O00232 (PSD12_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
26S proteasome non-ATPase regulatory subunit 12

Alternative name(s):
26S proteasome regulatory subunit RPN5
26S proteasome regulatory subunit p55

Gene names

Name:

PSMD12

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	456 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 p55 family. Contains 1 PCI domain.
Sequence caution	The sequence AAH65826.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Proteasome
Coding sequence diversity	Polymorphism
PTM	Acetylation
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 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 viral reproduction Traceable author statement. Source: Reactome
Cellular component	cytosol Traceable author statement. Source: Reactome nucleoplasm Traceable author statement. Source: Reactome proteasome regulatory particle Traceable author statement. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.4
	Chain	2 – 456	455	26S proteasome non-ATPase regulatory subunit 12		PRO_0000173861
Regions
	Domain	237 – 417	181	PCI
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.4 Ref.6
	Modified residue	221	1	N6-acetyllysine Ref.7
	Modified residue	368	1	N6-acetyllysine Ref.7
	Modified residue	448	1	N6-acetyllysine Ref.7
Natural variations
	Natural variant	358	1	V → A. Corresponds to variant rs2230680 [ dbSNP | Ensembl ].		VAR_051558
Experimental info
	Sequence conflict	300	1	P → S in BAD96399. Ref.2
	Sequence conflict	398	1	V → D in BAD96399. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	O00232 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 97D0BDBDB0C96195	FASTA	456	52,904
	10 20 30 40 50 60 MADGGSERAD GRIVKMEVDY SATVDQRLPE CAKLAKEGRL QEVIETLLSL EKQTRTASDM 70 80 90 100 110 120 VSTSRILVAV VKMCYEAKEW DLLNENIMLL SKRRSQLKQA VAKMVQQCCT YVEEITDLPI 130 140 150 160 170 180 KLRLIDTLRM VTEGKIYVEI ERARLTKTLA TIKEQNGDVK EAASILQELQ VETYGSMEKK 190 200 210 220 230 240 ERVEFILEQM RLCLAVKDYI RTQIISKKIN TKFFQEENTE KLKLKYYNLM IQLDQHEGSY 250 260 270 280 290 300 LSICKHYRAI YDTPCIQAES EKWQQALKSV VLYVILAPFD NEQSDLVHRI SGDKKLEEIP 310 320 330 340 350 360 KYKDLLKLFT TMELMRWSTL VEDYGMELRK GSLESPATDV FGSTEEGEKR WKDLKNRVVE 370 380 390 400 410 420 HNIRIMAKYY TRITMKRMAQ LLDLSVDESE AFLSNLVVNK TIFAKVDRLA GIINFQRPKD 430 440 450 PNNLLNDWSQ KLNSLMSLVN KTTHLIAKEE MIHNLQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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].
[2]	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]. Tissue: Brain.
[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: Muscle and Testis.
[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 2-12, ACETYLATION AT ALA-2. Tissue: Platelet.
[5]	"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Embryonic kidney.
[6]	"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: 19413330] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[7]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-221; LYS-368 AND LYS-448, MASS SPECTROMETRY.
[8]	"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	AB003103 mRNA. Translation: BAA19749.1. AK222679 mRNA. Translation: BAD96399.1. BC019062 mRNA. Translation: AAH19062.1. BC065826 mRNA. Translation: AAH65826.1. Different initiation.
IPI	IPI00185374.
PIR	JC6523. PC6501.
RefSeq	NP_002807.1. NM_002816.3.
UniGene	Hs.592689.
3D structure databases
ProteinModelPortal	O00232.
SMR	O00232. Positions 348-423.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-27549N.
IntAct	O00232. 14 interactions.
MINT	MINT-5003729.
STRING	O00232.
PTM databases
PhosphoSite	O00232.
Proteomic databases
PeptideAtlas	O00232.
PRIDE	O00232.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000356126; ENSP00000348442; ENSG00000197170.
GeneID	5718.
KEGG	hsa:5718.
UCSC	uc002jfy.1. human.
Organism-specific databases
CTD	5718.
GeneCards	GC17M065334.
H-InvDB	HIX0014093.
HGNC	HGNC:9557. PSMD12.
HPA	HPA023119.
MIM	604450. gene.
neXtProt	NX_O00232.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG12703.
GeneTree	ENSGT00530000063471.
HOGENOM	HBG749871.
HOVERGEN	HBG053739.
InParanoid	O00232.
OMA	WDALNEN.
OrthoDB	EOG46DM2P.
PhylomeDB	O00232.
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	O00232.
Bgee	O00232.
CleanEx	HS_PSMD12.
Genevestigator	O00232.
GermOnline	ENSG00000197170. Homo sapiens.
Family and domain databases
InterPro	IPR000717. PCI_dom. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K03035.
Pfam	PF01399. PCI. 1 hit. [Graphical view]
SMART	SM00088. PINT. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	22216.
SOURCE	Search...

Entry information

Entry name

PSD12_HUMAN

Accession

Primary (citable) accession number: O00232
Secondary accession number(s): Q53HA2, Q6P053

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 15, 2002
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 103 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.