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P70195 (PSB7_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 135. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:Psmb7
Synonyms:Mmc14
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length277 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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.

Catalytic activity

Cleavage of peptide bonds with very broad specificity.

Subunit structure

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. Ref.8

Subcellular location

Cytoplasm. Nucleus.

Induction

Up-regulated by the antioxidant dithiolethione (D3T) in colon (at protein level). Ref.7

Sequence similarities

Belongs to the peptidase T1B family.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4343Removed in mature form By similarity
PRO_0000026647
Chain44 – 277234Proteasome subunit beta type-7
PRO_0000026648

Sites

Active site441Nucleophile By similarity

Experimental info

Sequence conflict1081L → F in BAB28354. Ref.4
Sequence conflict2371K → E in BAB22385. Ref.4

Secondary structure

................................. 277
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P70195 [UniParc].

Last modified February 1, 1997. Version 1.
Checksum: 3B8BA01B1E6392F2

FASTA27729,891
        10         20         30         40         50         60 
MAAVSVFQPP VGGFSFDNCR RNAVLEADFA KKGFKLPKAR KTGTTIAGVV YKDGIVLGAD 

        70         80         90        100        110        120 
TRATEGMVVA DKNCSKIHFI SPNIYCCGAG TAADTDMTTQ LISSNLELHS LTTGRLPRVV 

       130        140        150        160        170        180 
TANRMLKQML FRYQGYIGAA LVLGGVDVTG PHLYSIYPHG STDKLPYVTM GSGSLAAMAV 

       190        200        210        220        230        240 
FEDKFRPDME EEEAKKLVSE AIAAGIFNDL GSGSNIDLCV ISKSKLDFLR PFSVPNKKGT 

       250        260        270 
RLGRYRCEKG TTAVLTEKVT PLEIEVLEET VQTMDTS 

« Hide

References

« Hide 'large scale' references
[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. expand/collapse author list , 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]"Mapping the murine cardiac 26S proteasome complexes."
Gomes A.V., Zong C., Edmondson R.D., Li X., Stefani E., Zhang J., Jones R.C., Thyparambil S., Wang G.W., Qiao X., Bardag-Gorce F., Ping P.
Circ. Res. 99:362-371(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE 20S PROTEASOME CORE COMPLEX.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS16010.1.
PIRJC6122.
RefSeqNP_035317.1. NM_011187.1.
UniGeneMm.389251.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
3UNBX-ray2.90H/V/j/x44-277[»]
3UNEX-ray3.20H/V/j/x44-277[»]
ProteinModelPortalP70195.
SMRP70195. Positions 44-263.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid202424. 1 interaction.
IntActP70195. 5 interactions.
MINTMINT-1856747.
STRING10090.ENSMUSP00000028083.

Protein family/group databases

MEROPST01.011.

PTM databases

PhosphoSiteP70195.

2D gel databases

REPRODUCTION-2DPAGEIPI00136483.
P70195.

Proteomic databases

MaxQBP70195.
PaxDbP70195.
PRIDEP70195.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000028083; ENSMUSP00000028083; ENSMUSG00000026750.
GeneID19177.
KEGGmmu:19177.
UCSCuc008jnp.1. mouse.

Organism-specific databases

CTD5695.
MGIMGI:107637. Psmb7.

Phylogenomic databases

eggNOGCOG0638.
GeneTreeENSGT00510000046533.
HOGENOMHOG000182856.
HOVERGENHBG093416.
InParanoidP70195.
KOK02739.
OMAQIWCAGA.
OrthoDBEOG7CRTQJ.
PhylomeDBP70195.
TreeFamTF106222.

Gene expression databases

ArrayExpressP70195.
BgeeP70195.
GenevestigatorP70195.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. 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]
PfamPF12465. Pr_beta_C. 1 hit.
PF00227. Proteasome. 1 hit.
[Graphical view]
PRINTSPR00141. PROTEASOME.
SUPFAMSSF56235. SSF56235. 1 hit.
PROSITEPS00854. PROTEASOME_BETA_1. 1 hit.
PS51476. PROTEASOME_BETA_2. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

NextBio295860.
PROP70195.
SOURCESearch...

Entry information

Entry namePSB7_MOUSE
AccessionPrimary (citable) accession number: P70195
Secondary accession number(s): O09084 expand/collapse secondary AC list , Q542F7, Q9CZH4, Q9DCF7
Entry history
Integrated into UniProtKB/Swiss-Prot: October 18, 2001
Last sequence update: February 1, 1997
Last modified: July 9, 2014
This is version 135 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot