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Reviewed, UniProtKB/Swiss-Prot O75832 (PSD10_HUMAN)

Last modified December 16, 2008. Version 80. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    26S proteasome non-ATPase regulatory subunit 10
Alternative name(s):
    26S proteasome regulatory subunit p28
    Gankyrin
Gene names
Name: PSMD10
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length226 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence 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.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 22622626S proteasome non-ATPase regulatory subunit 10
PRO_0000067045

Regions

Repeat3 – 3634ANK 1
Repeat37 – 6933ANK 2
Repeat70 – 10233ANK 3
Repeat103 – 13533ANK 4
Repeat136 – 16833ANK 5
Repeat169 – 20133ANK 6
Repeat202 – 22625ANK 7

Amino acid modifications

Modified residue11N-acetylmethionine Ref.5

Secondary structure

................................ 226
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75832-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 57158E33146EC7C8

FASTA22624,428
        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 

« Hide

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. expand/collapse author list , 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: 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.
RefSeqNP_002805.1.
UniGeneHs.522752

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1QYMX-ray2.80A2-226[»]
1TR4NMR-A1-226[»]
1UOHX-ray2.00A1-226[»]
ModBaseSearch...

Protein-protein interaction databases

IntActO75832. 21 interactions.

PTM databases

PhosphoSiteO75832.

2-D gel databases

OGPO75832.

Proteomic databases

PRIDEO75832.

Genome annotation databases

EnsemblENSG00000101843. Homo sapiens. [Contig view]
GeneID5716.
KEGGhsa:5716.
NMPDRfig|9606.3.peg.33217.

Organism-specific databases

GeneCardsGC0XM107133.
H-InvDBHIX0016981.
HGNCHGNC:9555. PSMD10.
HPACAB010434.
HPA002920.
MIM603480. gene.
PharmGKBPA33900.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO75832.
HOVERGENO75832.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressO75832.
CleanExHS_PSMD10.
GermOnlineENSG00000101843. Homo sapiens.

Family and domain databases

InterProIPR002110. ANK.
[Graphical view]
Gene3DG3DSA:1.25.40.20. ANK. 1 hit.
PfamPF00023. Ank. 5 hits.
[Graphical view]
PRINTSPR01415. ANKYRIN.
SMARTSM00248. ANK. 5 hits.
[Graphical view]
PROSITEPS50297. ANK_REP_REGION. 1 hit.
PS50088. ANK_REPEAT. 5 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

LinkHubO75832.
NextBio22206.
SOURCESearch...

Entry information

Entry namePSD10_HUMAN
AccessionPrimary (citable) accession number: O75832
Entry history
Integrated into UniProtKB/Swiss-Prot: May 10, 2002
Last sequence update: November 1, 1998
Last modified: December 16, 2008
This is version 80 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (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

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents