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A5LHX3

- PSB11_HUMAN

UniProt

A5LHX3 - PSB11_HUMAN

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Protein
Proteasome subunit beta type-11
Gene
PSMB11
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at transcript 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. 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 activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Active sitei50 – 501Nucleophile By similarity

GO - Molecular functioni

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

GO - Biological processi

  1. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  2. RNA metabolic process Source: Reactome
  3. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  4. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  5. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  6. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  7. apoptotic process Source: Reactome
  8. cellular nitrogen compound metabolic process Source: Reactome
  9. gene expression Source: Reactome
  10. mRNA metabolic process Source: Reactome
  11. mitotic cell cycle Source: Reactome
  12. negative regulation of apoptotic process Source: Reactome
  13. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  14. protein polyubiquitination Source: Reactome
  15. regulation of apoptotic process Source: Reactome
  16. regulation of cellular amino acid metabolic process Source: Reactome
  17. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  18. small molecule metabolic process Source: Reactome
  19. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Enzyme and pathway databases

ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiT01.016.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-11 (EC:3.4.25.1)
Alternative name(s):
Proteasome subunit beta-5t
Gene namesi
Name:PSMB11
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 14

Organism-specific databases

HGNCiHGNC:31963. PSMB11.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. nucleus Source: UniProtKB-SubCell
  3. proteasome core complex Source: InterPro
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA162400222.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 4949Removed in mature form By similarity
PRO_0000300011Add
BLAST
Chaini50 – 300251Proteasome subunit beta type-11
PRO_0000300012Add
BLAST

Keywords - PTMi

Zymogen

Proteomic databases

PaxDbiA5LHX3.
PRIDEiA5LHX3.

PTM databases

PhosphoSiteiA5LHX3.

Expressioni

Gene expression databases

BgeeiA5LHX3.
CleanExiHS_PSMB11.
GenevestigatoriA5LHX3.

Organism-specific databases

HPAiHPA056970.

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. Incorporated instead of PSMB5 and PSMB8.

Protein-protein interaction databases

STRINGi9606.ENSP00000386212.

Structurei

3D structure databases

ProteinModelPortaliA5LHX3.
SMRiA5LHX3. Positions 50-245.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiA5LHX3.
KOiK11598.
OMAiYRVLQRE.
OrthoDBiEOG7FNC86.
PhylomeDBiA5LHX3.
TreeFamiTF106223.

Family and domain databases

Gene3Di3.60.20.10. 1 hit.
InterProiIPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view]
PfamiPF00227. 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.

A5LHX3-1 [UniParc]FASTAAdd to Basket

« Hide

MALQDVCKWQ SPDTQGPSPH LPRAGGWAVP RGCDPQTFLQ IHGPRLAHGT    50
TTLAFRFRHG VIAAADTRSS CGSYVACPAS CKVIPVHQHL LGTTSGTSAD 100
CATWYRVLQR ELRLRELREG QLPSVASAAK LLSAMMSQYR GLDLCVATAL 150
CGWDRSGPEL FYVYSDGTRL QGDIFSVGSG SPYAYGVLDR GYRYDMSTQE 200
AYALARCAVA HATHRDAYSG GSVDLFHVRE SGWEHVSRSD ACVLYVELQK 250
LLEPEPEEDA SHAHPEPATA HRAAEDRELS VGPGEVTPGD SRMPAGTETV 300
Length:300
Mass (Da):32,530
Last modified:July 10, 2007 - v1
Checksum:i234ECBD1D230A7E8
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti49 – 491G → S.
Corresponds to variant rs34457782 [ dbSNP | Ensembl ].
VAR_051550

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB299437 mRNA. Translation: BAF63540.1.
AL132780 Genomic DNA. No translation available.
CCDSiCCDS41923.1.
RefSeqiNP_001093250.1. NM_001099780.1.
UniGeneiHs.508918.

Genome annotation databases

EnsembliENST00000408907; ENSP00000386212; ENSG00000222028.
GeneIDi122706.
KEGGihsa:122706.
UCSCiuc010ake.1. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AB299437 mRNA. Translation: BAF63540.1 .
AL132780 Genomic DNA. No translation available.
CCDSi CCDS41923.1.
RefSeqi NP_001093250.1. NM_001099780.1.
UniGenei Hs.508918.

3D structure databases

ProteinModelPortali A5LHX3.
SMRi A5LHX3. Positions 50-245.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

STRINGi 9606.ENSP00000386212.

Chemistry

ChEMBLi CHEMBL2364701.

Protein family/group databases

MEROPSi T01.016.

PTM databases

PhosphoSitei A5LHX3.

Proteomic databases

PaxDbi A5LHX3.
PRIDEi A5LHX3.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000408907 ; ENSP00000386212 ; ENSG00000222028 .
GeneIDi 122706.
KEGGi hsa:122706.
UCSCi uc010ake.1. human.

Organism-specific databases

CTDi 122706.
GeneCardsi GC14P023511.
H-InvDB HIX0026673.
HGNCi HGNC:31963. PSMB11.
HPAi HPA056970.
MIMi 611137. gene.
neXtProti NX_A5LHX3.
PharmGKBi PA162400222.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091082.
HOVERGENi HBG108297.
InParanoidi A5LHX3.
KOi K11598.
OMAi YRVLQRE.
OrthoDBi EOG7FNC86.
PhylomeDBi A5LHX3.
TreeFami TF106223.

Enzyme and pathway databases

Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).
REACT_111178. ER-Phagosome pathway.
REACT_1156. Orc1 removal from chromatin.
REACT_118656. Activation of NF-kappaB in B cells.
REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
REACT_13565. Regulation of ornithine decarboxylase (ODC).
REACT_150471. Separation of Sister Chromatids.
REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
REACT_172638. Asymmetric localization of PCP proteins.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_200766. degradation of AXIN.
REACT_200841. degradation of DVL.
REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

GenomeRNAii 122706.
NextBioi 80970.
PROi A5LHX3.
SOURCEi Search...

Gene expression databases

Bgeei A5LHX3.
CleanExi HS_PSMB11.
Genevestigatori A5LHX3.

Family and domain databases

Gene3Di 3.60.20.10. 1 hit.
InterProi IPR029055. Ntn_hydrolases_N.
IPR000243. Pept_T1A_subB.
IPR016050. Proteasome_bsu_CS.
IPR001353. Proteasome_sua/b.
IPR023333. Proteasome_suB-type.
[Graphical view ]
Pfami 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. "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].

Entry informationi

Entry nameiPSB11_HUMAN
AccessioniPrimary (citable) accession number: A5LHX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: September 11, 2007
Last sequence update: July 10, 2007
Last modified: September 3, 2014
This is version 66 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. Peptidase families
    Classification of peptidase families and list of entries
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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