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Entry version 142 (07 Apr 2021)
Sequence version 1 (01 Nov 1997)
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Protein

26S proteasome regulatory subunit 6A

Gene

Psmc3

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. PSMC3 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 bindingi227 – 234ATPSequence 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%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 6A
Alternative name(s):
26S proteasome AAA-ATPase subunit RPT5
Proteasome 26S subunit ATPase 3
Spermatogenic cell/sperm-associated Tat-binding protein homolog SATA
Tat-binding protein 1
Short name:
TBP-1
<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:Psmc3
Synonyms:Tbp1
<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: Unplaced

Organism-specific databases

Rat genome database

More...
RGDi
61905, Psmc3

<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 '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_00000847001 – 43926S proteasome regulatory subunit 6AAdd BLAST439

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 residuei1N-acetylmethionineBy similarity1
Modified residuei9PhosphoserineBy similarity1
Modified residuei376PhosphoserineBy similarity1

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
Q63569

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

More...
PaxDbi
Q63569

PeptideAtlas

More...
PeptideAtlasi
Q63569

PRoteomics IDEntifications database

More...
PRIDEi
Q63569

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
Q63569

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

More...
PhosphoSitePlusi
Q63569

<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. 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 PSMC3 and few additional components.

Interacts with PAAF1.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...
BioGRIDi
248298, 8 interactors

Protein interaction database and analysis system

More...
IntActi
Q63569, 3 interactors

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000015757

<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
Q63569

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
KOG0652, Eukaryota

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q63569

Database of Orthologous Groups

More...
OrthoDBi
571919at2759

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
IPR035254, PSMC3

The PANTHER Classification System

More...
PANTHERi
PTHR23073:SF90, PTHR23073:SF90, 1 hit

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>Sequence (1+)i

<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.

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

Q63569-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MNLLPTPESP VTRQEKMATV WDEAEQDGIG EEVLKMSTEE IVQRTRLLDS
60 70 80 90 100
EIKIMKSEVL RVTHELQAMK DKIKENSEKI KVNKTLPYLV SNVIELLDVD
110 120 130 140 150
PNDQEEDGAN IDLDSQRKGK CAVIKTSTRQ TYFLPVIGLV DAEKLKPGDL
160 170 180 190 200
VGVNKDSYLI LETLPTEYDS RVKAMEVDER PTEQYSDIGG LDKQIQELVE
210 220 230 240 250
AIVLPMNHKE KFENLGIQPP KGVLMYGPPG TGKTLLARAC AAQTKATFLK
260 270 280 290 300
LAGPQLVQMF IGDGAKLVRD AFALAKEKAP SIIFIDELDA IGTKRFDSEK
310 320 330 340 350
AGDREVQRTM LELLNQLDGF QPNTQVKVIA ATNRVDILDP ALLRSGRLDR
360 370 380 390 400
KIEFPMPNEE ARARIMQIHS RKMNVSPDVN YEELARCTDD FNGAQCKAVC
410 420 430
VEAGMIALRR GATELTHEDY MEGILEVQAK KKANLQYYA
Length:439
Mass (Da):49,160
Last modified:November 1, 1997 - 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:i292E780AEBD19BAE
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
Q6P6U2Q6P6U2_RAT
26S proteasome regulatory subunit 6...
Psmc3 rCG_27374
442Annotation 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>

<p>This subsection of the 'Sequence' section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAB70882 differs from that shown. Reason: Erroneous initiation.Curated

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 conflicti84K → N in AAB70882 (PubMed:9266764).Curated1
Sequence conflicti317L → M in AAB70882 (PubMed:9266764).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
D83522 mRNA Translation: BAA11939.1
U77918 mRNA Translation: AAB70882.1 Different initiation.

NCBI Reference Sequences

More...
RefSeqi
NP_113783.1, NM_031595.1

Genome annotation databases

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
29677

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:29677

UCSC genome browser

More...
UCSCi
RGD:61905, 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
D83522 mRNA Translation: BAA11939.1
U77918 mRNA Translation: AAB70882.1 Different initiation.
RefSeqiNP_113783.1, NM_031595.1

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 microscopy12.30M1-439[»]
6EPDelectron microscopy15.40M1-439[»]
6EPEelectron microscopy12.80M1-439[»]
6EPFelectron microscopy11.80M1-439[»]
SMRiQ63569
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi248298, 8 interactors
IntActiQ63569, 3 interactors
STRINGi10116.ENSRNOP00000015757

PTM databases

iPTMnetiQ63569
PhosphoSitePlusiQ63569

Proteomic databases

jPOSTiQ63569
PaxDbiQ63569
PeptideAtlasiQ63569
PRIDEiQ63569

Genome annotation databases

GeneIDi29677
KEGGirno:29677
UCSCiRGD:61905, rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
5702
RGDi61905, Psmc3

Phylogenomic databases

eggNOGiKOG0652, Eukaryota
InParanoidiQ63569
OrthoDBi571919at2759

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:Q63569

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
IPR035254, PSMC3
PANTHERiPTHR23073:SF90, PTHR23073:SF90, 1 hit
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 nameiPRS6A_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: Q63569
Secondary accession number(s): P97638
<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: November 1, 1997
Last sequence update: November 1, 1997
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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