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Protein

Proteasome subunit beta type-5

Gene

PSMB5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 unit is responsible of the chymotrypsin-like activity of the proteasome and is one of the principal target of the proteasome inhibitor bortezomib. May catalyze basal processing of intracellular antigens. Plays a role in the protection against oxidative damage through the Nrf2-ARE pathway (By similarity).By similarity2 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei60Nucleophile1
Binding sitei108Bortezomib; via amide nitrogenBy similarity1

GO - Molecular functioni

  • peptidase activity Source: MGI
  • threonine-type endopeptidase activity Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Hydrolase, Protease, Threonine protease

Keywords - Biological processi

Host-virus interaction

Enzyme and pathway databases

BioCyciZFISH:HS02145-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiP28074.

Protein family/group databases

MEROPSiT01.012.

Names & Taxonomyi

Protein namesi
Recommended name:
Proteasome subunit beta type-5 (EC:3.4.25.1)
Alternative name(s):
Macropain epsilon chain
Multicatalytic endopeptidase complex epsilon chain
Proteasome chain 6
Proteasome epsilon chain
Proteasome subunit MB1
Proteasome subunit X
Gene namesi
Name:PSMB5
Synonyms:LMPX, MB1, X
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 14

Organism-specific databases

HGNCiHGNC:9542. PSMB5.

Subcellular locationi

GO - Cellular componenti

  • centrosome Source: HPA
  • cytosol Source: Reactome
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome core complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi108A → T: Displays resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with V-109. 3 Publications1
Mutagenesisi108A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity. 3 Publications1
Mutagenesisi109A → V: Displays high resistance to the bortezomib, a proteasome inhibitor of the chymotrypsin-like activity; when associated with T-108. 1 Publication1

Organism-specific databases

DisGeNETi5693.
OpenTargetsiENSG00000100804.
PharmGKBiPA33887.

Chemistry databases

ChEMBLiCHEMBL4662.
DrugBankiDB00188. Bortezomib.
DB08889. Carfilzomib.
GuidetoPHARMACOLOGYi2406.

Polymorphism and mutation databases

BioMutaiPSMB5.
DMDMi187608890.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
PropeptideiPRO_00000265891 – 59Removed in mature form1 PublicationAdd BLAST59
ChainiPRO_000002659060 – 263Proteasome subunit beta type-5Add BLAST204

Keywords - PTMi

Zymogen

Proteomic databases

EPDiP28074.
MaxQBiP28074.
PaxDbiP28074.
PeptideAtlasiP28074.
PRIDEiP28074.
TopDownProteomicsiP28074-1. [P28074-1]

2D gel databases

REPRODUCTION-2DPAGEIPI00479306.

PTM databases

iPTMnetiP28074.
PhosphoSitePlusiP28074.
SwissPalmiP28074.

Expressioni

Inductioni

Down-regulated by IFNG/IFN-gamma (at protein level). Induced in breast cancer tissue. Up-regulated by sulforaphane in breast cancer cells.4 Publications

Gene expression databases

BgeeiENSG00000100804.
CleanExiHS_PSMB5.
ExpressionAtlasiP28074. baseline and differential.
GenevisibleiP28074. HS.

Organism-specific databases

HPAiHPA049518.
HPA061796.

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. This subunit can be displaced by the equivalent immune-specific subunit PSMB8. Directly interacts with POMP. Interacts with HIV-1 TAT protein. Interacts with ABCB1 and TAP1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
POMPQ9Y2443EBI-357828,EBI-696895
PSMB1P206183EBI-357828,EBI-372273
PSMB7Q994367EBI-357828,EBI-603319

Protein-protein interaction databases

BioGridi111666. 100 interactors.
DIPiDIP-27540N.
IntActiP28074. 34 interactors.
MINTiMINT-1161576.
STRINGi9606.ENSP00000355325.

Chemistry databases

BindingDBiP28074.

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi62 – 67Combined sources6
Beta strandi70 – 75Combined sources6
Beta strandi79 – 81Combined sources3
Beta strandi84 – 88Combined sources5
Beta strandi93 – 97Combined sources5
Beta strandi100 – 103Combined sources4
Helixi108 – 129Combined sources22
Helixi135 – 147Combined sources13
Turni148 – 151Combined sources4
Beta strandi156 – 164Combined sources9
Beta strandi167 – 174Combined sources8
Beta strandi179 – 181Combined sources3
Beta strandi183 – 188Combined sources6
Helixi191 – 201Combined sources11
Helixi208 – 225Combined sources18
Beta strandi231 – 239Combined sources9
Beta strandi242 – 250Combined sources9
Helixi251 – 258Combined sources8

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60L/Z60-260[»]
4R67X-ray2.893/L/Z/n60-260[»]
5A0Qelectron microscopy3.50L/Z60-263[»]
5GJQelectron microscopy4.50e/s1-263[»]
5GJRelectron microscopy3.50e/s1-263[»]
5L4Gelectron microscopy4.025/Y1-263[»]
5LE5X-ray1.80K/Y60-263[»]
5LEXX-ray2.20K/Y60-263[»]
5LEYX-ray1.90K/Y60-263[»]
5LEZX-ray2.19K/Y60-263[»]
5LF0X-ray2.41K/Y60-263[»]
5LF1X-ray2.00K/Y60-263[»]
5LF3X-ray2.10K/Y60-263[»]
5LF4X-ray1.99K/Y60-263[»]
5LF6X-ray2.07K/Y60-263[»]
5LF7X-ray2.00K/Y60-263[»]
5T0Celectron microscopy3.80AR/BR2-263[»]
5T0Gelectron microscopy4.40R2-263[»]
5T0Helectron microscopy6.80R2-263[»]
5T0Ielectron microscopy8.00R2-263[»]
5T0Jelectron microscopy8.00R2-263[»]
ProteinModelPortaliP28074.
SMRiP28074.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the peptidase T1B family.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
HOVERGENiHBG108297.
InParanoidiP28074.
KOiK02737.
OMAiYEPATPN.
OrthoDBiEOG091G0BPS.
PhylomeDBiP28074.
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 (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P28074-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MALASVLERP LPVNQRGFFG LGGRADLLDL GPGSLSDGLS LAAPGWGVPE
60 70 80 90 100
EPGIEMLHGT TTLAFKFRHG VIVAADSRAT AGAYIASQTV KKVIEINPYL
110 120 130 140 150
LGTMAGGAAD CSFWERLLAR QCRIYELRNK ERISVAAASK LLANMVYQYK
160 170 180 190 200
GMGLSMGTMI CGWDKRGPGL YYVDSEGNRI SGATFSVGSG SVYAYGVMDR
210 220 230 240 250
GYSYDLEVEQ AYDLARRAIY QATYRDAYSG GAVNLYHVRE DGWIRVSSDN
260
VADLHEKYSG STP
Length:263
Mass (Da):28,480
Last modified:April 29, 2008 - v3
Checksum:iAED4A73DF41AA6EF
GO
Isoform 2 (identifier: P28074-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     169-263: GLYYVDSEGN...LHEKYSGSTP → VSEVLCLKPKSFGMYLFCGCAERIGNMARPLLRGQ

Show »
Length:203
Mass (Da):21,845
Checksum:i29788AD9561905AE
GO
Isoform 3 (identifier: P28074-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-103: Missing.

Note: No experimental confirmation available.
Show »
Length:160
Mass (Da):17,782
Checksum:i47A97A3A9A849846
GO

Sequence cautioni

The sequence AAP35423 differs from that shown. Reason: Erroneous initiation.Curated
The sequence BAA06097 differs from that shown. Reason: Erroneous initiation.Curated
The sequence CAD97956 differs from that shown. Reason: Erroneous initiation.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti3 – 6LASV → IRGR in BAA06097 (PubMed:8066462).Curated4
Sequence conflicti3 – 5LAS → HEG in BC004146 (PubMed:15489334).Curated3
Sequence conflicti85I → F AA sequence (PubMed:2306472).Curated1
Sequence conflicti109A → G in AAB33092 (PubMed:7820546).Curated1
Sequence conflicti158T → S in AAB33092 (PubMed:7820546).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_05154924R → C.Corresponds to variant rs11543947dbSNPEnsembl.1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0456861 – 103Missing in isoform 3. 1 PublicationAdd BLAST103
Alternative sequenceiVSP_041263169 – 263GLYYV…SGSTP → VSEVLCLKPKSFGMYLFCGC AERIGNMARPLLRGQ in isoform 2. 2 PublicationsAdd BLAST95

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95586 Genomic DNA. Translation: CAA64838.1.
AK300714 mRNA. Translation: BAG62391.1.
AK311895 mRNA. Translation: BAG34836.1.
BX538001 mRNA. Translation: CAD97956.1. Different initiation.
AL132780 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66193.1.
CH471078 Genomic DNA. Translation: EAW66195.1.
BC004146 mRNA. No translation available.
BC057840 mRNA. Translation: AAH57840.1.
BC107720 mRNA. Translation: AAI07721.1.
CD048996 mRNA. No translation available.
BX248299 mRNA. Translation: CAD62626.1.
D29011 mRNA. Translation: BAA06097.1. Different initiation.
S74378 mRNA. Translation: AAB33092.1.
BT006777 mRNA. Translation: AAP35423.1. Different initiation.
CCDSiCCDS45083.1. [P28074-3]
CCDS45084.1. [P28074-2]
CCDS9584.1. [P28074-1]
PIRiA54589.
I52906.
PC2328.
S08189.
RefSeqiNP_001124197.1. NM_001130725.1. [P28074-3]
NP_001138404.1. NM_001144932.2. [P28074-2]
NP_002788.1. NM_002797.4. [P28074-1]
UniGeneiHs.422990.

Genome annotation databases

EnsembliENST00000361611; ENSP00000355325; ENSG00000100804. [P28074-1]
ENST00000425762; ENSP00000395206; ENSG00000100804. [P28074-3]
ENST00000493471; ENSP00000452424; ENSG00000100804. [P28074-2]
GeneIDi5693.
KEGGihsa:5693.
UCSCiuc001wii.3. human. [P28074-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95586 Genomic DNA. Translation: CAA64838.1.
AK300714 mRNA. Translation: BAG62391.1.
AK311895 mRNA. Translation: BAG34836.1.
BX538001 mRNA. Translation: CAD97956.1. Different initiation.
AL132780 Genomic DNA. No translation available.
CH471078 Genomic DNA. Translation: EAW66193.1.
CH471078 Genomic DNA. Translation: EAW66195.1.
BC004146 mRNA. No translation available.
BC057840 mRNA. Translation: AAH57840.1.
BC107720 mRNA. Translation: AAI07721.1.
CD048996 mRNA. No translation available.
BX248299 mRNA. Translation: CAD62626.1.
D29011 mRNA. Translation: BAA06097.1. Different initiation.
S74378 mRNA. Translation: AAB33092.1.
BT006777 mRNA. Translation: AAP35423.1. Different initiation.
CCDSiCCDS45083.1. [P28074-3]
CCDS45084.1. [P28074-2]
CCDS9584.1. [P28074-1]
PIRiA54589.
I52906.
PC2328.
S08189.
RefSeqiNP_001124197.1. NM_001130725.1. [P28074-3]
NP_001138404.1. NM_001144932.2. [P28074-2]
NP_002788.1. NM_002797.4. [P28074-1]
UniGeneiHs.422990.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
4R3OX-ray2.60L/Z60-260[»]
4R67X-ray2.893/L/Z/n60-260[»]
5A0Qelectron microscopy3.50L/Z60-263[»]
5GJQelectron microscopy4.50e/s1-263[»]
5GJRelectron microscopy3.50e/s1-263[»]
5L4Gelectron microscopy4.025/Y1-263[»]
5LE5X-ray1.80K/Y60-263[»]
5LEXX-ray2.20K/Y60-263[»]
5LEYX-ray1.90K/Y60-263[»]
5LEZX-ray2.19K/Y60-263[»]
5LF0X-ray2.41K/Y60-263[»]
5LF1X-ray2.00K/Y60-263[»]
5LF3X-ray2.10K/Y60-263[»]
5LF4X-ray1.99K/Y60-263[»]
5LF6X-ray2.07K/Y60-263[»]
5LF7X-ray2.00K/Y60-263[»]
5T0Celectron microscopy3.80AR/BR2-263[»]
5T0Gelectron microscopy4.40R2-263[»]
5T0Helectron microscopy6.80R2-263[»]
5T0Ielectron microscopy8.00R2-263[»]
5T0Jelectron microscopy8.00R2-263[»]
ProteinModelPortaliP28074.
SMRiP28074.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111666. 100 interactors.
DIPiDIP-27540N.
IntActiP28074. 34 interactors.
MINTiMINT-1161576.
STRINGi9606.ENSP00000355325.

Chemistry databases

BindingDBiP28074.
ChEMBLiCHEMBL4662.
DrugBankiDB00188. Bortezomib.
DB08889. Carfilzomib.
GuidetoPHARMACOLOGYi2406.

Protein family/group databases

MEROPSiT01.012.

PTM databases

iPTMnetiP28074.
PhosphoSitePlusiP28074.
SwissPalmiP28074.

Polymorphism and mutation databases

BioMutaiPSMB5.
DMDMi187608890.

2D gel databases

REPRODUCTION-2DPAGEIPI00479306.

Proteomic databases

EPDiP28074.
MaxQBiP28074.
PaxDbiP28074.
PeptideAtlasiP28074.
PRIDEiP28074.
TopDownProteomicsiP28074-1. [P28074-1]

Protocols and materials databases

DNASUi5693.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000361611; ENSP00000355325; ENSG00000100804. [P28074-1]
ENST00000425762; ENSP00000395206; ENSG00000100804. [P28074-3]
ENST00000493471; ENSP00000452424; ENSG00000100804. [P28074-2]
GeneIDi5693.
KEGGihsa:5693.
UCSCiuc001wii.3. human. [P28074-1]

Organism-specific databases

CTDi5693.
DisGeNETi5693.
GeneCardsiPSMB5.
HGNCiHGNC:9542. PSMB5.
HPAiHPA049518.
HPA061796.
MIMi600306. gene.
neXtProtiNX_P28074.
OpenTargetsiENSG00000100804.
PharmGKBiPA33887.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0175. Eukaryota.
ENOG410XQRP. LUCA.
GeneTreeiENSGT00510000046395.
HOVERGENiHBG108297.
InParanoidiP28074.
KOiK02737.
OMAiYEPATPN.
OrthoDBiEOG091G0BPS.
PhylomeDBiP28074.
TreeFamiTF106223.

Enzyme and pathway databases

BioCyciZFISH:HS02145-MONOMER.
ReactomeiR-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-202424. Downstream TCR signaling.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-350562. Regulation of ornithine decarboxylase (ODC).
R-HSA-382556. ABC-family proteins mediated transport.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5678895. Defective CFTR causes cystic fibrosis.
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5689603. UCH proteinases.
R-HSA-5689880. Ub-specific processing proteases.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69481. G2/M Checkpoints.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-8854050. FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.
SIGNORiP28074.

Miscellaneous databases

ChiTaRSiPSMB5. human.
GeneWikiiPSMB5.
GenomeRNAii5693.
PROiP28074.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100804.
CleanExiHS_PSMB5.
ExpressionAtlasiP28074. baseline and differential.
GenevisibleiP28074. HS.

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]
ProtoNetiSearch...

Entry informationi

Entry nameiPSB5_HUMAN
AccessioniPrimary (citable) accession number: P28074
Secondary accession number(s): B2R4N9
, B4DUM9, D3DS43, E9PAV2, Q16242, Q6PEW2, Q7Z3B5, Q86T01, Q9TNN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: April 29, 2008
Last modified: November 30, 2016
This is version 192 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

3D-structure, Complete proteome, Direct protein sequencing, 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. Peptidase families
    Classification of peptidase families and list of entries
  7. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.