianti638 – 6381K → E.
Corresponds to variant rs3183982 [ dbSNP | Ensembl ].
VAR_053020
Natural varianti730 – 7301S → L.1 Publication
Corresponds to variant rs1127732 [ dbSNP | Ensembl ].
VAR_024381

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei239 – 2391K → KYFYFQ in isoform 2. 1 PublicationVSP_044860
Alternative sequencei240 – 27132EVFPV…QKKFG → VSYCFYKHLLTLHVKYLDFF VYKKQVETYKEI in isoform 3. 1 PublicationVSP_057190Add
BLAST
Alternative sequencei272 – 868597Missing in isoform 3. 1 PublicationVSP_057191Add
BLAST

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

Cross-referencesi

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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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. Positions 2-702.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi115332. 111 interactions.
DIPiDIP-29327N.
IntActiQ8WUM4. 54 interactions.
MINTiMINT-4999333.
STRINGi9606.ENSP00000411825.

PTM databases

iPTMnetiQ8WUM4.
PhosphoSiteiQ8WUM4.
SwissPalmiQ8WUM4.

Polymorphism and mutation databases

BioMutaiPDCD6IP.
DMDMi31076831.

2D gel databases

UCD-2DPAGEQ8WUM4.

Proteomic databases

EPDiQ8WUM4.
MaxQBiQ8WUM4.
PaxDbiQ8WUM4.
PeptideAtlasiQ8WUM4.
PRIDEiQ8WUM4.

Protocols and materials databases

DNASUi10015.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi10015.
GeneCardsiPDCD6IP.
H-InvDBHIX0163463.
HGNCiHGNC:8766. PDCD6IP.
HPAiCAB016212.
HPA011905.
MIMi608074. gene.
neXtProtiNX_Q8WUM4.
PharmGKBiPA33116.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2220. Eukaryota.
ENOG410XQX6. LUCA.
GeneTreeiENSGT00780000121909.
HOGENOMiHOG000006938.
HOVERGENiHBG053533.
InParanoidiQ8WUM4.
KOiK12200.
OMAiQVKECYQ.
OrthoDBiEOG7V49XV.
PhylomeDBiQ8WUM4.
TreeFamiTF323502.

Enzyme and pathway databases

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

Miscellaneous databases

ChiTaRSiPDCD6IP. human.
EvolutionaryTraceiQ8WUM4.
GeneWikiiPDCD6IP.
GenomeRNAii10015.
PROiQ8WUM4.
SOURCEiSearch...

Gene expression databases

BgeeiQ8WUM4.
CleanExiHS_PDCD6IP.
ExpressionAtlasiQ8WUM4. baseline and differential.
GenevisibleiQ8WUM4. HS.

Family and domain databases

Gene3Di1.25.40.280. 1 hit.
InterProiIPR025304. ALIX_V_dom.
IPR004328. BRO1_dom.
[Graphical view]
PfamiPF13949. ALIX_LYPXL_bnd. 1 hit.
PF03097. BRO1. 1 hit.
[Graphical view]
SMARTiSM01041. BRO1. 1 hit.
[Graphical view]
PROSITEiPS51180. BRO1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Overexpression of Hp95 induces G1 phase arrest in confluent HeLa cells."
    Wu Y., Pan S., Che S., He G., Nelman-Gonzalez M., Weil M.M., Kuang J.
    Differentiation 67:139-153(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-550.
  2. "Discovery of novel human transcript variants by analysis of intronic single-block EST with polyadenylation site."
    Wang P., Yu P., Gao P., Shi T., Ma D.
    BMC Genomics 10:518-518(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
  3. "Molecular cloning of human ALG-2 interacting protein 1 (AIP1)."
    Li H., Shioda T., Isselbacher K.J.
    Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-309 AND LEU-730.
  4. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  5. "The DNA sequence, annotation and analysis of human chromosome 3."
    Muzny D.M., Scherer S.E., Kaul R., Wang J., Yu J., Sudbrak R., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J.
    , Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Wei S., Wheeler D.A., Wright M.W., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clendenning J., Clerc-Blankenburg K.P., Chen R., Chen Z., Davis C., Delgado O., Dinh H.H., Dong W., Draper H., Ernst S., Fu G., Gonzalez-Garay M.L., Garcia D.K., Gillett W., Gu J., Hao B., Haugen E., Havlak P., He X., Hennig S., Hu S., Huang W., Jackson L.R., Jacob L.S., Kelly S.H., Kube M., Levy R., Li Z., Liu B., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Palmeiri A., Pasternak S., Perez L.M., Phelps K.A., Plopper F.J., Qiang B., Raymond C., Rodriguez R., Saenphimmachak C., Santibanez J., Shen H., Shen Y., Subramanian S., Tabor P.E., Verduzco D., Waldron L., Wang J., Wang J., Wang Q., Williams G.A., Wong G.K.-S., Yao Z., Zhang J., Zhang X., Zhao G., Zhou J., Zhou Y., Nelson D., Lehrach H., Reinhardt R., Naylor S.L., Yang H., Olson M., Weinstock G., Gibbs R.A.
    Nature 440:1194-1198(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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 AND 2), VARIANTS MET-7 AND ILE-378.
    Tissue: Lymph and Testis.
  7. Bienvenut W.V., Glen H., Frame M.C.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-23; 111-120; 216-229; 439-446; 457-469 AND 542-553, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Osteosarcoma.
  8. "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.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 209-868 (ISOFORM 1), VARIANT ILE-378.
    Tissue: Placenta.
  9. "Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
    DNA Res. 7:65-73(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 323-868 (ISOFORM 1), VARIANT SER-550.
    Tissue: Brain.
  10. "The ALG-2-interacting protein Alix associates with CHMP4b, a human homologue of yeast Snf7 that is involved in multivesicular body sorting."
    Katoh K., Shibata H., Suzuki H., Narai A., Ishidoh K., Kominami E., Yoshimori T., Maki M.
    J. Biol. Chem. 278:39104-39113(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHMP4A AND CHMP4B.
  11. "AIP1/ALIX is a binding partner for HIV-1 p6 and EIAV p9 functioning in virus budding."
    Strack B., Calistri A., Craig S., Popova E., Goettlinger H.G.
    Cell 114:689-699(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP4A; CHMP4B; CHMP4C; HIV-1 P6 AND EIAV P9.
  12. Cited for: FUNCTION IN HIV-1 BUDDING, SELF-ASSOCIATION, INTERACTION WITH TSG101; CHMP4A; CHMP4B CHMP4C, SUBCELLULAR LOCATION.
  13. "Divergent retroviral late-budding domains recruit vacuolar protein sorting factors by using alternative adaptor proteins."
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:12414-12419(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: SELF-ASSOCIATION, INTERACTION WITH TSG101; CHMP4A; CHMP4B; CHMP4C AND EIAV P9.
  14. Erratum
    Martin-Serrano J., Yarovoy A., Perez-Caballero D., Bieniasz P.D.
    Proc. Natl. Acad. Sci. U.S.A. 100:152845-152845(2003)
  15. "CHMP4b is a major binding partner of the ALG-2-interacting protein Alix among the three CHMP4 isoforms."
    Katoh K., Shibata H., Hatta K., Maki M.
    Arch. Biochem. Biophys. 421:159-165(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHMP4A; CHMP4B AND CHMP4C.
  16. "Structure and function of human Vps20 and Snf7 proteins."
    Peck J.W., Bowden E.T., Burbelo P.D.
    Biochem. J. 377:693-700(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CHMP4A; CHMP4B AND CHMP4C.
  17. Cited for: FUNCTION IN ENDOSOME ORGANIZATION.
  18. "Identification of Rab GTPase-activating protein-like protein (RabGAPLP) as a novel Alix/AIP1-interacting protein."
    Ichioka F., Horii M., Katoh K., Terasawa Y., Shibata H., Maki M.
    Biosci. Biotechnol. Biochem. 69:861-865(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH SGSM3, SUBCELLULAR LOCATION.
  19. "Tsg101 and Alix interact with murine leukemia virus Gag and cooperate with Nedd4 ubiquitin ligases during budding."
    Segura-Morales C., Pescia C., Chatellard-Causse C., Sadoul R., Bertrand E., Basyuk E.
    J. Biol. Chem. 280:27004-27012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH MURINE LEUKEMIA VIRUS GAG POLYPROTEIN.
  20. Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
    Tissue: Melanoma.
  21. "The Ca2+-binding protein ALG-2 is recruited to endoplasmic reticulum exit sites by Sec31A and stabilizes the localization of Sec31A."
    Yamasaki A., Tani K., Yamamoto A., Kitamura N., Komada M.
    Mol. Biol. Cell 17:4876-4887(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH PDCD6.
  22. "Human ESCRT and ALIX proteins interact with proteins of the midbody and function in cytokinesis."
    Morita E., Sandrin V., Chung H.Y., Morham S.G., Gygi S.P., Rodesch C.K., Sundquist W.I.
    EMBO J. 26:4215-4227(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CEP55 AND CD2AP, MUTAGENESIS OF ILE-212; PHE-676 AND 800-GLY--PRO-802.
  23. "Potent rescue of human immunodeficiency virus type 1 late domain mutants by ALIX/AIP1 depends on its CHMP4 binding site."
    Usami Y., Popov S., Goettlinger H.G.
    J. Virol. 81:6614-6622(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN HIV-1 BUDDING, INTERACTION WITH CHMP4B, MUTAGENESIS OF PHE-199; LEU-216; PHE-317; ILE-318 AND TYR-319.
  24. "Parallels between cytokinesis and retroviral budding: a role for the ESCRT machinery."
    Carlton J.G., Martin-Serrano J.
    Science 316:1908-1912(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN CYTOKINESIS, SUBCELLULAR LOCATION, INTERACTION WITH CEP55.
  25. "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human phospholipid scramblase 3: differential binding to an alternatively spliced isoform and amino acid-substituted mutants."
    Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T., Maki M.
    J. Biol. Chem. 283:9623-9632(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH PDCD6.
  26. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-730; THR-738 AND THR-741, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  27. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  28. "Penta-EF-hand protein ALG-2 functions as a Ca2+-dependent adaptor that bridges Alix and TSG101."
    Okumura M., Ichioka F., Kobayashi R., Suzuki H., Yoshida H., Shibata H., Maki M.
    Biochem. Biophys. Res. Commun. 386:237-241(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TSG101.
  29. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-215, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  30. "Mutation of tyrosine residue 857 in the PDGF beta-receptor affects cell proliferation but not migration."
    Wardega P., Heldin C.H., Lennartsson J.
    Cell. Signal. 22:1363-1368(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION, INTERACTION WITH PDGFRB.
  31. "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 THR-738 AND THR-741, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  32. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  33. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  34. Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH SDCBP, MUTAGENESIS OF PHE-676.
  35. "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 THR-479 AND SER-481, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma and Erythroleukemia.
  36. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  37. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  38. "Structural and biochemical studies of ALIX/AIP1 and its role in retrovirus budding."
    Fisher R.D., Chung H.Y., Zhai Q., Robinson H., Sundquist W.I., Hill C.P.
    Cell 128:841-852(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS) OF 1-698, INTERACTION WITH CHMP4A; HIV-1 P6; EIAV P9; TSG101; SH3GL1 AND SH3GL2, MUTAGENESIS OF ILE-212; TYR-319; PHE-495; VAL-498; VAL-509; PHE-676; LEU-680; ILE-683; PRO-720 AND 757-ARG-PRO-758.
  39. "Structural basis for viral late-domain binding to Alix."
    Lee S., Joshi A., Nagashima K., Freed E.O., Hurley J.H.
    Nat. Struct. Mol. Biol. 14:194-199(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.87 ANGSTROMS) OF 360-702, INTERACTION WITH HIV-1 P6, MUTAGENESIS OF VAL-498; VAL-509; CYS-512; PHE-676 AND ILE-683.
  40. "Structural and functional studies of ALIX interactions with YPX(n)L late domains of HIV-1 and EIAV."
    Zhai Q., Fisher R.D., Chung H.Y., Myszka D.G., Sundquist W.I., Hill C.P.
    Nat. Struct. Mol. Biol. 15:43-49(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 2-698 IN COMPLEX WITH HIV-1 P6, X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 2-698 IN COMPLEX WITH HIV-1 P9, INTERACTION WITH EIAV P9.
  41. Cited for: X-RAY CRYSTALLOGRAPHY (2.15 ANGSTROMS) OF 1-359 IN COMPLEX WITH CHMP4A, X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS) OF 1-359 IN COMPLEX WITH CHMP4B, X-RAY CRYSTALLOGRAPHY (2.02 ANGSTROMS) OF 1-359 IN COMPLEX WITH CHMP4C.
  42. "Midbody targeting of the ESCRT machinery by a noncanonical coiled coil in CEP55."
    Lee H.H., Elia N., Ghirlando R., Lippincott-Schwartz J., Hurley J.H.
    Science 322:576-580(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.00 ANGSTROMS) OF 797-809 IN COMPLEX WITH CEP55, MUTAGENESIS OF PRO-801; PRO-802 AND TYR-806.
  43. "Structural basis for Ca2+ -dependent formation of ALG-2/Alix peptide complex: Ca2+/EF3-driven arginine switch mechanism."
    Suzuki H., Kawasaki M., Inuzuka T., Okumura M., Kakiuchi T., Shibata H., Wakatsuki S., Maki M.
    Structure 16:1562-1573(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 799-812 IN COMPLEX WITH PDCD6.
  44. "Exome-sequencing confirms DNAJC5 mutations as cause of adult neuronal ceroid-lipofuscinosis."
    Benitez B.A., Alvarado D., Cai Y., Mayo K., Chakraverty S., Norton J., Morris J.C., Sands M.S., Goate A., Cruchaga C.
    PLoS ONE 6:E26741-E26741(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT SER-429.

Entry informationi

Entry nameiPDC6I_HUMAN
AccessioniPrimary (citable) accession number: Q8WUM4
Secondary accession number(s): C5MQH7
, E9PFU1, Q6NUS1, Q9BX86, Q9NUN0, Q9P2H2, Q9UKL5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 23, 2003
Last sequence update: March 1, 2002
Last modified: July 6, 2016
This is version 155 of the entry and version 1 of the sequence. [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
  6. 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.