Statements in which the resource exists as a subject.
PredicateObject
rdf:type
biopax3:comment
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. CATALYTIC ACTIVITY: Cleavage of peptide bonds with very broad specificity. SUBUNIT: 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. Interacts with HIV- 1 TAT protein. SUBCELLULAR LOCATION: Cytoplasm. Nucleus. TISSUE SPECIFICITY: Expressed at a low level in colonic mucosa. Up-regulated in colorectal cancer tissues. SIMILARITY: Belongs to the peptidase T1B family. GENE SYNONYMS:PSMB7 Z. COPYRIGHT: Protein annotation is derived from the UniProt Consortium (http://www.uniprot.org/). Distributed under the Creative Commons Attribution-NoDerivs License., SEQUENCE 277 AA; 29965 MW; A610C949A0ACF1CE CRC64;
biopax3:xref
biopax3:displayName
PSB7_HUMAN
biopax3:name
3.4.25.1, Macropain chain Z, Multicatalytic endopeptidase complex chain Z, PSMB7, Proteasome subunit Z
biopax3:entityFeature
biopax3:organism
biopax3:sequence
MAAVSVYAPPVGGFSFDNCRRNAVLEADFAKRGYKLPKVRKTGTTIAGVVYKDGIVLGADTRATEGMVVADKNCSKIHFISPNIYCCGAGTAADTDMTTQLISSNLELHSLSTGRLPRVVTANRMLKQMLFRYQGYIGAALVLGGVDVTGPHLYSIYPHGSTDKLPYVTMGSGSLAAMAVFEDKFRPDMEEEEAKNLVSEAIAAGIFNDLGSGSNIDLCVISKNKLDFLRPYTVPNKKGTRLGRYRCEKGTTAVLTEKITPLEIEVLEETVQTMDTS
biopax3:standardName
Proteasome subunit beta type-7