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Entry version 133 (26 Feb 2020)
Sequence version 2 (05 Oct 2010)
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Protein

E3 ubiquitin-protein ligase ubr-1

Gene

ubr-1

Organism
Caenorhabditis elegans
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

E3 ubiquitin-protein ligase which is a component of the N-end rule pathway (By similarity). Recognizes and binds to proteins bearing specific N-terminal residues that are destabilizing according to the N-end rule, leading to their ubiquitination and subsequent degradation (By similarity). In complex with ced-3, required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 to regulate seam cell fate patterning during larval development (PubMed:28602583). Negatively regulates glutamate metabolism through the aspartate aminotransferase got-1.2 (PubMed:29649217). Modulation of glutamate levels most likely controls locomotory behavior, in particular backwards locomotion or 'reversals' (PubMed:29649217).By similarity2 Publications

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

  • S-ubiquitinyl-[E2 ubiquitin-conjugating enzyme]-L-cysteine + [acceptor protein]-L-lysine = [E2 ubiquitin-conjugating enzyme]-L-cysteine + N(6)-ubiquitinyl-[acceptor protein]-L-lysine. EC:2.3.2.27

<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: protein ubiquitination

This protein is involved in the pathway protein ubiquitination, which is part of Protein modification.
View all proteins of this organism that are known to be involved in the pathway protein ubiquitination and in Protein modification.

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri93 – 164UBR-typePROSITE-ProRule annotationAdd BLAST72
Zinc fingeri1217 – 1335RING-type; atypicalAdd BLAST119

<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

Molecular functionTransferase
Biological processUbl conjugation pathway
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-CEL-983168 Antigen processing: Ubiquitination & Proteasome degradation

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00143

<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:
E3 ubiquitin-protein ligase ubr-1 (EC:2.3.2.27)
Alternative name(s):
N-recognin-1
RING-type E3 ubiquitin transferase ubr-1
Ubiquitin-protein ligase E3-alpha
<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:ubr-1Imported
ORF Names:C32E8.11Imported
<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>OrganismiCaenorhabditis elegans
<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 identifieri6239 [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 lineageiEukaryotaMetazoaEcdysozoaNematodaChromadoreaRhabditidaRhabditinaRhabditomorphaRhabditoideaRhabditidaePeloderinaeCaenorhabditis
<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
  • UP000001940 <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 I

Organism-specific databases

WormBase

More...
WormBasei
C32E8.11 ; CE40441 ; WBGene00016326 ; ubr-1

<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

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular%5Flocation%5Fsection">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei1695 – 1715HelicalSequence analysisAdd BLAST21

Keywords - Cellular componenti

Membrane

<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

<p>This subsection of the 'Pathology and Biotech' section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

RNAi-mediated knockdown enhances the excessive seam cell proliferation phenotype of the ain-1 ku322 mutant.1 Publication

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology%5Fand%5Fbiotech%5Fsection">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi18 – 25Missing in hp820; animals are viable, but display defective locomotion that progressively develops from the late larval stage into adulthood. Animals are capable of backwards locomotion or 'reversals' movements, but exhibit limited body flexing, with decreased body curvature during reversals, increased duration of reversals and a reduced frequency of reversal initiation compared to wild-type. Reduced bending is due to a defective activation pattern of A class motor neurons, whereby the posterior clusters of A class motor neurons DA7, VA10 and VA11, that innervate body wall muscles to execute reversals, are activated at the same time, which is in contrast to wild-type. Animals also display morphological and synaptic activity defects in AVA and AVE interneurons. Increases glutamate levels which is likely through increased got-1.2 activity. Defective reversals movement phenotype and increased glutamate levels are rescued in the got-1.2 hp731 mutant. 1 Publication8
Mutagenesisi34 – 2058Missing in hp821; animals are viable, but display defective locomotion that progressively develops from the late larval stage into adulthood. Animals are capable of backwards locomotion or 'reversals' movements, but exhibit limited body flexing, with decreased body curvature during reversals, increased duration of reversals and a reduced frequency of reversal initiation compared to wild-type. Reduced bending is due to a defective activation pattern of A class motor neurons, whereby the posterior clusters of A class motor neurons DA7, VA10 and VA11, that innervate body wall muscles to execute reversals, are activated at the same time, which is in contrast to wild-type. Animals also display morphological and synaptic activity defects in AVA and AVE interneurons. Increases glutamate levels which is likely through increased got-1.2 activity. Defective reversals movement phenotype and increased glutamate levels are rescued in the got-1.2 hp731 mutant. 1 PublicationAdd BLAST2025
Mutagenesisi136 – 163Missing in tm5996; increases lin-28 protein levels 30 hours post feeding. Enhances the excessive seam cell proliferation phenotype and enhances the delay in temporal cell fate patterning of seam cells during the progression of larval development of the ain-1 ku322 mutant. 1 PublicationAdd BLAST28
Mutagenesisi1864 – 2058Missing in hp684; animals are viable, but display defective locomotion that progressively develops from the late larval stage into adulthood. Animals are capable of backwards locomotion or 'reversals' movements, but exhibit limited body flexing, with decreased body curvature during reversals, increased duration of reversals and a reduced frequency of reversal initiation compared to wild-type. Reduced bending is due to a defective activation pattern of A class motor neurons, whereby the posterior clusters of A class motor neurons DA7, VA10 and VA11, that innervate body wall muscles to execute reversals, are activated at the same time, which is in contrast to wild-type. Animals also display morphological and synaptic activity defects in AVA and AVE interneurons. Increases glutamate levels which is likely through increased got-1.2 activity. Defective reversals movement phenotype and increased glutamate levels are rescued in the got-1.2 hp731 mutant. 1 PublicationAdd BLAST195

<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_00000561381 – 2058E3 ubiquitin-protein ligase ubr-1Add BLAST2058

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
P91133

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

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PaxDbi
P91133

PeptideAtlas

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PeptideAtlasi
P91133

PRoteomics IDEntifications database

More...
PRIDEi
P91133

<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 provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified 'at protein level'.<br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Expressed in pharyngeal muscles, body wall muscles and a subset of neurons throughout postembryonic development (PubMed:29649217). Prominently expressed in premotor interneurons, but not expressed in ventral cord motor neurons (PubMed:29649217). Weakly expressed in hypodermal seam cells (PubMed:29649217).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
WBGene00016326 Expressed in multi-cellular organism and 4 other tissues

<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

Interacts with ubc-1 (Probable).

Component of a complex containing at least ced-3, ubr-1 and possibly ate-1 (PubMed:28602583). Within complex interacts with ced-3 (via the p17 subunit); this interaction is required for the ced-3-mediated cleavage and subsequent degradation of the heterochronic protein lin-28 (PubMed:28602583).

1 Publication1 Publication

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

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BioGridi
37427, 6 interactors

Protein interaction database and analysis system

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IntActi
P91133, 1 interactor

STRING: functional protein association networks

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STRINGi
6239.C32E8.11

<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

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SMRi
P91133

Database of comparative protein structure models

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ModBasei
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 general information on the biological role of a domain. The term 'domain' is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

The RING-H2 zinc finger is an atypical RING finger with a His ligand in place of the fourth Cys of the classical motif.

<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 UBR1 family.Curated

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri93 – 164UBR-typePROSITE-ProRule annotationAdd BLAST72
Zinc fingeri1217 – 1335RING-type; atypicalAdd BLAST119

Keywords - Domaini

Transmembrane, Transmembrane helix, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG1140 Eukaryota
ENOG410XPQU LUCA

Ensembl GeneTree

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GeneTreei
ENSGT00950000183075

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
CLU_001801_2_0_1

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P91133

KEGG Orthology (KO)

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KOi
K10626

Identification of Orthologs from Complete Genome Data

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OMAi
PEWECAF

Database of Orthologous Groups

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OrthoDBi
81415at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P91133

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

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Gene3Di
3.30.1390.10, 1 hit

Integrated resource of protein families, domains and functional sites

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InterProi
View protein in InterPro
IPR003769 ClpS_core
IPR014719 Ribosomal_L7/12_C/ClpS-like
IPR039164 UBR1-like
IPR003126 Znf_UBR

The PANTHER Classification System

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PANTHERi
PTHR21497 PTHR21497, 1 hit

Pfam protein domain database

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Pfami
View protein in Pfam
PF02617 ClpS, 1 hit
PF02207 zf-UBR, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

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SMARTi
View protein in SMART
SM00396 ZnF_UBR1, 1 hit

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54736 SSF54736, 1 hit

PROSITE; a protein domain and family database

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PROSITEi
View protein in PROSITE
PS51157 ZF_UBR, 1 hit

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

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

P91133-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MIVDLIQSAR QGEWAQVRQL LLKHWLVQVP EVFEVNSDLP WDNTAANERI
60 70 80 90 100
LGSQGEILLA PLVSAFVLDV RNTKSTLEAM NGIAGVDPAR RGQICGHVFK
110 120 130 140 150
NGELTYTCLD CATDGTCVMC LQCFEVSIHK SHKYKMHSSS GSGYCDCGDA
160 170 180 190 200
DAWTEGYACA NHEKKDDEEA AVLAPELKKR CEQLVEIILQ FSLSMITHKD
210 220 230 240 250
DLKLPEIFEK MKPEVTNEAQ QYLTVLYNDE THTYESVIKV LELYIHCTKD
260 270 280 290 300
QAMLVATIVD REGRSAVKLG SKADCTKAKD DVQRKTARDP TSIRRSSNHN
310 320 330 340 350
LPLSVKVMDT TLFALQNFSI SLLTWLNTQM DVFPPLREIV GEILLSSKFA
360 370 380 390 400
LKKNYTRKMK SEDQRLVAGI IRNVMVLPDD EEEELFALDG RMDVDEMDDD
410 420 430 440 450
DIGGEALQME IDADDEEEIT AALAGVSEHQ ESPGPSRDSS TFTMLENILL
460 470 480 490 500
QDTQMWKAGR SILHQMLMRT VFMIYDQKVR FAKAFMLHYN EIYEDFIKDD
510 520 530 540 550
HEMDVSVVGL SVQFMTVPSL ARKLVAEDQA FSVISKAIRD QTDKFVKYYN
560 570 580 590 600
DGKIARFDFT SRSFPPELRR SLHITRDMAY ILNAVPSESD WNRELIDGFV
610 620 630 640 650
QGFADFLLFL QHLQGMDEVK RQAVEHQVWE SEWETAFNIL LRLKDAISMI
660 670 680 690 700
IGWAETNEEV HNRLMIMCLE LMNRMPPVYT KSEEDTYELT VTINGESCRI
710 720 730 740 750
SHFDVLKSST SVHQPVVRII AGLFSASNYT GFLLNRSNNS HTSLNQERIK
760 770 780 790 800
ELINCKDETN LYELSLRVLV LCAQSNATLW RRNGFSLINQ IHNYFSPLCR
810 820 830 840 850
NEMFDRDVLM MQVGAALTPS TKFIFHLLHR FRLFKWATSE FEQDKANEKP
860 870 880 890 900
AKPESEDLSK TLVMIAEEFI QCLILILCER YTYGVGKTRP MDQMKREVIH
910 920 930 940 950
ILCTGSHTFS HIQQKMSHDI NSKRLSLHEA VNLVADFRKP LATTAGQFHC
960 970 980 990 1000
KESSLPTYSP FFMHYSKSDQ SAAEQSQARV RAKMEKSVRA CAPPILPDFQ
1010 1020 1030 1040 1050
TFFERIPEIL TTNVLIHVVR LIIDRTARRS RFSSDRLFHK TLYLIGIALN
1060 1070 1080 1090 1100
EEEKNPSFGF TQRAEESIGL LSLLEGLVGK PESSICPILL EVTVEKYRKL
1110 1120 1130 1140 1150
IKARAGVPEA APAPENKPAQ SEEEIKAKRA ARAAEMRQKA MAKMSNMQSK
1160 1170 1180 1190 1200
FMKKIEDEEK KDESQTPSEK SETVVKKDDY DNKHFFDEDV VKQVGHDFPV
1210 1220 1230 1240 1250
CIGANKWHAE LVKPRTLTCI LCQEDEIIAP QQGKPMVCAA FIQQSQLFTH
1260 1270 1280 1290 1300
KNKNGELMTA SSGTISTRDL LTAPATLQYG VDVSTCSHSM HYECYRSLAE
1310 1320 1330 1340 1350
ANRSRESLRA RQVGQHSHKM VDTENGEYQC PLCKRLSNAA IPVLPAYQLT
1360 1370 1380 1390 1400
NQNGFSTVSG AGKENFDTWV ARVKRNLEMP LSSESVSKKG HSRKRSHSER
1410 1420 1430 1440 1450
SLLDLEKLSK DPDTANTSAG VLQFGAMEMS SATHMPASAE SQMLMTTSPS
1460 1470 1480 1490 1500
QDDVEFYNEL AAMFVDQDVN NTTSPAATPE TIPAIGSSSR IPESQESGKK
1510 1520 1530 1540 1550
PLSSQIQHVL YSLIRPFPAL INSNRICSSS FEGFEEPIKD LGKNMMKFRK
1560 1570 1580 1590 1600
RGNELKTNFI EKHLKGYVIS TVTWQSTAHV ARAISSYLHY DKKPLFGALN
1610 1620 1630 1640 1650
TRQRDCLSAM ARLCASLSHN MQFLLHAVSD MLRVFLCEPP RPKLAQTPGS
1660 1670 1680 1690 1700
PLLSAPSTSS FTPAPAQIPH SGTNFAFLVQ LFNPAGPRKN VNLNILQIDI
1710 1720 1730 1740 1750
LSLAISLMMT IGWTWNNGTQ SMNSSSTHQK ARLLTPDGSV DEAYVLRLSL
1760 1770 1780 1790 1800
LAHYFQIIAT HSEADGNDVN MEEEQESQME VDPVAAQTIR KLYALCHPFD
1810 1820 1830 1840 1850
GPLRRVDILW RKMEEGAQSL LRPIALLYHF ITLVDPPEAL KDPSINSSEP
1860 1870 1880 1890 1900
LFRYLGLPHK IEEQISGSML EKLFTMWSSS IPSDQALRQD LVVQPVRPNL
1910 1920 1930 1940 1950
LVELPEKYSQ LINQVATFKC PTIPIEESTS NVPTLCLVCG TILCSQAYCC
1960 1970 1980 1990 2000
QKIINKQSYG ACRYHMSQCS GSVGMFLRVR DCSLVLMTTR KRGCFRPAPY
2010 2020 2030 2040 2050
VDEFGEVDQG FRRGNPLHLN PELYQKLKSL WLQQGITEEV VNYNEIDFRN

VQYDWGHF
Length:2,058
Mass (Da):232,816
Last modified:October 5, 2010 - v2
<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:iDBAE0014CE89F7AC
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
BX284601 Genomic DNA Translation: CCD66417.1

Protein sequence database of the Protein Information Resource

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PIRi
T25604

NCBI Reference Sequences

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RefSeqi
NP_491231.2, NM_058830.4

Genome annotation databases

Ensembl metazoan genome annotation project

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EnsemblMetazoai
C32E8.11.1; C32E8.11.1; WBGene00016326

Database of genes from NCBI RefSeq genomes

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GeneIDi
171953

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
cel:CELE_C32E8.11

UCSC genome browser

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UCSCi
C32E8.11 c. elegans

<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
BX284601 Genomic DNA Translation: CCD66417.1
PIRiT25604
RefSeqiNP_491231.2, NM_058830.4

3D structure databases

SMRiP91133
ModBaseiSearch...

Protein-protein interaction databases

BioGridi37427, 6 interactors
IntActiP91133, 1 interactor
STRINGi6239.C32E8.11

Proteomic databases

EPDiP91133
PaxDbiP91133
PeptideAtlasiP91133
PRIDEiP91133

Genome annotation databases

EnsemblMetazoaiC32E8.11.1; C32E8.11.1; WBGene00016326
GeneIDi171953
KEGGicel:CELE_C32E8.11
UCSCiC32E8.11 c. elegans

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
171953
WormBaseiC32E8.11 ; CE40441 ; WBGene00016326 ; ubr-1

Phylogenomic databases

eggNOGiKOG1140 Eukaryota
ENOG410XPQU LUCA
GeneTreeiENSGT00950000183075
HOGENOMiCLU_001801_2_0_1
InParanoidiP91133
KOiK10626
OMAiPEWECAF
OrthoDBi81415at2759
PhylomeDBiP91133

Enzyme and pathway databases

UniPathwayiUPA00143
ReactomeiR-CEL-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

Protein Ontology

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PROi
PR:P91133

Gene expression databases

BgeeiWBGene00016326 Expressed in multi-cellular organism and 4 other tissues

Family and domain databases

Gene3Di3.30.1390.10, 1 hit
InterProiView protein in InterPro
IPR003769 ClpS_core
IPR014719 Ribosomal_L7/12_C/ClpS-like
IPR039164 UBR1-like
IPR003126 Znf_UBR
PANTHERiPTHR21497 PTHR21497, 1 hit
PfamiView protein in Pfam
PF02617 ClpS, 1 hit
PF02207 zf-UBR, 1 hit
SMARTiView protein in SMART
SM00396 ZnF_UBR1, 1 hit
SUPFAMiSSF54736 SSF54736, 1 hit
PROSITEiView protein in PROSITE
PS51157 ZF_UBR, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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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 nameiUBR1_CAEEL
<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: P91133
<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: August 16, 2005
Last sequence update: October 5, 2010
Last modified: February 26, 2020
This is version 133 of the entry and version 2 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 programCaenorhabditis annotation project

<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

Reference proteome

Documents

  1. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  2. SIMILARITY comments
    Index of protein domains and families
  3. Caenorhabditis elegans
    Caenorhabditis elegans: entries, gene names and cross-references to WormBase
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