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Protein

26S protease regulatory subunit 6B

Gene

PSMC4

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

The 26S protease is involved in the ATP-dependent degradation of ubiquitinated proteins. The regulatory (or ATPase) complex confers ATP dependency and substrate specificity to the 26S complex.1 Publication

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Nucleotide bindingi206 – 213ATPSequence analysis8

GO - Molecular functioni

  • ATPase activity Source: ProtInc
  • ATP binding Source: UniProtKB-KW
  • proteasome-activating ATPase activity Source: GO_Central
  • TBP-class protein binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BioCyciZFISH:ENSG00000013275-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.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 6B
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT3
MB67-interacting protein
MIP224
Proteasome 26S subunit ATPase 4
Tat-binding protein 7
Short name:
TBP-7
Gene namesi
Name:PSMC4
Synonyms:MIP224, TBP7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 19

Organism-specific databases

HGNCiHGNC:9551. PSMC4.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • cytosolic proteasome complex Source: GO_Central
  • inclusion body Source: Ensembl
  • membrane Source: UniProtKB
  • nuclear proteasome complex Source: GO_Central
  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • proteasome accessory complex Source: UniProtKB
  • proteasome complex Source: UniProtKB
  • proteasome regulatory particle, base subcomplex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

Pathology & Biotechi

Organism-specific databases

DisGeNETi5704.
OpenTargetsiENSG00000013275.
ENSG00000281221.
PharmGKBiPA33896.

Polymorphism and mutation databases

BioMutaiPSMC4.
DMDMi20532409.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000846861 – 41826S protease regulatory subunit 6BAdd BLAST418

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei1N-acetylmethionineCombined sources1 Publication1
Modified residuei21PhosphoserineCombined sources1
Modified residuei25PhosphothreonineCombined sources1
Modified residuei28PhosphoserineCombined sources1
Modified residuei397N6-acetyllysineCombined sources1
Modified residuei401N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP43686.
MaxQBiP43686.
PaxDbiP43686.
PeptideAtlasiP43686.
PRIDEiP43686.

2D gel databases

OGPiP43686.

PTM databases

iPTMnetiP43686.
PhosphoSitePlusiP43686.
SwissPalmiP43686.

Expressioni

Gene expression databases

BgeeiENSG00000013275.
CleanExiHS_PSMC4.
ExpressionAtlasiP43686. baseline and differential.
GenevisibleiP43686. HS.

Organism-specific databases

HPAiHPA002044.
HPA005471.

Interactioni

Subunit structurei

Interacts with NR1I3. Interacts with PAAF1. Interacts with TRIM5.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
PSMC1P621912EBI-743997,EBI-357598
PSMC5P6219513EBI-743997,EBI-357745
PSMC6P623333EBI-743997,EBI-357669
PSMD10O7583217EBI-743997,EBI-752185

GO - Molecular functioni

Protein-protein interaction databases

BioGridi111677. 124 interactors.
DIPiDIP-29274N.
IntActiP43686. 44 interactors.
MINTiMINT-5004247.
STRINGi9606.ENSP00000157812.

Structurei

Secondary structure

1418
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Helixi338 – 348Combined sources11
Turni349 – 351Combined sources3
Helixi361 – 364Combined sources4
Helixi372 – 388Combined sources17
Beta strandi392 – 394Combined sources3
Helixi396 – 406Combined sources11

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DVWX-ray2.30B337-418[»]
5GJQelectron microscopy4.50K1-418[»]
5GJRelectron microscopy3.50K/y1-418[»]
5L4Gelectron microscopy4.02K1-418[»]
5T0Celectron microscopy3.80AD/BD1-418[»]
5T0Gelectron microscopy4.40D1-418[»]
5T0Helectron microscopy6.80D1-418[»]
5T0Ielectron microscopy8.00D1-418[»]
5T0Jelectron microscopy8.00D1-418[»]
ProteinModelPortaliP43686.
SMRiP43686.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP43686.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0727. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074962.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP43686.
KOiK03063.
OMAiGYKNNTK.
OrthoDBiEOG091G07NC.
PhylomeDBiP43686.
TreeFamiTF106227.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P43686-1) [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
MEEIGILVEK AQDEIPALSV SRPQTGLSFL GPEPEDLEDL YSRYKKLQQE
60 70 80 90 100
LEFLEVQEEY IKDEQKNLKK EFLHAQEEVK RIQSIPLVIG QFLEAVDQNT
110 120 130 140 150
AIVGSTTGSN YYVRILSTID RELLKPNASV ALHKHSNALV DVLPPEADSS
160 170 180 190 200
IMMLTSDQKP DVMYADIGGM DIQKQEVREA VELPLTHFEL YKQIGIDPPR
210 220 230 240 250
GVLMYGPPGC GKTMLAKAVA HHTTAAFIRV VGSEFVQKYL GEGPRMVRDV
260 270 280 290 300
FRLAKENAPA IIFIDEIDAI ATKRFDAQTG ADREVQRILL ELLNQMDGFD
310 320 330 340 350
QNVNVKVIMA TNRADTLDPA LLRPGRLDRK IEFPLPDRRQ KRLIFSTITS
360 370 380 390 400
KMNLSEEVDL EDYVARPDKI SGADINSICQ ESGMLAVREN RYIVLAKDFE
410
KAYKTVIKKD EQEHEFYK
Length:418
Mass (Da):47,366
Last modified:May 10, 2002 - v2
Checksum:i80F9523C61B88F0C
GO
Isoform 2 (identifier: P43686-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     46-76: Missing.

Note: No experimental confirmation available.
Show »
Length:387
Mass (Da):43,508
Checksum:iFA64D44EE00E9A7B
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti73L → F in AAC32612 (Ref. 4) Curated1
Sequence conflicti110N → S in AAC32612 (Ref. 4) Curated1
Sequence conflicti118T → A no nucleotide entry (PubMed:8419915).Curated1
Sequence conflicti157D → G in AAC32612 (Ref. 4) Curated1
Sequence conflicti185L → V in AAC32612 (Ref. 4) Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_00002246 – 76Missing in isoform 2. 1 PublicationAdd BLAST31

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038965 mRNA. Translation: AAC26843.1.
U27515 mRNA. Translation: AAC99817.1.
AF020736 mRNA. Translation: AAC32612.1.
BT007232 mRNA. Translation: AAP35896.1.
AC007842 Genomic DNA. Translation: AAD39267.1.
BC000343 mRNA. Translation: AAH00343.1.
BC010396 mRNA. Translation: AAH10396.1.
BC014488 mRNA. Translation: AAH14488.1.
CCDSiCCDS12547.1. [P43686-1]
CCDS46076.1. [P43686-2]
RefSeqiNP_006494.1. NM_006503.3. [P43686-1]
NP_694546.1. NM_153001.2. [P43686-2]
UniGeneiHs.211594.

Genome annotation databases

EnsembliENST00000157812; ENSP00000157812; ENSG00000013275. [P43686-1]
ENST00000455878; ENSP00000413869; ENSG00000013275. [P43686-2]
ENST00000629691; ENSP00000487367; ENSG00000281221. [P43686-1]
ENST00000630857; ENSP00000485851; ENSG00000281221. [P43686-2]
GeneIDi5704.
KEGGihsa:5704.
UCSCiuc002omq.5. human. [P43686-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF038965 mRNA. Translation: AAC26843.1.
U27515 mRNA. Translation: AAC99817.1.
AF020736 mRNA. Translation: AAC32612.1.
BT007232 mRNA. Translation: AAP35896.1.
AC007842 Genomic DNA. Translation: AAD39267.1.
BC000343 mRNA. Translation: AAH00343.1.
BC010396 mRNA. Translation: AAH10396.1.
BC014488 mRNA. Translation: AAH14488.1.
CCDSiCCDS12547.1. [P43686-1]
CCDS46076.1. [P43686-2]
RefSeqiNP_006494.1. NM_006503.3. [P43686-1]
NP_694546.1. NM_153001.2. [P43686-2]
UniGeneiHs.211594.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
2DVWX-ray2.30B337-418[»]
5GJQelectron microscopy4.50K1-418[»]
5GJRelectron microscopy3.50K/y1-418[»]
5L4Gelectron microscopy4.02K1-418[»]
5T0Celectron microscopy3.80AD/BD1-418[»]
5T0Gelectron microscopy4.40D1-418[»]
5T0Helectron microscopy6.80D1-418[»]
5T0Ielectron microscopy8.00D1-418[»]
5T0Jelectron microscopy8.00D1-418[»]
ProteinModelPortaliP43686.
SMRiP43686.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111677. 124 interactors.
DIPiDIP-29274N.
IntActiP43686. 44 interactors.
MINTiMINT-5004247.
STRINGi9606.ENSP00000157812.

PTM databases

iPTMnetiP43686.
PhosphoSitePlusiP43686.
SwissPalmiP43686.

Polymorphism and mutation databases

BioMutaiPSMC4.
DMDMi20532409.

2D gel databases

OGPiP43686.

Proteomic databases

EPDiP43686.
MaxQBiP43686.
PaxDbiP43686.
PeptideAtlasiP43686.
PRIDEiP43686.

Protocols and materials databases

DNASUi5704.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000157812; ENSP00000157812; ENSG00000013275. [P43686-1]
ENST00000455878; ENSP00000413869; ENSG00000013275. [P43686-2]
ENST00000629691; ENSP00000487367; ENSG00000281221. [P43686-1]
ENST00000630857; ENSP00000485851; ENSG00000281221. [P43686-2]
GeneIDi5704.
KEGGihsa:5704.
UCSCiuc002omq.5. human. [P43686-1]

Organism-specific databases

CTDi5704.
DisGeNETi5704.
GeneCardsiPSMC4.
HGNCiHGNC:9551. PSMC4.
HPAiHPA002044.
HPA005471.
MIMi602707. gene.
neXtProtiNX_P43686.
OpenTargetsiENSG00000013275.
ENSG00000281221.
PharmGKBiPA33896.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0727. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074962.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP43686.
KOiK03063.
OMAiGYKNNTK.
OrthoDBiEOG091G07NC.
PhylomeDBiP43686.
TreeFamiTF106227.

Enzyme and pathway databases

BioCyciZFISH:ENSG00000013275-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.

Miscellaneous databases

ChiTaRSiPSMC4. human.
EvolutionaryTraceiP43686.
GeneWikiiPSMC4.
GenomeRNAii5704.
PROiP43686.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000013275.
CleanExiHS_PSMC4.
ExpressionAtlasiP43686. baseline and differential.
GenevisibleiP43686. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
InterProiIPR005937. 26S_Psome_P45.
IPR003593. AAA+_ATPase.
IPR003959. ATPase_AAA_core.
IPR003960. ATPase_AAA_CS.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00004. AAA. 1 hit.
[Graphical view]
SMARTiSM00382. AAA. 1 hit.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01242. 26Sp45. 1 hit.
PROSITEiPS00674. AAA. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiPRS6B_HUMAN
AccessioniPrimary (citable) accession number: P43686
Secondary accession number(s): Q96FV5, Q9UBM3, Q9UEX3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: May 10, 2002
Last modified: November 30, 2016
This is version 175 of the entry and version 2 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 19
    Human chromosome 19: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.