Skip Header

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

UniProtKB - P35998 (PRS7_HUMAN)

Entry version 213 (10 Feb 2021)
Sequence version 3 (23 Jan 2007)
Previous versions | rss
Add a publicationFeedback
Protein

26S proteasome regulatory subunit 7

Gene

PSMC2

Organism
Homo sapiens (Human)
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. 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.2 Publications

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 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

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

<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

Pathway Commons web resource for biological pathway data

More...PathwayCommonsi		P35998

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-1169091, Activation of NF-kappaB in B cells
R-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974, ER-Phagosome pathway
R-HSA-1236978, Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084, Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113, SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154, APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534, Vpu mediated degradation of CD4
R-HSA-180585, Vif-mediated degradation of APOBEC3G
R-HSA-187577, SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253, Degradation of beta-catenin by the destruction complex
R-HSA-202424, Downstream TCR signaling
R-HSA-211733, Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813, Separation of Sister Chromatids
R-HSA-2871837, FCERI mediated NF-kB activation
R-HSA-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562, Regulation of ornithine decarboxylase (ODC)
R-HSA-382556, ABC-family proteins mediated transport
R-HSA-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870, Asymmetric localization of PCP proteins
R-HSA-4641257, Degradation of AXIN
R-HSA-4641258, Degradation of DVL
R-HSA-5358346, Hedgehog ligand biogenesis
R-HSA-5362768, Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761, Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764, CLEC7A (Dectin-1) signaling
R-HSA-5610780, Degradation of GLI1 by the proteasome
R-HSA-5610783, Degradation of GLI2 by the proteasome
R-HSA-5610785, GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684, Hedgehog 'on' state
R-HSA-5658442, Regulation of RAS by GAPs
R-HSA-5668541, TNFR2 non-canonical NF-kB pathway
R-HSA-5676590, NIK-->noncanonical NF-kB signaling
R-HSA-5678895, Defective CFTR causes cystic fibrosis
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-5689603, UCH proteinases
R-HSA-5689880, Ub-specific processing proteases
R-HSA-6798695, Neutrophil degranulation
R-HSA-68827, CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949, Orc1 removal from chromatin
R-HSA-69017, CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69481, G2/M Checkpoints
R-HSA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-75815, Ubiquitin-dependent degradation of Cyclin D
R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902, Regulation of RUNX2 expression and activity
R-HSA-8941858, Regulation of RUNX3 expression and activity
R-HSA-8948751, Regulation of PTEN stability and activity
R-HSA-8951664, Neddylation
R-HSA-9010553, Regulation of expression of SLITs and ROBOs
R-HSA-9020702, Interleukin-1 signaling
R-HSA-9604323, Negative regulation of NOTCH4 signaling
R-HSA-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 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%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:PSMC2
Synonyms:MSS1
<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>OrganismiHomo sapiens (Human)
<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 identifieri9606 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<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
  • UP000005640 <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 7

Organism-specific databases

Human Gene Nomenclature Database

More...HGNCi		HGNC:9548, PSMC2

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		154365, gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P35998

Eukaryotic Pathogen, Vector and Host Database Resources

More...VEuPathDBi		HostDB:ENSG00000161057.10

<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 provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

DisGeNET

More...DisGeNETi		5701

Open Targets

More...OpenTargetsi		ENSG00000161057

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA33893

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

More...Pharosi		P35998, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

More...ChEMBLi		CHEMBL2364701

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		PSMC2

Domain mapping of disease mutations (DMDM)

More...DMDMi		547930

<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 methionineiRemoved2 Publications
<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_00000847092 – 43326S proteasome regulatory subunit 7Add BLAST432

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-acetyllysineCombined sources1
Modified residuei422N6-acetyllysineCombined sources1

Keywords - PTMi

Acetylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P35998

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P35998

MassIVE - Mass Spectrometry Interactive Virtual Environment

More...MassIVEi		P35998

MaxQB - The MaxQuant DataBase

More...MaxQBi		P35998

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

More...PaxDbi		P35998

PeptideAtlas

More...PeptideAtlasi		P35998

PRoteomics IDEntifications database

More...PRIDEi		P35998

ProteomicsDB: a multi-organism proteome resource

More...ProteomicsDBi		55172 [P35998-1]
6682

2D gel databases

USC-OGP 2-DE database

More...OGPi		P35998

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		IPI00021435
P35998

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P35998

MetOSite database of methionine sulfoxide sites

More...MetOSitei		P35998

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

More...PhosphoSitePlusi		P35998

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P35998

<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

<p>This subsection of the 'Expression' section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Expression is not cell cycle-dependent and occurs throughout the cell cycle.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000161057, Expressed in biceps brachii and 249 other tissues

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P35998, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P35998, HS

Organism-specific databases

Human Protein Atlas

More...HPAi		ENSG00000161057, Low tissue specificity

<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 PSMC2 and few additional components (PubMed:27428775, PubMed:27342858).

Interacts with NDC80/HEC; this interaction is detected only during M phase.

Interacts and SQSTM1 (PubMed:15340068). Interacts with PAAF1 (PubMed:15831487). Directly interacts with TRIM5 (PubMed:22078707).

7 Publications

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction%5Fsection">Interaction</a>' section provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="https://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated at every <a href="http://www.uniprot.org/help/synchronization">UniProt release</a>.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

Hide details

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

More...BioGRIDi		111674, 239 interactors

ComplexPortal: manually curated resource of macromolecular complexes

More...ComplexPortali		CPX-5993, 26S Proteasome complex

CORUM comprehensive resource of mammalian protein complexes

More...CORUMi		P35998

Database of interacting proteins

More...DIPi		DIP-27554N

Protein interaction database and analysis system

More...IntActi		P35998, 94 interactors

Molecular INTeraction database

More...MINTi		P35998

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000391211

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

More...RNActi		P35998, protein

<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		P35998

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

Ensembl GeneTree

More...GeneTreei		ENSGT01000000214468

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		CLU_000688_6_1_1

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P35998

Identification of Orthologs from Complete Genome Data

More...OMAi		IHANTMN

Database for complete collections of gene phylogenies

More...PhylomeDBi		P35998

TreeFam database of animal gene trees

More...TreeFami		TF105661

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%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>Sequences (2+)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.

<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.

This entry describes 2 <p>This subsection of the 'Sequence' section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform. This section is only present in reviewed entries, i.e. in UniProtKB/Swiss-Prot.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 1 potential isoform that is computationally mapped.Show allAlign All

Isoform 1 (identifier: P35998-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the <div> <p><b>What is the canonical sequence?</b><p><a href='/help/canonical_and_isoforms' target='_top'>More...</a></p>canonicali sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« 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 NRTDACFIRV 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):48,634
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:i85FD95F6DF7A3E84
GO
Isoform 2 (identifier: P35998-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-137: Missing.

Show »
Length:296
Mass (Da):33,274
Checksum:iFB08EBF831391C10
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
C9JLS9C9JLS9_HUMAN
26S proteasome regulatory subunit 7
PSMC2
130Annotation score:

Annotation score:1 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 conflicti15D → V in BAE45763 (PubMed:12880961).Curated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0561781 – 137Missing in isoform 2. 1 PublicationAdd BLAST137

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
D11094 mRNA Translation: BAA01868.1
AB075520 mRNA Translation: BAE45763.1
AK298821 mRNA Translation: BAH12878.1
AC004668 Genomic DNA No translation available.
AC093701 Genomic DNA No translation available.
CH236947 Genomic DNA Translation: EAL24412.1
CH471070 Genomic DNA Translation: EAW83332.1
BC002589 mRNA Translation: AAH02589.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS5731.1 [P35998-1]

Protein sequence database of the Protein Information Resource

More...PIRi		S24353

NCBI Reference Sequences

More...RefSeqi		NP_001191382.1, NM_001204453.1
NP_002794.1, NM_002803.3 [P35998-1]

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000292644; ENSP00000292644; ENSG00000161057 [P35998-1]
ENST00000435765; ENSP00000391211; ENSG00000161057 [P35998-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5701

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5701

UCSC genome browser

More...UCSCi		uc003vbs.4, human [P35998-1]

Keywords - Coding sequence diversityi

Alternative splicing

<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
D11094 mRNA Translation: BAA01868.1
AB075520 mRNA Translation: BAE45763.1
AK298821 mRNA Translation: BAH12878.1
AC004668 Genomic DNA No translation available.
AC093701 Genomic DNA No translation available.
CH236947 Genomic DNA Translation: EAL24412.1
CH471070 Genomic DNA Translation: EAW83332.1
BC002589 mRNA Translation: AAH02589.1
CCDSiCCDS5731.1 [P35998-1]
PIRiS24353
RefSeqiNP_001191382.1, NM_001204453.1
NP_002794.1, NM_002803.3 [P35998-1]

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
5GJQelectron microscopy4.50H1-433[»]
5GJRelectron microscopy3.50H/v1-433[»]
5L4Gelectron microscopy4.02H1-433[»]
5LN3electron microscopy6.80H1-433[»]
5M32electron microscopy3.80c1-433[»]
5T0Celectron microscopy3.80AA/BA1-433[»]
5T0Gelectron microscopy4.40A1-433[»]
5T0Helectron microscopy6.80A1-433[»]
5T0Ielectron microscopy8.00A1-433[»]
5T0Jelectron microscopy8.00A1-433[»]
5VFPelectron microscopy4.20A35-433[»]
5VFQelectron microscopy4.20A35-433[»]
5VFRelectron microscopy4.90A35-433[»]
5VFSelectron microscopy3.60A1-433[»]
5VFTelectron microscopy7.00A73-433[»]
5VFUelectron microscopy5.80A73-433[»]
5VGZelectron microscopy3.70A73-155[»]
5VHFelectron microscopy5.70A73-424[»]
5VHHelectron microscopy6.10A73-424[»]
5VHIelectron microscopy6.80A73-424[»]
5VHJelectron microscopy8.50A180-424[»]
5VHMelectron microscopy8.30A159-424[»]
5VHNelectron microscopy7.30A159-424[»]
5VHOelectron microscopy8.30A158-424[»]
5VHPelectron microscopy7.90A159-424[»]
5VHQelectron microscopy8.90A159-424[»]
5VHRelectron microscopy7.70A159-424[»]
5VHSelectron microscopy8.80A73-424[»]
6MSBelectron microscopy3.00A1-433[»]
6MSDelectron microscopy3.20A1-433[»]
6MSEelectron microscopy3.30M/m94-136[»]
6MSGelectron microscopy3.50A1-433[»]
6MSHelectron microscopy3.60A1-433[»]
6MSJelectron microscopy3.30A1-433[»]
6MSKelectron microscopy3.20A1-433[»]
6WJDelectron microscopy4.80A1-433[»]
6WJNelectron microscopy5.70A35-433[»]
SMRiP35998
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi111674, 239 interactors
ComplexPortaliCPX-5993, 26S Proteasome complex
CORUMiP35998
DIPiDIP-27554N
IntActiP35998, 94 interactors
MINTiP35998
STRINGi9606.ENSP00000391211

Chemistry databases

ChEMBLiCHEMBL2364701

PTM databases

iPTMnetiP35998
MetOSiteiP35998
PhosphoSitePlusiP35998
SwissPalmiP35998

Genetic variation databases

BioMutaiPSMC2
DMDMi547930

2D gel databases

OGPiP35998
REPRODUCTION-2DPAGEiIPI00021435
P35998

Proteomic databases

EPDiP35998
jPOSTiP35998
MassIVEiP35998
MaxQBiP35998
PaxDbiP35998
PeptideAtlasiP35998
PRIDEiP35998
ProteomicsDBi55172 [P35998-1]
6682

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...Antibodypediai		16901, 347 antibodies

The DNASU plasmid repository

More...DNASUi		5701

Genome annotation databases

EnsembliENST00000292644; ENSP00000292644; ENSG00000161057 [P35998-1]
ENST00000435765; ENSP00000391211; ENSG00000161057 [P35998-1]
GeneIDi5701
KEGGihsa:5701
UCSCiuc003vbs.4, human [P35998-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5701
DisGeNETi5701

GeneCards: human genes, protein and diseases

More...GeneCardsi		PSMC2
HGNCiHGNC:9548, PSMC2
HPAiENSG00000161057, Low tissue specificity
MIMi154365, gene
neXtProtiNX_P35998
OpenTargetsiENSG00000161057
PharmGKBiPA33893
VEuPathDBiHostDB:ENSG00000161057.10

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG0729, Eukaryota
GeneTreeiENSGT01000000214468
HOGENOMiCLU_000688_6_1_1
InParanoidiP35998
OMAiIHANTMN
PhylomeDBiP35998
TreeFamiTF105661

Enzyme and pathway databases

PathwayCommonsiP35998
ReactomeiR-HSA-1169091, Activation of NF-kappaB in B cells
R-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236974, ER-Phagosome pathway
R-HSA-1236978, Cross-presentation of soluble exogenous antigens (endosomes)
R-HSA-174084, Autodegradation of Cdh1 by Cdh1:APC/C
R-HSA-174113, SCF-beta-TrCP mediated degradation of Emi1
R-HSA-174154, APC/C:Cdc20 mediated degradation of Securin
R-HSA-174178, APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-HSA-174184, Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-HSA-180534, Vpu mediated degradation of CD4
R-HSA-180585, Vif-mediated degradation of APOBEC3G
R-HSA-187577, SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253, Degradation of beta-catenin by the destruction complex
R-HSA-202424, Downstream TCR signaling
R-HSA-211733, Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2467813, Separation of Sister Chromatids
R-HSA-2871837, FCERI mediated NF-kB activation
R-HSA-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-350562, Regulation of ornithine decarboxylase (ODC)
R-HSA-382556, ABC-family proteins mediated transport
R-HSA-450408, AUF1 (hnRNP D0) binds and destabilizes mRNA
R-HSA-4608870, Asymmetric localization of PCP proteins
R-HSA-4641257, Degradation of AXIN
R-HSA-4641258, Degradation of DVL
R-HSA-5358346, Hedgehog ligand biogenesis
R-HSA-5362768, Hh mutants that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761, Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764, CLEC7A (Dectin-1) signaling
R-HSA-5610780, Degradation of GLI1 by the proteasome
R-HSA-5610783, Degradation of GLI2 by the proteasome
R-HSA-5610785, GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684, Hedgehog 'on' state
R-HSA-5658442, Regulation of RAS by GAPs
R-HSA-5668541, TNFR2 non-canonical NF-kB pathway
R-HSA-5676590, NIK-->noncanonical NF-kB signaling
R-HSA-5678895, Defective CFTR causes cystic fibrosis
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-5689603, UCH proteinases
R-HSA-5689880, Ub-specific processing proteases
R-HSA-6798695, Neutrophil degranulation
R-HSA-68827, CDT1 association with the CDC6:ORC:origin complex
R-HSA-68949, Orc1 removal from chromatin
R-HSA-69017, CDK-mediated phosphorylation and removal of Cdc6
R-HSA-69481, G2/M Checkpoints
R-HSA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-75815, Ubiquitin-dependent degradation of Cyclin D
R-HSA-8852276, The role of GTSE1 in G2/M progression after G2 checkpoint
R-HSA-8854050, FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-HSA-8939236, RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-HSA-8939902, Regulation of RUNX2 expression and activity
R-HSA-8941858, Regulation of RUNX3 expression and activity
R-HSA-8948751, Regulation of PTEN stability and activity
R-HSA-8951664, Neddylation
R-HSA-9010553, Regulation of expression of SLITs and ROBOs
R-HSA-9020702, Interleukin-1 signaling
R-HSA-9604323, Negative regulation of NOTCH4 signaling
R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

More...BioGRID-ORCSi		5701, 701 hits in 897 CRISPR screens

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...ChiTaRSi		PSMC2, human

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		PSMC2

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5701
PharosiP35998, Tbio

Protein Ontology

More...PROi		PR:P35998
RNActiP35998, protein

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000161057, Expressed in biceps brachii and 249 other tissues
ExpressionAtlasiP35998, baseline and differential
GenevisibleiP35998, HS

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_HUMAN
<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: P35998
Secondary accession number(s): A4D0Q1
, B7Z5E2, Q3LIA5, Q9UDI3
<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 1, 1994
Last sequence update: January 23, 2007
Last modified: February 10, 2021
This is version 213 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
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again