Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

26S protease regulatory subunit 7

Gene

Psmc2

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: Annotation score: 4 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 bindingi216 – 2238ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • hydrolase activity Source: InterPro
  • TBP-class protein binding Source: RGD
  • transcription factor binding Source: RGD

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
26S protease regulatory subunit 7
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT1
Proteasome 26S subunit ATPase 2
Protein MSS1
Gene namesi
Name:Psmc2
Synonyms:Mss1
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi3428. Psmc2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasmic mRNA processing body Source: UniProtKB
  • nucleus Source: RGD
  • proteasome accessory complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 43343226S protease regulatory subunit 7PRO_0000084711Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei116 – 1161N6-acetyllysineBy similarity
Modified residuei422 – 4221N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

PaxDbiQ63347.
PRIDEiQ63347.

PTM databases

iPTMnetiQ63347.
PhosphoSiteiQ63347.

Interactioni

Subunit structurei

Interacts with NDC80 and SQSTM1. Interacts with PAAF1 (By similarity). Interacts with TRIM5 (By similarity).By similarity

GO - Molecular functioni

  • TBP-class protein binding Source: RGD
  • transcription factor binding Source: RGD

Protein-protein interaction databases

BioGridi247611. 6 interactions.
IntActiQ63347. 3 interactions.
MINTiMINT-1794034.
STRINGi10116.ENSRNOP00000016450.

Structurei

3D structure databases

ProteinModelPortaliQ63347.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

eggNOGiKOG0729. Eukaryota.
COG1222. LUCA.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiQ63347.
KOiK03061.
PhylomeDBiQ63347.

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.

Q63347-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPDYLGADQR KTKEDEKDDK PIRALDEGDI ALLKTYGQST YSRQIKQVED
60 70 80 90 100
DIQQLLKKIN ELTGIKESDT GLAPPALWDL AADKQTLQSE QPLQVARCTK
110 120 130 140 150
IINADSEDPK YIINVKQFAK FVVDLSDQVA PTDIEEGMRV GVDRNKYQIH
160 170 180 190 200
IPLPPKIDPT VTMMQVEEKP DVTYSDVGGC KEQIEKLREV VETPLLHPER
210 220 230 240 250
FVNLGIEPPK GVLLFGPPGT GKTLCARAVA NRTDACFIPV IGSELVQKYV
260 270 280 290 300
GEGARMVREL FEMARTKKAC LIFFDEIDAI GGARFDDGAG GDNEVQRTML
310 320 330 340 350
ELINQLDGFD PRGNIKVLMA TNRPDTLDPA LMRPGRLDRK IEFSLPDLEG
360 370 380 390 400
RTHIFKIHAR SMSVERDIRF ELLARLCPNS TGAEIRSVCT EAGMFAIRAR
410 420 430
RKIATEKDFL EAVNKVIKSY AKFSATPRYM TYN
Length:433
Mass (Da):48,575
Last modified:January 23, 2007 - v3
Checksum:iDFFF1E1FBE92B56D
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti239 – 2391P → R in AAH61542 (PubMed:15489334).Curated
Sequence conflicti361 – 3611S → A in AAH61542 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50694 mRNA. Translation: BAA09339.1.
BC061542 mRNA. Translation: AAH61542.1.
U13895 mRNA. Translation: AAC53589.2.
RefSeqiNP_150239.1. NM_033236.1.
UniGeneiRn.1202.

Genome annotation databases

GeneIDi25581.
KEGGirno:25581.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D50694 mRNA. Translation: BAA09339.1.
BC061542 mRNA. Translation: AAH61542.1.
U13895 mRNA. Translation: AAC53589.2.
RefSeqiNP_150239.1. NM_033236.1.
UniGeneiRn.1202.

3D structure databases

ProteinModelPortaliQ63347.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi247611. 6 interactions.
IntActiQ63347. 3 interactions.
MINTiMINT-1794034.
STRINGi10116.ENSRNOP00000016450.

PTM databases

iPTMnetiQ63347.
PhosphoSiteiQ63347.

Proteomic databases

PaxDbiQ63347.
PRIDEiQ63347.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi25581.
KEGGirno:25581.

Organism-specific databases

CTDi5701.
RGDi3428. Psmc2.

Phylogenomic databases

eggNOGiKOG0729. Eukaryota.
COG1222. LUCA.
HOGENOMiHOG000225143.
HOVERGENiHBG000109.
InParanoidiQ63347.
KOiK03061.
PhylomeDBiQ63347.

Miscellaneous databases

NextBioi607227.
PROiQ63347.

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.
  3. "Gene expression of the proteasome in rat lens development."
    Cai H., Singh I., Wagner B.J.
    Exp. Eye Res. 66:339-346(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 14-155.
    Strain: Sprague-Dawley.
    Tissue: Lens.
  4. Lubec G., Afjehi-Sadat L., Chen W.-Q.
    Submitted (APR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 147-156; 269-284 AND 340-351, IDENTIFICATION BY MASS SPECTROMETRY.
    Strain: Sprague-Dawley.
    Tissue: Hippocampus and Spinal cord.

Entry informationi

Entry nameiPRS7_RAT
AccessioniPrimary (citable) accession number: Q63347
Secondary accession number(s): Q62690, Q6P7R9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: May 11, 2016
This is version 117 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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.