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Entry version 138 (13 Nov 2019)
Sequence version 3 (23 Jan 2007)
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Protein

26S proteasome regulatory subunit 7

Gene

Psmc2

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

Annotation score:4 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. PSMC2 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_section">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 bindingi216 – 223ATPSequence 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-6798695 Neutrophil degranulation
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_and_taxonomy_section">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 7
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT1
Proteasome 26S subunit ATPase 2
Protein MSS1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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:Psmc2
Synonyms:Mss1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_and_taxonomy_section">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_manual">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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
3428 Psmc2

<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

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, 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 ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000847111 – 43326S proteasome regulatory subunit 7Add BLAST433

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 residuei116N6-acetyllysineBy similarity1
Modified residuei422N6-acetyllysineBy similarity1

Keywords - PTMi

Acetylation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q63347

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

More...
PaxDbi
Q63347

PRoteomics IDEntifications database

More...
PRIDEi
Q63347

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q63347

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

More...
PhosphoSitePlusi
Q63347

<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_section">'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_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Component of the 19S proteasome regulatory particle complex. The 26S proteasome consists of a 20S core particle (CP) and two 19S regulatory subunits (RP). The regulatory particle is made of a lid composed of 9 subunits, a base containing 6 ATPases including PSMC2 and few additional components.

Interacts with NDC80 and SQSTM1.

Interacts with PAAF1.

Interacts with HIV-1 Tat.

Interacts with TRIM5.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
247611, 6 interactors

Protein interaction database and analysis system

More...
IntActi
Q63347, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000016450

<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
Q63347

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

<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
KOG0729 Eukaryota
COG1222 LUCA

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...
HOGENOMi
HOG000225143

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q63347

KEGG Orthology (KO)

More...
KOi
K03061

Database of Orthologous Groups

More...
OrthoDBi
571919at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q63347

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
IPR035245 PSMC2

The PANTHER Classification System

More...
PANTHERi
PTHR23073:SF13 PTHR23073:SF13, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00004 AAA, 1 hit
PF17862 AAA_lid_3, 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_length">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>Sequence (1+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">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.

This entry has 1 described isoform and 1 potential isoform that is computationally mapped.Show allAlign All

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
<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:iDFFF1E1FBE92B56D
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
G3V7L6G3V7L6_RAT
26S proteasome regulatory subunit 7
Psmc2 rCG_24399
433Annotation score:

Annotation score:2 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 Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti239P → R in AAH61542 (PubMed:15489334).Curated1
Sequence conflicti361S → A in AAH61542 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
D50694 mRNA Translation: BAA09339.1
BC061542 mRNA Translation: AAH61542.1
U13895 mRNA Translation: AAC53589.2

NCBI Reference Sequences

More...
RefSeqi
NP_150239.1, NM_033236.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
25581

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:25581

<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
D50694 mRNA Translation: BAA09339.1
BC061542 mRNA Translation: AAH61542.1
U13895 mRNA Translation: AAC53589.2
RefSeqiNP_150239.1, NM_033236.1

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 microscopy12.30H1-433[»]
6EPDelectron microscopy15.40H1-433[»]
6EPEelectron microscopy12.80H1-433[»]
6EPFelectron microscopy11.80H1-433[»]
SMRiQ63347
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGridi247611, 6 interactors
IntActiQ63347, 3 interactors
STRINGi10116.ENSRNOP00000016450

PTM databases

iPTMnetiQ63347
PhosphoSitePlusiQ63347

Proteomic databases

jPOSTiQ63347
PaxDbiQ63347
PRIDEiQ63347

Genome annotation databases

GeneIDi25581
KEGGirno:25581

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5701
RGDi3428 Psmc2

Phylogenomic databases

eggNOGiKOG0729 Eukaryota
COG1222 LUCA
HOGENOMiHOG000225143
InParanoidiQ63347
KOiK03061
OrthoDBi571919at2759
PhylomeDBiQ63347

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-6798695 Neutrophil degranulation
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:Q63347

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
IPR035245 PSMC2
PANTHERiPTHR23073:SF13 PTHR23073:SF13, 1 hit
PfamiView protein in Pfam
PF00004 AAA, 1 hit
PF17862 AAA_lid_3, 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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<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 nameiPRS7_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: Q63347
Secondary accession number(s): Q62690, Q6P7R9
<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_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: January 23, 2007
Last modified: November 13, 2019
This is version 138 of the entry and version 3 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, Complete proteome, Direct protein sequencing, Reference proteome

Documents

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