Reviewed,
UniProtKB/Swiss-Prot O75832 (PSD10_HUMAN)
Last modified
December 16, 2008.
Version 80.
History...
Clusters with 100%,
90%,
50% identity |
Documents (4) |
Third-party data |
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Names and origin
| Protein names | Recommended name: 26S proteasome non-ATPase regulatory subunit 10 Alternative name(s): 26S proteasome regulatory subunit p28 Gankyrin | ||
| Gene names |
| ||
| Organism | Homo sapiens (Human) | ||
| Taxonomic identifier | 9606 [NCBI] | ||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 226 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence at protein level. |
General annotation (Comments)
| Function | Acts as a regulatory subunit of the 26S proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins. |
| Subunit structure | Component of the PA700 complex. |
| Sequence similarities | Contains 7 ANK repeats. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Proteasome |
| Domain | ANK repeat Repeat |
| PTM | Acetylation |
| Technical term | 3D-structure |
Gene Ontology (GO) | |
| Biological process | anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of ubiquitin-protein ligase activity during mitotic cell cycleInferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycleInferred from Experiment. Source: Reactome |
| Cellular component | cytoskeleton Inferred from direct assay. Source: HPA cytosolInferred from electronic annotation. Source: UniProtKB-KW proteasome regulatory particle Ref.1Traceable author statement. Source: ProtInc |
| Molecular function | protein binding Inferred from physical interaction. Source: IntAct |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| DOK2 | O60496 | 1 | EBI-752185,EBI-1046024 | |
| ELOVL1 | Q9BW60 | 1 | EBI-752185,EBI-1050331 | |
| HIST1H2BC | P62807 | 1 | EBI-752185,EBI-354552 | |
| MAGEA4 | P43358 | 4 | EBI-752185,EBI-743122 | |
| PAAF1 | Q9BRP4 | 1 | EBI-752185,EBI-1056358 | |
| PSMC1 | P62191 | 1 | EBI-752185,EBI-357598 | |
| PSMC2 | P35998 | 1 | EBI-752185,EBI-359710 | |
| PSMC3 | P17980 | 1 | EBI-752185,EBI-359720 | |
| PSMC4 | P43686 | 2 | EBI-752185,EBI-743997 | |
| PSMC5 | P62195 | 1 | EBI-752185,EBI-357745 | |
| PSMC6 | P62333 | 1 | EBI-752185,EBI-357669 | |
| PSMD1 | Q99460 | 1 | EBI-752185,EBI-357874 | |
| PSMD11 | O00231 | 1 | EBI-752185,EBI-357816 | |
| PSMD12 | O00232 | 1 | EBI-752185,EBI-359733 | |
| PSMD2 | Q13200 | 1 | EBI-752185,EBI-357648 | |
| PSMD3 | O43242 | 1 | EBI-752185,EBI-357622 | |
| PSMD4 | P55036 | 1 | EBI-752185,EBI-359318 | |
| PSMD6 | Q15008 | 1 | EBI-752185,EBI-359701 | |
| PSMD7 | P51665 | 1 | EBI-752185,EBI-357659 | |
| RB1 | P06400 | 1 | EBI-752185,EBI-491274 |
Sequence annotation (Features)
| Feature key | Position(s) | Length | Description | Graphical view | Feature identifier | |||||||||||||||||||||||||||||||||||
Molecule processing | ||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Chain | 1 – 226 | 226 | 26S proteasome non-ATPase regulatory subunit 10 | PRO_0000067045 | ||||||||||||||||||||||||||||||||||||
Regions | ||||||||||||||||||||||||||||||||||||||||
| Repeat | 3 – 36 | 34 | ANK 1 | |||||||||||||||||||||||||||||||||||||
| Repeat | 37 – 69 | 33 | ANK 2 | |||||||||||||||||||||||||||||||||||||
| Repeat | 70 – 102 | 33 | ANK 3 | |||||||||||||||||||||||||||||||||||||
| Repeat | 103 – 135 | 33 | ANK 4 | |||||||||||||||||||||||||||||||||||||
| Repeat | 136 – 168 | 33 | ANK 5 | |||||||||||||||||||||||||||||||||||||
| Repeat | 169 – 201 | 33 | ANK 6 | |||||||||||||||||||||||||||||||||||||
| Repeat | 202 – 226 | 25 | ANK 7 | |||||||||||||||||||||||||||||||||||||
Amino acid modifications | ||||||||||||||||||||||||||||||||||||||||
| Modified residue | 1 | 1 | N-acetylmethionine Ref.5 | |||||||||||||||||||||||||||||||||||||
Secondary structure | ||||||||||||||||||||||||||||||||||||||||
Helix Strand Turn | ||||||||||||||||||||||||||||||||||||||||
| Beta strand | 6 – 8 | 3 | ||||||||||||||||||||||||||||||||||||||
| Helix | 9 – 15 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 19 – 28 | 10 | ||||||||||||||||||||||||||||||||||||||
| Helix | 30 – 34 | 5 | ||||||||||||||||||||||||||||||||||||||
| Helix | 43 – 50 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 53 – 62 | 10 | ||||||||||||||||||||||||||||||||||||||
| Helix | 76 – 83 | 8 | ||||||||||||||||||||||||||||||||||||||
| Helix | 86 – 94 | 9 | ||||||||||||||||||||||||||||||||||||||
| Helix | 109 – 115 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 119 – 127 | 9 | ||||||||||||||||||||||||||||||||||||||
| Helix | 142 – 148 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 152 – 160 | 9 | ||||||||||||||||||||||||||||||||||||||
| Helix | 175 – 181 | 7 | ||||||||||||||||||||||||||||||||||||||
| Helix | 185 – 193 | 9 | ||||||||||||||||||||||||||||||||||||||
| Helix | 208 – 211 | 4 | ||||||||||||||||||||||||||||||||||||||
| Helix | 216 – 224 | 9 | ||||||||||||||||||||||||||||||||||||||
Sequences
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References
| « Hide 'large scale' references | |
| [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: 9714768] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. |
| [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. Tissue: Placenta. |
| [3] | "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. Bentley D.R.Nature 434:325-337(2005) [PubMed: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [4] | "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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Lung. |
| [5] | "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: 17323924] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, MASS SPECTROMETRY. |
| [6] | "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: 15379554] [Abstract] Cited for: STRUCTURE BY NMR, DOMAINS ANKYRIN REPEATS. |
| [7] | "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: 14573599] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), ANKYRIN REPEATS. |
| [8] | "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: 14997555] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-226. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| AB009619 mRNA. Translation: BAA33215.1. D83197 mRNA. Translation: BAA34594.1. AL031177 Genomic DNA. Translation: CAA20117.1. BC011960 mRNA. Translation: AAH11960.1. | |||||||||||||||||||||||||
| RefSeq | NP_002805.1. | ||||||||||||||||||||||||
| UniGene | Hs.522752 | ||||||||||||||||||||||||
3D structure databases | |||||||||||||||||||||||||
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| ModBase | Search... | ||||||||||||||||||||||||
Protein-protein interaction databases | |||||||||||||||||||||||||
| IntAct | O75832. 21 interactions. | ||||||||||||||||||||||||
PTM databases | |||||||||||||||||||||||||
| PhosphoSite | O75832. | ||||||||||||||||||||||||
2-D gel databases | |||||||||||||||||||||||||
| OGP | O75832. | ||||||||||||||||||||||||
Proteomic databases | |||||||||||||||||||||||||
| PRIDE | O75832. | ||||||||||||||||||||||||
Genome annotation databases | |||||||||||||||||||||||||
| Ensembl | ENSG00000101843. Homo sapiens. [Contig view] | ||||||||||||||||||||||||
| GeneID | 5716. | ||||||||||||||||||||||||
| KEGG | hsa:5716. | ||||||||||||||||||||||||
| NMPDR | fig|9606.3.peg.33217. | ||||||||||||||||||||||||
Organism-specific databases | |||||||||||||||||||||||||
| GeneCards | GC0XM107133. | ||||||||||||||||||||||||
| H-InvDB | HIX0016981. | ||||||||||||||||||||||||
| HGNC | HGNC:9555. PSMD10. | ||||||||||||||||||||||||
| HPA | CAB010434. HPA002920. | ||||||||||||||||||||||||
| MIM | 603480. gene. | ||||||||||||||||||||||||
| PharmGKB | PA33900. | ||||||||||||||||||||||||
| GenAtlas | Search... | ||||||||||||||||||||||||
Phylogenomic databases | |||||||||||||||||||||||||
| HOGENOM | O75832. | ||||||||||||||||||||||||
| HOVERGEN | O75832. | ||||||||||||||||||||||||
Enzyme and pathway databases | |||||||||||||||||||||||||
| Reactome | REACT_11045. Signaling by Wnt. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_9035. APC/C:Cdh1-mediated degradation of Skp2. | ||||||||||||||||||||||||
Gene expression databases | |||||||||||||||||||||||||
| ArrayExpress | O75832. | ||||||||||||||||||||||||
| CleanEx | HS_PSMD10. | ||||||||||||||||||||||||
| GermOnline | ENSG00000101843. Homo sapiens. | ||||||||||||||||||||||||
Family and domain databases | |||||||||||||||||||||||||
| InterPro | IPR002110. ANK. [Graphical view] | ||||||||||||||||||||||||
| Gene3D | G3DSA:1.25.40.20. ANK. 1 hit. | ||||||||||||||||||||||||
| Pfam | PF00023. Ank. 5 hits. [Graphical view] | ||||||||||||||||||||||||
| PRINTS | PR01415. ANKYRIN. | ||||||||||||||||||||||||
| SMART | SM00248. ANK. 5 hits. [Graphical view] | ||||||||||||||||||||||||
| PROSITE | PS50297. ANK_REP_REGION. 1 hit. PS50088. ANK_REPEAT. 5 hits. [Graphical view] | ||||||||||||||||||||||||
| ProtoNet | Search... | ||||||||||||||||||||||||
Other Resources | |||||||||||||||||||||||||
| LinkHub | O75832. | ||||||||||||||||||||||||
| NextBio | 22206. | ||||||||||||||||||||||||
| SOURCE | Search... | ||||||||||||||||||||||||
Entry information
| Entry name | PSD10_HUMAN | ||||||||
| Accession | Primary (citable) accession number: O75832 | ||||||||
| Entry history |
| ||||||||
| Entry status | Reviewed (UniProtKB/Swiss-Prot) | ||||||||
| Annotation project | HPI (Human Proteome Initiative) | ||||||||
Relevant documents
| Human chromosome X Human chromosome X: entries, gene names and cross-references to MIM |
| MIM cross-references Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot |
| PDB cross-references Index of Protein Data Bank (PDB) cross-references |
| SIMILARITY comments Index of protein domains and families |

Clusters with


