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Protein

26S protease regulatory subunit 6B

Gene

Psmc4

Organism
Mus musculus (Mouse)
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.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi206 – 2138ATPSequence analysis

GO - Molecular functioni

GO - Biological processi

  • blastocyst development Source: MGI
  • protein catabolic process Source: InterPro
Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-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
CIP21
MB67-interacting protein
MIP224
Proteasome 26S subunit ATPase 4
Tat-binding protein 7
Short name:
TBP-7
Gene namesi
Name:Psmc4
Synonyms:Tbp7
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:1346093. Psmc4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 41841826S protease regulatory subunit 6BPRO_0000084687Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine1 Publication
Modified residuei21 – 211PhosphoserineBy similarity
Modified residuei25 – 251PhosphothreonineBy similarity
Modified residuei28 – 281PhosphoserineBy similarity
Modified residuei397 – 3971N6-acetyllysineBy similarity
Modified residuei401 – 4011N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

EPDiP54775.
MaxQBiP54775.
PaxDbiP54775.
PRIDEiP54775.

2D gel databases

REPRODUCTION-2DPAGEP54775.

PTM databases

iPTMnetiP54775.
PhosphoSiteiP54775.

Expressioni

Gene expression databases

BgeeiP54775.
GenevisibleiP54775. MM.

Interactioni

Subunit structurei

Interacts with PAAF1 (By similarity). Interacts with NR1I3. Interacts with TRIM5 (By similarity).By similarity

Protein-protein interaction databases

BioGridi204845. 5 interactions.
IntActiP54775. 5 interactions.
MINTiMINT-4108735.
STRINGi10090.ENSMUSP00000032824.

Structurei

Secondary structure

1
418
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi338 – 34912Combined sources
Helixi361 – 3644Combined sources
Helixi372 – 38413Combined sources
Helixi385 – 3873Combined sources
Beta strandi392 – 3943Combined sources
Helixi396 – 40611Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AJIX-ray2.05B/D337-418[»]
ProteinModelPortaliP54775.
SMRiP54775. Positions 41-418.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54775.

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0727. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074962.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP54775.
KOiK03063.
OMAiICRTETH.
OrthoDBiEOG7F24ST.
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]

Sequencei

Sequence statusi: Complete.

P54775-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MEEIGILVEK IQDEIPALSV 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):47,408
Last modified:July 27, 2011 - v2
Checksum:i6FD2C1E3EB1FF5F0
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti104 – 1041G → A in AAA88243 (PubMed:8603043).Curated
Sequence conflicti104 – 1041G → A in BAB16348 (PubMed:10945464).Curated
Sequence conflicti115 – 1162IL → MV in AAA88243 (PubMed:8603043).Curated
Sequence conflicti115 – 1162IL → MV in BAB16348 (PubMed:10945464).Curated
Sequence conflicti146 – 1461E → A in AAA88243 (PubMed:8603043).Curated
Sequence conflicti146 – 1461E → A in BAB16348 (PubMed:10945464).Curated
Sequence conflicti381 – 3822ES → AR in AAA88243 (PubMed:8603043).Curated
Sequence conflicti381 – 3822ES → AR in BAB16348 (PubMed:10945464).Curated
Sequence conflicti390 – 3912NR → TA in AAA88243 (PubMed:8603043).Curated
Sequence conflicti390 – 3912NR → TA in BAB16348 (PubMed:10945464).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76223 mRNA. Translation: AAA88243.1.
AB040869 Genomic DNA. Translation: BAB16348.1.
AK077507 mRNA. Translation: BAC36835.1.
AK153991 mRNA. Translation: BAE32301.1.
AK160718 mRNA. Translation: BAE35967.1.
AK167041 mRNA. Translation: BAE39209.1.
CH466593 Genomic DNA. Translation: EDL24160.1.
BC012708 mRNA. Translation: AAH12708.1.
CCDSiCCDS21034.1.
RefSeqiNP_036004.2. NM_011874.2.
UniGeneiMm.29582.

Genome annotation databases

EnsembliENSMUST00000032824; ENSMUSP00000032824; ENSMUSG00000030603.
GeneIDi23996.
KEGGimmu:23996.
UCSCiuc009fxp.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
L76223 mRNA. Translation: AAA88243.1.
AB040869 Genomic DNA. Translation: BAB16348.1.
AK077507 mRNA. Translation: BAC36835.1.
AK153991 mRNA. Translation: BAE32301.1.
AK160718 mRNA. Translation: BAE35967.1.
AK167041 mRNA. Translation: BAE39209.1.
CH466593 Genomic DNA. Translation: EDL24160.1.
BC012708 mRNA. Translation: AAH12708.1.
CCDSiCCDS21034.1.
RefSeqiNP_036004.2. NM_011874.2.
UniGeneiMm.29582.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3AJIX-ray2.05B/D337-418[»]
ProteinModelPortaliP54775.
SMRiP54775. Positions 41-418.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi204845. 5 interactions.
IntActiP54775. 5 interactions.
MINTiMINT-4108735.
STRINGi10090.ENSMUSP00000032824.

PTM databases

iPTMnetiP54775.
PhosphoSiteiP54775.

2D gel databases

REPRODUCTION-2DPAGEP54775.

Proteomic databases

EPDiP54775.
MaxQBiP54775.
PaxDbiP54775.
PRIDEiP54775.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000032824; ENSMUSP00000032824; ENSMUSG00000030603.
GeneIDi23996.
KEGGimmu:23996.
UCSCiuc009fxp.1. mouse.

Organism-specific databases

CTDi5704.
MGIiMGI:1346093. Psmc4.

Phylogenomic databases

eggNOGiKOG0727. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074962.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP54775.
KOiK03063.
OMAiICRTETH.
OrthoDBiEOG7F24ST.
TreeFamiTF106227.

Enzyme and pathway databases

ReactomeiR-MMU-1169091. Activation of NF-kappaB in B cells.
R-MMU-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-MMU-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-MMU-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-MMU-174154. APC/C:Cdc20 mediated degradation of Securin.
R-MMU-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-MMU-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-MMU-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-MMU-195253. Degradation of beta-catenin by the destruction complex.
R-MMU-202424. Downstream TCR signaling.
R-MMU-2467813. Separation of Sister Chromatids.
R-MMU-2871837. FCERI mediated NF-kB activation.
R-MMU-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-MMU-350562. Regulation of ornithine decarboxylase (ODC).
R-MMU-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-MMU-4608870. Asymmetric localization of PCP proteins.
R-MMU-4641257. Degradation of AXIN.
R-MMU-4641258. Degradation of DVL.
R-MMU-5358346. Hedgehog ligand biogenesis.
R-MMU-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-MMU-5607764. CLEC7A (Dectin-1) signaling.
R-MMU-5610780. Degradation of GLI1 by the proteasome.
R-MMU-5610785. GLI3 is processed to GLI3R by the proteasome.
R-MMU-5632684. Hedgehog 'on' state.
R-MMU-5658442. Regulation of RAS by GAPs.
R-MMU-5668541. TNFR2 non-canonical NF-kB pathway.
R-MMU-5676590. NIK-->noncanonical NF-kB signaling.
R-MMU-5687128. MAPK6/MAPK4 signaling.
R-MMU-68827. CDT1 association with the CDC6:ORC:origin complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-MMU-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-MMU-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-MMU-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

EvolutionaryTraceiP54775.
NextBioi303909.
PROiP54775.
SOURCEiSearch...

Gene expression databases

BgeeiP54775.
GenevisibleiP54775. MM.

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...

Publicationsi

« Hide 'large scale' publications
  1. "A component of the 26S proteasome binds on orphan member of the nuclear hormone receptor superfamily."
    Choi H.S., Seol W., Moore D.D.
    J. Steroid Biochem. Mol. Biol. 56:23-30(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH NR1I3.
    Tissue: Liver.
  2. "Mouse proteasomal ATPases Psmc3 and Psmc4: genomic organization and gene targeting."
    Sakao Y., Kawai T., Takeuchi O., Copeland N.G., Gilbert D.J., Jenkins N.A., Takeda K., Akira S.
    Genomics 67:1-7(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J and NOD.
    Tissue: Head and Thymus.
  4. Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.
    Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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].
    Strain: FVB/N.
    Tissue: Liver.
  6. Lubec G., Kang S.U.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 201-212, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: C57BL/6J.
    Tissue: Brain.
  7. Cited for: IDENTIFICATION IN THE 19S PROTEASOME REGULATORY COMPLEX, ACETYLATION AT MET-1.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiPRS6B_MOUSE
AccessioniPrimary (citable) accession number: P54775
Secondary accession number(s): Q6ZWN9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: July 27, 2011
Last modified: May 11, 2016
This is version 127 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. 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.