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Q13200 (PSMD2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
Protein 55.11
Tumor necrosis factor type 1 receptor-associated protein 2
Gene names
Name:PSMD2
Synonyms:TRAP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length908 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

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.

Sequence caution

The sequence AAA87705.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentProteasome
   Coding sequence diversityPolymorphism
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processDNA 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

RNA metabolic process

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

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

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

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic 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

regulation of protein catabolic process

Inferred from electronic annotation. Source: InterPro

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

proteasome accessory complex

Inferred from sequence or structural similarity. Source: UniProtKB

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

proteasome regulatory particle

Traceable author statement Ref.1. Source: ProtInc

   Molecular_functionenzyme regulator activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 90890826S proteasome non-ATPase regulatory subunit 2
PRO_0000173810

Regions

Repeat409 – 44234PC 1
Repeat443 – 47937PC 2
Repeat480 – 51435PC 3
Repeat517 – 55135PC 4
Repeat560 – 58930PC 5
Repeat692 – 72332PC 6
Repeat742 – 75716PC 7
Compositional bias623 – 64119Glu/Lys-rich

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue161Phosphoserine Ref.6 Ref.7 Ref.8 Ref.9 Ref.10 Ref.12 Ref.13 Ref.15
Modified residue241Phosphothreonine Ref.7 Ref.13
Modified residue291Phosphoserine Ref.7
Modified residue1941Phosphotyrosine Ref.7
Modified residue3611Phosphoserine Ref.12 Ref.13 Ref.15
Modified residue5511N6-acetyllysine By similarity

Natural variations

Natural variant1761A → T.
Corresponds to variant rs11545172 [ dbSNP | Ensembl ].
VAR_051554
Natural variant3131E → D.
Corresponds to variant rs11545169 [ dbSNP | Ensembl ].
VAR_051555
Natural variant7241N → Y. Ref.2 Ref.3
Corresponds to variant rs17856236 [ dbSNP | Ensembl ].
VAR_067451

Experimental info

Sequence conflict101P → R in CAA60167. Ref.5
Sequence conflict211P → S Ref.4
Sequence conflict321E → G Ref.4
Sequence conflict431Q → L Ref.4
Sequence conflict571E → V Ref.4
Sequence conflict601V → A in BAA11226. Ref.1
Sequence conflict2261Y → S in AAA87705. Ref.4
Sequence conflict2601S → T in CAA60167. Ref.5
Sequence conflict281 – 2833IFT → SS in AAA87705. Ref.4
Sequence conflict4151G → A in BAA11226. Ref.1
Sequence conflict7311M → MGM Ref.4
Sequence conflict900 – 9089LRKNPNYDL → FGRTPIMISK Ref.3
Sequence conflict900 – 9089LRKNPNYDL → FGRTPIMISK Ref.5

Sequences

Sequence LengthMass (Da)Tools
Q13200 [UniParc].

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

FASTA908100,200
        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 

« Hide

References

« Hide '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] [Europe PMC] [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]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (AUG-2003) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-724.
[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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT TYR-724.
Tissue: Lung, Muscle and Skin.
[4]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 21-908.
[5]"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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 10-908.
Tissue: Liver.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24; SER-29 AND TYR-194, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[8]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[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-16, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[13]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16; THR-24 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"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].
[15]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D78151 mRNA. Translation: BAA11226.1.
BT009736 mRNA. Translation: AAP88738.1.
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.
RefSeqNP_001265637.1. NM_001278708.1.
NP_001265638.1. NM_001278709.1.
NP_002799.3. NM_002808.4.
UniGeneHs.518464.

3D structure databases

ProteinModelPortalQ13200.
SMRQ13200. Positions 437-572.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111681. 128 interactions.
IntActQ13200. 34 interactions.
MINTMINT-1142723.
STRING9606.ENSP00000310129.

Chemistry

DrugBankDB00188. Bortezomib.

PTM databases

PhosphoSiteQ13200.

Polymorphism databases

DMDM6174930.

Proteomic databases

PaxDbQ13200.
PeptideAtlasQ13200.
PRIDEQ13200.

Protocols and materials databases

DNASU5708.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000310118; ENSP00000310129; ENSG00000175166.
GeneID5708.
KEGGhsa:5708.
UCSCuc003fnn.1. human.

Organism-specific databases

CTD5708.
GeneCardsGC03P184016.
HGNCHGNC:9559. PSMD2.
HPAHPA045192.
MIM606223. gene.
neXtProtNX_Q13200.
PharmGKBPA33905.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5110.
HOVERGENHBG001842.
InParanoidQ13200.
KOK03028.
OMAIAQGLTH.
OrthoDBEOG70KGNV.
PhylomeDBQ13200.
TreeFamTF105739.

Enzyme and pathway databases

ReactomeREACT_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

ArrayExpressQ13200.
BgeeQ13200.
CleanExHS_PSMD2.
GenevestigatorQ13200.

Family and domain databases

InterProIPR016643. 26S_Psome_Rpn1.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PfamPF01851. PC_rep. 2 hits.
[Graphical view]
PIRSFPIRSF015965. 26S_Psome_Rpn1. 1 hit.
SUPFAMSSF48371. SSF48371. 4 hits.
ProtoNetSearch...

Other

ChiTaRSPSMD2. human.
GeneWikiPSMD2.
GenomeRNAi5708.
NextBio22178.
PROQ13200.
SOURCESearch...

Entry information

Entry namePSMD2_HUMAN
AccessionPrimary (citable) accession number: Q13200
Secondary accession number(s): Q12932 expand/collapse secondary AC list , Q15321, Q53XQ4, Q96I12
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: July 15, 1999
Last modified: April 16, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

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

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 3

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