Reviewed, UniProtKB/Swiss-Prot O00231 (PSD11_HUMAN)

Names and origin

Protein names

Recommended name:
    26S proteasome non-ATPase regulatory subunit 11
Alternative name(s):
    26S proteasome regulatory subunit S9
    26S proteasome regulatory subunit p44.5

Gene names

Name:

PSMD11

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	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	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	Belongs to the proteasome subunit S9 family. Contains 1 PCI domain.

Ontologies

Keywords
Cellular component	Proteasome
PTM	Acetylation Phosphoprotein
Technical term	Direct protein sequencing
Gene Ontology (GO)
Biological process	anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Inferred from Experiment. Source: Reactome negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle Inferred from Experiment. Source: Reactome
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW proteasome complex Ref.1 Traceable author statement. Source: ProtInc
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
PAAF1	Q9BRP4	1	EBI-357816,EBI-1056358
PSMC4	P43686	1	EBI-357816,EBI-743997
PSMD10	O75832	1	EBI-357816,EBI-752185
PSMD6	Q15008	1	EBI-357816,EBI-359701

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4 Ref.5
	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.5 Ref.7
	Modified residue	14	1	Phosphoserine Ref.7 Ref.8
	Modified residue	79	1	Phosphoserine Ref.7
	Modified residue	272	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	113	1	C → S in AAB58732. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	O00231-1 [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

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: 9119060] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], 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: 9426256] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"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.
[4]	"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: 12665801] [Abstract] Cited for: PROTEIN SEQUENCE OF 2-11. Tissue: Platelet.
[5]	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.
[6]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-272, MASS SPECTROMETRY. Tissue: Epithelium.
[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-14 AND SER-79, ACETYLATION AT ALA-2, MASS SPECTROMETRY.
[8]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-14, MASS SPECTROMETRY.
[9]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	AF001212 mRNA. Translation: AAB58732.1. AB003102 mRNA. Translation: BAA19748.1. BC000437 mRNA. Translation: AAH00437.1. BC004430 mRNA. Translation: AAH04430.1.
IPI	IPI00105598.
PIR	JC6524.
RefSeq	NP_002806.2.
UniGene	Hs.655396
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	O00231. 32 interactions.
PTM databases
PhosphoSite	O00231.
2-D gel databases
OGP	O00231.
Proteomic databases
PRIDE	O00231.
Genome annotation databases
Ensembl	ENSG00000108671. Homo sapiens. [Contig view]
GeneID	5717.
KEGG	hsa:5717.
Organism-specific databases
GeneCards	GC17P027795.
H-InvDB	HIX0013704.
HGNC	HGNC:9556. PSMD11.
MIM	604449. gene.
PharmGKB	PA33902.
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	O00231.
OMA	O00231. HAADERD.
Enzyme and pathway databases
Reactome	REACT_11045. Signaling by Wnt. REACT_13. Metabolism of amino acids. REACT_13635. Regulation of activated PAK-2p34 by proteasome mediated degradation. 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_9035. APC/C:Cdh1-mediated degradation of Skp2.
Gene expression databases
ArrayExpress	O00231.
Bgee	O00231.
CleanEx	HS_PSMD11.
GermOnline	ENSG00000108671. Homo sapiens.
Family and domain databases
InterPro	IPR013143. PAM. IPR000717. PCI. IPR011991. Wing_hlx_DNA_bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
Pfam	PF01399. PCI. 1 hit. [Graphical view]
SMART	SM00753. PAM. 1 hit. SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	22212.
SOURCE	Search...

Entry information

Entry name

PSD11_HUMAN

Accession

Primary (citable) accession number: O00231
Secondary accession number(s): O00495

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2002
Last sequence update:	January 23, 2007
Last modified:	June 16, 2009
This is version 81 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)