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A5LHX3 (PSB11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | 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-11

EC=3.4.25.1
Alternative name(s):
Proteasome subunit beta-5t
Gene names
Name:PSMB11
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length300 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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. Incorporated instead of PSMB5 or PSMB8, this unit reduces the chymotrypsin-like activity of the proteasome By similarity. Plays a pivotal role in development of CD8-positive T cells 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. Incorporated instead of PSMB5 and PSMB8.

Subcellular location

Cytoplasm By similarity. Nucleus By similarity.

Sequence similarities

Belongs to the peptidase T1B family.

Ontologies

Keywords
   Cellular componentCytoplasm
Nucleus
Proteasome
   Coding sequence diversityPolymorphism
   Molecular functionHydrolase
Protease
Threonine protease
   PTMZymogen
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processDNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest

Traceable author statement. Source: Reactome

RNA metabolic process

Traceable author statement. Source: Reactome

anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I

Traceable author statement. Source: Reactome

antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent

Traceable author statement. Source: Reactome

antigen processing and presentation of peptide antigen via MHC class I

Traceable author statement. Source: Reactome

apoptotic process

Traceable author statement. Source: Reactome

cellular nitrogen compound metabolic process

Traceable author statement. Source: Reactome

gene expression

Traceable author statement. Source: Reactome

mRNA metabolic process

Traceable author statement. Source: Reactome

mitotic cell cycle

Traceable author statement. Source: Reactome

negative regulation of apoptotic process

Traceable author statement. Source: Reactome

positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

protein polyubiquitination

Traceable author statement. Source: Reactome

regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of cellular amino acid metabolic process

Traceable author statement. Source: Reactome

regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle

Traceable author statement. Source: Reactome

small molecule metabolic process

Traceable author statement. Source: Reactome

viral process

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

proteasome core complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionthreonine-type endopeptidase activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Propeptide1 – 4949Removed in mature form By similarity
PRO_0000300011
Chain50 – 300251Proteasome subunit beta type-11
PRO_0000300012

Sites

Active site501Nucleophile By similarity

Natural variations

Natural variant491G → S.
Corresponds to variant rs34457782 [ dbSNP | Ensembl ].
VAR_051550

Sequences

Sequence LengthMass (Da)Tools
A5LHX3 [UniParc].

Last modified July 10, 2007. Version 1.
Checksum: 234ECBD1D230A7E8

FASTA30032,530
        10         20         30         40         50         60 
MALQDVCKWQ SPDTQGPSPH LPRAGGWAVP RGCDPQTFLQ IHGPRLAHGT TTLAFRFRHG 

        70         80         90        100        110        120 
VIAAADTRSS CGSYVACPAS CKVIPVHQHL LGTTSGTSAD CATWYRVLQR ELRLRELREG 

       130        140        150        160        170        180 
QLPSVASAAK LLSAMMSQYR GLDLCVATAL CGWDRSGPEL FYVYSDGTRL QGDIFSVGSG 

       190        200        210        220        230        240 
SPYAYGVLDR GYRYDMSTQE AYALARCAVA HATHRDAYSG GSVDLFHVRE SGWEHVSRSD 

       250        260        270        280        290        300 
ACVLYVELQK LLEPEPEEDA SHAHPEPATA HRAAEDRELS VGPGEVTPGD SRMPAGTETV 

« Hide

References

« Hide 'large scale' references
[1]"Regulation of CD8+ T cell development by thymus-specific proteasomes."
Murata S., Sasaki K., Kishimoto T., Niwa S., Hayashi H., Takahama Y., Tanaka K.
Science 316:1349-1353(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AB299437 mRNA. Translation: BAF63540.1.
AL132780 Genomic DNA. No translation available.
CCDSCCDS41923.1.
RefSeqNP_001093250.1. NM_001099780.1.
UniGeneHs.508918.

3D structure databases

ProteinModelPortalA5LHX3.
SMRA5LHX3. Positions 50-245.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

STRING9606.ENSP00000386212.

Chemistry

ChEMBLCHEMBL2364701.

Protein family/group databases

MEROPST01.016.

PTM databases

PhosphoSiteA5LHX3.

Proteomic databases

PaxDbA5LHX3.
PRIDEA5LHX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000408907; ENSP00000386212; ENSG00000222028.
GeneID122706.
KEGGhsa:122706.
UCSCuc010ake.1. human.

Organism-specific databases

CTD122706.
GeneCardsGC14P023511.
H-InvDBHIX0026673.
HGNCHGNC:31963. PSMB11.
HPAHPA056970.
MIM611137. gene.
neXtProtNX_A5LHX3.
PharmGKBPA162400222.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG0638.
HOGENOMHOG000091082.
HOVERGENHBG108297.
InParanoidA5LHX3.
KOK11598.
OMAYRVLQRE.
OrthoDBEOG7FNC86.
PhylomeDBA5LHX3.
TreeFamTF106223.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
REACT_111217. Metabolism.
REACT_115566. Cell Cycle.
REACT_116125. Disease.
REACT_13505. Proteasome mediated degradation of PAK-2p34.
REACT_21257. Metabolism of RNA.
REACT_21300. Mitotic M-M/G1 phases.
REACT_383. DNA Replication.
REACT_578. Apoptosis.
REACT_6850. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
REACT_6900. Immune System.
REACT_71. Gene Expression.

Gene expression databases

BgeeA5LHX3.
CleanExHS_PSMB11.
GenevestigatorA5LHX3.

Family and domain databases

Gene3D3.60.20.10. 1 hit.
InterProIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamPF00227. 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

GenomeRNAi122706.
NextBio80970.
PROA5LHX3.
SOURCESearch...

Entry information

Entry namePSB11_HUMAN
AccessionPrimary (citable) accession number: A5LHX3
Entry history
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 10, 2007
Last modified: July 9, 2014
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

Peptidase families

Classification of peptidase families and list of entries

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM