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O00487 (PSDE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 124. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
26S proteasome non-ATPase regulatory subunit 14

EC=3.4.19.-
Alternative name(s):
26S proteasome regulatory subunit RPN11
26S proteasome-associated PAD1 homolog 1
Gene names
Name:PSMD14
Synonyms:POH1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length310 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Metalloprotease component of the 26S proteasome that specifically cleaves 'Lys-63'-linked polyubiquitin chains. The 26S proteasome is involved in the ATP-dependent degradation of ubiquitinated proteins. Plays a role in response to double-strand breaks (DSBs): acts as a regulator of non-homologous end joining (NHEJ) by cleaving 'Lys-63'-linked polyubiquitin, thereby promoting retention of JMJD2A/KDM4A on chromatin and restricting TP53BP1 accumulation. Also involved in homologous recombination repair by promoting RAD51 loading. Ref.1 Ref.8 Ref.12

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. Interacts with TXNL1. Ref.8 Ref.9 Ref.12

Tissue specificity

Widely expressed. Highest levels in heart and skeletal muscle. Ref.1

Sequence similarities

Belongs to the peptidase M67A family. PSMD14 subfamily.

Contains 1 MPN (JAB/Mov34) domain.

Ontologies

Keywords
   Biological processDNA damage
DNA repair
Ubl conjugation pathway
   Cellular componentProteasome
   LigandMetal-binding
Zinc
   Molecular functionHydrolase
Metalloprotease
Protease
   PTMPhosphoprotein
   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

double-strand break repair via homologous recombination

Inferred from mutant phenotype Ref.12. Source: UniProtKB

double-strand break repair via nonhomologous end joining

Inferred from mutant phenotype Ref.12. Source: UniProtKB

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 endopeptidase activity

Inferred from mutant phenotype PubMed 18162577. Source: GOC

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

Traceable author statement. Source: Reactome

protein K63-linked deubiquitination

Inferred from mutant phenotype Ref.12. 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 proteasomal protein catabolic process

Inferred from mutant phenotype PubMed 18162577. Source: UniProtKB

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

ubiquitin-dependent protein catabolic process

Traceable author statement Ref.1. Source: UniProtKB

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleoplasm

Traceable author statement. Source: Reactome

proteasome accessory complex

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome complex

Traceable author statement Ref.8. Source: UniProtKB

proteasome regulatory particle, lid subcomplex

Inferred from mutant phenotype Ref.12. Source: UniProtKB

   Molecular_functionendopeptidase activator activity

Inferred from mutant phenotype PubMed 18162577. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

metallopeptidase activity

Traceable author statement Ref.8. Source: UniProtKB

proteasome binding

Inferred from direct assay PubMed 18162577. Source: UniProtKB

ubiquitin thiolesterase activity

Inferred from mutant phenotype Ref.12. Source: UniProtKB

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 31031026S proteasome non-ATPase regulatory subunit 14
PRO_0000213952

Regions

Domain26 – 139114MPN
Motif113 – 12614JAMM motif

Sites

Metal binding1131Zinc; catalytic Probable
Metal binding1151Zinc; catalytic Probable
Metal binding1261Zinc; catalytic By similarity

Amino acid modifications

Modified residue1501Phosphoserine Ref.7
Modified residue2241Phosphoserine Ref.6

Experimental info

Mutagenesis113 – 1153HSH → ASA: Abolishes ubiquitin thioesterase activity, leading to prevent maintenance of JMJD2A/KDM4A on chromatin. Ref.12

Sequences

Sequence LengthMass (Da)Tools
O00487 [UniParc].

Last modified July 1, 1997. Version 1.
Checksum: 18ACE876C7682039

FASTA31034,577
        10         20         30         40         50         60 
MDRLLRLGGG MPGLGQGPPT DAPAVDTAEQ VYISSLALLK MLKHGRAGVP MEVMGLMLGE 

        70         80         90        100        110        120 
FVDDYTVRVI DVFAMPQSGT GVSVEAVDPV FQAKMLDMLK QTGRPEMVVG WYHSHPGFGC 

       130        140        150        160        170        180 
WLSGVDINTQ QSFEALSERA VAVVVDPIQS VKGKVVIDAF RLINANMMVL GHEPRQTTSN 

       190        200        210        220        230        240 
LGHLNKPSIQ ALIHGLNRHY YSITINYRKN ELEQKMLLNL HKKSWMEGLT LQDYSEHCKH 

       250        260        270        280        290        300 
NESVVKEMLE LAKNYNKAVE EEDKMTPEQL AIKNVGKQDP KRHLEEHVDV LMTSNIVQCL 

       310 
AAMLDTVVFK 

« Hide

References

« Hide 'large scale' references
[1]"Resistance to diverse drugs and ultraviolet light conferred by overexpression of a novel human 26 S proteasome subunit."
Spataro V., Toda T., Craig R., Seeger M., Dubiel W., Harris A.L., Norbury C.
J. Biol. Chem. 272:30470-30475(1997) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY.
Tissue: Lung.
[2]"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].
Tissue: Brain.
[3]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].
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Testis.
[5]Lubec G., Afjehi-Sadat L.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 199-208, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[6]"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-224, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[7]"Quantitative phosphoproteome profiling of Wnt3a-mediated signaling network: indicating the involvement of ribonucleoside-diphosphate reductase M2 subunit phosphorylation at residue serine 20 in canonical Wnt signal transduction."
Tang L.-Y., Deng N., Wang L.-S., Dai J., Wang Z.-L., Jiang X.-S., Li S.-J., Li L., Sheng Q.-H., Wu D.-Q., Li L., Zeng R.
Mol. Cell. Proteomics 6:1952-1967(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"K63-specific deubiquitination by two JAMM/MPN+ complexes: BRISC-associated Brcc36 and proteasomal Poh1."
Cooper E.M., Cutcliffe C., Kristiansen T.Z., Pandey A., Pickart C.M., Cohen R.E.
EMBO J. 28:621-631(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PROBABLE FUNCTION, IDENTIFICATION IN THE PROTEASOME.
[9]"Thioredoxin Txnl1/TRP32 is a redox-active cofactor of the 26 S proteasome."
Andersen K.M., Madsen L., Prag S., Johnsen A.H., Semple C.A., Hendil K.B., Hartmann-Petersen R.
J. Biol. Chem. 284:15246-15254(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TXNL1.
[10]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"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].
[12]"The proteasomal de-ubiquitinating enzyme POH1 promotes the double-strand DNA break response."
Butler L.R., Densham R.M., Jia J., Garvin A.J., Stone H.R., Shah V., Weekes D., Festy F., Beesley J., Morris J.R.
EMBO J. 31:3918-3934(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE PROTEASOME, MUTAGENESIS OF 113-HIS--HIS-115.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
U86782 mRNA. Translation: AAC51866.1.
AK055128 mRNA. Translation: BAG51474.1.
CH471058 Genomic DNA. Translation: EAX11370.1.
BC066336 mRNA. Translation: AAH66336.1.
RefSeqNP_005796.1. NM_005805.5.
UniGeneHs.740477.

3D structure databases

ProteinModelPortalO00487.
SMRO00487. Positions 26-310.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid115508. 57 interactions.
IntActO00487. 23 interactions.
MINTMINT-5003743.
STRING9606.ENSP00000386541.

Chemistry

BindingDBO00487.
ChEMBLCHEMBL2007629.

Protein family/group databases

MEROPSM67.001.

PTM databases

PhosphoSiteO00487.

2D gel databases

OGPO00487.
REPRODUCTION-2DPAGEIPI00024821.

Proteomic databases

PaxDbO00487.
PeptideAtlasO00487.
PRIDEO00487.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000409682; ENSP00000386541; ENSG00000115233.
GeneID10213.
KEGGhsa:10213.
UCSCuc002ubu.3. human.

Organism-specific databases

CTD10213.
GeneCardsGC02P162164.
HGNCHGNC:16889. PSMD14.
HPAHPA002114.
MIM607173. gene.
neXtProtNX_O00487.
PharmGKBPA134957776.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG1310.
HOGENOMHOG000183690.
HOVERGENHBG053742.
InParanoidO00487.
KOK03030.
OMAQDPKKHL.
OrthoDBEOG7T7GTF.
PhylomeDBO00487.
TreeFamTF105748.

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

ArrayExpressO00487.
BgeeO00487.
CleanExHS_PSMD14.
GenevestigatorO00487.

Family and domain databases

InterProIPR000555. JAMM/MPN+_dom.
IPR024969. Rpn11/EIF3F_C.
[Graphical view]
PfamPF01398. JAB. 1 hit.
PF13012. MitMem_reg. 1 hit.
[Graphical view]
SMARTSM00232. JAB_MPN. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiPSMD14.
GenomeRNAi10213.
NextBio38668.
PROO00487.
SOURCESearch...

Entry information

Entry namePSDE_HUMAN
AccessionPrimary (citable) accession number: O00487
Secondary accession number(s): B3KNW2, O00176
Entry history
Integrated into UniProtKB/Swiss-Prot: August 31, 2004
Last sequence update: July 1, 1997
Last modified: April 16, 2014
This is version 124 of the entry and version 1 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

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM