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Protein

Proteasome subunit beta type-2

Gene

PSMB2

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

Functioni

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex).3 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 Publication

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processHost-virus interaction

Enzyme and pathway databases

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-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
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:3.4.25.11 Publication)
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

EuPathDBiHostDB:ENSG00000126067.11
HGNCiHGNC:9539 PSMB2
MIMi602175 gene
neXtProtiNX_P49721

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5690
OpenTargetsiENSG00000126067
PharmGKBiPA33884

Chemistry databases

ChEMBLiCHEMBL3492
DrugBankiDB08889 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-2DPAGEiIPI00028006
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 a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. Interacts with HIV-1 TAT protein (PubMed:14550573).7 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111663, 99 interactors
CORUMiP49721
DIPiDIP-33848N
IntActiP49721, 36 interactors
MINTiP49721
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[»]
5LN3electron microscopy6.8041-201[»]
5M32electron microscopy3.80J/X1-196[»]
5T0Celectron microscopy3.80AQ/BQ1-201[»]
5T0Gelectron microscopy4.40Q1-201[»]
5T0Helectron microscopy6.80Q1-201[»]
5T0Ielectron microscopy8.00Q1-201[»]
5T0Jelectron microscopy8.00Q1-201[»]
6AVOelectron microscopy3.80T/V1-201[»]
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
OMAiQLYSMRN
OrthoDBiEOG091G0K9M
PhylomeDBiP49721
TreeFamiTF106219

Family and domain databases

CDDicd03758 proteasome_beta_type_2, 1 hit
Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR035206 Proteasome_beta2
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF6 PTHR11599:SF6, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 1 hit

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 Genomic DNA No translation available.
AL357035 Genomic DNA No translation available.
AL157951 Genomic DNA No translation available.
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

Similar proteinsi

Entry informationi

Entry nameiPSB2_HUMAN
AccessioniPrimary (citable) accession number: P49721
Secondary accession number(s): D3DPS0, P31145, Q9BWZ9
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 23, 2018
This is version 190 of the entry and version 1 of the sequence. See 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

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