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Protein

Proteasome subunit beta type-3

Gene

PSMB3

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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.

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiT01.983.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-3 (EC:3.4.25.1)
Alternative name(s):
Proteasome chain 13
Proteasome component C10-II
Proteasome theta chain
Gene namesi
Name:PSMB3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:9540. PSMB3.

Subcellular locationi

GO - Cellular componenti

  • actin cytoskeleton Source: HPA
  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • Golgi apparatus Source: HPA
  • mitochondrion Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA33885.

Polymorphism and mutation databases

BioMutaiPSMB3.
DMDMi20532411.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed3 Publications
Chaini2 – 205204Proteasome subunit beta type-3PRO_0000148057Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserine3 Publications
Modified residuei77 – 771N6-acetyllysine1 Publication

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP49720.
PaxDbiP49720.
PeptideAtlasiP49720.
PRIDEiP49720.

2D gel databases

OGPiP49720.
REPRODUCTION-2DPAGEIPI00028004.

PTM databases

PhosphoSiteiP49720.

Expressioni

Inductioni

Up-regulated in asthenozoospermic sperm.1 Publication

Gene expression databases

BgeeiP49720.
CleanExiHS_PSMB3.
ExpressionAtlasiP49720. baseline and differential.
GenevisibleiP49720. HS.

Organism-specific databases

HPAiHPA042775.
HPA048147.

Interactioni

Subunit structurei

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.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMB2P497214EBI-603340,EBI-359335
TRIM27P143733EBI-603340,EBI-719493

Protein-protein interaction databases

BioGridi111664. 73 interactions.
IntActiP49720. 23 interactions.
MINTiMINT-5001041.
STRINGi9606.ENSP00000225426.

Structurei

Secondary structure

1
205
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Turni4 – 74Combined sources
Beta strandi10 – 156Combined sources
Beta strandi17 – 259Combined sources
Beta strandi28 – 303Combined sources
Beta strandi33 – 375Combined sources
Beta strandi42 – 443Combined sources
Beta strandi49 – 524Combined sources
Helixi57 – 7721Combined sources
Beta strandi78 – 803Combined sources
Helixi84 – 9613Combined sources
Turni97 – 1004Combined sources
Beta strandi108 – 1125Combined sources
Beta strandi114 – 1163Combined sources
Beta strandi119 – 1246Combined sources
Beta strandi130 – 1323Combined sources
Beta strandi134 – 1407Combined sources
Helixi143 – 15311Combined sources
Helixi160 – 17516Combined sources
Beta strandi178 – 1814Combined sources
Beta strandi185 – 20016Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60J/X2-205[»]
4R67X-ray2.89J/X/l/z2-205[»]
ProteinModelPortaliP49720.
SMRiP49720. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
HOVERGENiHBG004446.
InParanoidiP49720.
KOiK02735.
OMAiYIEPVIA.
OrthoDBiEOG783MWB.
PhylomeDBiP49720.
TreeFamiTF106216.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P49720-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSIMSYNGGA VMAMKGKNCV AIAADRRFGI QAQMVTTDFQ KIFPMGDRLY
60 70 80 90 100
IGLAGLATDV QTVAQRLKFR LNLYELKEGR QIKPYTLMSM VANLLYEKRF
110 120 130 140 150
GPYYTEPVIA GLDPKTFKPF ICSLDLIGCP MVTDDFVVSG TCAEQMYGMC
160 170 180 190 200
ESLWEPNMDP DHLFETISQA MLNAVDRDAV SGMGVIVHII EKDKITTRTL

KARMD
Length:205
Mass (Da):22,949
Last modified:May 10, 2002 - v2
Checksum:i624972384C0112FD
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti34 – 341M → L.1 Publication
Corresponds to variant rs4907 [ dbSNP | Ensembl ].
VAR_034415

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26598 mRNA. Translation: BAA05645.1.
BC013008 mRNA. Translation: AAH13008.1.
CCDSiCCDS11328.1.
PIRiS55041.
RefSeqiNP_002786.2. NM_002795.3.
UniGeneiHs.82793.

Genome annotation databases

EnsembliENST00000619426; ENSP00000483688; ENSG00000277791.
ENST00000619951; ENSP00000483956; ENSG00000275903.
GeneIDi5691.
KEGGihsa:5691.
UCSCiuc002hqr.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26598 mRNA. Translation: BAA05645.1.
BC013008 mRNA. Translation: AAH13008.1.
CCDSiCCDS11328.1.
PIRiS55041.
RefSeqiNP_002786.2. NM_002795.3.
UniGeneiHs.82793.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60J/X2-205[»]
4R67X-ray2.89J/X/l/z2-205[»]
ProteinModelPortaliP49720.
SMRiP49720. Positions 2-205.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111664. 73 interactions.
IntActiP49720. 23 interactions.
MINTiMINT-5001041.
STRINGi9606.ENSP00000225426.

Chemistry

ChEMBLiCHEMBL2364701.

Protein family/group databases

MEROPSiT01.983.

PTM databases

PhosphoSiteiP49720.

Polymorphism and mutation databases

BioMutaiPSMB3.
DMDMi20532411.

2D gel databases

OGPiP49720.
REPRODUCTION-2DPAGEIPI00028004.

Proteomic databases

MaxQBiP49720.
PaxDbiP49720.
PeptideAtlasiP49720.
PRIDEiP49720.

Protocols and materials databases

DNASUi5691.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000619426; ENSP00000483688; ENSG00000277791.
ENST00000619951; ENSP00000483956; ENSG00000275903.
GeneIDi5691.
KEGGihsa:5691.
UCSCiuc002hqr.3. human.

Organism-specific databases

CTDi5691.
GeneCardsiGC17P036909.
H-InvDBHIX0030292.
HGNCiHGNC:9540. PSMB3.
HPAiHPA042775.
HPA048147.
MIMi602176. gene.
neXtProtiNX_P49720.
PharmGKBiPA33885.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00550000074820.
HOGENOMiHOG000090523.
HOVERGENiHBG004446.
InParanoidiP49720.
KOiK02735.
OMAiYIEPVIA.
OrthoDBiEOG783MWB.
PhylomeDBiP49720.
TreeFamiTF106216.

Enzyme and pathway databases

ReactomeiREACT_11063. Degradation of beta-catenin by the destruction complex.
REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_188323. CLEC7A (Dectin-1) signaling.
REACT_188330. Dectin-1 mediated noncanonical NF-kB signaling.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_263873. degradation of AXIN.
REACT_263883. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
REACT_264438. degradation of DVL.
REACT_264478. Asymmetric localization of PCP proteins.
REACT_264605. Hedgehog ligand biogenesis.
REACT_267700. Degradation of GLI2 by the proteasome.
REACT_268156. Degradation of GLI1 by the proteasome.
REACT_268366. GLI3 is processed to GLI3R by the proteasome.
REACT_268718. Hedgehog 'on' state.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSiPSMB3. human.
GeneWikiiPSMB3.
GenomeRNAii5691.
NextBioi22106.
PROiP49720.
SOURCEiSearch...

Gene expression databases

BgeeiP49720.
CleanExiHS_PSMB3.
ExpressionAtlasiP49720. baseline and differential.
GenevisibleiP49720. HS.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. Proteasome. 1 hit.
[Graphical view]
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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], VARIANT LEU-34.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  3. Bienvenut W.V., von Kriegsheim A.F., Kolch W.
    Submitted (JUL-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-15; 28-41; 49-66; 71-77; 100-115 AND 178-192, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Ovarian carcinoma.
  4. Lubec G., Vishwanath V.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 29-42; 50-67 AND 101-116, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Brain and Cajal-Retzius cell.
  5. "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 49-66 AND 99-111.
    Tissue: Keratinocyte.
  6. "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 100-115.
    Tissue: Placenta.
  7. "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.
  8. "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.
  9. "Identification of proteomic differences in asthenozoospermic sperm samples."
    Martinez-Heredia J., de Mateo S., Vidal-Taboada J.M., Ballesca J.L., Oliva R.
    Hum. Reprod. 23:783-791(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  10. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  11. "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-77, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "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 SER-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
  14. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiPSB3_HUMAN
AccessioniPrimary (citable) accession number: P49720
Secondary accession number(s): P31147, Q0P6J7, Q96E27
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: May 10, 2002
Last modified: July 22, 2015
This is version 162 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.