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P49721 (PSB2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 150. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | 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:
Proteasome subunit beta type-2

EC=3.4.25.1
Alternative name(s):
Macropain subunit C7-I
Multicatalytic endopeptidase complex subunit C7-I
Proteasome component C7-I
Gene names
Name:PSMB2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length201 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

The proteasome is a multicatalytic proteinase complex which is characterized by its ability to cleave peptides with Arg, Phe, Tyr, Leu, and Glu adjacent to the leaving group at neutral or slightly basic pH. The proteasome has an ATP-dependent proteolytic activity. This subunit has a trypsin-like activity.

Catalytic activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

The 26S proteasome consists of a 20S proteasome core and two 19S regulatory subunits. The 20S proteasome core is composed of 28 subunits that are arranged in four stacked rings, resulting in a barrel-shaped structure. The two end rings are each formed by seven alpha subunits, and the two central rings are each formed by seven beta subunits. The catalytic chamber with the active sites is on the inside of the barrel. Interacts with HIV-1 TAT protein. Ref.10

Subcellular location

Cytoplasm. Nucleus.

Induction

Up-regulated in ovarian cancer cell lines. Ref.13

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Keywords
   Biological processHost-virus interaction
   Cellular componentCytoplasm
Nucleus
Proteasome
   Molecular functionHydrolase
Protease
Threonine protease
   PTMAcetylation
   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 ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

response to organic cyclic compound

Inferred from electronic annotation. Source: Ensembl

response to organonitrogen compound

Inferred from electronic annotation. Source: Ensembl

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 19056867PubMed 20458337PubMed 23376485. Source: UniProt

nucleoplasm

Traceable author statement. Source: Reactome

nucleus

Inferred from direct assay PubMed 21630459. Source: UniProt

proteasome complex

Traceable author statement PubMed 8811196. Source: ProtInc

proteasome core complex

Inferred from sequence or structural similarity. Source: UniProtKB

   Molecular_functionprotein binding

Inferred from physical interaction PubMed 14733938PubMed 17948026. Source: IntAct

threonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

PSMB3P497204EBI-359335,EBI-603340

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 201201Proteasome subunit beta type-2
PRO_0000148043

Amino acid modifications

Modified residue11N-acetylmethionine Ref.12 Ref.16

Sequences

Sequence LengthMass (Da)Tools
P49721 [UniParc].

Last modified October 1, 1996. Version 1.
Checksum: 04D085D7BAA76130

FASTA20122,836
        10         20         30         40         50         60 
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA GDTVQFAEYI 

        70         80         90        100        110        120 
QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV NLLLAGYDEH EGPALYYMDY 

       130        140        150        160        170        180 
LAALAKAPFA AHGYGAFLTL SILDRYYTPT ISRERAVELL RKCLEELQKR FILNLPTFSV 

       190        200 
RIIDKNGIHD LDNISFPKQG S 

« Hide

References

« Hide 'large scale' references
[1]"Sequence analyses and inter-species comparisons of three novel human proteasomal subunits, HsN3, HsC7-I and HsC10-II, confine potential proteolytic active-site residues."
Nothwang H.G., Tamura T., Tanaka K., Ichihara A.
Biochim. Biophys. Acta 1219:361-368(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[3]"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 (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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].
Tissue: Brain.
[7]Lubec G., Vishwanath V.
Submitted (MAR-2007) to UniProtKB
Cited for: PROTEIN SEQUENCE OF 71-85 AND 171-181, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Brain and Cajal-Retzius cell.
[8]"Microsequences of 145 proteins recorded in the two-dimensional gel protein database of normal human epidermal keratinocytes."
Rasmussen H.H., van Damme J., Puype M., Gesser B., Celis J.E., Vandekerckhove J.
Electrophoresis 13:960-969(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 172-177 AND 186-193.
Tissue: Keratinocyte.
[9]"Human proteasome subunits from 2-dimensional gels identified by partial sequencing."
Kristensen P., Johnsen A.H., Uerkvitz W., Tanaka K., Hendil K.B.
Biochem. Biophys. Res. Commun. 205:1785-1789(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 72-85.
Tissue: Placenta.
[10]"Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH HIV-1 TAT.
[11]"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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"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].
[13]"Screening for genetic abnormalities involved in ovarian carcinogenesis using retroviral expression libraries."
Wada T., Yamashita Y., Saga Y., Takahashi K., Koinuma K., Choi Y.L., Kaneda R., Fujiwara S., Soda M., Watanabe H., Kurashina K., Hatanaka H., Enomoto M., Takada S., Mano H., Suzuki M.
Int. J. Oncol. 35:973-976(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INDUCTION.
[14]"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.
[15]"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].
[16]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(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
D26599 mRNA. Translation: BAA05646.1.
CR456862 mRNA. Translation: CAG33143.1.
BT007137 mRNA. Translation: AAP35801.1.
AL354864, AL157951, AL357035 Genomic DNA. Translation: CAC36031.2.
AL357035, AL354864, AL157951 Genomic DNA. Translation: CAI22074.1.
AL157951, AL354864, AL357035 Genomic DNA. Translation: CAI23521.1.
CH471059 Genomic DNA. Translation: EAX07406.1.
CH471059 Genomic DNA. Translation: EAX07407.1.
BC101836 mRNA. Translation: AAI01837.1.
BC105126 mRNA. Translation: AAI05127.1.
BC107901 mRNA. Translation: AAI07902.1.
CCDSCCDS394.1.
PIRS55040.
RefSeqNP_002785.1. NM_002794.4.
UniGeneHs.471441.

3D structure databases

ProteinModelPortalP49721.
SMRP49721. Positions 1-199.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid111663. 76 interactions.
IntActP49721. 19 interactions.
MINTMINT-1144735.
STRING9606.ENSP00000362334.

Chemistry

BindingDBP49721.
ChEMBLCHEMBL3492.
DrugBankDB00188. Bortezomib.

Protein family/group databases

MEROPST01.984.

PTM databases

PhosphoSiteP49721.

Polymorphism databases

DMDM1709762.

2D gel databases

OGPP49721.
REPRODUCTION-2DPAGEIPI00028006.
P49721.

Proteomic databases

MaxQBP49721.
PaxDbP49721.
PeptideAtlasP49721.
PRIDEP49721.

Protocols and materials databases

DNASU5690.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000373237; ENSP00000362334; ENSG00000126067.
GeneID5690.
KEGGhsa:5690.
UCSCuc001bzf.2. human.

Organism-specific databases

CTD5690.
GeneCardsGC01M036042.
HGNCHGNC:9539. PSMB2.
HPAHPA026322.
HPA026324.
MIM602175. gene.
neXtProtNX_P49721.
PharmGKBPA33884.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000188743.
HOVERGENHBG000815.
KOK02734.
OMAHFVRGEL.
OrthoDBEOG7N63NQ.
PhylomeDBP49721.
TreeFamTF106219.

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

BgeeP49721.
CleanExHS_PSMB2.
GenevestigatorP49721.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPSMB2. human.
GeneWikiPSMB2.
GenomeRNAi5690.
NextBio22102.
PROP49721.
SOURCESearch...

Entry information

Entry namePSB2_HUMAN
AccessionPrimary (citable) accession number: P49721
Secondary accession number(s): D3DPS0, P31145, Q9BWZ9
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: July 9, 2014
This is version 150 of the entry and version 1 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

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM