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O00231 (PSD11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
26S proteasome non-ATPase regulatory subunit 11
Alternative name(s):
26S proteasome regulatory subunit RPN6
26S proteasome regulatory subunit S9
26S proteasome regulatory subunit p44.5
Gene names
Name:PSMD11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length422 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Component of the lid subcomplex of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. In the complex, PSMD11 is required for proteasome assembly. Plays a key role in increased proteasome activity in embryonic stem cells (ESCs): its high expression in ESCs promotes enhanced assembly of the 26S proteasome, followed by higher proteasome activity. Ref.15

Subunit structure

Component of the lid subcomplex of the 19S proteasome regulatory particle complex (also named PA700 complex). The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. Ref.15

Subcellular location

Nucleus By similarity. Cytoplasmcytosol By similarity.

Tissue specificity

Highly expressed in embryonic stem cells (ESCs). Expression decreases as ESCs differentiate. Ref.15

Induction

By FOXO4; expression in embryonic stem cells (ESCs) is mediated by FOXO4. Ref.15

Post-translational modification

Phosphorylated by AMPK. Ref.12

Sequence similarities

Belongs to the proteasome subunit S9 family.

Contains 1 PCI domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityAlternative splicing
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

G1/S transition of mitotic cell cycle

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

proteasome assembly

Inferred from mutant phenotype Ref.15. Source: UniProtKB

protein polyubiquitination

Traceable author statement. Source: Reactome

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of cellular amino acid metabolic process

Traceable author statement. Source: Reactome

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

stem cell differentiation

Inferred from mutant phenotype Ref.15. Source: UniProtKB

ubiquitin-dependent protein catabolic process

Inferred from mutant phenotype Ref.15. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

proteasome accessory complex

Inferred from direct assay Ref.15. Source: UniProtKB

proteasome complex

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 23455924. Source: IntAct

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PRMT6Q96LA82EBI-357816,EBI-912440

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: O00231-1)

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.
Isoform 2 (identifier: O00231-2)

The sequence of this isoform differs from the canonical sequence as follows:
     375-375: H → HA
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7 Ref.8
Chain2 – 42242126S proteasome non-ATPase regulatory subunit 11
PRO_0000173857

Regions

Domain222 – 389168PCI

Amino acid modifications

Modified residue21N-acetylalanine Ref.8 Ref.11 Ref.14 Ref.16
Modified residue141Phosphoserine Ref.9 Ref.10

Natural variations

Alternative sequence3751H → HA in isoform 2.
VSP_044400

Experimental info

Mutagenesis141S → A: Does not affect phosphorylation by AMPK; when associated with A-79 and A-272. Ref.12
Mutagenesis791S → A: Does not affect phosphorylation by AMPK; when associated with A-14 and A-272. Ref.12
Mutagenesis2721S → A: Does not affect phosphorylation by AMPK; when associated with A14- and A-79. Ref.12
Sequence conflict1131C → S in AAB58732. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: CE113054CBEBDB05

FASTA42247,464
        10         20         30         40         50         60 
MAAAAVVEFQ RAQSLLSTDR EASIDILHSI VKRDIQENDE EAVQVKEQSI LELGSLLAKT 

        70         80         90        100        110        120 
GQAAELGGLL KYVRPFLNSI SKAKAARLVR SLLDLFLDME AATGQEVELC LECIEWAKSE 

       130        140        150        160        170        180 
KRTFLRQALE ARLVSLYFDT KRYQEALHLG SQLLRELKKM DDKALLVEVQ LLESKTYHAL 

       190        200        210        220        230        240 
SNLPKARAAL TSARTTANAI YCPPKLQATL DMQSGIIHAA EEKDWKTAYS YFYEAFEGYD 

       250        260        270        280        290        300 
SIDSPKAITS LKYMLLCKIM LNTPEDVQAL VSGKLALRYA GRQTEALKCV AQASKNRSLA 

       310        320        330        340        350        360 
DFEKALTDYR AELRDDPIIS THLAKLYDNL LEQNLIRVIE PFSRVQIEHI SSLIKLSKAD 

       370        380        390        400        410        420 
VERKLSQMIL DKKFHGILDQ GEGVLIIFDE PPVDKTYEAA LETIQNMSKV VDSLYNKAKK 


LT 

« Hide

Isoform 2 [UniParc].

Checksum: BDE786518637385D
Show »

FASTA42347,535

References

« Hide 'large scale' references
[1]"Molecular cloning and expression of subunit 9 of the 26S proteasome."
Hoffman L., Rechsteiner M.
FEBS Lett. 404:179-184(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), PARTIAL PROTEIN SEQUENCE.
[2]"cDNA cloning and functional analysis of p44.5 and p55, two regulatory subunits of the 26S proteasome."
Saito A., Watanabe T.K., Shimada Y., Fujiwara T., Slaughter C.A., DeMartino G.N., Tanahashi N., Tanaka K.
Gene 203:241-250(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[3]"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. expand/collapse author list , 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 1).
Tissue: Heart.
[4]Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Pancreas.
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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] (ISOFORM 1).
Tissue: Lung.
[7]"Exploring proteomes and analyzing protein processing by mass spectrometric identification of sorted N-terminal peptides."
Gevaert K., Goethals M., Martens L., Van Damme J., Staes A., Thomas G.R., Vandekerckhove J.
Nat. Biotechnol. 21:566-569(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 2-11.
Tissue: Platelet.
[8]Bienvenut W.V., Potts A., Brablan J., Quadroni M.
Submitted (JUL-2004) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 2-11, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: B-cell lymphoma.
[9]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Two-hybrid analysis identifies PSMD11, a non-ATPase subunit of the proteasome, as a novel interaction partner of AMP-activated protein kinase."
Moreno D., Viana R., Sanz P.
Int. J. Biochem. Cell Biol. 41:2431-2439(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION, MUTAGENESIS OF SER-14; SER-79 AND SER-272.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]"Increased proteasome activity in human embryonic stem cells is regulated by PSMD11."
Vilchez D., Boyer L., Morantte I., Lutz M., Merkwirth C., Joyce D., Spencer B., Page L., Masliah E., Berggren W.T., Gage F.H., Dillin A.
Nature 489:304-308(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, TISSUE SPECIFICITY, INDUCTION.
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF001212 mRNA. Translation: AAB58732.1.
AB003102 mRNA. Translation: BAA19748.1.
AK290602 mRNA. Translation: BAF83291.1.
AK223196 mRNA. Translation: BAD96916.1.
CH471147 Genomic DNA. Translation: EAW80229.1.
CH471147 Genomic DNA. Translation: EAW80230.1.
BC000437 mRNA. Translation: AAH00437.1.
BC004430 mRNA. Translation: AAH04430.1.
CCDSCCDS11272.1. [O00231-1]
PIRJC6524.
RefSeqNP_001257411.1. NM_001270482.1. [O00231-1]
NP_002806.2. NM_002815.3. [O00231-1]
UniGeneHs.443379.

3D structure databases

ProteinModelPortalO00231.
SMRO00231. Positions 38-390.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111689. 107 interactions.
IntActO00231. 48 interactions.
MINTMINT-1154929.
STRING9606.ENSP00000261712.

PTM databases

PhosphoSiteO00231.

2D gel databases

OGPO00231.

Proteomic databases

MaxQBO00231.
PaxDbO00231.
PRIDEO00231.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000261712; ENSP00000261712; ENSG00000108671. [O00231-1]
ENST00000457654; ENSP00000393185; ENSG00000108671. [O00231-1]
GeneID5717.
KEGGhsa:5717.
UCSCuc002hhm.4. human. [O00231-1]

Organism-specific databases

CTD5717.
GeneCardsGC17P030771.
HGNCHGNC:9556. PSMD11.
HPAHPA042275.
MIM604449. gene.
neXtProtNX_O00231.
PharmGKBPA33902.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5159.
HOVERGENHBG053738.
InParanoidO00231.
KOK03036.
OMANLDMQSG.
OrthoDBEOG7F24T1.
PhylomeDBO00231.
TreeFamTF106230.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

ArrayExpressO00231.
BgeeO00231.
CleanExHS_PSMD11.
GenevestigatorO00231.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
1.25.40.10. 1 hit.
InterProIPR013143. PAM.
IPR000717. PCI_dom.
IPR011990. TPR-like_helical.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF01399. PCI. 1 hit.
[Graphical view]
SMARTSM00753. PAM. 1 hit.
SM00088. PINT. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPSMD11.
GenomeRNAi5717.
NextBio22212.
PROO00231.
SOURCESearch...

Entry information

Entry namePSD11_HUMAN
AccessionPrimary (citable) accession number: O00231
Secondary accession number(s): A8K3I7 expand/collapse secondary AC list , E1P663, O00495, Q53FT5
Entry history
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: January 23, 2007
Last modified: July 9, 2014
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM