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Protein

Proteasome subunit beta type-2

Gene

PSMB2

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. This subunit has a trypsin-like 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

BioCyciZFISH:HS04992-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.984.

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:PSMB2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:9539. PSMB2.

Subcellular locationi

GO - Cellular componenti

  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: HPA
  • 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

DisGeNETi5690.
OpenTargetsiENSG00000126067.
PharmGKBiPA33884.

Chemistry databases

ChEMBLiCHEMBL3492.
DrugBankiDB00188. Bortezomib.
DB08889. Carfilzomib.

Polymorphism and mutation databases

BioMutaiPSMB2.
DMDMi1709762.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001480431 – 201Proteasome subunit beta type-2Add BLAST201

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

EPDiP49721.
MaxQBiP49721.
PaxDbiP49721.
PeptideAtlasiP49721.
PRIDEiP49721.
TopDownProteomicsiP49721.

2D gel databases

OGPiP49721.
REPRODUCTION-2DPAGEIPI00028006.
P49721.

PTM databases

iPTMnetiP49721.
PhosphoSitePlusiP49721.
SwissPalmiP49721.

Expressioni

Inductioni

Up-regulated in ovarian cancer cell lines.1 Publication

Gene expression databases

BgeeiENSG00000126067.
CleanExiHS_PSMB2.
ExpressionAtlasiP49721. baseline and differential.
GenevisibleiP49721. HS.

Organism-specific databases

HPAiHPA026322.
HPA026324.

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
KCTD9Q7L2733EBI-359335,EBI-4397613
KRT13A1A4E93EBI-359335,EBI-10171552
PSMB3P497204EBI-359335,EBI-603340

Protein-protein interaction databases

BioGridi111663. 97 interactors.
DIPiDIP-33848N.
IntActiP49721. 34 interactors.
MINTiMINT-1144735.
STRINGi9606.ENSP00000362334.

Chemistry databases

BindingDBiP49721.

Structurei

Secondary structure

1201
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi4 – 8Combined sources5
Beta strandi13 – 18Combined sources6
Beta strandi21 – 23Combined sources3
Beta strandi26 – 31Combined sources6
Beta strandi35 – 39Combined sources5
Beta strandi42 – 49Combined sources8
Helixi52 – 71Combined sources20
Helixi77 – 89Combined sources13
Turni91 – 93Combined sources3
Beta strandi94 – 96Combined sources3
Beta strandi100 – 108Combined sources9
Turni109 – 111Combined sources3
Beta strandi112 – 118Combined sources7
Beta strandi124 – 126Combined sources3
Beta strandi128 – 133Combined sources6
Helixi136 – 146Combined sources11
Helixi153 – 170Combined sources18
Beta strandi171 – 173Combined sources3
Beta strandi177 – 184Combined sources8
Beta strandi187 – 190Combined sources4

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60K/Y1-199[»]
4R67X-ray2.890/K/Y/m1-199[»]
5A0Qelectron microscopy3.50K/Y1-201[»]
5GJQelectron microscopy4.50d/r1-201[»]
5GJRelectron microscopy3.50d/r1-201[»]
5L4Gelectron microscopy4.022/V1-201[»]
5LE5X-ray1.80J/X1-201[»]
5LEXX-ray2.20J/X1-201[»]
5LEYX-ray1.90J/X1-201[»]
5LEZX-ray2.19J/X1-201[»]
5LF0X-ray2.41J/X1-201[»]
5LF1X-ray2.00J/X1-201[»]
5LF3X-ray2.10J/X1-201[»]
5LF4X-ray1.99J/X1-201[»]
5LF6X-ray2.07J/X1-201[»]
5LF7X-ray2.00J/X1-201[»]
5T0Celectron microscopy3.80AQ/BQ1-201[»]
5T0Gelectron microscopy4.40Q1-201[»]
5T0Helectron microscopy6.80Q1-201[»]
5T0Ielectron microscopy8.00Q1-201[»]
5T0Jelectron microscopy8.00Q1-201[»]
ProteinModelPortaliP49721.
SMRiP49721.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0177. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00640000091536.
HOGENOMiHOG000188743.
HOVERGENiHBG000815.
InParanoidiP49721.
KOiK02734.
OMAiDRYHDPE.
OrthoDBiEOG091G0K9M.
PhylomeDBiP49721.
TreeFamiTF106219.

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.

P49721-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEYLIGIQGP DYVLVASDRV AASNIVQMKD DHDKMFKMSE KILLLCVGEA
60 70 80 90 100
GDTVQFAEYI QKNVQLYKMR NGYELSPTAA ANFTRRNLAD CLRSRTPYHV
110 120 130 140 150
NLLLAGYDEH EGPALYYMDY LAALAKAPFA AHGYGAFLTL SILDRYYTPT
160 170 180 190 200
ISRERAVELL RKCLEELQKR FILNLPTFSV RIIDKNGIHD LDNISFPKQG

S
Length:201
Mass (Da):22,836
Last modified:October 1, 1996 - v1
Checksum:i04D085D7BAA76130
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS394.1.
PIRiS55040.
RefSeqiNP_002785.1. NM_002794.4.
UniGeneiHs.471441.

Genome annotation databases

EnsembliENST00000373237; ENSP00000362334; ENSG00000126067.
GeneIDi5690.
KEGGihsa:5690.
UCSCiuc001bzf.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS394.1.
PIRiS55040.
RefSeqiNP_002785.1. NM_002794.4.
UniGeneiHs.471441.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60K/Y1-199[»]
4R67X-ray2.890/K/Y/m1-199[»]
5A0Qelectron microscopy3.50K/Y1-201[»]
5GJQelectron microscopy4.50d/r1-201[»]
5GJRelectron microscopy3.50d/r1-201[»]
5L4Gelectron microscopy4.022/V1-201[»]
5LE5X-ray1.80J/X1-201[»]
5LEXX-ray2.20J/X1-201[»]
5LEYX-ray1.90J/X1-201[»]
5LEZX-ray2.19J/X1-201[»]
5LF0X-ray2.41J/X1-201[»]
5LF1X-ray2.00J/X1-201[»]
5LF3X-ray2.10J/X1-201[»]
5LF4X-ray1.99J/X1-201[»]
5LF6X-ray2.07J/X1-201[»]
5LF7X-ray2.00J/X1-201[»]
5T0Celectron microscopy3.80AQ/BQ1-201[»]
5T0Gelectron microscopy4.40Q1-201[»]
5T0Helectron microscopy6.80Q1-201[»]
5T0Ielectron microscopy8.00Q1-201[»]
5T0Jelectron microscopy8.00Q1-201[»]
ProteinModelPortaliP49721.
SMRiP49721.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111663. 97 interactors.
DIPiDIP-33848N.
IntActiP49721. 34 interactors.
MINTiMINT-1144735.
STRINGi9606.ENSP00000362334.

Chemistry databases

BindingDBiP49721.
ChEMBLiCHEMBL3492.
DrugBankiDB00188. Bortezomib.
DB08889. Carfilzomib.

Protein family/group databases

MEROPSiT01.984.

PTM databases

iPTMnetiP49721.
PhosphoSitePlusiP49721.
SwissPalmiP49721.

Polymorphism and mutation databases

BioMutaiPSMB2.
DMDMi1709762.

2D gel databases

OGPiP49721.
REPRODUCTION-2DPAGEIPI00028006.
P49721.

Proteomic databases

EPDiP49721.
MaxQBiP49721.
PaxDbiP49721.
PeptideAtlasiP49721.
PRIDEiP49721.
TopDownProteomicsiP49721.

Protocols and materials databases

DNASUi5690.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000373237; ENSP00000362334; ENSG00000126067.
GeneIDi5690.
KEGGihsa:5690.
UCSCiuc001bzf.4. human.

Organism-specific databases

CTDi5690.
DisGeNETi5690.
GeneCardsiPSMB2.
HGNCiHGNC:9539. PSMB2.
HPAiHPA026322.
HPA026324.
MIMi602175. gene.
neXtProtiNX_P49721.
OpenTargetsiENSG00000126067.
PharmGKBiPA33884.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0177. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00640000091536.
HOGENOMiHOG000188743.
HOVERGENiHBG000815.
InParanoidiP49721.
KOiK02734.
OMAiDRYHDPE.
OrthoDBiEOG091G0K9M.
PhylomeDBiP49721.
TreeFamiTF106219.

Enzyme and pathway databases

BioCyciZFISH:HS04992-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiPSMB2. human.
GeneWikiiPSMB2.
GenomeRNAii5690.
PROiP49721.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000126067.
CleanExiHS_PSMB2.
ExpressionAtlasiP49721. baseline and differential.
GenevisibleiP49721. 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...

Entry informationi

Entry nameiPSB2_HUMAN
AccessioniPrimary (citable) accession number: P49721
Secondary accession number(s): D3DPS0, P31145, Q9BWZ9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: November 30, 2016
This is version 177 of the entry and version 1 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 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Peptidase families
    Classification of peptidase families and list of entries
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.