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Entry version 62 (12 Aug 2020)
Sequence version 1 (10 Aug 2010)
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Protein

Polyubiquitin-B

Gene

Ubb

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

Annotation score:5 out of 5

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

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

Exists either covalently attached to another protein, or free (unanchored). When covalently bound, it is conjugated to target proteins via an isopeptide bond either as a monomer (monoubiquitin), a polymer linked via different Lys residues of the ubiquitin (polyubiquitin chains) or a linear polymer linked via the initiator Met of the ubiquitin (linear polyubiquitin chains). Polyubiquitin chains, when attached to a target protein, have different functions depending on the Lys residue of the ubiquitin that is linked: Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved in ERAD (endoplasmic reticulum-associated degradation) and in cell-cycle regulation; Lys-29-linked is involved in lysosomal degradation; Lys-33-linked is involved in kinase modification; Lys-48-linked is involved in protein degradation via the proteasome; Lys-63-linked is involved in endocytosis, DNA-damage responses as well as in signaling processes leading to activation of the transcription factor NF-kappa-B. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling.By similarity

Miscellaneous

Ubiquitin is encoded by 4 different genes. Uba52 and Rps27a genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains.
For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function%5Fsection">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei54Activating enzyme1
<p>This subsection describes interesting single amino acid sites on the sequence that are not defined in any other subsection. This subsection can be displayed in different sections ('Function', 'PTM / Processing', 'Pathology and Biotech') according to its content.<p><a href='/help/site' target='_top'>More...</a></p>Sitei68Essential for function1
Binding sitei72Activating enzyme1

<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

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-110312, Translesion synthesis by REV1
R-RNO-110314, Recognition of DNA damage by PCNA-containing replication complex
R-RNO-110320, Translesion Synthesis by POLH
R-RNO-1169091, Activation of NF-kappaB in B cells
R-RNO-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-RNO-1253288, Downregulation of ERBB4 signaling
R-RNO-1295596, Spry regulation of FGF signaling
R-RNO-1358803, Downregulation of ERBB2:ERBB3 signaling
R-RNO-168638, NOD1/2 Signaling Pathway
R-RNO-174048, APC/C:Cdc20 mediated degradation of Cyclin B
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-179409, APC-Cdc20 mediated degradation of Nek2A
R-RNO-182971, EGFR downregulation
R-RNO-187577, SCF(Skp2)-mediated degradation of p27/p21
R-RNO-195253, Degradation of beta-catenin by the destruction complex
R-RNO-201681, TCF dependent signaling in response to WNT
R-RNO-202424, Downstream TCR signaling
R-RNO-205043, NRIF signals cell death from the nucleus
R-RNO-209543, p75NTR recruits signalling complexes
R-RNO-209560, NF-kB is activated and signals survival
R-RNO-2122948, Activated NOTCH1 Transmits Signal to the Nucleus
R-RNO-2173788, Downregulation of TGF-beta receptor signaling
R-RNO-2173791, TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-RNO-2173795, Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-RNO-2173796, SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-RNO-2467813, Separation of Sister Chromatids
R-RNO-2559580, Oxidative Stress Induced Senescence
R-RNO-2559582, Senescence-Associated Secretory Phenotype (SASP)
R-RNO-2559585, Oncogene Induced Senescence
R-RNO-2565942, Regulation of PLK1 Activity at G2/M Transition
R-RNO-2672351, Stimuli-sensing channels
R-RNO-2871837, FCERI mediated NF-kB activation
R-RNO-3134975, Regulation of innate immune responses to cytosolic DNA
R-RNO-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-RNO-3769402, Deactivation of the beta-catenin transactivating complex
R-RNO-382556, ABC-family proteins mediated transport
R-RNO-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-RNO-450302, activated TAK1 mediates p38 MAPK activation
R-RNO-450321, JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
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-4641263, Regulation of FZD by ubiquitination
R-RNO-5205685, Pink/Parkin Mediated Mitophagy
R-RNO-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-RNO-5357905, Regulation of TNFR1 signaling
R-RNO-5357956, TNFR1-induced NFkappaB signaling pathway
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-5654726, Negative regulation of FGFR1 signaling
R-RNO-5654727, Negative regulation of FGFR2 signaling
R-RNO-5654732, Negative regulation of FGFR3 signaling
R-RNO-5654733, Negative regulation of FGFR4 signaling
R-RNO-5655862, Translesion synthesis by POLK
R-RNO-5656121, Translesion synthesis by POLI
R-RNO-5656169, Termination of translesion DNA synthesis
R-RNO-5658442, Regulation of RAS by GAPs
R-RNO-5668541, TNFR2 non-canonical NF-kB pathway
R-RNO-5675221, Negative regulation of MAPK pathway
R-RNO-5675482, Regulation of necroptotic cell death
R-RNO-5676590, NIK-->noncanonical NF-kB signaling
R-RNO-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-RNO-5685942, HDR through Homologous Recombination (HRR)
R-RNO-5687128, MAPK6/MAPK4 signaling
R-RNO-5689603, UCH proteinases
R-RNO-5689877, Josephin domain DUBs
R-RNO-5689880, Ub-specific processing proteases
R-RNO-5689896, Ovarian tumor domain proteases
R-RNO-5689901, Metalloprotease DUBs
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-5693607, Processing of DNA double-strand break ends
R-RNO-5696394, DNA Damage Recognition in GG-NER
R-RNO-5696395, Formation of Incision Complex in GG-NER
R-RNO-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-RNO-5696400, Dual Incision in GG-NER
R-RNO-6781823, Formation of TC-NER Pre-Incision Complex
R-RNO-6782135, Dual incision in TC-NER
R-RNO-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-RNO-6783310, Fanconi Anemia Pathway
R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation
R-RNO-6804757, Regulation of TP53 Degradation
R-RNO-6804760, Regulation of TP53 Activity through Methylation
R-RNO-6807004, Negative regulation of MET activity
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-69231, Cyclin D associated events in G1
R-RNO-69481, G2/M Checkpoints
R-RNO-69541, Stabilization of p53
R-RNO-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-RNO-75815, Ubiquitin-dependent degradation of Cyclin D
R-RNO-8849469, PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
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-8856825, Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828, Clathrin-mediated endocytosis
R-RNO-8863795, Downregulation of ERBB2 signaling
R-RNO-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-RNO-8866654, E3 ubiquitin ligases ubiquitinate target proteins
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-8948747, Regulation of PTEN localization
R-RNO-8948751, Regulation of PTEN stability and activity
R-RNO-8951664, Neddylation
R-RNO-901032, ER Quality Control Compartment (ERQC)
R-RNO-9013507, NOTCH3 Activation and Transmission of Signal to the Nucleus
R-RNO-9020702, Interleukin-1 signaling
R-RNO-9033241, Peroxisomal protein import
R-RNO-912631, Regulation of signaling by CBL
R-RNO-917729, Endosomal Sorting Complex Required For Transport (ESCRT)
R-RNO-917937, Iron uptake and transport
R-RNO-936440, Negative regulators of DDX58/IFIH1 signaling
R-RNO-937042, IRAK2 mediated activation of TAK1 complex
R-RNO-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-RNO-9645460, Alpha-protein kinase 1 signaling pathway
R-RNO-9646399, Aggrephagy
R-RNO-9664873, Pexophagy
R-RNO-975163, IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
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:
Polyubiquitin-B
Cleaved into the following chain:
<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:Ubb
<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
621562, Ubb

<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

<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>Keywords - Cellular componenti

Cytoplasm, Nucleus

<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_00001148061 – 76UbiquitinAdd BLAST76
ChainiPRO_000039623877 – 152UbiquitinAdd BLAST76
ChainiPRO_0000396239153 – 228UbiquitinAdd BLAST76
ChainiPRO_0000396240229 – 304UbiquitinAdd BLAST76
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes a propeptide, which is a part of a protein that is cleaved during maturation or activation. Once cleaved, a propeptide generally has no independent biological function.<p><a href='/help/propep' target='_top'>More...</a></p>PropeptideiPRO_00003962413051

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM / Processing</a> section describes <strong>covalent linkages</strong> of various types formed <strong>between two proteins (interchain cross-links)</strong> or <strong>between two parts of the same protein (intrachain cross-links)</strong>, except the disulfide bonds that are annotated in the <a href="http://www.uniprot.org/manual/disulfid">'Disulfide bond'</a> subsection.<p><a href='/help/crosslnk' target='_top'>More...</a></p>Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)
<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 residuei65Phosphoserine; by PINK1By similarity1
Modified residuei76ADP-ribosylglycineBy similarity1
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)
Cross-linki82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei141PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm%5Fprocessing%5Fsection">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PRKN), triggering mitophagy. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.By similarity
Mono-ADP-ribosylated at the C-terminus by PARP9, a component of the PPAR9-DTX3L complex. ADP-ribosylation requires processing by E1 and E2 enzymes and prevents ubiquitin conjugation to substrates such as histones.By similarity

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...
jPOSTi
P0CG51

PRoteomics IDEntifications database

More...
PRIDEi
P0CG51

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
P0CG51

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

More...
PhosphoSitePlusi
P0CG51

<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 SKP1-KMD2A and SKP1-KMD2B complexes.

By similarity

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
251381, 4 interactors

CORUM comprehensive resource of mammalian protein complexes

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CORUMi
P0CG51

<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
P0CG51

Database of comparative protein structure models

More...
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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family%5Fand%5Fdomains%5Fsection">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1 – 76Ubiquitin-like 1PROSITE-ProRule annotationAdd BLAST76
Domaini77 – 152Ubiquitin-like 2PROSITE-ProRule annotationAdd BLAST76
Domaini153 – 228Ubiquitin-like 3PROSITE-ProRule annotationAdd BLAST76
Domaini229 – 304Ubiquitin-like 4PROSITE-ProRule annotationAdd BLAST76

<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 ubiquitin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0CG51

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000626, Ubiquitin-like_dom
IPR029071, Ubiquitin-like_domsf
IPR019954, Ubiquitin_CS
IPR019956, Ubiquitin_dom

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00240, ubiquitin, 4 hits

Protein Motif fingerprint database; a protein domain database

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PRINTSi
PR00348, UBIQUITIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00213, UBQ, 4 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54236, SSF54236, 4 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00299, UBIQUITIN_1, 4 hits
PS50053, UBIQUITIN_2, 4 hits

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

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

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

P0CG51-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
110 120 130 140 150
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR
160 170 180 190 200
GGMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK
210 220 230 240 250
QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT
260 270 280 290 300
IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR

LRGGY
Length:305
Mass (Da):34,369
Last modified:August 10, 2010 - 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:i0B8C7878AE958E68
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
D16554 mRNA Translation: BAA03983.1
BC060312 mRNA Translation: AAH60312.1
BC070919 mRNA Translation: AAH70919.1

<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
D16554 mRNA Translation: BAA03983.1
BC060312 mRNA Translation: AAH60312.1
BC070919 mRNA Translation: AAH70919.1

3D structure databases

SMRiP0CG51
ModBaseiSearch...

Protein-protein interaction databases

BioGRIDi251381, 4 interactors
CORUMiP0CG51

PTM databases

iPTMnetiP0CG51
PhosphoSitePlusiP0CG51

Proteomic databases

jPOSTiP0CG51
PRIDEiP0CG51

Organism-specific databases

RGDi621562, Ubb

Phylogenomic databases

InParanoidiP0CG51

Enzyme and pathway databases

ReactomeiR-RNO-110312, Translesion synthesis by REV1
R-RNO-110314, Recognition of DNA damage by PCNA-containing replication complex
R-RNO-110320, Translesion Synthesis by POLH
R-RNO-1169091, Activation of NF-kappaB in B cells
R-RNO-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-RNO-1253288, Downregulation of ERBB4 signaling
R-RNO-1295596, Spry regulation of FGF signaling
R-RNO-1358803, Downregulation of ERBB2:ERBB3 signaling
R-RNO-168638, NOD1/2 Signaling Pathway
R-RNO-174048, APC/C:Cdc20 mediated degradation of Cyclin B
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-179409, APC-Cdc20 mediated degradation of Nek2A
R-RNO-182971, EGFR downregulation
R-RNO-187577, SCF(Skp2)-mediated degradation of p27/p21
R-RNO-195253, Degradation of beta-catenin by the destruction complex
R-RNO-201681, TCF dependent signaling in response to WNT
R-RNO-202424, Downstream TCR signaling
R-RNO-205043, NRIF signals cell death from the nucleus
R-RNO-209543, p75NTR recruits signalling complexes
R-RNO-209560, NF-kB is activated and signals survival
R-RNO-2122948, Activated NOTCH1 Transmits Signal to the Nucleus
R-RNO-2173788, Downregulation of TGF-beta receptor signaling
R-RNO-2173791, TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-RNO-2173795, Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-RNO-2173796, SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-RNO-2467813, Separation of Sister Chromatids
R-RNO-2559580, Oxidative Stress Induced Senescence
R-RNO-2559582, Senescence-Associated Secretory Phenotype (SASP)
R-RNO-2559585, Oncogene Induced Senescence
R-RNO-2565942, Regulation of PLK1 Activity at G2/M Transition
R-RNO-2672351, Stimuli-sensing channels
R-RNO-2871837, FCERI mediated NF-kB activation
R-RNO-3134975, Regulation of innate immune responses to cytosolic DNA
R-RNO-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-RNO-3769402, Deactivation of the beta-catenin transactivating complex
R-RNO-382556, ABC-family proteins mediated transport
R-RNO-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-RNO-450302, activated TAK1 mediates p38 MAPK activation
R-RNO-450321, JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
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-4641263, Regulation of FZD by ubiquitination
R-RNO-5205685, Pink/Parkin Mediated Mitophagy
R-RNO-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-RNO-5357905, Regulation of TNFR1 signaling
R-RNO-5357956, TNFR1-induced NFkappaB signaling pathway
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-5654726, Negative regulation of FGFR1 signaling
R-RNO-5654727, Negative regulation of FGFR2 signaling
R-RNO-5654732, Negative regulation of FGFR3 signaling
R-RNO-5654733, Negative regulation of FGFR4 signaling
R-RNO-5655862, Translesion synthesis by POLK
R-RNO-5656121, Translesion synthesis by POLI
R-RNO-5656169, Termination of translesion DNA synthesis
R-RNO-5658442, Regulation of RAS by GAPs
R-RNO-5668541, TNFR2 non-canonical NF-kB pathway
R-RNO-5675221, Negative regulation of MAPK pathway
R-RNO-5675482, Regulation of necroptotic cell death
R-RNO-5676590, NIK-->noncanonical NF-kB signaling
R-RNO-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-RNO-5685942, HDR through Homologous Recombination (HRR)
R-RNO-5687128, MAPK6/MAPK4 signaling
R-RNO-5689603, UCH proteinases
R-RNO-5689877, Josephin domain DUBs
R-RNO-5689880, Ub-specific processing proteases
R-RNO-5689896, Ovarian tumor domain proteases
R-RNO-5689901, Metalloprotease DUBs
R-RNO-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-RNO-5693607, Processing of DNA double-strand break ends
R-RNO-5696394, DNA Damage Recognition in GG-NER
R-RNO-5696395, Formation of Incision Complex in GG-NER
R-RNO-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-RNO-5696400, Dual Incision in GG-NER
R-RNO-6781823, Formation of TC-NER Pre-Incision Complex
R-RNO-6782135, Dual incision in TC-NER
R-RNO-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-RNO-6783310, Fanconi Anemia Pathway
R-RNO-6804756, Regulation of TP53 Activity through Phosphorylation
R-RNO-6804757, Regulation of TP53 Degradation
R-RNO-6804760, Regulation of TP53 Activity through Methylation
R-RNO-6807004, Negative regulation of MET activity
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-69231, Cyclin D associated events in G1
R-RNO-69481, G2/M Checkpoints
R-RNO-69541, Stabilization of p53
R-RNO-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-RNO-75815, Ubiquitin-dependent degradation of Cyclin D
R-RNO-8849469, PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
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-8856825, Cargo recognition for clathrin-mediated endocytosis
R-RNO-8856828, Clathrin-mediated endocytosis
R-RNO-8863795, Downregulation of ERBB2 signaling
R-RNO-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-RNO-8866654, E3 ubiquitin ligases ubiquitinate target proteins
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-8948747, Regulation of PTEN localization
R-RNO-8948751, Regulation of PTEN stability and activity
R-RNO-8951664, Neddylation
R-RNO-901032, ER Quality Control Compartment (ERQC)
R-RNO-9013507, NOTCH3 Activation and Transmission of Signal to the Nucleus
R-RNO-9020702, Interleukin-1 signaling
R-RNO-9033241, Peroxisomal protein import
R-RNO-912631, Regulation of signaling by CBL
R-RNO-917729, Endosomal Sorting Complex Required For Transport (ESCRT)
R-RNO-917937, Iron uptake and transport
R-RNO-936440, Negative regulators of DDX58/IFIH1 signaling
R-RNO-937042, IRAK2 mediated activation of TAK1 complex
R-RNO-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-RNO-9645460, Alpha-protein kinase 1 signaling pathway
R-RNO-9646399, Aggrephagy
R-RNO-9664873, Pexophagy
R-RNO-975163, IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-RNO-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

Protein Ontology

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PROi
PR:P0CG51

Family and domain databases

InterProiView protein in InterPro
IPR000626, Ubiquitin-like_dom
IPR029071, Ubiquitin-like_domsf
IPR019954, Ubiquitin_CS
IPR019956, Ubiquitin_dom
PfamiView protein in Pfam
PF00240, ubiquitin, 4 hits
PRINTSiPR00348, UBIQUITIN
SMARTiView protein in SMART
SM00213, UBQ, 4 hits
SUPFAMiSSF54236, SSF54236, 4 hits
PROSITEiView protein in PROSITE
PS00299, UBIQUITIN_1, 4 hits
PS50053, UBIQUITIN_2, 4 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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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 nameiUBB_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: P0CG51
Secondary accession number(s): P02248
, P02249, P02250, P62989, Q29120, Q63446, Q91887, Q91888
<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 10, 2010
Last sequence update: August 10, 2010
Last modified: August 12, 2020
This is version 62 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

Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
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