O00231 (PSD11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	422 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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.13
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.13
Subcellular location	Nucleus By similarity. Cytoplasm › cytosol By similarity.
Tissue specificity	Highly expressed in embryonic stem cells (ESCs). Expression decreases as ESCs differentiate. Ref.13
Induction	By FOXO4; expression in embryonic stem cells (ESCs) is mediated by FOXO4. Ref.13
Post-translational modification	Phosphorylated by AMPK. Ref.11
Sequence similarities	Belongs to the proteasome subunit S9 family. Contains 1 PCI domain.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Alternative splicing
PTM	Acetylation 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 exogenous peptide antigen via MHC class I, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome gene expression 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 proteasome assembly Inferred from mutant phenotype Ref.13. 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 small molecule metabolic process Traceable author statement. Source: Reactome stem cell differentiation Inferred from mutant phenotype Ref.13. Source: UniProtKB viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome accessory complex Inferred from direct assay Ref.13. Source: UniProtKB
Complete GO annotation...

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7 Ref.8
	Chain	2 – 422	421	26S proteasome non-ATPase regulatory subunit 11		PRO_0000173857
Regions
	Domain	222 – 389	168	PCI
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.8
	Modified residue	14	1	Phosphoserine Ref.9 Ref.10
Natural variations
	Alternative sequence	375	1	H → HA in isoform 2.		VSP_044400
Experimental info
	Mutagenesis	14	1	S → A: Does not affect phosphorylation by AMPK; when associated with A-79 and A-272. Ref.11
	Mutagenesis	79	1	S → A: Does not affect phosphorylation by AMPK; when associated with A-14 and A-272. Ref.11
	Mutagenesis	272	1	S → A: Does not affect phosphorylation by AMPK; when associated with A14- and A-79. Ref.11
	Sequence conflict	113	1	C → S in AAB58732. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: CE113054CBEBDB05	FASTA	422	47,464
	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
	Isoform 2 [UniParc]. Checksum: BDE786518637385D	FASTA	423	47,535
	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 DKKFHAGILD QGEGVLIIFD EPPVDKTYEA ALETIQNMSK VVDSLYNKAK KLT

References

	« Hide 'large scale' referencesShow '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. , 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. , 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, 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"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.
[12]	"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].
[13]	"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.
+	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.
IPI	IPI00105598.
PIR	JC6524.
RefSeq	NP_001257411.1. NM_001270482.1. NP_002806.2. NM_002815.3.
UniGene	Hs.443379.
3D structure databases
ProteinModelPortal	O00231.
ModBase	Search...
Protein-protein interaction databases
IntAct	O00231. 37 interactions.
MINT	MINT-1154929.
STRING	9606.ENSP00000261712.
PTM databases
PhosphoSite	O00231.
2D gel databases
OGP	O00231.
Proteomic databases
PaxDb	O00231.
PRIDE	O00231.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000261712; ENSP00000261712; ENSG00000108671. ENST00000457654; ENSP00000393185; ENSG00000108671.
GeneID	5717.
KEGG	hsa:5717.
UCSC	uc002hhm.3. human.
Organism-specific databases
CTD	5717.
GeneCards	GC17P030771.
HGNC	HGNC:9556. PSMD11.
HPA	HPA042275.
MIM	604449. gene.
neXtProt	NX_O00231.
PharmGKB	PA33902.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG5159.
HOVERGEN	HBG053738.
InParanoid	O00231.
KO	K03036.
OMA	SGILDQG.
OrthoDB	EOG41RPV3.
PhylomeDB	O00231.
Enzyme and pathway databases
Reactome	REACT_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
ArrayExpress	O00231.
Bgee	O00231.
CleanEx	HS_PSMD11.
Genevestigator	O00231.
GermOnline	ENSG00000108671. Homo sapiens.
Family and domain databases
Gene3D	1.10.10.10. 1 hit. 1.25.40.10. 1 hit.
InterPro	IPR013143. PAM. IPR000717. PCI_dom. IPR011990. TPR-like_helical. IPR011991. WHTH_DNA-bd_dom. [Graphical view]
Pfam	PF01399. PCI. 1 hit. [Graphical view]
SMART	SM00753. PAM. 1 hit. SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	5717.
NextBio	22212.
SOURCE	Search...

Entry information

Entry name

PSD11_HUMAN

Accession

Primary (citable) accession number: O00231
Secondary accession number(s): A8K3I7 , E1P663, O00495, Q53FT5

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2002
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 120 of the entry and version 3 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.