26S proteasome non-ATPase regulatory subunit 2

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Reviewed, UniProtKB/Swiss-Prot Q13200 (PSMD2_HUMAN)

Last modified November 25, 2008. Version 84. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    26S proteasome non-ATPase regulatory subunit 2
Alternative name(s):
    26S proteasome regulatory subunit RPN1
    26S proteasome regulatory subunit S2
    26S proteasome subunit p97
    Tumor necrosis factor type 1 receptor-associated protein 2
    55.11 protein

Gene names

Name:	PSMD2
Synonyms:	TRAP2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	908 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function

Acts as a regulatory subunit of the 26 proteasome which is involved in the ATP-dependent degradation of ubiquitinated proteins.

Binds to the intracellular domain of tumor necrosis factor type 1 receptor. The binding domain of TRAP1 and TRAP2 resides outside the death domain of TNFR1.

Tissue specificity

Found in skeletal muscle, liver, heart, brain, kidney, pancreas, lung and placenta.

Sequence similarities

Belongs to the proteasome subunit S2 family.

Contains 7 PC repeats.

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Ontologies

Keywords
Cellular component	Proteasome
Domain	Repeat
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 regulation of protein catabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	cytosol Inferred from electronic annotation. Source: UniProtKB-KW proteasome regulatory particle Ref.1 Traceable author statement. Source: ProtInc
Molecular function	enzyme regulator activity Inferred from electronic annotation. Source: InterPro protein binding Inferred from physical interaction. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct
MCC	P23508	1	EBI-357648,EBI-307531
NDRG1	Q92597	1	EBI-357648,EBI-716486
NEK6	Q9HC98	1	EBI-357648,EBI-740364
PAAF1	Q9BRP4	1	EBI-357648,EBI-1056358
PSMC4	P43686	1	EBI-357648,EBI-743997
PSMD10	O75832	1	EBI-357648,EBI-752185
PSMD6	Q15008	1	EBI-357648,EBI-359701
WDR8	Q9P2S5	1	EBI-357648,EBI-1054904

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 908

908

26S proteasome non-ATPase regulatory subunit 2

PRO_0000173810

Regions

Repeat

409 – 442

PC 1

Repeat

443 – 479

PC 2

Repeat

480 – 514

PC 3

Repeat

517 – 551

PC 4

Repeat

560 – 589

PC 5

Repeat

692 – 723

PC 6

Repeat

742 – 757

PC 7

Compositional bias

623 – 641

Glu/Lys-rich

Amino acid modifications

Modified residue

N-acetylmethionine

Modified residue

Phosphoserine

Modified residue

Phosphothreonine

Modified residue

361

Phosphoserine

Experimental info

Sequence conflict

P → R in CAA60167. Ref.4

Sequence conflict

P → S Ref.3

Sequence conflict

E → G Ref.3

Sequence conflict

Q → L Ref.3

Sequence conflict

E → V Ref.3

Sequence conflict

V → A in BAA11226. Ref.1

Sequence conflict

226

Y → S in AAA87705. Ref.3

Sequence conflict

260

S → T in CAA60167. Ref.4

Sequence conflict

281 – 283

IFT → SS in AAA87705. Ref.3

Sequence conflict

415

G → A in BAA11226. Ref.1

Sequence conflict

724

N → Y in AAH07897. Ref.2

Sequence conflict

731

M → MGM Ref.3

Sequence conflict

900 – 908

LRKNPNYDL → FGRTPIMISK Ref.3 Ref.4

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Sequences

Sequence

Length

Mass (Da)

Tools

Q13200-1 [UniParc].

Last modified July 15, 1999. Version 3.
Checksum: FAD71E7B26101BE3
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FASTA

908

100,200

        10         20         30         40         50         60 
MEEGGRDKAP VQPQQSPAAA PGGTDEKPSG KERRDAGDKD KEQELSEEDK QLQDELEMLV 

        70         80         90        100        110        120 
ERLGEKDTSL YRPALEELRR QIRSSTTSMT SVPKPLKFLR PHYGKLKEIY ENMAPGENKR 

       130        140        150        160        170        180 
FAADIISVLA MTMSGERECL KYRLVGSQEE LASWGHEYVR HLAGEVAKEW QELDDAEKVQ 

       190        200        210        220        230        240 
REPLLTLVKE IVPYNMAHNA EHEACDLLME IEQVDMLEKD IDENAYAKVC LYLTSCVNYV 

       250        260        270        280        290        300 
PEPENSALLR CALGVFRKFS RFPEALRLAL MLNDMELVED IFTSCKDVVV QKQMAFMLGR 

       310        320        330        340        350        360 
HGVFLELSED VEEYEDLTEI MSNVQLNSNF LALARELDIM EPKVPDDIYK THLENNRFGG 

       370        380        390        400        410        420 
SGSQVDSARM NLASSFVNGF VNAAFGQDKL LTDDGNKWLY KNKDHGMLSA AASLGMILLW 

       430        440        450        460        470        480 
DVDGGLTQID KYLYSSEDYI KSGALLACGI VNSGVRNECD PALALLSDYV LHNSNTMRLG 

       490        500        510        520        530        540 
SIFGLGLAYA GSNREDVLTL LLPVMGDSKS SMEVAGVTAL ACGMIAVGSC NGDVTSTILQ 

       550        560        570        580        590        600 
TIMEKSETEL KDTYARWLPL GLGLNHLGKG EAIEAILAAL EVVSEPFRSF ANTLVDVCAY 

       610        620        630        640        650        660 
AGSGNVLKVQ QLLHICSEHF DSKEKEEDKD KKEKKDKDKK EAPADMGAHQ GVAVLGIALI 

       670        680        690        700        710        720 
AMGEEIGAEM ALRTFGHLLR YGEPTLRRAV PLALALISVS NPRLNILDTL SKFSHDADPE 

       730        740        750        760        770        780 
VSYNSIFAMG MVGSGTNNAR LAAMLRQLAQ YHAKDPNNLF MVRLAQGLTH LGKGTLTLCP 

       790        800        810        820        830        840 
YHSDRQLMSQ VAVAGLLTVL VSFLDVRNII LGKSHYVLYG LVAAMQPRML VTFDEELRPL 

       850        860        870        880        890        900 
PVSVRVGQAV DVVGQAGKPK TITGFQTHTT PVLLAHGERA ELATEEFLPV TPILEGFVIL 


RKNPNYDL

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"cDNA cloning and functional analysis of the p97 subunit of the 26S proteasome, a polypeptide identical to the type-1 tumor-necrosis-factor-receptor-associated protein-2/55.11." Tsurumi C., Shimizu Y., Saeki M., Kato S., DeMartino G.N., Slaughter C.A., Fujimuro M., Yokosawa H., Yamasaki M., Hendil K.B., Toh-e A., Tanahashi N., Tanaka K. Eur. J. Biochem. 239:912-921(1996) [PubMed: 8774743] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 49-66; 81-85; 91-117; 138-145; 148-158; 182-193; 209-229; 438-441 AND 471-481. Tissue: Fibrosarcoma.
[2]	"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, Muscle and Skin.
[3]	"Two-hybrid cloning of a gene encoding TNF receptor-associated protein 2, a protein that interacts with the intracellular domain of the type 1 TNF receptor: identity with subunit 2 of the 26S protease." Dunbar J.D., Song H.Y., Guo D., Wu L.-W., Donner D.B. J. Immunol. 158:4252-4259(1997) [PubMed: 9126987] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-908.
[4]	"A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'." Boldin M.P., Mett I.L., Wallach D. FEBS Lett. 367:39-44(1995) [PubMed: 7601280] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-908. Tissue: Liver.
[5]	"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-16 AND THR-90, MASS SPECTROMETRY. Tissue: Epithelium.
[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: 17323924] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, ACETYLATION AT MET-1, MASS SPECTROMETRY.
[7]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, MASS SPECTROMETRY. Tissue: Epithelium.
[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-16, MASS SPECTROMETRY.
+	Additional computationally mapped references.

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Cross-references

Sequence databases
	D78151 mRNA. Translation: BAA11226.1. BC002368 mRNA. Translation: AAH02368.1. BC002997 mRNA. Translation: AAH02997.1. BC007897 mRNA. Translation: AAH07897.1. U12596 mRNA. Translation: AAA87705.1. Different initiation. X86446 mRNA. Translation: CAA60167.1.
RefSeq	NP_002799.3.
UniGene	Hs.518464
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q13200.
PTM databases
PhosphoSite	Q13200.
Proteomic databases
PeptideAtlas	Q13200.
Genome annotation databases
Ensembl	ENSG00000175166. Homo sapiens. [Contig view]
GeneID	5708.
KEGG	hsa:5708.
NMPDR	fig\|9606.3.peg.23594.
Organism-specific databases
H-InvDB	HIX0003912.
HGNC	HGNC:9559. PSMD2.
MIM	606223. gene.
PharmGKB	PA33905.
GenAtlas	Search...
GeneCards	Search...
Phylogenomic databases
HOVERGEN	Q13200.
Enzyme and pathway databases
Reactome	REACT_11045. Signaling by Wnt. REACT_152. Cell Cycle, Mitotic. REACT_1538. Cell Cycle Checkpoints. REACT_383. DNA Replication. 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	Q13200.
CleanEx	HS_PSMD2.
GermOnline	ENSG00000175166. Homo sapiens.
Family and domain databases
InterPro	IPR016643. 26S_Psome_Rpn1. IPR002015. APC_proteasome. [Graphical view]
Pfam	PF01851. PC_rep. 6 hits. [Graphical view]
PIRSF	PIRSF015965. 26S_Psome_Rpn1. 1 hit.
ProtoNet	Search...
Other Resources
DrugBank	DB00188. Bortezomib.
LinkHub	Q13200.
NextBio	22178.
SOURCE	Search...

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Entry information

Entry name

PSMD2_HUMAN

Accession

Primary (citable) accession number: Q13200
Secondary accession number(s): Q12932, Q15321, Q96I12

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1997
Last sequence update:	July 15, 1999
Last modified:	November 25, 2008
This is version 84 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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Relevant documents

Human chromosome 3

Human chromosome 3: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Keywords

Gene Ontology (GO)

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Experimental info

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents