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Protein

Proteasome subunit beta type-5

Gene

PSMB5

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

Functioni

Component of the 20S core proteasome complex involved in the proteolytic degradation of most intracellular proteins. This complex plays numerous essential roles within the cell by associating with different regulatory particles. Associated with two 19S regulatory particles, forms the 26S proteasome and thus participates in the ATP-dependent degradation of ubiquitinated proteins. The 26S proteasome plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins that could impair cellular functions, and by removing proteins whose functions are no longer required. Associated with the PA200 or PA28, the 20S proteasome mediates ubiquitin-independent protein degradation. This type of proteolysis is required in several pathways including spermatogenesis (20S-PA200 complex) or generation of a subset of MHC class I-presented antigenic peptides (20S-PA28 complex). Within the 20S core complex, PSMB5 displays a chymotrypsin-like activity.5 Publications

Catalytic activityi

Cleavage of peptide bonds with very broad specificity.1 Publication

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Active sitei60Nucleophile2 Publications1
Binding sitei108Bortezomib; via amide nitrogenBy similarity1

GO - Molecular functioni

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

GO - Biological processi

Keywordsi

Molecular functionHydrolase, Protease, Threonine protease
Biological processHost-virus interaction

Enzyme and pathway databases

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-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
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:3.4.25.11 Publication)
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

EuPathDBiHostDB:ENSG00000100804.18
HGNCiHGNC:9542 PSMB5
MIMi600306 gene
neXtProtiNX_P28074

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

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
ProteomicsDBi54448
54449 [P28074-2]
TopDownProteomicsiP28074-1 [P28074-1]

2D gel databases

REPRODUCTION-2DPAGEiIPI00479306

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 Expressed in 231 organ(s), highest expression level in gastrocnemius
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 a barrel-shaped complex made of 28 subunits that are arranged in four stacked rings. The two outer rings are each formed by seven alpha subunits, and the two inner rings are formed by seven beta subunits. The proteolytic activity is exerted by three beta-subunits PSMB5, PSMB6 and PSMB7. Directly interacts with POMP (PubMed:15944226). Interacts with ABCB1 and TAP1 (PubMed:15488952).8 Publications
(Microbial infection) Interacts with HIV-1 TAT protein.1 Publication

Binary interactionsi

Protein-protein interaction databases

BioGridi111666, 107 interactors
CORUMiP28074
DIPiDIP-27540N
IntActiP28074, 39 interactors
MINTiP28074
STRINGi9606.ENSP00000355325

Chemistry databases

BindingDBiP28074

Structurei

Secondary structure

1263
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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
OMAiNLGMAMQ
OrthoDBiEOG091G0BPS
PhylomeDBiP28074
TreeFamiTF106223

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR037558 Proteasome_beta_5
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF51 PTHR11599:SF51, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PRINTSiPR00141 PROTEASOME
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 1 hit

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

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

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

Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V3K3G3V3K3_HUMAN
Proteasome subunit beta type-5
PSMB5
84Annotation score:
H0YJM8H0YJM8_HUMAN
Proteasome subunit beta type-5
PSMB5
118Annotation score:
G8JLC2G8JLC2_HUMAN
Proteasome subunit beta type-5
PSMB5
77Annotation score:

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 dbSNP:rs11543947Ensembl.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

Similar proteinsi

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[»]
5L5WX-ray2.80K/Y60-197[»]
5L5XX-ray2.90K/Y60-197[»]
5L5YX-ray2.70K/Y60-197[»]
5L5ZX-ray2.70K/Y60-197[»]
5L60X-ray2.70K/Y60-197[»]
5L61X-ray2.80K/Y60-193[»]
5L62X-ray2.80K/Y60-197[»]
5L63X-ray2.70K/Y60-197[»]
5L64X-ray2.70K/Y60-197[»]
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[»]
5LN3electron microscopy6.8051-263[»]
5M32electron microscopy3.80K/Y60-263[»]
5T0Celectron microscopy3.80AR/BR2-263[»]
5T0Gelectron microscopy4.40R2-263[»]
5T0Helectron microscopy6.80R2-263[»]
5T0Ielectron microscopy8.00R2-263[»]
5T0Jelectron microscopy8.00R2-263[»]
5VFOelectron microscopy3.50R/r60-260[»]
5VFPelectron microscopy4.20R/r60-260[»]
5VFQelectron microscopy4.20R/r60-260[»]
5VFRelectron microscopy4.90R/r60-260[»]
5VFSelectron microscopy3.60R/r60-260[»]
5VFTelectron microscopy7.00R/r60-260[»]
5VFUelectron microscopy5.80R/r60-260[»]
ProteinModelPortaliP28074
SMRiP28074
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111666, 107 interactors
CORUMiP28074
DIPiDIP-27540N
IntActiP28074, 39 interactors
MINTiP28074
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-2DPAGEiIPI00479306

Proteomic databases

EPDiP28074
MaxQBiP28074
PaxDbiP28074
PeptideAtlasiP28074
PRIDEiP28074
ProteomicsDBi54448
54449 [P28074-2]
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
EuPathDBiHostDB:ENSG00000100804.18
GeneCardsiPSMB5
HGNCiHGNC:9542 PSMB5
HPAiHPA049518
HPA061796
MIMi600306 gene
neXtProtiNX_P28074
OpenTargetsiENSG00000100804
PharmGKBiPA33887
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0175 Eukaryota
ENOG410XQRP LUCA
GeneTreeiENSGT00510000046395
HOVERGENiHBG108297
InParanoidiP28074
KOiK02737
OMAiNLGMAMQ
OrthoDBiEOG091G0BPS
PhylomeDBiP28074
TreeFamiTF106223

Enzyme and pathway databases

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-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902 Regulation of RUNX2 expression and activity
R-HSA-8941858 Regulation of RUNX3 expression and activity
R-HSA-8948751 Regulation of PTEN stability and activity
R-HSA-8951664 Neddylation
R-HSA-9010553 Regulation of expression of SLITs and ROBOs
R-HSA-9020702 Interleukin-1 signaling
R-HSA-9604323 Negative regulation of NOTCH4 signaling
R-HSA-983168 Antigen processing: Ubiquitination & Proteasome degradation
SIGNORiP28074

Miscellaneous databases

ChiTaRSiPSMB5 human
GeneWikiiPSMB5
GenomeRNAii5693
PROiPR:P28074
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000100804 Expressed in 231 organ(s), highest expression level in gastrocnemius
CleanExiHS_PSMB5
ExpressionAtlasiP28074 baseline and differential
GenevisibleiP28074 HS

Family and domain databases

Gene3Di3.60.20.10, 1 hit
InterProiView protein in InterPro
IPR029055 Ntn_hydrolases_N
IPR000243 Pept_T1A_subB
IPR037558 Proteasome_beta_5
IPR016050 Proteasome_bsu_CS
IPR001353 Proteasome_sua/b
IPR023333 Proteasome_suB-type
PANTHERiPTHR11599:SF51 PTHR11599:SF51, 1 hit
PfamiView protein in Pfam
PF00227 Proteasome, 1 hit
PRINTSiPR00141 PROTEASOME
SUPFAMiSSF56235 SSF56235, 1 hit
PROSITEiView protein in PROSITE
PS00854 PROTEASOME_BETA_1, 1 hit
PS51476 PROTEASOME_BETA_2, 1 hit
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 historyiIntegrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: April 29, 2008
Last modified: November 7, 2018
This is version 213 of the entry and version 3 of the sequence. See 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. SIMILARITY comments
    Index of protein domains and families
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Peptidase families
    Classification of peptidase families and list of entries
  4. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  5. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. Human chromosome 14
    Human chromosome 14: entries, gene names and cross-references to MIM
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