A5LHX3 (PSB11_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Proteasome subunit beta type-11
EC=3.4.25.1

Alternative name(s):
Proteasome subunit beta-5t

Gene names

Name:

PSMB11

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	300 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence 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 component	Cytoplasm Nucleus Proteasome
Coding sequence diversity	Polymorphism
Molecular function	Hydrolase Protease Threonine protease
PTM	Zymogen
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Traceable author statement. Source: Reactome M/G1 transition of mitotic cell cycle Traceable author statement. Source: Reactome S phase of mitotic cell cycle 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, TAP-dependent Traceable author statement. Source: Reactome apoptotic process Traceable author statement. Source: Reactome gene expression Traceable author statement. Source: Reactome mRNA metabolic 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 small molecule metabolic process Traceable author statement. Source: Reactome viral reproduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell proteasome core complex Inferred from electronic annotation. Source: InterPro
Molecular_function	threonine-type endopeptidase activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Propeptide	1 – 49	49	Removed in mature form By similarity		PRO_0000300011
	Chain	50 – 300	251	Proteasome subunit beta type-11		PRO_0000300012
Sites
	Active site	50	1	Nucleophile By similarity
Natural variations
	Natural variant	49	1	G → S. Corresponds to variant rs34457782 [ dbSNP | Ensembl ].		VAR_051550

Sequences

	Sequence		Length	Mass (Da)
	A5LHX3 [UniParc]. Last modified July 10, 2007. Version 1. Checksum: 234ECBD1D230A7E8	FASTA	300	32,530
	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

References

	« Hide 'large scale' referencesShow '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. , 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.
IPI	IPI00051808.
RefSeq	NP_001093250.1. NM_001099780.1.
UniGene	Hs.508918.
3D structure databases
ProteinModelPortal	A5LHX3.
ModBase	Search...
Protein-protein interaction databases
STRING	9606.ENSP00000386212.
Protein family/group databases
MEROPS	T01.016.
PTM databases
PhosphoSite	A5LHX3.
Proteomic databases
PaxDb	A5LHX3.
PRIDE	A5LHX3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000408907; ENSP00000386212; ENSG00000222028.
GeneID	122706.
KEGG	hsa:122706.
UCSC	uc010ake.1. human.
Organism-specific databases
CTD	122706.
GeneCards	GC14P023511.
H-InvDB	HIX0026673.
HGNC	HGNC:31963. PSMB11.
MIM	611137. gene.
neXtProt	NX_A5LHX3.
PharmGKB	PA162400222.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG0638.
HOGENOM	HOG000091082.
HOVERGEN	HBG108297.
InParanoid	A5LHX3.
KO	K11598.
OMA	SADCATW.
OrthoDB	EOG44J2JN.
PhylomeDB	A5LHX3.
Enzyme and pathway databases
Reactome	REACT_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
Bgee	A5LHX3.
CleanEx	HS_PSMB11.
Genevestigator	A5LHX3.
Family and domain databases
InterPro	IPR000243. Pept_T1A_subB. IPR016050. Proteasome_bsu_CS. IPR001353. Proteasome_sua/b. IPR023333. Proteasome_suB-type. [Graphical view]
Pfam	PF00227. Proteasome. 1 hit. [Graphical view]
PRINTS	PR00141. PROTEASOME.
PROSITE	PS00854. PROTEASOME_B_1. 1 hit. PS51476. PROTEASOME_B_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
GenomeRNAi	122706.
NextBio	80970.
SOURCE	Search...

Entry information

Entry name

PSB11_HUMAN

Accession

Primary (citable) accession number: A5LHX3

Entry history

Integrated into UniProtKB/Swiss-Prot:	September 11, 2007
Last sequence update:	July 10, 2007
Last modified:	May 1, 2013
This is version 52 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.