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Entry version 112 (29 Sep 2021)
Sequence version 1 (10 Aug 2010)
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Protein

Polyubiquitin-B

Gene

UBB

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

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.

2 Publications

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.
The mRNA encoding variant UBB(+1) is produced by an unknown mechanism involving the deletion of a GT dinucleotide in the close proximity of a GAGAG motif (PubMed:9422699). This variant mRNA is found in normal brain, but the encoded protein accumulates only in brain neurofibrillary tangles and neuritic plaques in Alzheimer disease and other tauopathies, as well as polyglutaminopathies (PubMed:14597671). UBB(+1) variant cannot be used for polyubiquitination, is not effectively degraded by the proteasome when ubiquitinated and ubiquitinated UBB(+1) is refractory to disassembly by deubiquitinating enzymes (DUBs). In healthy brain, UBB(+1) C-terminus can be cleaved by UCHL3 (PubMed:21762696).3 Publications
For a better understanding, features related to ubiquitin are only indicated for the first chain.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<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>Sitei54Interacts with activating enzyme1
Sitei68Essential for function1
Sitei72Interacts with activating 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

Pathway Commons web resource for biological pathway data

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PathwayCommonsi
P0CG47

Reactome - a knowledgebase of biological pathways and processes

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Reactomei
R-HSA-110312, Translesion synthesis by REV1
R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex
R-HSA-110320, Translesion Synthesis by POLH
R-HSA-1169091, Activation of NF-kappaB in B cells
R-HSA-1169408, ISG15 antiviral mechanism
R-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236382, Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1236974, ER-Phagosome pathway
R-HSA-1253288, Downregulation of ERBB4 signaling
R-HSA-1295596, Spry regulation of FGF signaling
R-HSA-1358803, Downregulation of ERBB2:ERBB3 signaling
R-HSA-162588, Budding and maturation of HIV virion
R-HSA-168638, NOD1/2 Signaling Pathway
R-HSA-168927, TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-168928, DDX58/IFIH1-mediated induction of interferon-alpha/beta
R-HSA-174048, APC/C:Cdc20 mediated degradation of Cyclin B
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-174490, Membrane binding and targetting of GAG proteins
R-HSA-175474, Assembly Of The HIV Virion
R-HSA-179409, APC-Cdc20 mediated degradation of Nek2A
R-HSA-180534, Vpu mediated degradation of CD4
R-HSA-180585, Vif-mediated degradation of APOBEC3G
R-HSA-182971, EGFR downregulation
R-HSA-187577, SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253, Degradation of beta-catenin by the destruction complex
R-HSA-201681, TCF dependent signaling in response to WNT
R-HSA-202424, Downstream TCR signaling
R-HSA-205043, NRIF signals cell death from the nucleus
R-HSA-209543, p75NTR recruits signalling complexes
R-HSA-209560, NF-kB is activated and signals survival
R-HSA-211733, Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2122947, NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2122948, Activated NOTCH1 Transmits Signal to the Nucleus
R-HSA-2173788, Downregulation of TGF-beta receptor signaling
R-HSA-2173791, TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-HSA-2173795, Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-HSA-2173796, SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-2467813, Separation of Sister Chromatids
R-HSA-2559580, Oxidative Stress Induced Senescence
R-HSA-2559582, Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559585, Oncogene Induced Senescence
R-HSA-2565942, Regulation of PLK1 Activity at G2/M Transition
R-HSA-2644606, Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2672351, Stimuli-sensing channels
R-HSA-2691232, Constitutive Signaling by NOTCH1 HD Domain Mutants
R-HSA-2871837, FCERI mediated NF-kB activation
R-HSA-2894862, Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-2979096, NOTCH2 Activation and Transmission of Signal to the Nucleus
R-HSA-3134975, Regulation of innate immune responses to cytosolic DNA
R-HSA-3322077, Glycogen synthesis
R-HSA-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-3769402, Deactivation of the beta-catenin transactivating complex
R-HSA-3785653, Myoclonic epilepsy of Lafora
R-HSA-382556, ABC-family proteins mediated transport
R-HSA-400253, Circadian Clock
R-HSA-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-450302, activated TAK1 mediates p38 MAPK activation
R-HSA-450321, JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
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-4641263, Regulation of FZD by ubiquitination
R-HSA-5205685, PINK1-PRKN Mediated Mitophagy
R-HSA-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-HSA-5357905, Regulation of TNFR1 signaling
R-HSA-5357956, TNFR1-induced NFkappaB signaling pathway
R-HSA-5358346, Hedgehog ligand biogenesis
R-HSA-5362768, Hh mutants 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-5654726, Negative regulation of FGFR1 signaling
R-HSA-5654727, Negative regulation of FGFR2 signaling
R-HSA-5654732, Negative regulation of FGFR3 signaling
R-HSA-5654733, Negative regulation of FGFR4 signaling
R-HSA-5655862, Translesion synthesis by POLK
R-HSA-5656121, Translesion synthesis by POLI
R-HSA-5656169, Termination of translesion DNA synthesis
R-HSA-5658442, Regulation of RAS by GAPs
R-HSA-5668541, TNFR2 non-canonical NF-kB pathway
R-HSA-5675221, Negative regulation of MAPK pathway
R-HSA-5675482, Regulation of necroptotic cell death
R-HSA-5676590, NIK-->noncanonical NF-kB signaling
R-HSA-5678895, Defective CFTR causes cystic fibrosis
R-HSA-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-HSA-5685942, HDR through Homologous Recombination (HRR)
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-5689603, UCH proteinases
R-HSA-5689877, Josephin domain DUBs
R-HSA-5689880, Ub-specific processing proteases
R-HSA-5689896, Ovarian tumor domain proteases
R-HSA-5689901, Metalloprotease DUBs
R-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693607, Processing of DNA double-strand break ends
R-HSA-5696394, DNA Damage Recognition in GG-NER
R-HSA-5696395, Formation of Incision Complex in GG-NER
R-HSA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400, Dual Incision in GG-NER
R-HSA-6781823, Formation of TC-NER Pre-Incision Complex
R-HSA-6781827, Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135, Dual incision in TC-NER
R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6783310, Fanconi Anemia Pathway
R-HSA-6804756, Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757, Regulation of TP53 Degradation
R-HSA-6804760, Regulation of TP53 Activity through Methylation
R-HSA-6807004, Negative regulation of MET activity
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-69231, Cyclin D associated events in G1
R-HSA-69481, G2/M Checkpoints
R-HSA-69541, Stabilization of p53
R-HSA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-75815, Ubiquitin-dependent degradation of Cyclin D
R-HSA-8849469, PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
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-8856825, Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828, Clathrin-mediated endocytosis
R-HSA-8863795, Downregulation of ERBB2 signaling
R-HSA-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-HSA-8866654, E3 ubiquitin ligases ubiquitinate target proteins
R-HSA-8875360, InlB-mediated entry of Listeria monocytogenes into host cell
R-HSA-8876493, InlA-mediated entry of Listeria monocytogenes into host cells
R-HSA-8932339, ROS sensing by NFE2L2
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-8948747, Regulation of PTEN localization
R-HSA-8948751, Regulation of PTEN stability and activity
R-HSA-8951664, Neddylation
R-HSA-901032, ER Quality Control Compartment (ERQC)
R-HSA-9010553, Regulation of expression of SLITs and ROBOs
R-HSA-9013507, NOTCH3 Activation and Transmission of Signal to the Nucleus
R-HSA-9013973, TICAM1-dependent activation of IRF3/IRF7
R-HSA-9014325, TICAM1,TRAF6-dependent induction of TAK1 complex
R-HSA-9020702, Interleukin-1 signaling
R-HSA-9033241, Peroxisomal protein import
R-HSA-912631, Regulation of signaling by CBL
R-HSA-917729, Endosomal Sorting Complex Required For Transport (ESCRT)
R-HSA-917937, Iron uptake and transport
R-HSA-936440, Negative regulators of DDX58/IFIH1 signaling
R-HSA-936964, Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-HSA-937039, IRAK1 recruits IKK complex
R-HSA-937041, IKK complex recruitment mediated by RIP1
R-HSA-937042, IRAK2 mediated activation of TAK1 complex
R-HSA-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-HSA-9604323, Negative regulation of NOTCH4 signaling
R-HSA-9613829, Chaperone Mediated Autophagy
R-HSA-9615710, Late endosomal microautophagy
R-HSA-9636383, Prevention of phagosomal-lysosomal fusion
R-HSA-9637628, Modulation by Mtb of host immune system
R-HSA-9645460, Alpha-protein kinase 1 signaling pathway
R-HSA-9646399, Aggrephagy
R-HSA-9648002, RAS processing
R-HSA-9664873, Pexophagy
R-HSA-9683683, Maturation of protein E
R-HSA-9694493, Maturation of protein E
R-HSA-9705462, Inactivation of CSF3 (G-CSF) signaling
R-HSA-9706369, Negative regulation of FLT3
R-HSA-9706377, FLT3 signaling by CBL mutants
R-HSA-9708530, Regulation of BACH1 activity
R-HSA-975110, TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-HSA-975144, IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-HSA-975163, IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-HSA-977225, Amyloid fiber formation
R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P0CG47, Predicted

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Polyubiquitin-B
Cleaved into the following chain:
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: 'Name', 'Synonyms', 'Ordered locus names' and 'ORF names'.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:UBB
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the 'taxonomic identifier' or 'taxid'.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components.<br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 17

Organism-specific databases

Human Gene Nomenclature Database

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HGNCi
HGNC:12463, UBB

Online Mendelian Inheritance in Man (OMIM)

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MIMi
191339, gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P0CG47

Eukaryotic Pathogen, Vector and Host Database Resources

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VEuPathDBi
HostDB:ENSG00000170315

<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

<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 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

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'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>Mutagenesisi48K → R: No effect on HLTF-mediated polyubiquitination of PCNA. 1 Publication1
Mutagenesisi63K → R: Abolishes HLTF-mediated polyubiquitination of PCNA. 1 Publication1
Mutagenesisi65S → A: Prevents phosphorylation in case of mitophagy. 3 Publications1
Mutagenesisi65S → D: Phosphomimetic mutant that binds and activates PRKN. 1 Publication1
Mutagenesisi68H → G: Loss of DTX3L-mediated polyubiquitination of histone H3 and H4. 1 Publication1
Mutagenesisi72R → G: No effect on ADP-ribosylation. 1 Publication1
Mutagenesisi72R → K: No effect on ADP-ribosylation, when associated with K-74. 1 Publication1
Mutagenesisi74R → G: No effect on ADP-ribosylation. 1 Publication1
Mutagenesisi74R → K: No effect on ADP-ribosylation, when associated with K-72. 1 Publication1
Mutagenesisi76G → A: Loss of ADP-ribosylation. 1 Publication1

Organism-specific databases

DisGeNET

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DisGeNETi
7314

MalaCards human disease database

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MalaCardsi
UBB

Open Targets

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OpenTargetsi
ENSG00000170315

Orphanet; a database dedicated to information on rare diseases and orphan drugs

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Orphaneti
99771, Bifid uvula
101023, Cleft hard palate
99772, Cleft velum
155878, Submucosal cleft palate

Miscellaneous databases

Pharos NIH Druggable Genome Knowledgebase

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Pharosi
P0CG47, Tbio

Chemistry databases

ChEMBL database of bioactive drug-like small molecules

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ChEMBLi
CHEMBL4523178

Drug and drug target database

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DrugBanki
DB02542, (4s)-5-Fluoro-L-Leucine

Genetic variation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
UBB

Domain mapping of disease mutations (DMDM)

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DMDMi
302595875

<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_00003961741 – 76UbiquitinAdd BLAST76
ChainiPRO_000039617577 – 152UbiquitinAdd BLAST76
ChainiPRO_0000396176153 – 228UbiquitinAdd BLAST76
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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_00003961772291

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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-linki6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
<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 PINK14 Publications1
Modified residuei76ADP-ribosylglycine1 Publication1
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">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 (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). 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 (PubMed:25527291).4 Publications
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.1 Publication

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

Encyclopedia of Proteome Dynamics

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EPDi
P0CG47

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0CG47

MassIVE - Mass Spectrometry Interactive Virtual Environment

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MassIVEi
P0CG47

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

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PaxDbi
P0CG47

PeptideAtlas

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PeptideAtlasi
P0CG47

PRoteomics IDEntifications database

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PRIDEi
P0CG47

ProteomicsDB: a multi-organism proteome resource

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ProteomicsDBi
52474

Consortium for Top Down Proteomics

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TopDownProteomicsi
P0CG47

PTM databases

GlyGen: Computational and Informatics Resources for Glycoscience

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GlyGeni
P0CG47, 1 site, 1 O-linked glycan (1 site)

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P0CG47

MetOSite database of methionine sulfoxide sites

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MetOSitei
P0CG47

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

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PhosphoSitePlusi
P0CG47

SwissPalm database of S-palmitoylation events

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SwissPalmi
P0CG47

<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

Gene expression databases

Bgee dataBase for Gene Expression Evolution

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Bgeei
ENSG00000170315, Expressed in hypothalamus and 248 other tissues

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P0CG47, baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P0CG47, HS

Organism-specific databases

Human Protein Atlas

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HPAi
ENSG00000170315, 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_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with SKP1-KMD2A and SKP1-KMD2B complexes.

1 Publication

<p>This subsection of the '<a href="http://www.uniprot.org/help/interaction_section">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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGRID)

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BioGRIDi
113162, 255 interactors

Protein interaction database and analysis system

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IntActi
P0CG47, 214 interactors

Molecular INTeraction database

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MINTi
P0CG47

STRING: functional protein association networks

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STRINGi
9606.ENSP00000304697

Miscellaneous databases

RNAct, Protein-RNA interaction predictions for model organisms.

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RNActi
P0CG47, 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

Secondary structure

1229
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Biological Magnetic Resonance Data Bank

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BMRBi
P0CG47

Small Angle Scattering Biological Data Bank

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SASBDBi
P0CG47

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
P0CG47

Database of comparative protein structure models

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ModBasei
Search...

Protein Data Bank in Europe - Knowledge Base

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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

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">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

<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

evolutionary genealogy of genes: Non-supervised Orthologous Groups

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eggNOGi
KOG0001, Eukaryota

Ensembl GeneTree

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GeneTreei
ENSGT00940000162439

InParanoid: Eukaryotic Ortholog Groups

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InParanoidi
P0CG47

Identification of Orthologs from Complete Genome Data

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OMAi
CKDAAIN

Database of Orthologous Groups

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OrthoDBi
1536766at2759

Database for complete collections of gene phylogenies

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PhylomeDBi
P0CG47

TreeFam database of animal gene trees

More...
TreeFami
TF300820

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

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Pfami
View protein in Pfam
PF00240, ubiquitin, 3 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

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SMARTi
View protein in SMART
SM00213, UBQ, 3 hits

Superfamily database of structural and functional annotation

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SUPFAMi
SSF54236, SSF54236, 3 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00299, UBIQUITIN_1, 3 hits
PS50053, UBIQUITIN_2, 3 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_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequence (1+)i

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

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is 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 has 1 described isoform and 4 potential isoforms that are computationally mapped.Show allAlign All

P0CG47-1 [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
QLEDGRTLSD YNIQKESTLH LVLRLRGGC
Length:229
Mass (Da):25,762
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:i33011162F1C48BB1
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 are 4 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
J3QS39J3QS39_HUMAN
Polyubiquitin-B
UBB
93Annotation 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>
B4DV12B4DV12_HUMAN
Polyubiquitin-B
UBB
153Annotation 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>
J3QSA3J3QSA3_HUMAN
Polyubiquitin-B
UBB
43Annotation 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>
J3QKN0J3QKN0_HUMAN
Polyubiquitin-B
UBB
206Annotation 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>

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the 'Sequence' section describes natural variant(s) of the protein sequence.<p><a href='/help/variant' target='_top'>More...</a></p>Natural variantiVAR_06624876 – 229GMQIF…LRGGC → YADLREDPDRQDHHPGSGAQ in UBB(+1); loss of polyubiquitination; impairs the ubiquitin-proteasome pathway; refractory to disassembly by DUBs; slow degradation by UCHL3. Add BLAST154

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
X04803 Genomic DNA Translation: CAA28495.1
AB089617 Genomic DNA Translation: BAC56955.1
AC093484 Genomic DNA No translation available.
BC000379 mRNA Translation: AAH00379.1
BC009301 mRNA Translation: AAH09301.1
BC015127 mRNA Translation: AAH15127.1
BC026301 mRNA Translation: AAH26301.1
BC031027 mRNA Translation: AAH31027.1
BC046123 mRNA Translation: AAH46123.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS11177.1

Protein sequence database of the Protein Information Resource

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PIRi
A26437, UQHUB

NCBI Reference Sequences

More...
RefSeqi
NP_001268645.1, NM_001281716.1
NP_001268646.1, NM_001281717.1
NP_001268647.1, NM_001281718.1
NP_001268648.1, NM_001281719.1
NP_001268649.1, NM_001281720.1
NP_061828.1, NM_018955.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000302182; ENSP00000304697; ENSG00000170315
ENST00000395837; ENSP00000379178; ENSG00000170315
ENST00000395839; ENSP00000379180; ENSG00000170315
ENST00000614404; ENSP00000478771; ENSG00000170315

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7314

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7314

<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
X04803 Genomic DNA Translation: CAA28495.1
AB089617 Genomic DNA Translation: BAC56955.1
AC093484 Genomic DNA No translation available.
BC000379 mRNA Translation: AAH00379.1
BC009301 mRNA Translation: AAH09301.1
BC015127 mRNA Translation: AAH15127.1
BC026301 mRNA Translation: AAH26301.1
BC031027 mRNA Translation: AAH31027.1
BC046123 mRNA Translation: AAH46123.1
CCDSiCCDS11177.1
PIRiA26437, UQHUB
RefSeqiNP_001268645.1, NM_001281716.1
NP_001268646.1, NM_001281717.1
NP_001268647.1, NM_001281718.1
NP_001268648.1, NM_001281719.1
NP_001268649.1, NM_001281720.1
NP_061828.1, NM_018955.3

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
2KHWNMR-B153-228[»]
2MBBNMR-B153-228[»]
2MRONMR-A153-228[»]
2MSGNMR-A153-224[»]
2N13NMR-B153-228[»]
C153-229[»]
4UELX-ray2.30B153-228[»]
4UF6X-ray3.69B/E/H/K153-227[»]
4WHVX-ray8.30A/F/G/L153-228[»]
4WLRX-ray2.00C153-228[»]
4WURX-ray3.16B153-228[»]
4XOFX-ray1.15A153-228[»]
4ZFRX-ray1.72B153-228[»]
4ZFTX-ray2.30B/D153-228[»]
4ZPZX-ray1.54A/B153-225[»]
4ZUXX-ray3.82X/c/h/m153-228[»]
5BNBX-ray2.49E/F/G/I153-229[»]
5CAWX-ray2.62B/D153-228[»]
5CRAX-ray2.64C/D153-227[»]
5CVMX-ray1.90B153-211[»]
5CVNX-ray3.36D153-228[»]
5CVOX-ray3.88C/F153-228[»]
5D0KX-ray2.65B/E/H/K153-228[»]
5D0MX-ray1.91B153-228[»]
5DFLX-ray2.10B153-228[»]
5DK8X-ray1.32A/B154-227[»]
5E6JX-ray2.85C/F153-227[»]
5EDVX-ray3.48E/F/G/H153-228[»]
5EMZX-ray1.66A/B/C/D/E/F1-76[»]
5EYAX-ray2.40C/D153-228[»]
5GJQelectron microscopy4.50y153-228[»]
5GO7X-ray1.80A1-76[»]
5GO8X-ray2.21A1-76[»]
5GOBX-ray1.15A1-76[»]
5GOCX-ray1.73A1-76[»]
5GODX-ray1.15A/B1-76[»]
5GOGX-ray1.98A1-76[»]
5GOHX-ray1.95A1-76[»]
5GOIX-ray1.59A/B1-76[»]
5GOJX-ray1.55A1-76[»]
5GOKX-ray1.84A1-76[»]
5H7SX-ray3.49E/F1-76[»]
5IBKX-ray2.50C/F151-226[»]
5IFRX-ray2.20B153-227[»]
5JBYX-ray1.99A/C/E153-228[»]
5JG6X-ray2.00B/C76-153[»]
5JP3X-ray2.90B/D/F/H153-227[»]
5JTJX-ray3.32B153-228[»]
5JTVX-ray3.31B/D/F/H1-76[»]
5K9PX-ray1.55A153-228[»]
5KGFelectron microscopy4.54M/O153-228[»]
5KHYX-ray3.50A153-225[»]
B153-227[»]
5KYCX-ray1.43C153-228[»]
5KYDX-ray1.62D153-228[»]
5KYEX-ray1.97C/D153-228[»]
5KYFX-ray1.45C153-228[»]
5L8HX-ray1.85B1-76[»]
5L8WX-ray2.79C1-75[»]
5L9Telectron microscopy6.40S1-73[»]
5LN1X-ray3.14U1-76[»]
5LRVX-ray2.80B1-76[»]
C1-75[»]
5LRWX-ray2.00B/D1-75[»]
5LRXX-ray2.85B/D1-76[»]
5M93X-ray1.79A/B/C1-76[»]
5MNJX-ray2.16B/F1-76[»]
5N2WX-ray2.68B1-76[»]
5N38X-ray2.60B1-76[»]
5NL5X-ray1.96A/B/C1-76[»]
5NLJX-ray1.53A/B/C1-76[»]
5NVGX-ray1.07A1-76[»]
5O44X-ray3.14B/C1-74[»]
D/F1-76[»]
5O6TX-ray1.57C/D1-76[»]
5OHKX-ray2.34B1-76[»]
5OHLX-ray2.50I/J/K/L/M/N/O/P1-76[»]
5OHNX-ray3.60B/D1-76[»]
5OHPX-ray2.80B/C1-76[»]
5TOFX-ray1.12A1-76[»]
5TOGX-ray1.08A1-76[»]
5TUTX-ray2.60B1-76[»]
5TXKX-ray1.84B1-76[»]
5UJLNMR-A/B1-76[»]
5UJNNMR-A/B1-76[»]
5ULFX-ray1.80B/D1-76[»]
5ULHX-ray1.95B1-76[»]
5ULKX-ray2.38B1-76[»]
5V1YX-ray1.42C/D1-76[»]
5V1ZX-ray2.00C/D1-76[»]
5VEYNMR-B1-76[»]
5VF0NMR-A1-76[»]
5VNZX-ray3.41C/F1-76[»]
5VO0X-ray3.90C/F1-76[»]
5VZMNMR-A153-228[»]
5VZWX-ray2.28C/D153-228[»]
5W46X-ray1.18A/B153-228[»]
5WFIX-ray1.85C/D1-76[»]
5X3MX-ray1.82A1-76[»]
5X3NX-ray1.65A1-76[»]
5X3OX-ray2.19A1-76[»]
5XBONMR-A1-76[»]
5XDPX-ray2.38A1-76[»]
5XK4NMR-A153-228[»]
5XK5NMR-A153-228[»]
5XPKX-ray2.27A153-228[»]
5YDRX-ray2.00A/D153-225[»]
5YIJX-ray3.18C/D/G153-228[»]
5YIKX-ray3.10C/D/F153-228[»]
5YMYNMR-A/B1-76[»]
5YT6X-ray1.50A/C/E/G1-76[»]
5ZBUX-ray3.20E1-76[»]
5ZD0NMR-A153-228[»]
6ASRX-ray2.36A/C153-228[»]
6BVAX-ray2.66A/B76-152[»]
6BYHX-ray2.61C/D/H76-152[»]
6C16X-ray3.27D/H77-152[»]
6CP2X-ray2.90C75-152[»]
6DGFX-ray2.34B1-74[»]
6EI1X-ray1.73B153-227[»]
6FDKX-ray1.60B1-76[»]
6FGEX-ray1.74C153-227[»]
6FTXelectron microscopy4.50N/O1-76[»]
6FX4X-ray2.50B/D1-76[»]
6FYHX-ray2.91B1-76[»]
6GLCX-ray1.80B153-228[»]
6GZSX-ray1.90B1-75[»]
6H4HX-ray3.50C/D1-75[»]
6HEIX-ray1.64B1-75[»]
6HEKX-ray3.03B/D1-76[»]
6IF1X-ray2.47C/D1-76[»]
6ISUX-ray1.87B/C1-76[»]
6JB6X-ray2.70B1-76[»]
6JB7X-ray2.10B1-76[»]
6JMAelectron microscopy6.80Y1-76[»]
6K4INMR-A1-76[»]
6K9PX-ray2.05G1-76[»]
6KOWNMR-A1-76[»]
6KOXNMR-A1-76[»]
6LP2X-ray2.48C1-75[»]
6MSBelectron microscopy3.00u/w1-76[»]
6MSDelectron microscopy3.20u/w1-76[»]
6MSEelectron microscopy3.30u1-76[»]
6MSGelectron microscopy3.50u1-76[»]
6N13NMR-D1-76[»]
6NJ9electron microscopy2.96L/N1-76[»]
6NJGX-ray2.35A1-78[»]
6O96electron microscopy3.50L1-76[»]
6OAMX-ray2.50C/D1-75[»]
6PGVX-ray2.30B1-75[»]
6PZVX-ray3.01A/B/E/F1-76[»]
6QF8NMR-A1-76[»]
6QK9X-ray2.23A/B/C/D/E/F/G/H/I/J/K/L1-74[»]
6QMLX-ray2.10B/E1-76[»]
6TBMelectron microscopy20.00R153-227[»]
6UH5electron microscopy3.50Q1-76[»]
6XAAX-ray2.70B1-76[»]
7AY2X-ray3.20C/F1-75[»]
7BBDX-ray2.20B1-74[»]
7CAPX-ray1.33A/B/C1-76[»]
7JMSX-ray2.78B/D/F/H1-75[»]
7LYCelectron microscopy2.94K1-76[»]
BMRBiP0CG47
SASBDBiP0CG47
SMRiP0CG47
ModBaseiSearch...
PDBe-KBiSearch...

Protein-protein interaction databases

BioGRIDi113162, 255 interactors
IntActiP0CG47, 214 interactors
MINTiP0CG47
STRINGi9606.ENSP00000304697

Chemistry databases

ChEMBLiCHEMBL4523178
DrugBankiDB02542, (4s)-5-Fluoro-L-Leucine

Protein family/group databases

MoonDBiP0CG47, Predicted

PTM databases

GlyGeniP0CG47, 1 site, 1 O-linked glycan (1 site)
iPTMnetiP0CG47
MetOSiteiP0CG47
PhosphoSitePlusiP0CG47
SwissPalmiP0CG47

Genetic variation databases

BioMutaiUBB
DMDMi302595875

Proteomic databases

EPDiP0CG47
jPOSTiP0CG47
MassIVEiP0CG47
PaxDbiP0CG47
PeptideAtlasiP0CG47
PRIDEiP0CG47
ProteomicsDBi52474
TopDownProteomicsiP0CG47

Protocols and materials databases

Antibodypedia a portal for validated antibodies

More...
Antibodypediai
4579, 649 antibodies

The DNASU plasmid repository

More...
DNASUi
7314

Genome annotation databases

EnsembliENST00000302182; ENSP00000304697; ENSG00000170315
ENST00000395837; ENSP00000379178; ENSG00000170315
ENST00000395839; ENSP00000379180; ENSG00000170315
ENST00000614404; ENSP00000478771; ENSG00000170315
GeneIDi7314
KEGGihsa:7314

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
7314
DisGeNETi7314

GeneCards: human genes, protein and diseases

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GeneCardsi
UBB
HGNCiHGNC:12463, UBB
HPAiENSG00000170315, Low tissue specificity
MalaCardsiUBB
MIMi191339, gene
neXtProtiNX_P0CG47
OpenTargetsiENSG00000170315
Orphaneti99771, Bifid uvula
101023, Cleft hard palate
99772, Cleft velum
155878, Submucosal cleft palate
VEuPathDBiHostDB:ENSG00000170315

GenAtlas: human gene database

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GenAtlasi
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Phylogenomic databases

eggNOGiKOG0001, Eukaryota
GeneTreeiENSGT00940000162439
InParanoidiP0CG47
OMAiCKDAAIN
OrthoDBi1536766at2759
PhylomeDBiP0CG47
TreeFamiTF300820

Enzyme and pathway databases

PathwayCommonsiP0CG47
ReactomeiR-HSA-110312, Translesion synthesis by REV1
R-HSA-110314, Recognition of DNA damage by PCNA-containing replication complex
R-HSA-110320, Translesion Synthesis by POLH
R-HSA-1169091, Activation of NF-kappaB in B cells
R-HSA-1169408, ISG15 antiviral mechanism
R-HSA-1234176, Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-HSA-1236382, Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants
R-HSA-1236974, ER-Phagosome pathway
R-HSA-1253288, Downregulation of ERBB4 signaling
R-HSA-1295596, Spry regulation of FGF signaling
R-HSA-1358803, Downregulation of ERBB2:ERBB3 signaling
R-HSA-162588, Budding and maturation of HIV virion
R-HSA-168638, NOD1/2 Signaling Pathway
R-HSA-168927, TICAM1, RIP1-mediated IKK complex recruitment
R-HSA-168928, DDX58/IFIH1-mediated induction of interferon-alpha/beta
R-HSA-174048, APC/C:Cdc20 mediated degradation of Cyclin B
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-174490, Membrane binding and targetting of GAG proteins
R-HSA-175474, Assembly Of The HIV Virion
R-HSA-179409, APC-Cdc20 mediated degradation of Nek2A
R-HSA-180534, Vpu mediated degradation of CD4
R-HSA-180585, Vif-mediated degradation of APOBEC3G
R-HSA-182971, EGFR downregulation
R-HSA-187577, SCF(Skp2)-mediated degradation of p27/p21
R-HSA-195253, Degradation of beta-catenin by the destruction complex
R-HSA-201681, TCF dependent signaling in response to WNT
R-HSA-202424, Downstream TCR signaling
R-HSA-205043, NRIF signals cell death from the nucleus
R-HSA-209543, p75NTR recruits signalling complexes
R-HSA-209560, NF-kB is activated and signals survival
R-HSA-211733, Regulation of activated PAK-2p34 by proteasome mediated degradation
R-HSA-2122947, NOTCH1 Intracellular Domain Regulates Transcription
R-HSA-2122948, Activated NOTCH1 Transmits Signal to the Nucleus
R-HSA-2173788, Downregulation of TGF-beta receptor signaling
R-HSA-2173791, TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-HSA-2173795, Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-HSA-2173796, SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-HSA-2467813, Separation of Sister Chromatids
R-HSA-2559580, Oxidative Stress Induced Senescence
R-HSA-2559582, Senescence-Associated Secretory Phenotype (SASP)
R-HSA-2559585, Oncogene Induced Senescence
R-HSA-2565942, Regulation of PLK1 Activity at G2/M Transition
R-HSA-2644606, Constitutive Signaling by NOTCH1 PEST Domain Mutants
R-HSA-2672351, Stimuli-sensing channels
R-HSA-2691232, Constitutive Signaling by NOTCH1 HD Domain Mutants
R-HSA-2871837, FCERI mediated NF-kB activation
R-HSA-2894862, Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants
R-HSA-2979096, NOTCH2 Activation and Transmission of Signal to the Nucleus
R-HSA-3134975, Regulation of innate immune responses to cytosolic DNA
R-HSA-3322077, Glycogen synthesis
R-HSA-349425, Autodegradation of the E3 ubiquitin ligase COP1
R-HSA-3769402, Deactivation of the beta-catenin transactivating complex
R-HSA-3785653, Myoclonic epilepsy of Lafora
R-HSA-382556, ABC-family proteins mediated transport
R-HSA-400253, Circadian Clock
R-HSA-445989, TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-HSA-450302, activated TAK1 mediates p38 MAPK activation
R-HSA-450321, JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
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-4641263, Regulation of FZD by ubiquitination
R-HSA-5205685, PINK1-PRKN Mediated Mitophagy
R-HSA-532668, N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-HSA-5357905, Regulation of TNFR1 signaling
R-HSA-5357956, TNFR1-induced NFkappaB signaling pathway
R-HSA-5358346, Hedgehog ligand biogenesis
R-HSA-5362768, Hh mutants 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-5654726, Negative regulation of FGFR1 signaling
R-HSA-5654727, Negative regulation of FGFR2 signaling
R-HSA-5654732, Negative regulation of FGFR3 signaling
R-HSA-5654733, Negative regulation of FGFR4 signaling
R-HSA-5655862, Translesion synthesis by POLK
R-HSA-5656121, Translesion synthesis by POLI
R-HSA-5656169, Termination of translesion DNA synthesis
R-HSA-5658442, Regulation of RAS by GAPs
R-HSA-5668541, TNFR2 non-canonical NF-kB pathway
R-HSA-5675221, Negative regulation of MAPK pathway
R-HSA-5675482, Regulation of necroptotic cell death
R-HSA-5676590, NIK-->noncanonical NF-kB signaling
R-HSA-5678895, Defective CFTR causes cystic fibrosis
R-HSA-5684264, MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-HSA-5685942, HDR through Homologous Recombination (HRR)
R-HSA-5687128, MAPK6/MAPK4 signaling
R-HSA-5689603, UCH proteinases
R-HSA-5689877, Josephin domain DUBs
R-HSA-5689880, Ub-specific processing proteases
R-HSA-5689896, Ovarian tumor domain proteases
R-HSA-5689901, Metalloprotease DUBs
R-HSA-5693565, Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-HSA-5693607, Processing of DNA double-strand break ends
R-HSA-5696394, DNA Damage Recognition in GG-NER
R-HSA-5696395, Formation of Incision Complex in GG-NER
R-HSA-5696397, Gap-filling DNA repair synthesis and ligation in GG-NER
R-HSA-5696400, Dual Incision in GG-NER
R-HSA-6781823, Formation of TC-NER Pre-Incision Complex
R-HSA-6781827, Transcription-Coupled Nucleotide Excision Repair (TC-NER)
R-HSA-6782135, Dual incision in TC-NER
R-HSA-6782210, Gap-filling DNA repair synthesis and ligation in TC-NER
R-HSA-6783310, Fanconi Anemia Pathway
R-HSA-6804756, Regulation of TP53 Activity through Phosphorylation
R-HSA-6804757, Regulation of TP53 Degradation
R-HSA-6804760, Regulation of TP53 Activity through Methylation
R-HSA-6807004, Negative regulation of MET activity
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-69231, Cyclin D associated events in G1
R-HSA-69481, G2/M Checkpoints
R-HSA-69541, Stabilization of p53
R-HSA-69601, Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-HSA-75815, Ubiquitin-dependent degradation of Cyclin D
R-HSA-8849469, PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
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-8856825, Cargo recognition for clathrin-mediated endocytosis
R-HSA-8856828, Clathrin-mediated endocytosis
R-HSA-8863795, Downregulation of ERBB2 signaling
R-HSA-8866652, Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-HSA-8866654, E3 ubiquitin ligases ubiquitinate target proteins
R-HSA-8875360, InlB-mediated entry of Listeria monocytogenes into host cell
R-HSA-8876493, InlA-mediated entry of Listeria monocytogenes into host cells
R-HSA-8932339, ROS sensing by NFE2L2
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-8948747, Regulation of PTEN localization
R-HSA-8948751, Regulation of PTEN stability and activity
R-HSA-8951664, Neddylation
R-HSA-901032, ER Quality Control Compartment (ERQC)
R-HSA-9010553, Regulation of expression of SLITs and ROBOs
R-HSA-9013507, NOTCH3 Activation and Transmission of Signal to the Nucleus
R-HSA-9013973, TICAM1-dependent activation of IRF3/IRF7
R-HSA-9014325, TICAM1,TRAF6-dependent induction of TAK1 complex
R-HSA-9020702, Interleukin-1 signaling
R-HSA-9033241, Peroxisomal protein import
R-HSA-912631, Regulation of signaling by CBL
R-HSA-917729, Endosomal Sorting Complex Required For Transport (ESCRT)
R-HSA-917937, Iron uptake and transport
R-HSA-936440, Negative regulators of DDX58/IFIH1 signaling
R-HSA-936964, Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-HSA-937039, IRAK1 recruits IKK complex
R-HSA-937041, IKK complex recruitment mediated by RIP1
R-HSA-937042, IRAK2 mediated activation of TAK1 complex
R-HSA-937072, TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-HSA-9604323, Negative regulation of NOTCH4 signaling
R-HSA-9613829, Chaperone Mediated Autophagy
R-HSA-9615710, Late endosomal microautophagy
R-HSA-9636383, Prevention of phagosomal-lysosomal fusion
R-HSA-9637628, Modulation by Mtb of host immune system
R-HSA-9645460, Alpha-protein kinase 1 signaling pathway
R-HSA-9646399, Aggrephagy
R-HSA-9648002, RAS processing
R-HSA-9664873, Pexophagy
R-HSA-9683683, Maturation of protein E
R-HSA-9694493, Maturation of protein E
R-HSA-9705462, Inactivation of CSF3 (G-CSF) signaling
R-HSA-9706369, Negative regulation of FLT3
R-HSA-9706377, FLT3 signaling by CBL mutants
R-HSA-9708530, Regulation of BACH1 activity
R-HSA-975110, TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling
R-HSA-975144, IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-HSA-975163, IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-HSA-977225, Amyloid fiber formation
R-HSA-983168, Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

BioGRID ORCS database of CRISPR phenotype screens

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BioGRID-ORCSi
7314, 368 hits in 949 CRISPR screens

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

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ChiTaRSi
UBB, human

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Ubiquitin_B

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

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GenomeRNAii
7314
PharosiP0CG47, Tbio

Protein Ontology

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PROi
PR:P0CG47
RNActiP0CG47, protein

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000170315, Expressed in hypothalamus and 248 other tissues
ExpressionAtlasiP0CG47, baseline and differential
GenevisibleiP0CG47, HS

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, 3 hits
PRINTSiPR00348, UBIQUITIN
SMARTiView protein in SMART
SM00213, UBQ, 3 hits
SUPFAMiSSF54236, SSF54236, 3 hits
PROSITEiView protein in PROSITE
PS00299, UBIQUITIN_1, 3 hits
PS50053, UBIQUITIN_2, 3 hits

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 nameiUBB_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: P0CG47
Secondary accession number(s): P02248
, P02249, P02250, P62988, Q29120, Q6LBL4, Q6LDU5, Q8WYN8, Q91887, Q91888, Q9BWD6, Q9BX98, Q9UEF2, Q9UEG1, Q9UEK8, Q9UPK7
<p>This subsection of the 'Entry information' section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification ('Last modified'). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: September 29, 2021
This is version 112 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
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 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with genetic variants
    List of human entries with genetic variants
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families
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