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Entry version 142 (07 Apr 2021)
Sequence version 1 (21 Jun 2004)
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Protein

26S proteasome regulatory subunit 8

Gene

Psmc5

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the 'correct annotation' for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the 'protein existence' evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Component of the 26S proteasome, a multiprotein complex involved in the ATP-dependent degradation of ubiquitinated proteins. This complex plays a key role in the maintenance of protein homeostasis by removing misfolded or damaged proteins, which could impair cellular functions, and by removing proteins whose functions are no longer required. Therefore, the proteasome participates in numerous cellular processes, including cell cycle progression, apoptosis, or DNA damage repair. PSMC5 belongs to the heterohexameric ring of AAA (ATPases associated with diverse cellular activities) proteins that unfolds ubiquitinated target proteins that are concurrently translocated into a proteolytic chamber and degraded into peptides.

By similarity

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes a region in the protein which binds nucleotide phosphates. It always involves more than one amino acid and includes all residues involved in nucleotide-binding.<p><a href='/help/np_bind' target='_top'>More...</a></p>Nucleotide bindingi190 – 197ATPSequence analysis8

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

LigandATP-binding, Nucleotide-binding

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-1169091, Activation of NF-kappaB in B cells
R-RNO-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-RNO-1236978, Cross-presentation of soluble exogenous antigens (endosomes)
R-RNO-174084, Autodegradation of Cdh1 by Cdh1:APC/C
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-382556, ABC-family proteins mediated transport
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-5689603, UCH proteinases
R-RNO-5689880, Ub-specific processing proteases
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-69481, G2/M Checkpoints
R-RNO-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-RNO-75815, Ubiquitin-dependent degradation of Cyclin D
R-RNO-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-RNO-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-RNO-8939902, Regulation of RUNX2 expression and activity
R-RNO-8941858, Regulation of RUNX3 expression and activity
R-RNO-8948751, Regulation of PTEN stability and activity
R-RNO-8951664, Neddylation
R-RNO-9020702, Interleukin-1 signaling
R-RNO-983168, Antigen processing: Ubiquitination & Proteasome degradation

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
26S proteasome regulatory subunit 8
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT6
Proteasome 26S subunit ATPase 5
Proteasome subunit p45
Thyroid hormone receptor-interacting protein 1
Short name:
TRIP1
p45/SUG
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Psmc5
Synonyms:Sug1
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names%5Fand%5Ftaxonomy%5Fsection">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes%5Fmanual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 10

Organism-specific databases

Rat genome database

More...
RGDi
708376, Psmc5

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Keywords - Cellular componenti

Cytoplasm, Nucleus, Proteasome

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section indicates that the initiator methionine is cleaved from the mature protein.<p><a href='/help/init_met' target='_top'>More...</a></p>Initiator methionineiRemovedBy similarity
<p>This subsection of the 'PTM / Processing' section describes the extent of a polypeptide chain in the mature protein following processing or proteolytic cleavage.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000847242 – 40626S proteasome regulatory subunit 8Add BLAST405

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'PTM / Processing' section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei2N-acetylalanineBy similarity1
Modified residuei120PhosphoserineBy similarity1
Modified residuei222N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P62198

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
P62198

PRoteomics IDEntifications database

More...
PRIDEi
P62198

2D gel databases

The World-2DPAGE database

More...
World-2DPAGEi
0004:P62198

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P62198

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
P62198

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000010038, Expressed in brain and 22 other tissues

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P62198, RN

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction%5Fsection">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the 19S proteasome regulatory particle complex (By similarity). The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP) (By similarity). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC5 and few additional components (By similarity).

Component of a complex with USP49 and RUVBL1 (By similarity).

Interacts with PRPF19 (By similarity).

Interacts with TRIM5 (By similarity).

Interacts with NDC80 (By similarity).

Interacts with PAAF1 (By similarity).

Interacts, in vitro, with the thyroid hormone receptor (in a thyroid hormone T3-dependent manner) and with retinoid X receptor (RXR) (PubMed:7776974).

Interacts with ERCC6 (By similarity).

By similarity1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
249685, 18 interactors

Protein interaction database and analysis system

More...
IntActi
P62198, 4 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000013997

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
P62198

Database of comparative protein structure models

More...
ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

More...
PDBe-KBi
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Family and Domains' section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni186 – 406May mediate interaction with PRPF9By similarityAdd BLAST221

<p>This subsection of the 'Family and domains' section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the AAA ATPase family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG0728, Eukaryota

Ensembl GeneTree

More...
GeneTreei
ENSGT01020000230346

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
CLU_000688_2_0_1

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P62198

Identification of Orthologs from Complete Genome Data

More...
OMAi
MALDTFF

Database of Orthologous Groups

More...
OrthoDBi
571919at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P62198

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR005937, 26S_Psome_P45-like
IPR003593, AAA+_ATPase
IPR041569, AAA_lid_3
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR027417, P-loop_NTPase
IPR032501, Prot_ATP_ID_OB

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004, AAA, 1 hit
PF17862, AAA_lid_3, 1 hit
PF16450, Prot_ATP_ID_OB, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00382, AAA, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF52540, SSF52540, 1 hit

TIGRFAMs; a protein family database

More...
TIGRFAMsi
TIGR01242, 26Sp45, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00674, AAA, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence%5Flength">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences%5Fsection">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> displayed by default in the entry is in its mature form or if it represents the precursor.<p><a href='/help/sequence_processing' target='_top'>More...</a></p>Sequence processingi: The displayed sequence is further processed into a mature form.

P62198-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MALDGPEQME LEEGKAGSGL RQYYLSKIEE LQLIVNDKSQ NLRRLQAQRN
60 70 80 90 100
ELNAKVRLLR EELQLLQEQG SYVGEVVRAM DKKKVLVKVH PEGKFVVDVD
110 120 130 140 150
KNIDINDVTP NCRVALRNDS YTLHKILPNK VDPLVSLMMV EKVPDSTYEM
160 170 180 190 200
IGGLDKQIKE IKEVIELPVK HPELFEALGI AQPKGVLLYG PPGTGKTLLA
210 220 230 240 250
RAVAHHTDCT FIRVSGSELV QKFIGEGARM VRELFVMARE HAPSIIFMDE
260 270 280 290 300
IDSIGSSRLE GGSGGDSEVQ RTMLELLNQL DGFEATKNIK VIMATNRIDI
310 320 330 340 350
LDSALLRPGR IDRKIEFPPP NEEARLDILK IHSRKMNLTR GINLRKIAEL
360 370 380 390 400
MPGASGAEVK GVCTEAGMYA LRERRVHVTQ EDFEMAVAKV MQKDSEKNMS

IKKLWK
Length:406
Mass (Da):45,626
Last modified:June 21, 2004 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i29C6410C4A85A7F7
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D83521 mRNA Translation: BAA11938.1
AB000491 mRNA Translation: BAA22933.1
AB000493 Genomic DNA Translation: BAA22935.1
BC058462 mRNA Translation: AAH58462.1

Protein sequence database of the Protein Information Resource

More...
PIRi
T43799

NCBI Reference Sequences

More...
RefSeqi
NP_112411.1, NM_031149.1

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000013997; ENSRNOP00000013997; ENSRNOG00000010038

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
81827

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:81827

UCSC genome browser

More...
UCSCi
RGD:708376, rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D83521 mRNA Translation: BAA11938.1
AB000491 mRNA Translation: BAA22933.1
AB000493 Genomic DNA Translation: BAA22935.1
BC058462 mRNA Translation: AAH58462.1
PIRiT43799
RefSeqiNP_112411.1, NM_031149.1

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...
PDBei

Protein Data Bank RCSB

More...
RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
6EPCelectron microscopy12.30J1-406[»]
6EPDelectron microscopy15.40J1-406[»]
6EPEelectron microscopy12.80J1-406[»]
6EPFelectron microscopy11.80J1-406[»]
SMRiP62198
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi249685, 18 interactors
IntActiP62198, 4 interactors
STRINGi10116.ENSRNOP00000013997

PTM databases

iPTMnetiP62198
PhosphoSitePlusiP62198

2D gel databases

World-2DPAGEi0004:P62198

Proteomic databases

jPOSTiP62198
PaxDbiP62198
PRIDEiP62198

Genome annotation databases

EnsembliENSRNOT00000013997; ENSRNOP00000013997; ENSRNOG00000010038
GeneIDi81827
KEGGirno:81827
UCSCiRGD:708376, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5705
RGDi708376, Psmc5

Phylogenomic databases

eggNOGiKOG0728, Eukaryota
GeneTreeiENSGT01020000230346
HOGENOMiCLU_000688_2_0_1
InParanoidiP62198
OMAiMALDTFF
OrthoDBi571919at2759
PhylomeDBiP62198

Enzyme and pathway databases

ReactomeiR-RNO-1169091, Activation of NF-kappaB in B cells
R-RNO-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-RNO-1236978, Cross-presentation of soluble exogenous antigens (endosomes)
R-RNO-174084, Autodegradation of Cdh1 by Cdh1:APC/C
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-382556, ABC-family proteins mediated transport
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-5689603, UCH proteinases
R-RNO-5689880, Ub-specific processing proteases
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-69481, G2/M Checkpoints
R-RNO-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-RNO-75815, Ubiquitin-dependent degradation of Cyclin D
R-RNO-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-RNO-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-RNO-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-RNO-8939902, Regulation of RUNX2 expression and activity
R-RNO-8941858, Regulation of RUNX3 expression and activity
R-RNO-8948751, Regulation of PTEN stability and activity
R-RNO-8951664, Neddylation
R-RNO-9020702, Interleukin-1 signaling
R-RNO-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

Protein Ontology

More...
PROi
PR:P62198

Gene expression databases

BgeeiENSRNOG00000010038, Expressed in brain and 22 other tissues
GenevisibleiP62198, RN

Family and domain databases

InterProiView protein in InterPro
IPR005937, 26S_Psome_P45-like
IPR003593, AAA+_ATPase
IPR041569, AAA_lid_3
IPR003959, ATPase_AAA_core
IPR003960, ATPase_AAA_CS
IPR027417, P-loop_NTPase
IPR032501, Prot_ATP_ID_OB
PfamiView protein in Pfam
PF00004, AAA, 1 hit
PF17862, AAA_lid_3, 1 hit
PF16450, Prot_ATP_ID_OB, 1 hit
SMARTiView protein in SMART
SM00382, AAA, 1 hit
SUPFAMiSSF52540, SSF52540, 1 hit
TIGRFAMsiTIGR01242, 26Sp45, 1 hit
PROSITEiView protein in PROSITE
PS00674, AAA, 1 hit

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
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<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the 'Entry information' section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiPRS8_RAT
<p>This subsection of the 'Entry information' section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called 'Primary (citable) accession number'.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P62198
Secondary accession number(s): O35051
, P47210, P52915, P52916
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical%5Fand%5Fisoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 21, 2004
Last sequence update: June 21, 2004
Last modified: April 7, 2021
This is version 142 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the 'Entry information' section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn't fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
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