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Protein

Proteasome subunit beta type-7

Gene

Psmb7

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei44 – 441NucleophileBy similarity

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiR-RNO-1169091. Activation of NF-kappaB in B cells.
R-RNO-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-RNO-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-RNO-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-RNO-174154. APC/C:Cdc20 mediated degradation of Securin.
R-RNO-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-RNO-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-RNO-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-RNO-195253. Degradation of beta-catenin by the destruction complex.
R-RNO-202424. Downstream TCR signaling.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2871837. FCERI mediated NF-kB activation.
R-RNO-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-RNO-350562. Regulation of ornithine decarboxylase (ODC).
R-RNO-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-RNO-4608870. Asymmetric localization of PCP proteins.
R-RNO-4641257. Degradation of AXIN.
R-RNO-4641258. Degradation of DVL.
R-RNO-5358346. Hedgehog ligand biogenesis.
R-RNO-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-RNO-5607764. CLEC7A (Dectin-1) signaling.
R-RNO-5610780. Degradation of GLI1 by the proteasome.
R-RNO-5610785. GLI3 is processed to GLI3R by the proteasome.
R-RNO-5632684. Hedgehog 'on' state.
R-RNO-5658442. Regulation of RAS by GAPs.
R-RNO-5668541. TNFR2 non-canonical NF-kB pathway.
R-RNO-5676590. NIK-->noncanonical NF-kB signaling.
R-RNO-5687128. MAPK6/MAPK4 signaling.
R-RNO-68827. CDT1 association with the CDC6:ORC:origin complex.
R-RNO-68949. Orc1 removal from chromatin.
R-RNO-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-RNO-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-RNO-69481. G2/M Checkpoints.
R-RNO-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-RNO-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Protein family/group databases

MEROPSiT01.011.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-7 (EC:3.4.25.1)
Alternative name(s):
Macropain chain Z
Multicatalytic endopeptidase complex chain Z
Proteasome subunit Z
Gene namesi
Name:Psmb7
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 3

Organism-specific databases

RGDi621093. Psmb7.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4343Removed in mature formBy similarityPRO_0000026649Add
BLAST
Chaini44 – 277234Proteasome subunit beta type-7PRO_0000026650Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiQ9JHW0.
PRIDEiQ9JHW0.

2D gel databases

World-2DPAGE0004:Q9JHW0.

PTM databases

iPTMnetiQ9JHW0.

Expressioni

Gene expression databases

ExpressionAtlasiQ9JHW0. baseline and differential.
GenevisibleiQ9JHW0. RN.

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. This subunit can be displaced by the equivalent immune-specific subunit PSMB10 (By similarity).By similarity

Protein-protein interaction databases

BioGridi250112. 1 interaction.
IntActiQ9JHW0. 1 interaction.
STRINGi10116.ENSRNOP00000016876.

Structurei

3D structure databases

ProteinModelPortaliQ9JHW0.
SMRiQ9JHW0. Positions 44-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiQ9JHW0.
KOiK02739.
OMAiANMEREE.
OrthoDBiEOG7CRTQJ.
PhylomeDBiQ9JHW0.
TreeFamiTF106222.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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.

Q9JHW0-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MAAVSVFQAP VGGFSFDNCR RNAVLEADFA KKGFKLPKAR KTGTTIAGVV
60 70 80 90 100
YKDGIVLGAD TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ
110 120 130 140 150
LISSNLELHS LTTGRLPRVV TANRMLKQML FRYQGYIGAA LVLGGVDVTG
160 170 180 190 200
PHLYSIYPHG STDKLPYVTM GSGSLAAMAV FEDKFRPDME EEEAKKLVSE
210 220 230 240 250
AIAAGIFNDL GSGSNIDLCV ISKSKLDFLR PYSVPNKKGT RFGRYRCEKG
260 270
TTAVLTEKVT PLELEVLEEI VQTMDTS
Length:277
Mass (Da):29,927
Last modified:October 1, 2000 - v1
Checksum:i6F26D115159A0A41
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285103 mRNA. Translation: AAF97811.1.
BC060551 mRNA. Translation: AAH60551.1.
PIRiS09082.
RefSeqiNP_445984.1. NM_053532.1.
UniGeneiRn.3846.

Genome annotation databases

EnsembliENSRNOT00000016876; ENSRNOP00000016876; ENSRNOG00000011732.
ENSRNOT00000085981; ENSRNOP00000073989; ENSRNOG00000011732.
GeneIDi85492.
KEGGirno:85492.
UCSCiRGD:621093. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF285103 mRNA. Translation: AAF97811.1.
BC060551 mRNA. Translation: AAH60551.1.
PIRiS09082.
RefSeqiNP_445984.1. NM_053532.1.
UniGeneiRn.3846.

3D structure databases

ProteinModelPortaliQ9JHW0.
SMRiQ9JHW0. Positions 44-263.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250112. 1 interaction.
IntActiQ9JHW0. 1 interaction.
STRINGi10116.ENSRNOP00000016876.

Protein family/group databases

MEROPSiT01.011.

PTM databases

iPTMnetiQ9JHW0.

2D gel databases

World-2DPAGE0004:Q9JHW0.

Proteomic databases

PaxDbiQ9JHW0.
PRIDEiQ9JHW0.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000016876; ENSRNOP00000016876; ENSRNOG00000011732.
ENSRNOT00000085981; ENSRNOP00000073989; ENSRNOG00000011732.
GeneIDi85492.
KEGGirno:85492.
UCSCiRGD:621093. rat.

Organism-specific databases

CTDi5695.
RGDi621093. Psmb7.

Phylogenomic databases

eggNOGiKOG0173. Eukaryota.
COG0638. LUCA.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiQ9JHW0.
KOiK02739.
OMAiANMEREE.
OrthoDBiEOG7CRTQJ.
PhylomeDBiQ9JHW0.
TreeFamiTF106222.

Enzyme and pathway databases

ReactomeiR-RNO-1169091. Activation of NF-kappaB in B cells.
R-RNO-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-RNO-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-RNO-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-RNO-174154. APC/C:Cdc20 mediated degradation of Securin.
R-RNO-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-RNO-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-RNO-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-RNO-195253. Degradation of beta-catenin by the destruction complex.
R-RNO-202424. Downstream TCR signaling.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2871837. FCERI mediated NF-kB activation.
R-RNO-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-RNO-350562. Regulation of ornithine decarboxylase (ODC).
R-RNO-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-RNO-4608870. Asymmetric localization of PCP proteins.
R-RNO-4641257. Degradation of AXIN.
R-RNO-4641258. Degradation of DVL.
R-RNO-5358346. Hedgehog ligand biogenesis.
R-RNO-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-RNO-5607764. CLEC7A (Dectin-1) signaling.
R-RNO-5610780. Degradation of GLI1 by the proteasome.
R-RNO-5610785. GLI3 is processed to GLI3R by the proteasome.
R-RNO-5632684. Hedgehog 'on' state.
R-RNO-5658442. Regulation of RAS by GAPs.
R-RNO-5668541. TNFR2 non-canonical NF-kB pathway.
R-RNO-5676590. NIK-->noncanonical NF-kB signaling.
R-RNO-5687128. MAPK6/MAPK4 signaling.
R-RNO-68827. CDT1 association with the CDC6:ORC:origin complex.
R-RNO-68949. Orc1 removal from chromatin.
R-RNO-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-RNO-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-RNO-69481. G2/M Checkpoints.
R-RNO-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-RNO-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiQ9JHW0.

Gene expression databases

ExpressionAtlasiQ9JHW0. baseline and differential.
GenevisibleiQ9JHW0. RN.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR024689. Proteasome_bsu_C.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSiPR00141. PROTEASOME.
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. Kang J.S., Liu H.L., Li R.X.
    Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Brain.
  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: Pituitary.
  3. Lubec G., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 44-72; 165-184 AND 226-237, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus.
  4. "Quantitative maps of protein phosphorylation sites across 14 different rat organs and tissues."
    Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C., Olsen J.V.
    Nat. Commun. 3:876-876(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiPSB7_RAT
AccessioniPrimary (citable) accession number: Q9JHW0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: October 1, 2000
Last modified: June 8, 2016
This is version 120 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Peptidase families
    Classification of peptidase families and list of entries
  2. 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.