O00487 (PSDE_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

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	310 AA.
Sequence status	Complete.
Protein existence	Evidence 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. The function of the 'Lys-63'-specific deubiquitination of the proteasome is unclear. Ref.1 Ref.9
Subunit structure	Component of the 19S regulatory cap of the 26S proteasome.
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 process	Ubl conjugation pathway
Cellular component	Proteasome
Ligand	Metal-binding Zinc
Molecular function	Hydrolase Metalloprotease Protease
PTM	Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA 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 M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle 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 peptide antigen via MHC class I Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome mRNA metabolic 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 protein K63-linked deubiquitination Traceable author statement Ref.9. 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. Source: UniProtKB viral reproduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome complex Traceable author statement Ref.9. Source: UniProtKB
Molecular function	endopeptidase activator activity Inferred from mutant phenotype. Source: UniProtKB metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW metallopeptidase activity Traceable author statement Ref.9. Source: UniProtKB proteasome binding Inferred from direct assay. Source: UniProtKB ubiquitin thiolesterase activity Traceable author statement Ref.9. Source: UniProtKB
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 310	310	26S proteasome non-ATPase regulatory subunit 14		PRO_0000213952
Regions
	Domain	26 – 139	114	MPN
	Motif	113 – 126	14	JAMM motif
Sites
	Metal binding	113	1	Zinc; catalytic Probable
	Metal binding	115	1	Zinc; catalytic Probable
	Metal binding	126	1	Zinc; catalytic By similarity
Amino acid modifications
	Modified residue	32	1	Phosphotyrosine Ref.6
	Modified residue	150	1	Phosphoserine Ref.8
	Modified residue	224	1	Phosphoserine Ref.7

Sequences

	Sequence		Length	Mass (Da)
	O00487 [UniParc]. Last modified July 1, 1997. Version 1. Checksum: 18ACE876C7682039	FASTA	310	34,577
	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

References

	« Hide 'large scale' referencesShow '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: 9374539] [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. , 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: 14702039] [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. , 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: 15489334] [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, MASS SPECTROMETRY. Tissue: Brain and Cajal-Retzius cell.
[6]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-32, MASS SPECTROMETRY.
[7]	"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[8]	"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: 17693683] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-150, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[9]	"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: 19214193] [Abstract] Cited for: PROBABLE FUNCTION, IDENTIFICATION IN THE PROTEASOME.
[10]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	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.
IPI	IPI00024821.
RefSeq	NP_005796.1. NM_005805.4.
UniGene	Hs.567410.
3D structure databases
ProteinModelPortal	O00487.
SMR	O00487. Positions 31-165.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00487. 21 interactions.
STRING	O00487.
Protein family/group databases
MEROPS	M67.001.
PTM databases
PhosphoSite	O00487.
2D gel databases
OGP	O00487.
REPRODUCTION-2DPAGE	IPI00024821.
Proteomic databases
PeptideAtlas	O00487.
PRIDE	O00487.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000409682; ENSP00000386541; ENSG00000115233.
GeneID	10213.
KEGG	hsa:10213.
UCSC	uc002ubu.1. human.
Organism-specific databases
CTD	10213.
GeneCards	GC02P162164.
H-InvDB	HIX0002542.
HGNC	HGNC:16889. PSMD14.
HPA	HPA002114.
MIM	607173. gene.
neXtProt	NX_O00487.
PharmGKB	PA134957776.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG05900.
HOGENOM	HBG499867.
HOVERGEN	HBG053742.
InParanoid	O00487.
OMA	QDPKKHL.
OrthoDB	EOG4R23V7.
PhylomeDB	O00487.
Enzyme and pathway databases
Reactome	REACT_111102. Signal Transduction. REACT_111217. Metabolism. REACT_13505. Proteasome mediated degradation of PAK-2p34. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. REACT_578. Apoptosis. REACT_6185. HIV Infection. REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A. REACT_6900. Immune System.
Gene expression databases
ArrayExpress	O00487.
Bgee	O00487.
CleanEx	HS_PSMD14.
Genevestigator	O00487.
GermOnline	ENSG00000115233. Homo sapiens.
Family and domain databases
InterPro	IPR000555. Mov34_MPN_PAD1. [Graphical view]
KO	K03030.
Pfam	PF01398. Mov34. 1 hit. [Graphical view]
SMART	SM00232. JAB_MPN. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	38668.
SOURCE	Search...

Entry information

Entry name

PSDE_HUMAN

Accession

Primary (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:	January 25, 2012
This is version 99 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.