ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry Q13200


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name PSMD2_HUMAN
Primary accession number Q13200
Secondary accession numbers Q12932 Q15321 Q96I12
Integrated into Swiss-Prot on November 1, 1997
Sequence was last modified on July 15, 1999 (Sequence version 3)
Annotations were last modified on    July 22, 2008 (Entry version 82)
Name and origin of the protein
Protein name 26S proteasome non-ATPase regulatory subunit 2
Synonyms 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 name
Name: PSMD2
Synonyms: TRAP2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 49-66; 81-85; 91-117; 138-145; 148-158; 182-193; 209-229; 438-441 AND 471-481.
TISSUE=Fibrosarcoma;
PubMed=8774743 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"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.";
Eur. J. Biochem. 239:912-921(1996).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Lung, Muscle, and Skin;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[3]
NUCLEOTIDE SEQUENCE [MRNA] OF 21-908.
PubMed=9126987 [NCBI, ExPASy, EBI, Israel, Japan]
Dunbar J.D., Song H.Y., Guo D., Wu L.-W., Donner D.B.;
"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.";
J. Immunol. 158:4252-4259(1997).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 10-908.
TISSUE=Liver;
DOI=10.1016/0014-5793(95)00534-G; PubMed=7601280 [NCBI, ExPASy, EBI, Israel, Japan]
Boldin M.P., Mett I.L., Wallach D.;
"A protein related to a proteasomal subunit binds to the intracellular domain of the p55 TNF receptor upstream to its 'death domain'.";
FEBS Lett. 367:39-44(1995).
[5]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND THR-90, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16 AND SER-361, ACETYLATION AT MET-1, AND MASS SPECTROMETRY.
DOI=10.1021/bi061994u; PubMed=17323924 [NCBI, ExPASy, EBI, Israel, Japan]
Wang X., Chen C.-F., Baker P.R., Chen P.-L., Kaiser P., Huang L.;
"Mass spectrometric characterization of the affinity-purified human 26S proteasome complex.";
Biochemistry 46:3553-3565(2007).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-16, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"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.";
J. Proteome Res. 6:4150-4162(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
D78151; BAA11226.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002368; AAH02368.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC002997; AAH02997.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC007897; AAH07897.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
U12596; AAA87705.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
X86446; CAA60167.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_002799.3; -.
UniGene Hs.518464
3D structure databases
ModBase Q13200.
Protein-protein interaction databases
IntAct Q13200; -.
PTM databases
PhosphoSite 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.
Organism-specific databases
H-InvDB HIX0003912; -.
HGNC HGNC:9559; PSMD2.
GenAtlas PSMD2.
MIM 606223; gene. [NCBI / EBI]
PharmGKB PA33905; -.
GeneCards Q13200.
Gene expression databases
ArrayExpress Q13200; -.
CleanEx HS_PSMD2; -.
GermOnline ENSG00000175166; Homo sapiens.
Ontologies
GO
GO:0005838; Cellular component: proteasome regulatory particle (traceable author statement from ProtInc).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from UniProtKB).
GO:0031145; Biological process: anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process (inferred from experiment from Reactome).
GO:0051436; Biological process: negative regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
GO:0051437; Biological process: positive regulation of ubiquitin-protein ligase activity during mitotic cell cycle (inferred from experiment from Reactome).
QuickGo view.
Family and domain databases
InterPro IPR016643; 26S_Psome_Rpn1.
IPR002015; APC_proteasome.
Graphical view of domain structure.
Pfam PF01851; PC_rep; 6.
Pfam graphical view of domain structure.
PIRSF PIRSF015965; 26S_Psome_Rpn1; 1.
BLOCKS 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; -.
Phylogenomic databases
HOVERGEN Q13200; -.
Other
DrugBank DB00188; Bortezomib.
LinkHub Q13200; -.
SOURCE PSMD2; Homo sapiens.
ProtoNet Q13200.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Direct protein sequencing; Phosphoprotein; Proteasome; Repeat.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   908  908     26S proteasome non-ATPase regulatory subunit 2. PRO_0000173810
REPEAT   409   442  34     PC 1. 
REPEAT   443   479  37     PC 2. 
REPEAT   480   514  35     PC 3. 
REPEAT   517   551  35     PC 4. 
REPEAT   560   589  30     PC 5. 
REPEAT   692   723  32     PC 6. 
REPEAT   742   757  16     PC 7. 
COMPBIAS   623   641  19     Glu/Lys-rich. 
MOD_RES   1     1        N-acetylmethionine. 
MOD_RES   16    16        Phosphoserine. 
MOD_RES   90    90        Phosphothreonine. 
MOD_RES   361   361        Phosphoserine. 
CONFLICT   10    10        P -> R (in Ref. 4; CAA60167). 
CONFLICT   21    21        P -> S (in Ref. 3). 
CONFLICT   32    32        E -> G (in Ref. 3). 
CONFLICT   43    43        Q -> L (in Ref. 3). 
CONFLICT   57    57        E -> V (in Ref. 3). 
CONFLICT   60    60        V -> A (in Ref. 1; BAA11226). 
CONFLICT   226   226        Y -> S (in Ref. 3; AAA87705). 
CONFLICT   260   260        S -> T (in Ref. 4; CAA60167). 
CONFLICT   281   283        IFT -> SS (in Ref. 3; AAA87705). 
CONFLICT   415   415        G -> A (in Ref. 1; BAA11226). 
CONFLICT   724   724        N -> Y (in Ref. 2; AAH07897). 
CONFLICT   731   731        M -> MGM (in Ref. 3). 
CONFLICT   900   908        LRKNPNYDL -> FGRTPIMISK (in Ref. 3 and 4). 
Sequence information
Length: 908 AA [This is the length of the unprocessed precursor] Molecular weight: 100200 Da [This is the MW of the unprocessed precursor] CRC64: FAD71E7B26101BE3 [This is a checksum on the sequence]
        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 

Q13200 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by ch flag SIB Switzerland Mirror sites: Australia  Brazil  Canada  China  Korea
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!