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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

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-446652. Interleukin-1 family signaling.
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-8941858. Regulation of RUNX3 expression and activity.
R-HSA-8948751. Regulation of PTEN stability and activity.
R-HSA-8951664. Neddylation.
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.

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. 98 interactors.
CORUMiP49721.
DIPiDIP-33848N.
IntActiP49721. 37 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[»]
5LN3electron microscopy6.8041-201[»]
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.
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:SF95. PTHR11599:SF95. 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, 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.

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: September 27, 2017
This is version 184 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