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Protein

26S proteasome non-ATPase regulatory subunit 10

Gene

PSMD10

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

Functioni

Acts as a chaperone during the assembly of the 26S proteasome, specifically of the PA700/19S regulatory complex (RC). In the initial step of the base subcomplex assembly is part of an intermediate PSMD10:PSMC4:PSMC5:PAAF1 module which probably assembles with a PSMD5:PSMC2:PSMC1:PSMD2 module. Independently of the proteasome, regulates EGF-induced AKT activation through inhibition of the RHOA/ROCK/PTEN pahway, leading to prolonged AKT activation. Plays an important role in RAS-induced tumorigenesis.
Acts as an proto-oncoprotein by being involved in negative regulation of tumor suppressors RB1 and p53/TP53. Overexpression is leading to phosphorylation of RB1 and proteasomal degradation of RB1. Regulates CDK4-mediated phosphorylation of RB1 by competing with CDKN2A for binding with CDK4. Facilitates binding of MDM2 to p53/TP53 and the mono- and polyubiquitination of p53/TP53 by MDM2 suggesting a function in targeting the TP53:MDM2 complex to the 26S proteasome. Involved in p53-independent apoptosis. Involved in regulation of NF-kappa-B by retaining it in the cytoplasm. Binds to the NF-kappa-B component RELA and accelerates its XPO1/CRM1-mediated nuclear export.

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Chaperone

Keywords - Biological processi

Apoptosis

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S proteasome non-ATPase regulatory subunit 10
Alternative name(s):
26S proteasome regulatory subunit p28
Gankyrin
p28(GANK)
Gene namesi
Name:PSMD10
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:9555. PSMD10.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • intermediate filament cytoskeleton Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome regulatory particle Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi182 – 1821E → A: Abolishes interaction with RB1. 1 Publication

Organism-specific databases

PharmGKBiPA33900.

Chemistry

ChEMBLiCHEMBL2331054.

Polymorphism and mutation databases

BioMutaiPSMD10.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 22622626S proteasome non-ATPase regulatory subunit 10PRO_0000067045Add
BLAST

Proteomic databases

EPDiO75832.
MaxQBiO75832.
PaxDbiO75832.
PRIDEiO75832.
TopDownProteomicsiO75832-1. [O75832-1]

2D gel databases

OGPiO75832.

PTM databases

iPTMnetiO75832.
PhosphoSiteiO75832.

Expressioni

Tissue specificityi

Tends to be up-regulated in cancer cells with RAS mutations, including lung cancers and adenocarconimas (at protein level).2 Publications

Gene expression databases

BgeeiO75832.
CleanExiHS_PSMD10.
ExpressionAtlasiO75832. baseline and differential.
GenevisibleiO75832. HS.

Organism-specific databases

HPAiCAB010434.
HPA002920.

Interactioni

Subunit structurei

Part of transient complex containing PSMD10, PSMC4, PSMC5 and PAAF1 formed during the assembly of the 26S proteasome. Stays associated throughout the assembly of the PA700/19S RC and is released upon association with the 20S core. Interacts with PSMC4. Interacts with RB1. Interacts with CDK4. Interacts with MDM2. Interacts with RELA. Associates with a CDK4:CCND2 serine/threonine kinase complex. Interacts with ARHGDIA and increases the interaction between ARHGDIA and RHOA, hence promotes ARHGDIA inactivation of RHOA and ROCK.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
MAGEA4P433585EBI-752185,EBI-743122
PSMC4P4368613EBI-752185,EBI-743997

GO - Molecular functioni

  • transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi111688. 65 interactions.
DIPiDIP-39026N.
IntActiO75832. 23 interactions.
MINTiMINT-254757.
STRINGi9606.ENSP00000217958.

Structurei

Secondary structure

1
226
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 83Combined sources
Helixi9 – 157Combined sources
Helixi19 – 2810Combined sources
Helixi30 – 345Combined sources
Turni38 – 403Combined sources
Helixi43 – 508Combined sources
Helixi53 – 6210Combined sources
Beta strandi71 – 733Combined sources
Helixi76 – 838Combined sources
Helixi86 – 949Combined sources
Helixi109 – 1157Combined sources
Helixi119 – 1279Combined sources
Helixi142 – 1487Combined sources
Helixi152 – 1609Combined sources
Helixi175 – 1817Combined sources
Helixi185 – 1939Combined sources
Helixi208 – 2114Combined sources
Helixi216 – 2249Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QYMX-ray2.80A2-226[»]
1TR4NMR-A1-226[»]
1UOHX-ray2.00A1-226[»]
4NIKX-ray2.50A1-226[»]
ProteinModelPortaliO75832.
SMRiO75832. Positions 4-226.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75832.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati3 – 3634ANK 1Add
BLAST
Repeati37 – 6933ANK 2Add
BLAST
Repeati70 – 10233ANK 3Add
BLAST
Repeati103 – 13533ANK 4Add
BLAST
Repeati136 – 16833ANK 5Add
BLAST
Repeati169 – 20133ANK 6Add
BLAST
Repeati202 – 22625ANK 7Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 7171Interaction with RB1Add
BLAST
Regioni1 – 3737Required for nuclear localizationAdd
BLAST
Regioni39 – 226188Interaction with RELAAdd
BLAST
Regioni171 – 22656Interaction with RB1Add
BLAST

Sequence similaritiesi

Contains 7 ANK repeats.PROSITE-ProRule annotation

Keywords - Domaini

ANK repeat, Repeat

Phylogenomic databases

eggNOGiKOG4412. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129743.
HOGENOMiHOG000158359.
HOVERGENiHBG053737.
InParanoidiO75832.
KOiK06694.
OMAiCSAGHTN.
OrthoDBiEOG7B5WX7.
PhylomeDBiO75832.
TreeFamiTF106234.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75832-1) [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
MEGCVSNLMV CNLAYSGKLE ELKESILADK SLATRTDQDS RTALHWACSA
60 70 80 90 100
GHTEIVEFLL QLGVPVNDKD DAGWSPLHIA ASAGRDEIVK ALLGKGAQVN
110 120 130 140 150
AVNQNGCTPL HYAASKNRHE IAVMLLEGGA NPDAKDHYEA TAMHRAAAKG
160 170 180 190 200
NLKMIHILLY YKASTNIQDT EGNTPLHLAC DEERVEEAKL LVSQGASIYI
210 220
ENKEEKTPLQ VAKGGLGLIL KRMVEG
Length:226
Mass (Da):24,428
Last modified:November 1, 1998 - v1
Checksum:i57158E33146EC7C8
GO
Isoform 2 (identifier: O75832-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     150-226: GNLKMIHILL...GLILKRMVEG → DT

Show »
Length:151
Mass (Da):16,137
Checksum:iBEA968FE1439F3CC
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti196 – 1961A → T in AAV38495 (Ref. 5) Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei150 – 22677GNLKM…RMVEG → DT in isoform 2. 2 PublicationsVSP_043043Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009619 mRNA. Translation: BAA33215.1.
D83197 mRNA. Translation: BAA34594.1.
AY057056 mRNA. Translation: AAL25260.1.
AK295996 mRNA. Translation: BAG58771.1.
BT019689 mRNA. Translation: AAV38495.1.
AL031177 Genomic DNA. Translation: CAA20117.1.
AL031177 Genomic DNA. Translation: CAI43131.1.
BC011960 mRNA. Translation: AAH11960.1.
CCDSiCCDS14536.1. [O75832-1]
CCDS14537.1. [O75832-2]
RefSeqiNP_002805.1. NM_002814.3. [O75832-1]
NP_736606.1. NM_170750.2. [O75832-2]
UniGeneiHs.522752.

Genome annotation databases

EnsembliENST00000217958; ENSP00000217958; ENSG00000101843. [O75832-1]
ENST00000361815; ENSP00000354906; ENSG00000101843. [O75832-2]
GeneIDi5716.
KEGGihsa:5716.
UCSCiuc004enp.3. human. [O75832-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB009619 mRNA. Translation: BAA33215.1.
D83197 mRNA. Translation: BAA34594.1.
AY057056 mRNA. Translation: AAL25260.1.
AK295996 mRNA. Translation: BAG58771.1.
BT019689 mRNA. Translation: AAV38495.1.
AL031177 Genomic DNA. Translation: CAA20117.1.
AL031177 Genomic DNA. Translation: CAI43131.1.
BC011960 mRNA. Translation: AAH11960.1.
CCDSiCCDS14536.1. [O75832-1]
CCDS14537.1. [O75832-2]
RefSeqiNP_002805.1. NM_002814.3. [O75832-1]
NP_736606.1. NM_170750.2. [O75832-2]
UniGeneiHs.522752.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1QYMX-ray2.80A2-226[»]
1TR4NMR-A1-226[»]
1UOHX-ray2.00A1-226[»]
4NIKX-ray2.50A1-226[»]
ProteinModelPortaliO75832.
SMRiO75832. Positions 4-226.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111688. 65 interactions.
DIPiDIP-39026N.
IntActiO75832. 23 interactions.
MINTiMINT-254757.
STRINGi9606.ENSP00000217958.

Chemistry

ChEMBLiCHEMBL2331054.

PTM databases

iPTMnetiO75832.
PhosphoSiteiO75832.

Polymorphism and mutation databases

BioMutaiPSMD10.

2D gel databases

OGPiO75832.

Proteomic databases

EPDiO75832.
MaxQBiO75832.
PaxDbiO75832.
PRIDEiO75832.
TopDownProteomicsiO75832-1. [O75832-1]

Protocols and materials databases

DNASUi5716.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217958; ENSP00000217958; ENSG00000101843. [O75832-1]
ENST00000361815; ENSP00000354906; ENSG00000101843. [O75832-2]
GeneIDi5716.
KEGGihsa:5716.
UCSCiuc004enp.3. human. [O75832-1]

Organism-specific databases

CTDi5716.
GeneCardsiPSMD10.
HGNCiHGNC:9555. PSMD10.
HPAiCAB010434.
HPA002920.
MIMi300880. gene.
neXtProtiNX_O75832.
PharmGKBiPA33900.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4412. Eukaryota.
COG0666. LUCA.
GeneTreeiENSGT00840000129743.
HOGENOMiHOG000158359.
HOVERGENiHBG053737.
InParanoidiO75832.
KOiK06694.
OMAiCSAGHTN.
OrthoDBiEOG7B5WX7.
PhylomeDBiO75832.
TreeFamiTF106234.

Enzyme and pathway databases

ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPSMD10. human.
EvolutionaryTraceiO75832.
GeneWikiiPSMD10.
GenomeRNAii5716.
NextBioi22206.
PROiO75832.
SOURCEiSearch...

Gene expression databases

BgeeiO75832.
CleanExiHS_PSMD10.
ExpressionAtlasiO75832. baseline and differential.
GenevisibleiO75832. HS.

Family and domain databases

Gene3Di1.25.40.20. 2 hits.
InterProiIPR002110. Ankyrin_rpt.
IPR020683. Ankyrin_rpt-contain_dom.
[Graphical view]
PfamiPF00023. Ank. 1 hit.
PF12796. Ank_2. 2 hits.
[Graphical view]
PRINTSiPR01415. ANKYRIN.
SMARTiSM00248. ANK. 5 hits.
[Graphical view]
SUPFAMiSSF48403. SSF48403. 1 hit.
PROSITEiPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits of the 26S proteasome."
    Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A., Takeuchi J., Toh-e A., Tanaka K.
    Gene 216:113-122(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Enhanced expression of a novel tumour marker in the human hepatomas."
    Higashitsuji H., Fujita J.
    Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Placenta.
  3. "Involvement of p28-II in hepatocellular carcinoma."
    Wang H., Fu X., Wu M.
    Submitted (SEP-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Liver.
  4. "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] (ISOFORM 2).
    Tissue: Subthalamic nucleus.
  5. "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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  6. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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] (ISOFORM 1).
    Tissue: Lung.
  8. "Reduced stability of retinoblastoma protein by gankyrin, an oncogenic ankyrin-repeat protein overexpressed in hepatomas."
    Higashitsuji H., Itoh K., Nagao T., Dawson S., Nonoguchi K., Kido T., Mayer R.J., Arii S., Fujita J.
    Nat. Med. 6:96-99(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS POTENTIAL PROTO-ONCOGENE, INTERACTION WITH RB1, TISSUE SPECIFICITY, MUTAGENESIS OF GLU-182.
  9. "Novel insights into the INK4-CDK4/6-Rb pathway: counter action of gankyrin against INK4 proteins regulates the CDK4-mediated phosphorylation of Rb."
    Li J., Tsai M.D.
    Biochemistry 41:3977-3983(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDK4.
  10. "Gankyrin is an ankyrin-repeat oncoprotein that interacts with CDK4 kinase and the S6 ATPase of the 26 S proteasome."
    Dawson S., Apcher S., Mee M., Higashitsuji H., Baker R., Uhle S., Dubiel W., Fujita J., Mayer R.J.
    J. Biol. Chem. 277:10893-10902(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PSMC4.
  11. "The oncoprotein gankyrin binds to MDM2/HDM2, enhancing ubiquitylation and degradation of p53."
    Higashitsuji H., Higashitsuji H., Itoh K., Sakurai T., Nagao T., Sumitomo Y., Masuda T., Dawson S., Shimada Y., Mayer R.J., Fujita J.
    Cancer Cell 8:75-87(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN DEGRADATION OF TP53, INTERACTION WITH MDM2.
  12. "Mass spectrometric characterization of the affinity-purified human 26S proteasome complex."
    Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.
    Biochemistry 46:3553-3565(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  13. "Oncoprotein p28 GANK binds to RelA and retains NF-kappaB in the cytoplasm through nuclear export."
    Chen Y., Li H.H., Fu J., Wang X.F., Ren Y.B., Dong L.W., Tang S.H., Liu S.Q., Wu M.C., Wang H.Y.
    Cell Res. 17:1020-1029(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN REGULATION OF NF-KAPPA-B, INTERACTION WITH RELY, SUBCELLULAR LOCATION.
  14. "Assembly pathway of the Mammalian proteasome base subcomplex is mediated by multiple specific chaperones."
    Kaneko T., Hamazaki J., Iemura S., Sasaki K., Furuyama K., Natsume T., Tanaka K., Murata S.
    Cell 137:914-925(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION AS PROTEASOME CHAPERONE, SUBUNIT.
  15. "Involvement of the mitochondrial pathway in p53-independent apoptosis induced by p28GANK knockdown in Hep3B cells."
    Wang J., Wang X.F., Zhang L.G., Xie S.Y., Li Z.L., Li Y.J., Li H.H., Jiao F.
    Cytogenet. Genome Res. 125:87-97(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN APOPTOSIS.
  16. "Gankyrin plays an essential role in Ras-induced tumorigenesis through regulation of the RhoA/ROCK pathway in mammalian cells."
    Man J.H., Liang B., Gu Y.X., Zhou T., Li A.L., Li T., Jin B.F., Bai B., Zhang H.Y., Zhang W.N., Li W.H., Gong W.L., Li H.Y., Zhang X.M.
    J. Clin. Invest. 120:2829-2841(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN AKT ACTIVATION, INTERACTION WITH ARHGDIA, TISSUE SPECIFICITY.
  17. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  18. "Solution structure of the human oncogenic protein gankyrin containing seven ankyrin repeats and analysis of its structure-function relationship."
    Yuan C., Li J., Mahajan A., Poi M.J., Byeon I.-J., Tsai M.-D.
    Biochemistry 43:12152-12161(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR, DOMAINS ANK REPEATS.
  19. "The crystal structure of gankyrin, an oncoprotein found in complexes with cyclin-dependent kinase 4, a 19 S proteasomal ATPase regulator, and the tumor suppressors Rb and p53."
    Krzywda S., Brzozowski A.M., Higashitsuji H., Fujita J., Welchman R., Dawson S., Mayer R.J., Wilkinson A.J.
    J. Biol. Chem. 279:1541-1545(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), DOMAIN ANK REPEATS.
  20. "X-ray structure of human gankyrin, the product of a gene linked to hepatocellular carcinoma."
    Manjasetty B.A., Quedenau C., Sievert V., Bussow K., Niesen F., Delbruck H., Heinemann U.
    Proteins 55:214-217(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-226.

Entry informationi

Entry nameiPSD10_HUMAN
AccessioniPrimary (citable) accession number: O75832
Secondary accession number(s): Q5U0B2, Q8IZK9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: November 1, 1998
Last modified: May 11, 2016
This is version 164 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

Caution

Was initially identified as a genuine component of the 26S proteasome.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.