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P28062

- PSB8_HUMAN

UniProt

P28062 - PSB8_HUMAN

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Protein

Proteasome subunit beta type-8

Gene
PSMB8, LMP7, PSMB5i, RING10, Y2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein 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. This subunit is involved in antigen processing to generate class I binding peptides. Replacement of PSMB5 by PSMB8 increases the capacity of the immunoproteasome to cleave model peptides after hydrophobic and basic residues. Acts as a major component of interferon gamma-induced sensitivity. Plays a key role in apoptosis via the degradation of the apoptotic inhibitor MCL1. May be involved in the inflammatory response pathway. In cancer cells, substitution of isoform 1 (E2) by isoform 2 (E1) results in immunoproteasome deficiency. Required for the differentiation of preadipocytes into adipocytes.4 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sitei72 – 732Cleavage; by autocatalysis By similarity
Active sitei73 – 731Nucleophile By similarity

GO - Molecular functioni

  1. protein binding Source: IntAct
  2. threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

  1. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
  2. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
  3. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
  4. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
  5. apoptotic process Source: Reactome
  6. cellular nitrogen compound metabolic process Source: Reactome
  7. cytokine-mediated signaling pathway Source: Reactome
  8. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
  9. fat cell differentiation Source: UniProtKB
  10. G1/S transition of mitotic cell cycle Source: Reactome
  11. gene expression Source: Reactome
  12. mitotic cell cycle Source: Reactome
  13. mRNA metabolic process Source: Reactome
  14. negative regulation of apoptotic process Source: Reactome
  15. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  16. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  17. protein polyubiquitination Source: Reactome
  18. regulation of apoptotic process Source: Reactome
  19. regulation of cellular amino acid metabolic process Source: Reactome
  20. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
  21. RNA metabolic process Source: Reactome
  22. small molecule metabolic process Source: Reactome
  23. type I interferon signaling pathway Source: Reactome
  24. viral process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Differentiation, Host-virus interaction, Immunity

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_25162. Interferon alpha/beta signaling.
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_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
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_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Protein family/group databases

MEROPSiT01.015.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-8 (EC:3.4.25.1)
Alternative name(s):
Low molecular mass protein 7
Macropain subunit C13
Multicatalytic endopeptidase complex subunit C13
Proteasome component C13
Proteasome subunit beta-5i
Really interesting new gene 10 protein
Gene namesi
Name:PSMB8
Synonyms:LMP7, PSMB5i, RING10, Y2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:9545. PSMB8.

Subcellular locationi

Cytoplasm By similarity. Nucleus By similarity

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular vesicular exosome Source: UniProt
  3. nucleoplasm Source: Reactome
  4. proteasome complex Source: ProtInc
  5. proteasome core complex Source: UniProtKB
  6. spermatoproteasome complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Involvement in diseasei

Nakajo syndrome (NKJO) [MIM:256040]: An autosomal recessive autoinflammatory disorder characterized by early childhood onset of recurrent fever, joint stiffness and severe contractures of the hands and feet, and erythematous skin lesions with subsequent development of lipodystrophy and laboratory evidence of immune dysregulation. Accompanying features may include muscle weakness and atrophy, hepatosplenomegaly, and microcytic anemia.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti75 – 751T → M in NKJO; also found in patients with CANDLE syndrome; markedly decreased chymotrypsin-like activity consistent with a decrease in proteasomal activity and loss of function. 2 Publications
VAR_065291
Natural varianti201 – 2011G → V in NKJO; affects immunoproteasome assembly; reduced proteasome levels; reduced chymotrypsin-like activity consistent with a decrease in proteasomal activity. 2 Publications
VAR_066449
Mutation Met-75 has been found in chronic atypical neutrophilic dermatosis with lipodystrophy and elevated temperature syndrome (CANDLE syndrome). CANDLE patients have some overlapping features with NKJO patients, including a cutaneous eruption and lipodystrophy. They show a characteristic neutrophilic dermatosis with a mononuclear interstitial infiltrate in the dermis that seems pathognomonic for CANDLE syndrome (1 Publication).

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi256040. phenotype.
Orphaneti325004. CANDLE syndrome.
324999. JMP syndrome.
2615. Nakajo-Nishimura syndrome.
PharmGKBiPA33890.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Propeptidei1 – 7272Removed in mature form By similarityPRO_0000026597Add
BLAST
Chaini73 – 276204Proteasome subunit beta type-8PRO_0000026598Add
BLAST

Post-translational modificationi

Autocleaved. The resulting N-terminal Thr residue of the mature subunit is responsible for the nucleophile proteolytic activity By similarity.

Keywords - PTMi

Phosphoprotein, Zymogen

Proteomic databases

MaxQBiP28062.
PaxDbiP28062.
PRIDEiP28062.

PTM databases

PhosphoSiteiP28062.

Expressioni

Developmental stagei

Highly expressed in immature dendritic cells (at protein level).1 Publication

Inductioni

Up-regulated by IFNG/IFN-gamma and IRF1 (at protein level). Up-regulated by TNF (at protein level). Up-regulated by tetrodotoxin (TTX) in glial cells. Up-regulated in Crohn's bowel disease (CD). Down-regulated by the selective inhibitor PR-957. Down-regulated in mature dendritic cells by HSV-1 infection. Up-regulated by heat shock treatment.9 Publications

Gene expression databases

ArrayExpressiP28062.
BgeeiP28062.
CleanExiHS_PSMB8.
GenevestigatoriP28062.

Organism-specific databases

HPAiHPA046995.
HPA050327.

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. Component of the immunoproteasome, where it displaces the equivalent housekeeping subunit PSMB5. Component of the spermatoproteasome, a form of the proteasome specifically found in testis. Directly interacts with POMP. Interacts with HIV-1 TAT protein. Interacts with TAP1.3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
P279584EBI-372294,EBI-3649474From a different organism.

Protein-protein interaction databases

BioGridi111669. 43 interactions.
IntActiP28062. 8 interactions.
MINTiMINT-3010850.
STRINGi9606.ENSP00000402406.

Structurei

3D structure databases

ProteinModelPortaliP28062.
SMRiP28062. Positions 73-273.

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.

Phylogenomic databases

eggNOGiCOG0638.
HOGENOMiHOG000091082.
HOVERGENiHBG108297.
InParanoidiP28062.
KOiK02740.
OMAiSDLMHQY.
PhylomeDBiP28062.
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]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Note: Additional isoforms seem to exist.

Isoform 1 (identifier: P28062-1) [UniParc]FASTAAdd to Basket

Also known as: LMP7B, LMP7-E2

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

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MALLDVCGAP RGQRPESALP VAGSGRRSDP GHYSFSMRSP ELALPRGMQP    50
TEFFQSLGGD GERNVQIEMA HGTTTLAFKF QHGVIAAVDS RASAGSYISA 100
LRVNKVIEIN PYLLGTMSGC AADCQYWERL LAKECRLYYL RNGERISVSA 150
ASKLLSNMMC QYRGMGLSMG SMICGWDKKG PGLYYVDEHG TRLSGNMFST 200
GSGNTYAYGV MDSGYRPNLS PEEAYDLGRR AIAYATHRDS YSGGVVNMYH 250
MKEDGWVKVE STDVSDLLHQ YREANQ 276
Length:276
Mass (Da):30,354
Last modified:May 31, 2011 - v3
Checksum:i4F689501677DBD44
GO
Isoform 2 (identifier: P28062-2) [UniParc]FASTAAdd to Basket

Also known as: LMP7A, LMP7-E1

The sequence of this isoform differs from the canonical sequence as follows:
     1-49: MALLDVCGAP...PELALPRGMQ → MLIGTPTPRD...PVSSGCPGLE

Note: Contains a phosphothreonine at position 5.

Show »
Length:272
Mass (Da):29,770
Checksum:iE5A903101BE5C0B7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti8 – 81G → R in LMP7C.
Corresponds to variant rs114772012 [ dbSNP | Ensembl ].
VAR_006488
Natural varianti30 – 323PGH → RPD in LPM7C.
VAR_006489
Natural varianti49 – 491Q → K.1 Publication
Corresponds to variant rs2071543 [ dbSNP | Ensembl ].
VAR_065204
Natural varianti74 – 741T → S.
Corresponds to variant rs17220206 [ dbSNP | Ensembl ].
VAR_057046
Natural varianti75 – 751T → M in NKJO; also found in patients with CANDLE syndrome; markedly decreased chymotrypsin-like activity consistent with a decrease in proteasomal activity and loss of function. 2 Publications
VAR_065291
Natural varianti201 – 2011G → V in NKJO; affects immunoproteasome assembly; reduced proteasome levels; reduced chymotrypsin-like activity consistent with a decrease in proteasomal activity. 2 Publications
VAR_066449

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4949MALLD…PRGMQ → MLIGTPTPRDTTPSSWLTSS LLVEAAPLDDTTLPTPVSSG CPGLE in isoform 2. VSP_005287Add
BLAST

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66401 Genomic DNA. Translation: CAA47026.1.
X62598 mRNA. Translation: CAA44482.1.
Z14982 Genomic DNA. Translation: CAA78705.1.
Z14982 Genomic DNA. Translation: CAA78706.1.
L11045 Genomic DNA. No translation available.
X87344 Genomic DNA. Translation: CAA60786.1.
X87344 Genomic DNA. Translation: CAA60787.1.
U17496 mRNA. Translation: AAA56777.1.
U17497 mRNA. Translation: AAA56778.1.
AL671681 Genomic DNA. Translation: CAI17712.1.
AL671681 Genomic DNA. Translation: CAI17713.1.
AL669918 Genomic DNA. Translation: CAI18138.1.
AL669918 Genomic DNA. Translation: CAI18139.1.
AL935043 Genomic DNA. Translation: CAI18623.1.
AL935043 Genomic DNA. Translation: CAI18625.1.
BX682530, BX088556 Genomic DNA. Translation: CAM25945.1.
BX682530, BX088556 Genomic DNA. Translation: CAM25947.1.
BX088556, BX682530 Genomic DNA. Translation: CAM26261.1.
BX088556, BX682530 Genomic DNA. Translation: CAM26262.1.
CT009502 Genomic DNA. Translation: CAQ07779.1.
CT009502 Genomic DNA. Translation: CAQ07781.1.
BX927138 Genomic DNA. Translation: CAQ08445.1.
BX927138 Genomic DNA. Translation: CAQ08448.1.
CR762476 Genomic DNA. Translation: CAQ08492.1.
CR762476 Genomic DNA. Translation: CAQ08494.1.
CR753889 Genomic DNA. Translation: CAQ10284.1.
CR753889 Genomic DNA. Translation: CAQ10286.1.
CH471081 Genomic DNA. Translation: EAX03644.1.
CH471081 Genomic DNA. Translation: EAX03645.1.
BC001114 mRNA. Translation: AAH01114.1.
U32863 Genomic DNA. Translation: AAA80235.1.
U32862 Genomic DNA. Translation: AAA80234.1.
CCDSiCCDS4756.1. [P28062-2]
CCDS4757.1. [P28062-1]
PIRiA44324.
C44324.
G01564.
G02018.
RefSeqiNP_004150.1. NM_004159.4. [P28062-2]
NP_683720.2. NM_148919.3. [P28062-1]
UniGeneiHs.180062.

Genome annotation databases

EnsembliENST00000374881; ENSP00000364015; ENSG00000204264. [P28062-2]
ENST00000374882; ENSP00000364016; ENSG00000204264. [P28062-1]
ENST00000383236; ENSP00000372723; ENSG00000206298. [P28062-1]
ENST00000383238; ENSP00000372725; ENSG00000206298. [P28062-2]
ENST00000416134; ENSP00000397057; ENSG00000235715. [P28062-2]
ENST00000416564; ENSP00000408825; ENSG00000226201. [P28062-2]
ENST00000421445; ENSP00000402406; ENSG00000236443. [P28062-1]
ENST00000429645; ENSP00000394155; ENSG00000226201. [P28062-1]
ENST00000435978; ENSP00000414731; ENSG00000231631. [P28062-2]
ENST00000436627; ENSP00000392693; ENSG00000230669. [P28062-2]
ENST00000438442; ENSP00000404585; ENSG00000231631. [P28062-1]
ENST00000441960; ENSP00000407539; ENSG00000230034. [P28062-2]
ENST00000452573; ENSP00000412618; ENSG00000236443. [P28062-2]
ENST00000455660; ENSP00000406797; ENSG00000230669. [P28062-1]
ENST00000457261; ENSP00000414770; ENSG00000235715. [P28062-1]
ENST00000546794; ENSP00000448520; ENSG00000230034. [P28062-1]
GeneIDi5696.
KEGGihsa:5696.
UCSCiuc003oce.3. human. [P28062-1]
uc003ocf.3. human. [P28062-2]

Polymorphism databases

DMDMi334302881.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X66401 Genomic DNA. Translation: CAA47026.1 .
X62598 mRNA. Translation: CAA44482.1 .
Z14982 Genomic DNA. Translation: CAA78705.1 .
Z14982 Genomic DNA. Translation: CAA78706.1 .
L11045 Genomic DNA. No translation available.
X87344 Genomic DNA. Translation: CAA60786.1 .
X87344 Genomic DNA. Translation: CAA60787.1 .
U17496 mRNA. Translation: AAA56777.1 .
U17497 mRNA. Translation: AAA56778.1 .
AL671681 Genomic DNA. Translation: CAI17712.1 .
AL671681 Genomic DNA. Translation: CAI17713.1 .
AL669918 Genomic DNA. Translation: CAI18138.1 .
AL669918 Genomic DNA. Translation: CAI18139.1 .
AL935043 Genomic DNA. Translation: CAI18623.1 .
AL935043 Genomic DNA. Translation: CAI18625.1 .
BX682530 , BX088556 Genomic DNA. Translation: CAM25945.1 .
BX682530 , BX088556 Genomic DNA. Translation: CAM25947.1 .
BX088556 , BX682530 Genomic DNA. Translation: CAM26261.1 .
BX088556 , BX682530 Genomic DNA. Translation: CAM26262.1 .
CT009502 Genomic DNA. Translation: CAQ07779.1 .
CT009502 Genomic DNA. Translation: CAQ07781.1 .
BX927138 Genomic DNA. Translation: CAQ08445.1 .
BX927138 Genomic DNA. Translation: CAQ08448.1 .
CR762476 Genomic DNA. Translation: CAQ08492.1 .
CR762476 Genomic DNA. Translation: CAQ08494.1 .
CR753889 Genomic DNA. Translation: CAQ10284.1 .
CR753889 Genomic DNA. Translation: CAQ10286.1 .
CH471081 Genomic DNA. Translation: EAX03644.1 .
CH471081 Genomic DNA. Translation: EAX03645.1 .
BC001114 mRNA. Translation: AAH01114.1 .
U32863 Genomic DNA. Translation: AAA80235.1 .
U32862 Genomic DNA. Translation: AAA80234.1 .
CCDSi CCDS4756.1. [P28062-2 ]
CCDS4757.1. [P28062-1 ]
PIRi A44324.
C44324.
G01564.
G02018.
RefSeqi NP_004150.1. NM_004159.4. [P28062-2 ]
NP_683720.2. NM_148919.3. [P28062-1 ]
UniGenei Hs.180062.

3D structure databases

ProteinModelPortali P28062.
SMRi P28062. Positions 73-273.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111669. 43 interactions.
IntActi P28062. 8 interactions.
MINTi MINT-3010850.
STRINGi 9606.ENSP00000402406.

Chemistry

BindingDBi P28062.
ChEMBLi CHEMBL5620.

Protein family/group databases

MEROPSi T01.015.

PTM databases

PhosphoSitei P28062.

Polymorphism databases

DMDMi 334302881.

Proteomic databases

MaxQBi P28062.
PaxDbi P28062.
PRIDEi P28062.

Protocols and materials databases

DNASUi 5696.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000374881 ; ENSP00000364015 ; ENSG00000204264 . [P28062-2 ]
ENST00000374882 ; ENSP00000364016 ; ENSG00000204264 . [P28062-1 ]
ENST00000383236 ; ENSP00000372723 ; ENSG00000206298 . [P28062-1 ]
ENST00000383238 ; ENSP00000372725 ; ENSG00000206298 . [P28062-2 ]
ENST00000416134 ; ENSP00000397057 ; ENSG00000235715 . [P28062-2 ]
ENST00000416564 ; ENSP00000408825 ; ENSG00000226201 . [P28062-2 ]
ENST00000421445 ; ENSP00000402406 ; ENSG00000236443 . [P28062-1 ]
ENST00000429645 ; ENSP00000394155 ; ENSG00000226201 . [P28062-1 ]
ENST00000435978 ; ENSP00000414731 ; ENSG00000231631 . [P28062-2 ]
ENST00000436627 ; ENSP00000392693 ; ENSG00000230669 . [P28062-2 ]
ENST00000438442 ; ENSP00000404585 ; ENSG00000231631 . [P28062-1 ]
ENST00000441960 ; ENSP00000407539 ; ENSG00000230034 . [P28062-2 ]
ENST00000452573 ; ENSP00000412618 ; ENSG00000236443 . [P28062-2 ]
ENST00000455660 ; ENSP00000406797 ; ENSG00000230669 . [P28062-1 ]
ENST00000457261 ; ENSP00000414770 ; ENSG00000235715 . [P28062-1 ]
ENST00000546794 ; ENSP00000448520 ; ENSG00000230034 . [P28062-1 ]
GeneIDi 5696.
KEGGi hsa:5696.
UCSCi uc003oce.3. human. [P28062-1 ]
uc003ocf.3. human. [P28062-2 ]

Organism-specific databases

CTDi 5696.
GeneCardsi GC06M032808.
GC06Mi32792.
GC06Mj32730.
GC06Mk32786.
GC06Ml32962.
GC06Mm32841.
GC06Mn32737.
GC06Mo32898.
HGNCi HGNC:9545. PSMB8.
HPAi HPA046995.
HPA050327.
MIMi 177046. gene.
256040. phenotype.
neXtProti NX_P28062.
Orphaneti 325004. CANDLE syndrome.
324999. JMP syndrome.
2615. Nakajo-Nishimura syndrome.
PharmGKBi PA33890.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0638.
HOGENOMi HOG000091082.
HOVERGENi HBG108297.
InParanoidi P28062.
KOi K02740.
OMAi SDLMHQY.
PhylomeDBi P28062.
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_25162. Interferon alpha/beta signaling.
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_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
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_9003. SCF(Skp2)-mediated degradation of p27/p21.
REACT_9031. Vpu mediated degradation of CD4.
REACT_9453. Vif-mediated degradation of APOBEC3G.

Miscellaneous databases

ChiTaRSi PSMB8. human.
GeneWikii PSMB8.
GenomeRNAii 5696.
NextBioi 22126.
PROi P28062.
SOURCEi Search...

Gene expression databases

ArrayExpressi P28062.
Bgeei P28062.
CleanExi HS_PSMB8.
Genevestigatori P28062.

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. "The major histocompatibility complex-encoded proteasome component LMP7: alternative first exons and post-translational processing."
    Glynne R., Kerr L.A., Mockridge I., Beck S., Kelly A., Trowsdale J.
    Eur. J. Immunol. 23:860-866(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "DNA sequence analysis of 66 kb of the human MHC class II region encoding a cluster of genes for antigen processing."
    Beck S., Kelly A., Radley E., Khurshid F., Alderton R.P., Trowsdale J.
    J. Mol. Biol. 228:433-441(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "A proteasome-related gene between the two ABC transporter loci in the class II region of the human MHC."
    Glynne R., Powis S.H., Beck S., Kelly A., Kerr L.A., Trowsdale J.
    Nature 353:357-360(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
  4. "Alternative exon usage and processing of the major histocompatibility complex-encoded proteasome subunits."
    Fruh K., Yang Y., Arnold D., Chambers J., Wu L., Waters J.B., Spies T., Peterson P.A.
    J. Biol. Chem. 267:22131-22140(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "Different genomic structure of mouse and human Lmp7 genes: characterization of MHC-encoded proteasome genes."
    Meinhardt T., Graf U., Hammerling G.J.
    Immunogenetics 38:373-379(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  6. "Evolutionary dynamics of non-coding sequences within the class II region of the human MHC."
    Beck S., Abdulla S., Alderton R.P., Glynne R.J., Gut I.G., Hosking L.K., Jackson A., Kelly A., Newell W.R., Sanseau P., Radley E., Thorpe K.L., Trowsdale J.
    J. Mol. Biol. 255:1-13(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  7. "Sequence analysis of the HLA-linked LMP7 gene."
    Maksymowych W.P.
    Submitted (NOV-1994) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ALLELE LMP7C), VARIANT LYS-49.
  8. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  10. "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] (ISOFORM 2).
    Tissue: Skin.
  11. "Two newly discovered alleles of major histocompatibility complex-encoded LMP7 in Korean populations."
    Kim T.G., Lee Y.H., Choi H.B., Han H.
    Hum. Immunol. 46:61-64(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 191-269.
    Tissue: Blood.
  12. "Replacement of proteasome subunits X and Y by LMP7 and LMP2 induced by interferon-gamma for acquirement of the functional diversity responsible for antigen processing."
    Akiyama K., Kagawa S., Tamura T., Shimbara N., Takashina M., Kristensen P., Hendil K.B., Tanaka K., Ichihara A.
    FEBS Lett. 343:85-88(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  13. "Proteasome subunits X and Y alter peptidase activities in opposite ways to the interferon-gamma-induced subunits LMP2 and LMP7."
    Gaczynska M., Goldberg A.L., Tanaka K., Hendil K.B., Rock K.L.
    J. Biol. Chem. 271:17275-17280(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  14. "Tumor necrosis factor-alpha induces coordinated changes in major histocompatibility class I presentation pathway, resulting in increased stability of class I complexes at the cell surface."
    Hallermalm K., Seki K., Wei C., Castelli C., Rivoltini L., Kiessling R., Levitskaya J.
    Blood 98:1108-1115(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY TNF AND IFNG.
  15. "Bipartite regulation of different components of the MHC class I antigen-processing machinery during dendritic cell maturation."
    Li J., Schuler-Thurner B., Schuler G., Huber C., Seliger B.
    Int. Immunol. 13:1515-1523(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE.
  16. "Human immunodeficiency virus-1 Tat protein interacts with distinct proteasomal alpha and beta subunits."
    Apcher G.S., Heink S., Zantopf D., Kloetzel P.-M., Schmid H.-P., Mayer R.J., Krueger E.
    FEBS Lett. 553:200-204(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH HIV-1 TAT.
  17. "Potential effects of tetrodotoxin exposure to human glial cells postulated using microarray approach."
    Raghavendra Prasad H.S., Qi Z., Srinivasan K.N., Gopalakrishnakone P.
    Toxicon 44:597-608(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY TETRODOTOXIN.
  18. "IRF-1 mediates upregulation of LMP7 by IFN-gamma and concerted expression of immunosubunits of the proteasome."
    Namiki S., Nakamura T., Oshima S., Yamazaki M., Sekine Y., Tsuchiya K., Okamoto R., Kanai T., Watanabe M.
    FEBS Lett. 579:2781-2787(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY IFNG AND IRF1.
  19. "Cytoplasmic domains of the transporter associated with antigen processing and P-glycoprotein interact with subunits of the proteasome."
    Begley G.S., Horvath A.R., Taylor J.C., Higgins C.F.
    Mol. Immunol. 42:137-141(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TAP1.
  20. "IFN-gamma-induced immune adaptation of the proteasome system is an accelerated and transient response."
    Heink S., Ludwig D., Kloetzel P.-M., Krueger E.
    Proc. Natl. Acad. Sci. U.S.A. 102:9241-9246(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POMP.
  21. "Tumor cell lines expressing the proteasome subunit isoform LMP7E1 exhibit immunoproteasome deficiency."
    Heink S., Fricke B., Ludwig D., Kloetzel P.M., Krueger E.
    Cancer Res. 66:649-652(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  22. "Heat shock up-regulates lmp2 and lmp7 and enhances presentation of immunoproteasome-dependent epitopes."
    Callahan M.K., Wohlfert E.A., Menoret A., Srivastava P.K.
    J. Immunol. 177:8393-8399(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY HEAT SHOCK.
  23. "Genome-wide gene expression differences in Crohn's disease and ulcerative colitis from endoscopic pinch biopsies: insights into distinctive pathogenesis."
    Wu F., Dassopoulos T., Cope L., Maitra A., Brant S.R., Harris M.L., Bayless T.M., Parmigiani G., Chakravarti S.
    Inflamm. Bowel Dis. 13:807-821(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  24. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-5 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  25. "Cardiovascular inflammation and lesion cell apoptosis: a novel connection via the interferon-inducible immunoproteasome."
    Yang Z., Gagarin D., St Laurent G. III, Hammell N., Toma I., Hu C.A., Iwasa A., McCaffrey T.A.
    Arterioscler. Thromb. Vasc. Biol. 29:1213-1219(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY IFNG, FUNCTION.
  26. "Herpes simplex virus type I infection of mature dendritic cells leads to reduced LMP7-mRNA-expression levels."
    Eisemann J., Prechtel A.T., Muehl-Zuerbes P., Steinkasserer A., Kummer M.
    Immunobiology 214:861-867(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION.
  27. "A selective inhibitor of the immunoproteasome subunit LMP7 blocks cytokine production and attenuates progression of experimental arthritis."
    Muchamuel T., Basler M., Aujay M.A., Suzuki E., Kalim K.W., Lauer C., Sylvain C., Ring E.R., Shields J., Jiang J., Shwonek P., Parlati F., Demo S.D., Bennett M.K., Kirk C.J., Groettrup M.
    Nat. Med. 15:781-787(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INDUCTION BY PR-957.
  28. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  29. Cited for: FUNCTION IN ADIPOCYTE DIFFERENTIATION, VARIANT NKJO VAL-201, CHARACTERIZATION OF VARIANT NKJO VAL-201.
  30. "PSMB8 encoding the beta5i proteasome subunit is mutated in joint contractures, muscle atrophy, microcytic anemia, and panniculitis-induced lipodystrophy syndrome."
    Agarwal A.K., Xing C., DeMartino G.N., Mizrachi D., Hernandez M.D., Sousa A.B., Martinez de Villarreal L., dos Santos H.G., Garg A.
    Am. J. Hum. Genet. 87:866-872(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT NKJO MET-75, CHARACTERIZATION OF VARIANT NKJO MET-75.
  31. "Mutations in proteasome subunit beta type 8 cause chronic atypical neutrophilic dermatosis with lipodystrophy and elevated temperature with evidence of genetic and phenotypic heterogeneity."
    Liu Y., Ramot Y., Torrelo A., Paller A.S., Si N., Babay S., Kim P.W., Sheikh A., Lee C.C., Chen Y., Vera A., Zhang X., Goldbach-Mansky R., Zlotogorski A.
    Arthritis Rheum. 64:895-907(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT OF VARIANT NKJO MET-75 IN CANDLE SYNDROME.
  32. Cited for: VARIANT NKJO VAL-201, CHARACTERIZATION OF VARIANT NKJO VAL-201.

Entry informationi

Entry nameiPSB8_HUMAN
AccessioniPrimary (citable) accession number: P28062
Secondary accession number(s): B0UZC0
, Q29824, Q5JNW6, Q5QNR8, Q96J48
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: May 31, 2011
Last modified: September 3, 2014
This is version 171 of the entry and version 3 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 6
    Human chromosome 6: 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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