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UniProtKB/Swiss-Prot entry O75832


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name PSD10_HUMAN
Primary accession number O75832
Secondary accession numbers None
Integrated into Swiss-Prot on May 10, 2002
Sequence was last modified on November 1, 1998 (Sequence version 1)
Annotations were last modified on    September 23, 2008 (Entry version 77)
Name and origin of the protein
Protein name 26S proteasome non-ATPase regulatory subunit 10
Synonyms 26S proteasome regulatory subunit p28
Gankyrin
Gene name
Name: PSMD10
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA].
DOI=10.1016/S0378-1119(98)00309-6; PubMed=9714768 [NCBI, ExPASy, EBI, Israel, Japan]
Hori T., Kato S., Saeki M., DeMartino G.N., Slaughter C.A., Takeuchi J., Toh-e A., Tanaka K.;
"cDNA cloning and functional analysis of p28 (Nas6p) and p40.5 (Nas7p), two novel regulatory subunits of the 26S proteasome.";
Gene 216:113-122(1998).
[2]
NUCLEOTIDE SEQUENCE.
TISSUE=Placenta;
Higashitsuji H., Fujita J.;
"Enhanced expression of a novel tumour marker in the human hepatomas.";
Submitted (JAN-1996) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature03440; PubMed=15772651 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence of the human X chromosome.";
Nature 434:325-337(2005).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
DOI=10.1021/bi061994u; PubMed=17323924 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[6]
STRUCTURE BY NMR, AND DOMAINS ANKYRIN REPEATS.
DOI=10.1021/bi049116o; PubMed=15379554 [NCBI, ExPASy, EBI, Israel, Japan]
Yuan C., Li J., Mahajan A., Poi M.J., Byeon I.-J., Tsai M.-D.;
"Solution structure of the human oncogenic protein gankyrin containing seven ankyrin repeats and analysis of its structure--function relationship.";
Biochemistry 43:12152-12161(2004).
[7]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), AND ANKYRIN REPEATS.
DOI=10.1074/jbc.M310265200; PubMed=14573599 [NCBI, ExPASy, EBI, Israel, Japan]
Krzywda S., Brzozowski A.M., Higashitsuji H., Fujita J., Welchman R., Dawson S., Mayer R.J., Wilkinson A.J.;
"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.";
J. Biol. Chem. 279:1541-1545(2004).
[8]
X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 2-226.
DOI=10.1002/prot.20028; PubMed=14997555 [NCBI, ExPASy, EBI, Israel, Japan]
Manjasetty B.A., Quedenau C., Sievert V., Bussow K., Niesen F., Delbruck H., Heinemann U.;
"X-ray structure of human gankyrin, the product of a gene linked to hepatocellular carcinoma.";
Proteins 55:214-217(2004).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AB009619; BAA33215.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
D83197; BAA34594.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL031177; CAA20117.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC011960; AAH11960.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_002805.1; -.
UniGene Hs.522752
3D structure databases
PDB
1QYM; X-ray; 2.80 A; A=2-226.[ExPASy / RCSB / EBI]
1TR4; NMR; -; A=1-226.[ExPASy / RCSB / EBI]
1UOH; X-ray; 2.00 A; A=1-226.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 1QYM; -.
1TR4; -.
1UOH; -.
ModBase O75832.
Protein-protein interaction databases
IntAct 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.
2D gel databases
OGP O75832; -.
Organism-specific databases
H-InvDB HIX0016981; -.
HGNC HGNC:9555; PSMD10.
GenAtlas PSMD10.
HPA CAB010434; -.
HPA002920; -.
MIM 603480; gene. [NCBI / EBI]
PharmGKB PA33900; -.
GeneCards O75832.
Gene expression databases
ArrayExpress O75832; -.
CleanEx HS_PSMD10; -.
GermOnline ENSG00000101843; Homo sapiens.
Ontologies
GO
GO:0005838; Cellular component: proteasome regulatory particle (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR002110; ANK.
Graphical view of domain structure.
Gene3D G3DSA:1.25.40.20; ANK; 1.
Pfam PF00023; Ank; 5.
Pfam graphical view of domain structure.
PRINTS PR01415; ANKYRIN.
SMART SM00248; ANK; 5.
SMART graphical view of domain structure.
PROSITE PS50297; ANK_REP_REGION; 1.
PS50088; ANK_REPEAT; 5.
PROSITE graphical view of domain structure (profiles).
BLOCKS O75832.
Genome annotation databases
Ensembl ENSG00000101843; Homo sapiens. [Contig view]
GeneID 5716; -.
KEGG hsa:5716; -.
NMPDR fig|9606.3.peg.33217; -.
Phylogenomic databases
HOGENOM O75832; -.
HOVERGEN O75832; -.
Other
LinkHub O75832; -.
SOURCE PSMD10; Homo sapiens.
ProtoNet O75832.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Acetylation; ANK repeat; Proteasome; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   226  226     26S proteasome non-ATPase regulatory subunit 10. PRO_0000067045
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. 
MOD_RES   1     1        N-acetylmethionine. 
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      
Sequence information
Length: 226 AA [This is the length of the unprocessed precursor] Molecular weight: 24428 Da [This is the MW of the unprocessed precursor] CRC64: 57158E33146EC7C8 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MEGCVSNLMV CNLAYSGKLE ELKESILADK SLATRTDQDS RTALHWACSA GHTEIVEFLL 

        70         80         90        100        110        120 
QLGVPVNDKD DAGWSPLHIA ASAGRDEIVK ALLGKGAQVN AVNQNGCTPL HYAASKNRHE 

       130        140        150        160        170        180 
IAVMLLEGGA NPDAKDHYEA TAMHRAAAKG NLKMIHILLY YKASTNIQDT EGNTPLHLAC 

       190        200        210        220 
DEERVEEAKL LVSQGASIYI ENKEEKTPLQ VAKGGLGLIL KRMVEG 

O75832 in FASTA format

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