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Protein

26S protease regulatory subunit 4

Gene

Psmc1

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at transcript 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 bindingi226 – 2338ATPSequence analysis

GO - Molecular functioni

  • ATPase activity Source: RGD
  • ATP binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: Ensembl
  • proteasome-activating ATPase activity Source: GO_Central
  • TBP-class protein binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiR-RNO-1169091. Activation of NF-kappaB in B cells.
R-RNO-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-RNO-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-RNO-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-RNO-174154. APC/C:Cdc20 mediated degradation of Securin.
R-RNO-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-RNO-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-RNO-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-RNO-195253. Degradation of beta-catenin by the destruction complex.
R-RNO-202424. Downstream TCR signaling.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2871837. FCERI mediated NF-kB activation.
R-RNO-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-RNO-350562. Regulation of ornithine decarboxylase (ODC).
R-RNO-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-RNO-4608870. Asymmetric localization of PCP proteins.
R-RNO-4641257. Degradation of AXIN.
R-RNO-4641258. Degradation of DVL.
R-RNO-5358346. Hedgehog ligand biogenesis.
R-RNO-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-RNO-5607764. CLEC7A (Dectin-1) signaling.
R-RNO-5610780. Degradation of GLI1 by the proteasome.
R-RNO-5610785. GLI3 is processed to GLI3R by the proteasome.
R-RNO-5632684. Hedgehog 'on' state.
R-RNO-5658442. Regulation of RAS by GAPs.
R-RNO-5668541. TNFR2 non-canonical NF-kB pathway.
R-RNO-5676590. NIK-->noncanonical NF-kB signaling.
R-RNO-5687128. MAPK6/MAPK4 signaling.
R-RNO-68827. CDT1 association with the CDC6:ORC:origin complex.
R-RNO-68949. Orc1 removal from chromatin.
R-RNO-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-RNO-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-RNO-69481. G2/M Checkpoints.
R-RNO-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-RNO-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 4
Short name:
P26s4
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT2
Proteasome 26S subunit ATPase 1
Gene namesi
Name:Psmc1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Chromosome 6

Organism-specific databases

RGDi621097. Psmc1.

Subcellular locationi

  • Cytoplasm By similarity
  • Nucleus By similarity
  • Membrane By similarity; Lipid-anchor By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 44043926S protease regulatory subunit 4PRO_0000084679Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Lipidationi2 – 21N-myristoyl glycineBy similarity
Modified residuei4 – 41PhosphoserineBy similarity
Modified residuei53 – 531PhosphothreonineBy similarity
Cross-linki237 – 237Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei258 – 2581N6-acetyllysineBy similarity
Modified residuei434 – 4341PhosphothreonineBy similarity
Modified residuei439 – 4391PhosphotyrosineBy similarity

Keywords - PTMi

Acetylation, Isopeptide bond, Lipoprotein, Myristate, Phosphoprotein, Ubl conjugation

Proteomic databases

PaxDbiP62193.
PRIDEiP62193.

PTM databases

iPTMnetiP62193.

Expressioni

Gene expression databases

GenevisibleiP62193. RN.

Interactioni

Subunit structurei

Interacts with SCA7. Interacts with NGLY1. Interacts with PAAF1 (By similarity).By similarity

GO - Molecular functioni

  • TBP-class protein binding Source: RGD

Protein-protein interaction databases

BioGridi250710. 4 interactions.
IntActiP62193. 3 interactions.
STRINGi10116.ENSRNOP00000005329.

Structurei

3D structure databases

ProteinModelPortaliP62193.
SMRiP62193. Positions 78-439.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0726. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074818.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP62193.
KOiK03062.
OMAiVLLHHKN.
OrthoDBiEOG7F24ST.
PhylomeDBiP62193.
TreeFamiTF106226.

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.

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

P62193-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MGQSQSGGHG PGGGKKDDKD KKKKYEPPVP TRVGKKKKKT KGPDAASKLP
60 70 80 90 100
LVTPHTQCRL KLLKLERIKD YLLMEEEFIR NQEQMKPLEE KQEEERSKVD
110 120 130 140 150
DLRGTPMSVG TLEEIIDDNH AIVSTSVGSE HYVSILSFVD KDLLEPGCSV
160 170 180 190 200
LLNHKVHAVI GVLMDDTDPL VTVMKVEKAP QETYADIGGL DNQIQEIKES
210 220 230 240 250
VELPLTHPEY YEEMGIKPPK GVILYGPPGT GKTLLAKAVA NQTSATFLRV
260 270 280 290 300
VGSELIQKYL GDGPKLVREL FRVAEEHAPS IVFIDEIDAI GTKRYDSNSG
310 320 330 340 350
GEREIQRTML ELLNQLDGFD SRGDVKVIMA TNRIETLDPA LIRPGRIDRK
360 370 380 390 400
IEFPLPDEKT KKRIFQIHTS RMTLADDVTL DDLIMAKDDL SGADIKAICT
410 420 430 440
EAGLMALRER RMKVTNEDFK KSKENVLYKK QEGTPEGLYL
Length:440
Mass (Da):49,185
Last modified:June 21, 2004 - v1
Checksum:iACA80782F4F96F49
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50696 mRNA. Translation: BAA09341.1.
BC063157 mRNA. Translation: AAH63157.1.
RefSeqiNP_476464.1. NM_057123.1.
UniGeneiRn.10526.

Genome annotation databases

EnsembliENSRNOT00000005329; ENSRNOP00000005329; ENSRNOG00000003951.
GeneIDi117263.
KEGGirno:117263.
UCSCiRGD:621097. rat.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50696 mRNA. Translation: BAA09341.1.
BC063157 mRNA. Translation: AAH63157.1.
RefSeqiNP_476464.1. NM_057123.1.
UniGeneiRn.10526.

3D structure databases

ProteinModelPortaliP62193.
SMRiP62193. Positions 78-439.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi250710. 4 interactions.
IntActiP62193. 3 interactions.
STRINGi10116.ENSRNOP00000005329.

PTM databases

iPTMnetiP62193.

Proteomic databases

PaxDbiP62193.
PRIDEiP62193.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSRNOT00000005329; ENSRNOP00000005329; ENSRNOG00000003951.
GeneIDi117263.
KEGGirno:117263.
UCSCiRGD:621097. rat.

Organism-specific databases

CTDi5700.
RGDi621097. Psmc1.

Phylogenomic databases

eggNOGiKOG0726. Eukaryota.
COG1222. LUCA.
GeneTreeiENSGT00550000074818.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiP62193.
KOiK03062.
OMAiVLLHHKN.
OrthoDBiEOG7F24ST.
PhylomeDBiP62193.
TreeFamiTF106226.

Enzyme and pathway databases

ReactomeiR-RNO-1169091. Activation of NF-kappaB in B cells.
R-RNO-1236978. Cross-presentation of soluble exogenous antigens (endosomes).
R-RNO-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-RNO-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-RNO-174154. APC/C:Cdc20 mediated degradation of Securin.
R-RNO-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-RNO-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-RNO-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-RNO-195253. Degradation of beta-catenin by the destruction complex.
R-RNO-202424. Downstream TCR signaling.
R-RNO-2467813. Separation of Sister Chromatids.
R-RNO-2871837. FCERI mediated NF-kB activation.
R-RNO-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-RNO-350562. Regulation of ornithine decarboxylase (ODC).
R-RNO-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-RNO-4608870. Asymmetric localization of PCP proteins.
R-RNO-4641257. Degradation of AXIN.
R-RNO-4641258. Degradation of DVL.
R-RNO-5358346. Hedgehog ligand biogenesis.
R-RNO-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-RNO-5607764. CLEC7A (Dectin-1) signaling.
R-RNO-5610780. Degradation of GLI1 by the proteasome.
R-RNO-5610785. GLI3 is processed to GLI3R by the proteasome.
R-RNO-5632684. Hedgehog 'on' state.
R-RNO-5658442. Regulation of RAS by GAPs.
R-RNO-5668541. TNFR2 non-canonical NF-kB pathway.
R-RNO-5676590. NIK-->noncanonical NF-kB signaling.
R-RNO-5687128. MAPK6/MAPK4 signaling.
R-RNO-68827. CDT1 association with the CDC6:ORC:origin complex.
R-RNO-68949. Orc1 removal from chromatin.
R-RNO-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-RNO-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-RNO-69481. G2/M Checkpoints.
R-RNO-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-RNO-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-RNO-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

PROiP62193.

Gene expression databases

GenevisibleiP62193. RN.

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. "Structures of the rat proteasomal ATPases: determination of highly conserved structural motifs and rules for their spacing."
    Makino Y., Yogosawa S., Kanemaki M., Yoshida T., Yamano K., Kishimoto T., Moncollin V., Egly J.-M., Muramatsu M., Tamura T.
    Biochem. Biophys. Res. Commun. 220:1049-1054(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: Sprague-Dawley.
    Tissue: Liver.
  2. "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].
    Tissue: Pituitary.

Entry informationi

Entry nameiPRS4_RAT
AccessioniPrimary (citable) accession number: P62193
Secondary accession number(s): P49014, Q03527, Q96AZ3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: July 6, 2016
This is version 104 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. 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.