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P70195

- PSB7_MOUSE

UniProt

P70195 - PSB7_MOUSE

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Protein

Proteasome subunit beta type-7

Gene

Psmb7

Organism
Mus musculus (Mouse)
Status
Reviewed - 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. This unit is responsible of the trypsin-like activity of the proteasome By similarity.By similarity

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

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

GO - Molecular functioni

  1. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. proteolysis involved in cellular protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

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
Synonyms:Mmc14
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:107637. Psmb7.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: Ensembl
  3. microtubule cytoskeleton Source: Ensembl
  4. nucleus Source: UniProtKB-KW
  5. proteasome core complex Source: UniProtKB
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_0000026647Add
BLAST
Chaini44 – 277234Proteasome subunit beta type-7PRO_0000026648Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

MaxQBiP70195.
PaxDbiP70195.
PRIDEiP70195.

2D gel databases

REPRODUCTION-2DPAGEIPI00136483.
P70195.

PTM databases

PhosphoSiteiP70195.

Expressioni

Inductioni

Up-regulated by the antioxidant dithiolethione (D3T) in colon (at protein level).1 Publication

Gene expression databases

BgeeiP70195.
ExpressionAtlasiP70195. baseline and differential.
GenevestigatoriP70195.

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 PSMB10.1 Publication

Protein-protein interaction databases

BioGridi202424. 1 interaction.
IntActiP70195. 5 interactions.
MINTiMINT-1856747.
STRINGi10090.ENSMUSP00000028083.

Structurei

Secondary structure

1
277
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi46 – 505
Beta strandi52 – 609
Beta strandi63 – 653
Beta strandi68 – 736
Beta strandi77 – 9115
Helixi92 – 11322
Helixi119 – 13214
Turni133 – 1353
Beta strandi139 – 1468
Beta strandi151 – 1566
Beta strandi162 – 1643
Beta strandi166 – 1716
Helixi174 – 18411
Helixi191 – 20818
Beta strandi216 – 2249
Beta strandi226 – 2338
Beta strandi254 – 2618

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90H/V/j/x44-277[»]
3UNEX-ray3.20H/V/j/x44-277[»]
ProteinModelPortaliP70195.
SMRiP70195. Positions 44-263.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiCOG0638.
GeneTreeiENSGT00510000046533.
HOGENOMiHOG000182856.
HOVERGENiHBG093416.
InParanoidiP70195.
KOiK02739.
OMAiQIWCAGA.
OrthoDBiEOG7CRTQJ.
PhylomeDBiP70195.
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.

P70195-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MAAVSVFQPP 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 PFSVPNKKGT RLGRYRCEKG
260 270
TTAVLTEKVT PLEIEVLEET VQTMDTS
Length:277
Mass (Da):29,891
Last modified:February 1, 1997 - v1
Checksum:i3B8BA01B1E6392F2
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti108 – 1081L → F in BAB28354. (PubMed:16141072)Curated
Sequence conflicti237 – 2371K → E in BAB22385. (PubMed:16141072)Curated

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D83585 mRNA. Translation: BAA12017.1.
Y10874 mRNA. Translation: CAA71824.1.
D85570 Genomic DNA. Translation: BAA22857.1.
AK002823 mRNA. Translation: BAB22385.1.
AK012613 mRNA. Translation: BAB28354.1.
AK013961 mRNA. Translation: BAB29085.1.
AK075759 mRNA. Translation: BAC35937.1.
AK088276 mRNA. Translation: BAC40251.1.
AK088765 mRNA. Translation: BAC40556.1.
AK168823 mRNA. Translation: BAE40650.1.
BC057662 mRNA. Translation: AAH57662.1.
CCDSiCCDS16010.1.
PIRiJC6122.
RefSeqiNP_035317.1. NM_011187.1.
UniGeneiMm.389251.

Genome annotation databases

EnsembliENSMUST00000028083; ENSMUSP00000028083; ENSMUSG00000026750.
GeneIDi19177.
KEGGimmu:19177.
UCSCiuc008jnp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
D83585 mRNA. Translation: BAA12017.1 .
Y10874 mRNA. Translation: CAA71824.1 .
D85570 Genomic DNA. Translation: BAA22857.1 .
AK002823 mRNA. Translation: BAB22385.1 .
AK012613 mRNA. Translation: BAB28354.1 .
AK013961 mRNA. Translation: BAB29085.1 .
AK075759 mRNA. Translation: BAC35937.1 .
AK088276 mRNA. Translation: BAC40251.1 .
AK088765 mRNA. Translation: BAC40556.1 .
AK168823 mRNA. Translation: BAE40650.1 .
BC057662 mRNA. Translation: AAH57662.1 .
CCDSi CCDS16010.1.
PIRi JC6122.
RefSeqi NP_035317.1. NM_011187.1.
UniGenei Mm.389251.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
3UNB X-ray 2.90 H/V/j/x 44-277 [» ]
3UNE X-ray 3.20 H/V/j/x 44-277 [» ]
ProteinModelPortali P70195.
SMRi P70195. Positions 44-263.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 202424. 1 interaction.
IntActi P70195. 5 interactions.
MINTi MINT-1856747.
STRINGi 10090.ENSMUSP00000028083.

Protein family/group databases

MEROPSi T01.011.

PTM databases

PhosphoSitei P70195.

2D gel databases

REPRODUCTION-2DPAGE IPI00136483.
P70195.

Proteomic databases

MaxQBi P70195.
PaxDbi P70195.
PRIDEi P70195.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000028083 ; ENSMUSP00000028083 ; ENSMUSG00000026750 .
GeneIDi 19177.
KEGGi mmu:19177.
UCSCi uc008jnp.1. mouse.

Organism-specific databases

CTDi 5695.
MGIi MGI:107637. Psmb7.

Phylogenomic databases

eggNOGi COG0638.
GeneTreei ENSGT00510000046533.
HOGENOMi HOG000182856.
HOVERGENi HBG093416.
InParanoidi P70195.
KOi K02739.
OMAi QIWCAGA.
OrthoDBi EOG7CRTQJ.
PhylomeDBi P70195.
TreeFami TF106222.

Enzyme and pathway databases

Reactomei REACT_197102. ER-Phagosome pathway.
REACT_198693. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_199105. ER-Phagosome pathway.
REACT_199114. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_199115. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_199121. Activation of NF-kappaB in B cells.
REACT_203517. SCF-beta-TrCP mediated degradation of Emi1.
REACT_203973. Asymmetric localization of PCP proteins.
REACT_207679. Separation of Sister Chromatids.
REACT_212633. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_218318. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_219129. degradation of AXIN.
REACT_219897. APC/C:Cdc20 mediated degradation of Securin.
REACT_220647. SCF(Skp2)-mediated degradation of p27/p21.
REACT_225686. Autodegradation of Cdh1 by Cdh1:APC/C.
REACT_226135. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_227429. degradation of DVL.

Miscellaneous databases

NextBioi 295860.
PROi P70195.
SOURCEi Search...

Gene expression databases

Bgeei P70195.
ExpressionAtlasi P70195. baseline and differential.
Genevestigatori P70195.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. 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 ]
Pfami PF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view ]
PRINTSi PR00141. PROTEASOME.
SUPFAMi SSF56235. SSF56235. 1 hit.
PROSITEi PS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Chromosomal localization of the proteasome Z subunit gene reveals an ancient chromosomal duplication involving the major histocompatibility complex."
    Kasahara M., Hayashi M., Tanaka K., Inoko H., Sugaya K., Ikemura T., Ishibashi T.
    Proc. Natl. Acad. Sci. U.S.A. 93:9096-9101(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: C57BL/6J.
    Tissue: Epididymis.
  2. "Molecular cloning of the mouse proteasome subunits MC14 and MECL-1: reciprocally regulated tisue expression of interferon-gamma-modulated proteasome subunits."
    Stohwasser R., Standera S., Peters I., Kloetzel P.-M., Groettrup M.
    Submitted (APR-1997) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE.
    Strain: C57BL/6.
    Tissue: Spleen.
  3. "The mouse genes encoding the third pair of beta-type proteasome subunits regulated reciprocally by IFN-gamma: structural comparison, chromosomal localization, and analysis of the promoter."
    Hayashi M., Ishibashi T., Tanaka K., Kasahara M.
    J. Immunol. 159:2760-2770(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/c.
  4. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Embryonic head, Heart, Testis and Thymus.
  5. "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].
    Strain: C57BL/6J.
    Tissue: Mammary gland.
  6. Lubec G., Yang J.W., Zigmond M.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 226-237.
    Tissue: Brain.
  7. "Tissue specific increase of the catalytic subunits of the 26S proteasome by indirect antioxidant dithiolethione in mice: enhanced activity for degradation of abnormal protein."
    Kwak M.K., Huang B., Chang H., Kim J.A., Kensler T.W.
    Life Sci. 80:2411-2420(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY DITHIOLETHIONE.
  8. Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.

Entry informationi

Entry nameiPSB7_MOUSE
AccessioniPrimary (citable) accession number: P70195
Secondary accession number(s): O09084
, Q542F7, Q9CZH4, Q9DCF7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: February 1, 1997
Last modified: October 29, 2014
This is version 138 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

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3