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Q99460 (PSMD1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 132. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
26S proteasome non-ATPase regulatory subunit 1
Alternative name(s):
26S proteasome regulatory subunit RPN2
26S proteasome regulatory subunit S1
26S proteasome subunit p112
Gene names
Name:PSMD1
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length953 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.

Subunit structure

Interacts with ADRM1. Ref.4 Ref.5

Sequence similarities

Belongs to the proteasome subunit S1 family.

Contains 10 PC repeats.

Sequence caution

The sequence AAH01053.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH14013.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH39845.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH47897.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH64398.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

The sequence AAH73833.1 differs from that shown. Reason: Contaminating sequence. Potential poly-A sequence.

Ontologies

Keywords
   Cellular componentProteasome
   Coding sequence diversityAlternative splicing
   DomainRepeat
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
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

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...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q99460-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q99460-2)

The sequence of this isoform differs from the canonical sequence as follows:
     797-827: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 95395326S proteasome non-ATPase regulatory subunit 1
PRO_0000173801

Regions

Repeat403 – 43634PC 1
Repeat441 – 47434PC 2
Repeat476 – 51035PC 3
Repeat511 – 54535PC 4
Repeat547 – 58034PC 5
Repeat581 – 61636PC 6
Repeat617 – 64933PC 7
Repeat651 – 68535PC 8
Repeat686 – 72641PC 9
Repeat729 – 76133PC 10
Compositional bias936 – 9438Poly-Glu

Amino acid modifications

Modified residue11N-acetylmethionine Ref.8 Ref.14
Modified residue2731Phosphothreonine Ref.6
Modified residue2901Phosphoserine Ref.6
Modified residue3101N6-acetyllysine Ref.10
Modified residue3111Phosphothreonine Ref.6 Ref.7 Ref.9 Ref.13
Modified residue3151Phosphoserine Ref.6 Ref.7 Ref.9 Ref.13
Modified residue7201N6-acetyllysine By similarity

Natural variations

Alternative sequence797 – 82731Missing in isoform 2.
VSP_011475

Experimental info

Sequence conflict851G → R in BAA07918. Ref.1
Sequence conflict6161R → S in BAA07918. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified August 31, 2004. Version 2.
Checksum: B8682146082D21FA

FASTA953105,836
        10         20         30         40         50         60 
MITSAAGIIS LLDEDEPQLK EFALHKLNAV VNDFWAEISE SVDKIEVLYE DEGFRSRQFA 

        70         80         90        100        110        120 
ALVASKVFYH LGAFEESLNY ALGAGDLFNV NDNSEYVETI IAKCIDHYTK QCVENADLPE 

       130        140        150        160        170        180 
GEKKPIDQRL EGIVNKMFQR CLDDHKYKQA IGIALETRRL DVFEKTILES NDVPGMLAYS 

       190        200        210        220        230        240 
LKLCMSLMQN KQFRNKVLRV LVKIYMNLEK PDFINVCQCL IFLDDPQAVS DILEKLVKED 

       250        260        270        280        290        300 
NLLMAYQICF DLYESASQQF LSSVIQNLRT VGTPIASVPG STNTGTVPGS EKDSDSMETE 

       310        320        330        340        350        360 
EKTSSAFVGK TPEASPEPKD QTLKMIKILS GEMAIELHLQ FLIRNNNTDL MILKNTKDAV 

       370        380        390        400        410        420 
RNSVCHTATV IANSFMHCGT TSDQFLRDNL EWLARATNWA KFTATASLGV IHKGHEKEAL 

       430        440        450        460        470        480 
QLMATYLPKD TSPGSAYQEG GGLYALGLIH ANHGGDIIDY LLNQLKNASN DIVRHGGSLG 

       490        500        510        520        530        540 
LGLAAMGTAR QDVYDLLKTN LYQDDAVTGE AAGLALGLVM LGSKNAQAIE DMVGYAQETQ 

       550        560        570        580        590        600 
HEKILRGLAV GIALVMYGRM EEADALIESL CRDKDPILRR SGMYTVAMAY CGSGNNKAIR 

       610        620        630        640        650        660 
RLLHVAVSDV NDDVRRAAVE SLGFILFRTP EQCPSVVSLL SESYNPHVRY GAAMALGICC 

       670        680        690        700        710        720 
AGTGNKEAIN LLEPMTNDPV NYVRQGALIA SALIMIQQTE ITCPKVNQFR QLYSKVINDK 

       730        740        750        760        770        780 
HDDVMAKFGA ILAQGILDAG GHNVTISLQS RTGHTHMPSV VGVLVFTQFW FWFPLSHFLS 

       790        800        810        820        830        840 
LAYTPTCVIG LNKDLKMPKV QYKSNCKPST FAYPAPLEVP KEKEKEKVST AVLSITAKAK 

       850        860        870        880        890        900 
KKEKEKEKKE EEKMEVDEAE KKEEKEKKKE PEPNFQLLDN PARVMPAQLK VLTMPETCRY 

       910        920        930        940        950 
QPFKPLSIGG IIILKDTSED IEELVEPVAA HGPKIEEEEQ EPEPPEPFEY IDD 

« Hide

Isoform 2 [UniParc].

Checksum: 1F727659749D4871
Show »

FASTA922102,258

References

« Hide 'large scale' references
[1]"cDNA cloning of p112, the largest regulatory subunit of the human 26s proteasome, and functional analysis of its yeast homologue, sen3p."
Yokota K., Kagawa S., Shimizu Y., Akioka H., Tsurumi C., Noda C., Fujimuro M., Yokosawa H., Fujiwara T., Takahashi E., Ohba M., Yamasaki M., DeMartino G.N., Slaughter C.A., Toh-e A., Tanaka K.
Mol. Biol. Cell 7:853-870(1996) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[2]"Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H. expand/collapse author list , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[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] (ISOFORMS 1 AND 2).
Tissue: Cervix, Liver, Lymph, Placenta, Testis and Uterus.
[4]"A novel proteasome-interacting protein recruits the deubiquitinating enzyme UCH37 to 26S proteasomes."
Hamazaki J., Iemura S., Natsume T., Yashiroda H., Tanaka K., Murata S.
EMBO J. 25:4524-4536(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADRM1.
[5]"Proteasome recruitment and activation of the Uch37 deubiquitinating enzyme by Adrm1."
Yao T., Song L., Xu W., DeMartino G.N., Florens L., Swanson S.K., Washburn M.P., Conaway R.C., Conaway J.W., Cohen R.E.
Nat. Cell Biol. 8:994-1002(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH ADRM1.
[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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-273; SER-290; THR-311 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[7]"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 THR-311 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[8]"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: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[9]"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 THR-311 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[10]"Lysine acetylation targets protein complexes and co-regulates major cellular functions."
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-310, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[12]"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].
[13]"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 THR-311 AND SER-315, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D44466 mRNA. Translation: BAA07918.1.
AC009407 Genomic DNA. Translation: AAX93127.1.
BC001053 mRNA. Translation: AAH01053.1. Sequence problems.
BC014013 mRNA. Translation: AAH14013.1. Sequence problems.
BC039845 mRNA. Translation: AAH39845.1. Sequence problems.
BC047897 mRNA. Translation: AAH47897.1. Sequence problems.
BC064398 mRNA. Translation: AAH64398.1. Sequence problems.
BC073833 mRNA. Translation: AAH73833.1. Sequence problems.
BC094720 mRNA. Translation: AAH94720.1.
BC112344 mRNA. Translation: AAI12345.1.
BC114434 mRNA. Translation: AAI14435.1.
RefSeqNP_001177966.1. NM_001191037.1.
NP_002798.2. NM_002807.3.
UniGeneHs.3887.

3D structure databases

ProteinModelPortalQ99460.
SMRQ99460. Positions 3-930.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111680. 99 interactions.
DIPDIP-27548N.
IntActQ99460. 34 interactions.
MINTMINT-1160606.

Chemistry

DrugBankDB00188. Bortezomib.

PTM databases

PhosphoSiteQ99460.

Polymorphism databases

DMDM51704332.

Proteomic databases

PaxDbQ99460.
PRIDEQ99460.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000308696; ENSP00000309474; ENSG00000173692. [Q99460-1]
ENST00000373635; ENSP00000362738; ENSG00000173692. [Q99460-2]
ENST00000409643; ENSP00000386932; ENSG00000173692. [Q99460-2]
GeneID5707.
KEGGhsa:5707.
UCSCuc002vrm.2. human. [Q99460-2]
uc002vrn.2. human. [Q99460-1]

Organism-specific databases

CTD5707.
GeneCardsGC02P231921.
HGNCHGNC:9554. PSMD1.
HPACAB021092.
HPA036736.
neXtProtNX_Q99460.
PharmGKBPA33899.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5116.
HOVERGENHBG007543.
InParanoidQ99460.
KOK03032.
OMACVENAEL.
OrthoDBEOG790G01.
PhylomeDBQ99460.
TreeFamTF105742.

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

ArrayExpressQ99460.
BgeeQ99460.
CleanExHS_PSMD1.
GenevestigatorQ99460.

Family and domain databases

Gene3D1.25.10.10. 2 hits.
InterProIPR016642. 26S_Psome_Rpn2.
IPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR002015. Proteasome/cyclosome_rpt.
[Graphical view]
PfamPF01851. PC_rep. 4 hits.
[Graphical view]
PIRSFPIRSF015947. 26S_Psome_Rpn2. 1 hit.
SUPFAMSSF48371. SSF48371. 3 hits.
ProtoNetSearch...

Other

ChiTaRSPSMD1. human.
GeneWikiPSMD1.
GenomeRNAi5707.
NextBio22174.
PROQ99460.

Entry information

Entry namePSMD1_HUMAN
AccessionPrimary (citable) accession number: Q99460
Secondary accession number(s): B8ZZH9 expand/collapse secondary AC list , Q24JU0, Q53TI2, Q6GMU5, Q6P2P4, Q6PJM7, Q6PKG9, Q86VU1, Q8IV79
Entry history
Integrated into UniProtKB/Swiss-Prot: December 15, 1998
Last sequence update: August 31, 2004
Last modified: April 16, 2014
This is version 132 of the entry and version 2 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

Human chromosome 2

Human chromosome 2: entries, gene names and cross-references to MIM