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Protein

Proteasome subunit beta type-7

Gene

PSMB7

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). Within the 20S core complex, PSMB7 displays a trypsin-like activity.3 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei44Nucleophile2 Publications1

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-6798695. Neutrophil degranulation.
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

MEROPSiT01.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-7 (EC:3.4.25.11 Publication)
Alternative name(s):
Macropain chain Z
Multicatalytic endopeptidase complex chain Z
Proteasome subunit Z
Gene namesi
Name:PSMB7
Synonyms:Z
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

EuPathDBiHostDB:ENSG00000136930.12.
HGNCiHGNC:9544. PSMB7.

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

DisGeNETi5695.
OpenTargetsiENSG00000136930.
PharmGKBiPA33889.

Chemistry databases

ChEMBLiCHEMBL3347256.

Polymorphism and mutation databases

BioMutaiPSMB7.
DMDMi17380263.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000266451 – 43Removed in mature formAdd BLAST43
ChainiPRO_000002664644 – 277Proteasome subunit beta type-7Add BLAST234

Keywords - PTMi

Zymogen

Proteomic databases

EPDiQ99436.
MaxQBiQ99436.
PaxDbiQ99436.
PeptideAtlasiQ99436.
PRIDEiQ99436.

PTM databases

iPTMnetiQ99436.
PhosphoSitePlusiQ99436.

Expressioni

Tissue specificityi

Expressed at a low level in colonic mucosa. Up-regulated in colorectal cancer tissues.1 Publication

Gene expression databases

BgeeiENSG00000136930.
CleanExiHS_PSMB7.
ExpressionAtlasiQ99436. baseline and differential.
GenevisibleiQ99436. HS.

Organism-specific databases

HPAiHPA052408.
HPA054902.

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).6 Publications

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi111668. 85 interactors.
CORUMiQ99436.
DIPiDIP-33843N.
IntActiQ99436. 31 interactors.
MINTiMINT-1351242.
STRINGi9606.ENSP00000259457.

Chemistry databases

BindingDBiQ99436.

Structurei

Secondary structure

1277
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi46 – 51Combined sources6
Beta strandi54 – 60Combined sources7
Beta strandi63 – 65Combined sources3
Beta strandi68 – 73Combined sources6
Beta strandi77 – 81Combined sources5
Beta strandi84 – 91Combined sources8
Helixi92 – 113Combined sources22
Helixi119 – 133Combined sources15
Beta strandi135 – 137Combined sources3
Beta strandi139 – 147Combined sources9
Beta strandi150 – 156Combined sources7
Turni158 – 160Combined sources3
Beta strandi162 – 164Combined sources3
Beta strandi166 – 171Combined sources6
Helixi174 – 184Combined sources11
Helixi191 – 208Combined sources18
Beta strandi216 – 222Combined sources7
Beta strandi225 – 233Combined sources9
Beta strandi254 – 261Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60I/W44-263[»]
4R67X-ray2.89I/W/k/y44-263[»]
5A0Qelectron microscopy3.50I/W44-277[»]
5GJQelectron microscopy4.50b/p1-277[»]
5GJRelectron microscopy3.50b/p1-277[»]
5L4Gelectron microscopy4.027/81-277[»]
5LE5X-ray1.80H/V44-277[»]
5LEXX-ray2.20H/V44-277[»]
5LEYX-ray1.90H/V44-277[»]
5LEZX-ray2.19H/V44-277[»]
5LF0X-ray2.41H/V44-277[»]
5LF1X-ray2.00H/V44-277[»]
5LF3X-ray2.10H/V44-277[»]
5LF4X-ray1.99H/V44-277[»]
5LF6X-ray2.07H/V44-277[»]
5LF7X-ray2.00H/V44-277[»]
5LN3electron microscopy6.8021-277[»]
5M32electron microscopy3.80H/V1-277[»]
5T0Celectron microscopy3.80AO/BO2-277[»]
5T0Gelectron microscopy4.40O2-277[»]
5T0Helectron microscopy6.80O2-277[»]
5T0Ielectron microscopy8.00O2-277[»]
5T0Jelectron microscopy8.00O2-277[»]
ProteinModelPortaliQ99436.
SMRiQ99436.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiQ99436.
KOiK02739.
OMAiDLCVIRK.
OrthoDBiEOG091G0E5S.
PhylomeDBiQ99436.
TreeFamiTF106222.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiView protein in InterPro
IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR035216. Proteasome_beta7.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
PANTHERiPTHR11599:SF42. PTHR11599:SF42. 1 hit.
PfamiView protein in Pfam
PF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
PRINTSiPR00141. PROTEASOME.
SUPFAMiSSF56235. SSF56235. 1 hit.
PROSITEiView protein in PROSITE
PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

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

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q99436-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAAVSVYAPP VGGFSFDNCR RNAVLEADFA KRGYKLPKVR KTGTTIAGVV
60 70 80 90 100
YKDGIVLGAD TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ
110 120 130 140 150
LISSNLELHS LSTGRLPRVV TANRMLKQML FRYQGYIGAA LVLGGVDVTG
160 170 180 190 200
PHLYSIYPHG STDKLPYVTM GSGSLAAMAV FEDKFRPDME EEEAKNLVSE
210 220 230 240 250
AIAAGIFNDL GSGSNIDLCV ISKNKLDFLR PYTVPNKKGT RLGRYRCEKG
260 270
TTAVLTEKIT PLEIEVLEET VQTMDTS
Length:277
Mass (Da):29,965
Last modified:May 1, 1997 - v1
Checksum:iA610C949A0ACF1CE
GO
Isoform 2 (identifier: Q99436-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     133-142: YQGYIGAALV → FWLLGSNGCI
     143-277: Missing.

Note: No experimental confirmation available.
Show »
Length:142
Mass (Da):15,323
Checksum:i2B639D6E1A7C144F
GO

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_01329239V → A1 PublicationCorresponds to variant dbSNP:rs4574Ensembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_056573133 – 142YQGYIGAALV → FWLLGSNGCI in isoform 2. 1 Publication10
Alternative sequenceiVSP_056574143 – 277Missing in isoform 2. 1 PublicationAdd BLAST135

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D38048 mRNA. Translation: BAA07238.1.
AK303460 mRNA. Translation: BAG64503.1.
AL137846 Genomic DNA. Translation: CAI10873.1.
CH471090 Genomic DNA. Translation: EAW87582.1.
CH471090 Genomic DNA. Translation: EAW87583.1.
BC000509 mRNA. Translation: AAH00509.1.
BC008414 mRNA. No translation available.
BC017116 mRNA. Translation: AAH17116.2.
CCDSiCCDS6855.1. [Q99436-1]
RefSeqiNP_002790.1. NM_002799.3. [Q99436-1]
UniGeneiHs.213470.

Genome annotation databases

EnsembliENST00000259457; ENSP00000259457; ENSG00000136930. [Q99436-1]
GeneIDi5695.
KEGGihsa:5695.
UCSCiuc004boj.5. human. [Q99436-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Similar proteinsi

Entry informationi

Entry nameiPSB7_HUMAN
AccessioniPrimary (citable) accession number: Q99436
Secondary accession number(s): B4E0P1
, Q5TBG6, Q96AG8, Q9BWA7
Entry historyiIntegrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: May 1, 1997
Last modified: October 25, 2017
This is version 181 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 9
    Human chromosome 9: 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