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Protein

Polyubiquitin-C

Gene

UBC

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

Ubiquitin: 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.
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 ‘Function’ 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

  • protease binding Source: UniProtKB
  • protein tag Source: GO_Central
  • RNA binding Source: UniProtKB
  • ubiquitin protein ligase binding Source: GO_Central

GO - Biological processi

Enzyme and pathway databases

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 Pink/Parkin 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 that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-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-69229 Ubiquitin-dependent degradation of Cyclin D1
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-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-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-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

SIGNOR Signaling Network Open Resource

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SIGNORi
P0CG48

Protein family/group databases

MoonDB Database of extreme multifunctional and moonlighting proteins

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MoonDBi
P0CG48 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-C
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:UBC
<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 12

Organism-specific databases

Eukaryotic Pathogen Database Resources

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EuPathDBi
HostDB:ENSG00000150991.14

Human Gene Nomenclature Database

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HGNCi
HGNC:12468 UBC

Online Mendelian Inheritance in Man (OMIM)

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MIMi
191340 gene

neXtProt; the human protein knowledge platform

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neXtProti
NX_P0CG48

<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; 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 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
7316

Open Targets

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OpenTargetsi
ENSG00000150991

Chemistry databases

Drug and drug target database

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DrugBanki
DB04464 N-Formylmethionine

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

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BioMutai
UBC

Domain mapping of disease mutations (DMDM)

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DMDMi
391358178

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003961781 – 76UbiquitinAdd BLAST76
ChainiPRO_000039617977 – 152UbiquitinAdd BLAST76
ChainiPRO_0000396180153 – 228UbiquitinAdd BLAST76
ChainiPRO_0000396181229 – 304UbiquitinAdd BLAST76
ChainiPRO_0000396182305 – 380UbiquitinAdd BLAST76
ChainiPRO_0000396183381 – 456UbiquitinAdd BLAST76
ChainiPRO_0000396184457 – 532UbiquitinAdd BLAST76
ChainiPRO_0000396185533 – 608UbiquitinAdd BLAST76
ChainiPRO_0000396186609 – 684UbiquitinAdd 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_00003961876851

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

Ubiquitin: 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
Ubiquitin: 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
P0CG48

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
P0CG48

MaxQB - The MaxQuant DataBase

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MaxQBi
P0CG48

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

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PaxDbi
P0CG48

PeptideAtlas

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PeptideAtlasi
P0CG48

PRoteomics IDEntifications database

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PRIDEi
P0CG48

ProteomicsDB human proteome resource

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ProteomicsDBi
52475

Consortium for Top Down Proteomics

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TopDownProteomicsi
P0CG48

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

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iPTMneti
P0CG48

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

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PhosphoSitePlusi
P0CG48

SwissPalm database of S-palmitoylation events

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SwissPalmi
P0CG48

<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
ENSG00000150991 Expressed in 239 organ(s), highest expression level in Brodmann (1909) area 46

ExpressionAtlas, Differential and Baseline Expression

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ExpressionAtlasi
P0CG48 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

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Genevisiblei
P0CG48 HS

Organism-specific databases

Human Protein Atlas

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HPAi
CAB000362
CAB005419
HPA041344
HPA049132

<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%27">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="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.<p><a href='/help/binary_interactions' target='_top'>More...</a></p>Binary interactionsi

WithEntry#Exp.IntActNotes
ABCG2Q9UNQ02EBI-3390054,EBI-1569435
ADRM1Q1618610EBI-3390054,EBI-954387
ASAP1Q9ULH12EBI-3390054,EBI-346622
ASAP2O431502EBI-3390054,EBI-310968
ATXN3P54252-12EBI-3390054,EBI-946068
BCL2L12Q9HB09-13EBI-3390054,EBI-6968951
BMI1P352262EBI-3390054,EBI-2341576
BUB1BO605663EBI-3390054,EBI-1001438
CDK1P064936EBI-3390054,EBI-444308
CSF3RQ990622EBI-3390054,EBI-7331284
DAXXQ9UER72EBI-3390054,EBI-77321
DAZAP2Q150384EBI-3390054,EBI-724310
DDI1P400872EBI-3390054,EBI-5717From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
DENRO435833EBI-3390054,EBI-716083
DESI1Q6ICB04EBI-3390054,EBI-2806959
DSK2P485102EBI-3390054,EBI-6174From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
DTX1Q86Y012EBI-3390054,EBI-1755174
ELAVL1Q157174EBI-3390054,EBI-374260
Fzd4Q610883EBI-3390054,EBI-7987880From Mus musculus.
GRK2P250983EBI-3390054,EBI-3904795
IKBKGQ9Y6K94EBI-3390054,EBI-81279
IkbkgO885223EBI-3390054,EBI-998011From Mus musculus.
KLF5Q138872EBI-3390054,EBI-2696013
LCKP062392EBI-3390054,EBI-1348
LEPRP48357-32EBI-3390054,EBI-7886448
MALT1Q9UDY84EBI-3390054,EBI-1047372
MAP3K4Q9Y6R42EBI-3390054,EBI-448104
MAP3K7O433184EBI-3390054,EBI-358684
MARCH5Q9NX472EBI-3390054,EBI-2341610
MDM2Q009876EBI-3390054,EBI-389668
MYCP011065EBI-3390054,EBI-447544
NCK2O436392EBI-3390054,EBI-713635
NFATC4Q149343EBI-3390054,EBI-3905796
NFKBIAP259633EBI-3390054,EBI-307386
PARP1P098742EBI-3390054,EBI-355676
PCGF2P352272EBI-3390054,EBI-2129767
POLHQ9Y2534EBI-3390054,EBI-2827270
POLIQ9UNA44EBI-3390054,EBI-741774
PRKCAP172522EBI-3390054,EBI-1383528
PSMD4P550364EBI-3390054,EBI-359318
RAD23P326282EBI-3390054,EBI-14668From Saccharomyces cerevisiae (strain ATCC 204508 / S288c).
RAD23BP547274EBI-3390054,EBI-954531
RAD23CQ84L312EBI-3390054,EBI-4437395From Arabidopsis thaliana.
Rbck1Q629212EBI-3390054,EBI-7266339From Rattus norvegicus.
RDH12Q96NR82EBI-3390054,EBI-3916363
RELAQ042066EBI-3390054,EBI-73886
revP043252EBI-3390054,EBI-7061954From Human immunodeficiency virus type 1 group M subtype B (isolate PCV12).
RPN10P550342EBI-3390054,EBI-2620423From Arabidopsis thaliana.
RPN13O487269EBI-3390054,EBI-7710745From Arabidopsis thaliana.
RYBPQ8N4883EBI-3390054,EBI-752324
SENP3Q9H4L42EBI-3390054,EBI-2880236
SH3KBP1Q96B976EBI-3390054,EBI-346595
SNX9Q9Y5X12EBI-3390054,EBI-77848
SQSTM1Q135013EBI-3390054,EBI-307104
STAMQ927832EBI-3390054,EBI-752333
TAX1BP1Q86VP17EBI-3390054,EBI-529518
TP53P0463715EBI-3390054,EBI-366083
TRAF6Q9Y4K33EBI-3390054,EBI-359276
Trpv4Q9EPK83EBI-3390054,EBI-7091763From Mus musculus.
XIAPP981703EBI-3390054,EBI-517127
ZFAND5O760803EBI-3390054,EBI-8028844
ZRANB1Q9UGI02EBI-3390054,EBI-527853

GO - Molecular functioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
113164, 1618 interactors

Protein interaction database and analysis system

More...
IntActi
P0CG48, 187 interactors

Molecular INTeraction database

More...
MINTi
P0CG48

STRING: functional protein association networks

More...
STRINGi
9606.ENSP00000344818

<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

1685
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

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PDBei

Protein Data Bank RCSB

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RCSB PDBi

Protein Data Bank Japan

More...
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C3TNMR-A1-76[»]
1CMXX-ray2.25B/D1-76[»]
1D3ZNMR-A1-76[»]
1F9JX-ray2.70A/B1-76[»]
1FXTNMR-B1-76[»]
1G6JNMR-A1-76[»]
1GJZNMR-A/B1-51[»]
1NBFX-ray2.30C/D1-76[»]
1OGWX-ray1.32A1-76[»]
1Q5WNMR-B1-76[»]
1S1QX-ray2.00B/D1-76[»]
1SIFX-ray2.18A6-76[»]
1TBEX-ray2.40A/B1-76[»]
1UBIX-ray1.80A1-76[»]
1UBQX-ray1.80A1-76[»]
1UD7NMR-A1-76[»]
1XD3X-ray1.45B/D1-75[»]
1XQQNMR-A1-76[»]
1YX5NMR-B1-76[»]
1YX6NMR-B1-76[»]
1ZGUNMR-B1-76[»]
1ZO6model-B/C1-76[»]
2AYOX-ray3.50B1-76[»]
2BGFNMR-A/B1-76[»]
2DENNMR-B1-76[»]
2FUHNMR-B1-76[»]
2G45X-ray1.99B/E1-76[»]
2GBJX-ray1.35A/B1-76[»]
2GBKX-ray1.99A/B/C/D10-76[»]
2GBMX-ray1.55A/B/C/D1-76[»]
2GBNX-ray1.60A1-76[»]
2GBRX-ray2.00A/B/C1-76[»]
2GMIX-ray2.50C1-76[»]
2HTHX-ray2.70A1-76[»]
2IBIX-ray2.20B1-75[»]
2J7QX-ray1.80B/D1-75[»]
2JF5X-ray1.95A/B1-76[»]
2JRINMR-B/C1-76[»]
2JY6NMR-A1-76[»]
2JZZNMR-A1-76[»]
2K25NMR-A1-75[»]
2K6DNMR-B1-75[»]
2K8BNMR-A1-76[»]
2K8CNMR-A1-76[»]
2KDFNMR-B/C1-76[»]
2KHWNMR-B1-76[»]
2KJHNMR-B1-75[»]
2KLGNMR-A1-76[»]
2KN5NMR-A1-76[»]
2KX0NMR-A74-151[»]
2L3ZNMR-A1-76[»]
2LD9NMR-A76-152[»]
2LVONMR-A1-76[»]
2LVPNMR-A/B1-76[»]
2LVQNMR-A/B1-76[»]
2LZ6NMR-A609-684[»]
2MBONMR-A/B609-684[»]
2MBQNMR-A/B609-684[»]
2MCNNMR-B609-684[»]
2MI8NMR-A609-684[»]
2MJ5NMR-A609-684[»]
2MORNMR-A609-684[»]
2MRENMR-A609-684[»]
2MWSNMR-A609-684[»]
2N2KNMR-A609-684[»]
B609-679[»]
2NR2NMR-A1-76[»]
2O6VX-ray2.20A/B/C/D/E/F/G/H1-76[»]
2OJRX-ray2.60A1-76[»]
2PE9NMR-A/B1-76[»]
2PEANMR-A/B1-76[»]
2RR9NMR-A/B1-76[»]
2RU6NMR-A609-684[»]
2W9NX-ray2.25A1-152[»]
2WDTX-ray2.30B/D1-75[»]
2XEWX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-76[»]
2Y5BX-ray2.70B/F1-152[»]
2Z59NMR-B1-76[»]
2ZCBX-ray1.60A/B/C1-76[»]
2ZVNX-ray3.00A/C/E/G1-152[»]
2ZVOX-ray2.90A/G1-152[»]
3A33X-ray2.20B1-76[»]
3ALBX-ray1.85A/B/C/D1-76[»]
3AULX-ray2.39A/B1-76[»]
3B08X-ray1.70A/D/G/J1-152[»]
3B0AX-ray1.90A/D1-152[»]
3BY4X-ray1.55B1-75[»]
3C0RX-ray2.31B/D1-75[»]
3DVGX-ray2.60X/Y1-76[»]
3DVNX-ray2.70U/V/X/Y1-76[»]
3EECX-ray3.00A/B1-76[»]
3EFUX-ray1.84A1-76[»]
3EHVX-ray1.81A/B/C1-76[»]
3H7PX-ray1.90A/B1-76[»]
3H7SX-ray2.30A/B1-76[»]
3HM3X-ray1.96A/B/C/D1-76[»]
3I3TX-ray2.59B/D/F/H1-75[»]
3IFWX-ray2.40B1-75[»]
3IHPX-ray2.80C/D1-75[»]
3JSVX-ray2.70A/B1-76[»]
3JVZX-ray3.30X/Y1-76[»]
3JW0X-ray3.10X/Y1-76[»]
3K9OX-ray1.80B76-151[»]
3K9PX-ray2.80B1-76[»]
3KVFX-ray2.80B1-75[»]
3KW5X-ray2.83B1-75[»]
3LDZX-ray2.60E/F/G1-73[»]
3MHSX-ray1.89D1-76[»]
3MTNX-ray2.70B/D1-76[»]
3N30X-ray3.00A/B1-76[»]
3N32X-ray1.80A1-76[»]
3N3KX-ray2.60B5-76[»]
3NS8X-ray1.71A/B1-76[»]
3O65X-ray2.70B/D/F/H1-75[»]
3OFIX-ray2.35C/D1-76[»]
3OJ3X-ray2.50A/B/C/D/E/F/G/H1-76[»]
3OJ4X-ray3.40B/E1-76[»]
3ONSX-ray1.80A1-72[»]
3PRMX-ray2.30B/D1-75[»]
3PT2X-ray2.50B1-75[»]
3PTFX-ray2.70C/D1-76[»]
3Q3FX-ray2.17A2-76[»]
3RULX-ray2.50A/B/C/D1-75[»]
3TMPX-ray1.91B/D/F/H1-76[»]
3U30X-ray2.43A/D1-152[»]
3UGBX-ray2.35B1-76[»]
3V6CX-ray1.70B74-150[»]
3V6EX-ray2.10B74-150[»]
3VFKX-ray2.80A1-75[»]
3VUWX-ray1.95A/B/C1-76[»]
3VUXX-ray1.70A/B/C1-76[»]
3VUYX-ray1.98A/B/C1-76[»]
3WXEX-ray2.50B533-680[»]
3WXFX-ray2.30B/D533-680[»]
3ZLZX-ray2.90A/B1-76[»]
3ZNHX-ray2.30B1-75[»]
3ZNIX-ray2.21D/H/L/P1-76[»]
3ZNZX-ray1.90B1-152[»]
4AP4X-ray2.21C/F608-684[»]
4AUQX-ray2.18C/F1-76[»]
4BOSX-ray2.35C/E609-684[»]
F612-625[»]
4BOZX-ray3.03B/C/E1-76[»]
4BVUX-ray2.70C609-684[»]
4DDGX-ray3.30D/E/F/G/H/I/M/N/O/P/Q/R1-76[»]
4DDIX-ray3.80G/H/I/J/K/L1-76[»]
4DHJX-ray2.35B/F/J/M1-76[»]
D/H1-75[»]
4DHZX-ray3.11B1-76[»]
E1-75[»]
4FJVX-ray2.05B/D1-76[»]
4HK2X-ray1.40A/B/C/D1-76[»]
4HXDX-ray2.85A/C1-75[»]
4I6LX-ray2.49B77-150[»]
4I6NX-ray1.70B/D1-75[»]
4IG7X-ray2.00B1-75[»]
4IUMX-ray1.45B1-75[»]
4JQWX-ray2.90C609-684[»]
4K1RX-ray1.63B/D607-684[»]
4K7SX-ray1.76A/B/C1-76[»]
4K7UX-ray1.76A/B/C1-76[»]
4K7WX-ray1.76A/B/C1-76[»]
4KSKX-ray2.40C/D76-152[»]
4KSLX-ray2.83C/D/F/H/J/L/N/P/R/T/V/X76-228[»]
4LCDX-ray3.10E/F609-683[»]
4LDTX-ray1.90B/D609-684[»]
4MDKX-ray2.61E/F/G/H608-684[»]
4MM3X-ray2.75A609-684[»]
4MSMX-ray1.74B/D609-684[»]
4MSQX-ray1.95B/D609-684[»]
4NQKX-ray3.70E/F/G/H/I/J608-684[»]
4UN2X-ray1.51A609-684[»]
4V3KX-ray2.04B/E609-684[»]
4V3LX-ray1.53B/D609-684[»]
4WZPX-ray1.90A/B/C/D/E/F/G/H153-228[»]
4XOKX-ray2.20A/B/C1-76[»]
4XOLX-ray2.91A/B1-76[»]
4ZQSX-ray1.80A/B533-684[»]
5A5Belectron microscopy9.509609-684[»]
5AF4X-ray1.85A/B/C/D/E/F/G/H1-76[»]
5AF5X-ray1.68A1-73[»]
5AF6X-ray3.40A/B/C/D/E1-76[»]
5AITX-ray3.40C/F609-684[»]
5AIUX-ray2.21C/F609-684[»]
5B83X-ray2.69A/D1-304[»]
5C7JX-ray3.00C/D1-74[»]
5C7MX-ray3.03B/C1-75[»]
5E6JX-ray2.85B/E609-683[»]
5H07X-ray2.59A1-228[»]
5NL4X-ray1.32A/B/C1-76[»]
5NLFX-ray1.50A/B/C1-76[»]
5NLIX-ray1.53A/B/C1-76[»]
5NMCX-ray1.70A/B/C1-76[»]
5OE7X-ray2.95B1-146[»]
5OHVX-ray2.80A/C1-76[»]
5OXHX-ray1.60A1-76[»]
5OXIX-ray1.63A/B1-76[»]
5UDHX-ray3.24E1-76[»]
5WQ4X-ray3.00A/B1-152[»]
5ZQ3X-ray2.18C/D609-684[»]
5ZQ4X-ray2.22C/D609-684[»]
5ZQ5X-ray2.49B/D609-684[»]
5ZQ6X-ray3.01B/D609-684[»]
5ZQ7X-ray2.85B/D609-684[»]
6A43X-ray2.40A1-76[»]
6A44X-ray2.40A1-76[»]
6AQRX-ray2.10D609-684[»]
6B7MX-ray1.70B/C609-684[»]
6B7OX-ray1.85B/C609-684[»]
6EQIX-ray3.10A1-76[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...
ProteinModelPortali
P0CG48

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

More...
SMRi
P0CG48

Database of comparative protein structure models

More...
ModBasei
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...
EvolutionaryTracei
P0CG48

<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
Domaini229 – 304Ubiquitin-like 4PROSITE-ProRule annotationAdd BLAST76
Domaini305 – 380Ubiquitin-like 5PROSITE-ProRule annotationAdd BLAST76
Domaini381 – 456Ubiquitin-like 6PROSITE-ProRule annotationAdd BLAST76
Domaini457 – 532Ubiquitin-like 7PROSITE-ProRule annotationAdd BLAST76
Domaini533 – 608Ubiquitin-like 8PROSITE-ProRule annotationAdd BLAST76
Domaini609 – 684Ubiquitin-like 9PROSITE-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

More...
eggNOGi
KOG0001 Eukaryota
COG5272 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000163900

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
P0CG48

KEGG Orthology (KO)

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KOi
K08770

Identification of Orthologs from Complete Genome Data

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OMAi
MASEMQI

Database of Orthologous Groups

More...
OrthoDBi
1536766at2759

TreeFam database of animal gene trees

More...
TreeFami
TF354256

Family and domain databases

Integrated resource of protein families, domains and functional sites

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

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00240 ubiquitin, 9 hits

Protein Motif fingerprint database; a protein domain database

More...
PRINTSi
PR00348 UBIQUITIN

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00213 UBQ, 9 hits

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF54236 SSF54236, 9 hits

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00299 UBIQUITIN_1, 9 hits
PS50053 UBIQUITIN_2, 9 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>.<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 10 potential isoforms that are computationally mapped.Show allAlign All

P0CG48-1 [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
310 320 330 340 350
LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA
360 370 380 390 400
GKQLEDGRTL SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS
410 420 430 440 450
DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV
460 470 480 490 500
LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
510 520 530 540 550
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE
560 570 580 590 600
PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
610 620 630 640 650
LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR
660 670 680
LIFAGKQLED GRTLSDYNIQ KESTLHLVLR LRGGV
Length:685
Mass (Da):77,039
Last modified:June 13, 2012 - v3
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iB6E7BC06FEE77196
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 10 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
Q96C32Q96C32_HUMAN
Polyubiquitin-C
UBC
305Annotation 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>
Q5PY61Q5PY61_HUMAN
Polyubiquitin-C
UBC
229Annotation 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>
F5H265F5H265_HUMAN
Polyubiquitin-C
UBC
149Annotation 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>
F5GZ39F5GZ39_HUMAN
Polyubiquitin-C
UBC
61Annotation 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>
F5GYU3F5GYU3_HUMAN
Polyubiquitin-C
UBC
134Annotation 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>
F5H388F5H388_HUMAN
Polyubiquitin-C
UBC
155Annotation 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>
F5H2Z3F5H2Z3_HUMAN
Polyubiquitin-C
UBC
136Annotation 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>
F5H6Q2F5H6Q2_HUMAN
Polyubiquitin-C
UBC
122Annotation 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>
F5GXK7F5GXK7_HUMAN
Polyubiquitin-C
UBC
169Annotation 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>
F5H747F5H747_HUMAN
Polyubiquitin-C
UBC
160Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti190P → S in AC126309 (PubMed:16541075).Curated1
Sequence conflicti397V → G in BAA09860 (PubMed:8917096).Curated1

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
M26880 mRNA Translation: AAA36789.1
AB009010 mRNA Translation: BAA23632.1
AB089613 Genomic DNA Translation: BAC56951.1
AC126309 Genomic DNA No translation available.
BC039193 mRNA Translation: AAH39193.1
D63791 Genomic DNA Translation: BAA09860.1
AB003730 Genomic DNA Translation: BAA23486.1
M17597 mRNA Translation: AAA36787.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS9260.1

Protein sequence database of the Protein Information Resource

More...
PIRi
A02574 UQHU
A22005 UQHUC
A29526

NCBI Reference Sequences

More...
RefSeqi
NP_066289.3, NM_021009.6

UniGene gene-oriented nucleotide sequence clusters

More...
UniGenei
Hs.520348
Hs.707528
Hs.731841

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENST00000339647; ENSP00000344818; ENSG00000150991
ENST00000536769; ENSP00000441543; ENSG00000150991

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
7316

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
hsa:7316

UCSC genome browser

More...
UCSCi
uc001ugs.5 human

<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
M26880 mRNA Translation: AAA36789.1
AB009010 mRNA Translation: BAA23632.1
AB089613 Genomic DNA Translation: BAC56951.1
AC126309 Genomic DNA No translation available.
BC039193 mRNA Translation: AAH39193.1
D63791 Genomic DNA Translation: BAA09860.1
AB003730 Genomic DNA Translation: BAA23486.1
M17597 mRNA Translation: AAA36787.1
CCDSiCCDS9260.1
PIRiA02574 UQHU
A22005 UQHUC
A29526
RefSeqiNP_066289.3, NM_021009.6
UniGeneiHs.520348
Hs.707528
Hs.731841

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1C3TNMR-A1-76[»]
1CMXX-ray2.25B/D1-76[»]
1D3ZNMR-A1-76[»]
1F9JX-ray2.70A/B1-76[»]
1FXTNMR-B1-76[»]
1G6JNMR-A1-76[»]
1GJZNMR-A/B1-51[»]
1NBFX-ray2.30C/D1-76[»]
1OGWX-ray1.32A1-76[»]
1Q5WNMR-B1-76[»]
1S1QX-ray2.00B/D1-76[»]
1SIFX-ray2.18A6-76[»]
1TBEX-ray2.40A/B1-76[»]
1UBIX-ray1.80A1-76[»]
1UBQX-ray1.80A1-76[»]
1UD7NMR-A1-76[»]
1XD3X-ray1.45B/D1-75[»]
1XQQNMR-A1-76[»]
1YX5NMR-B1-76[»]
1YX6NMR-B1-76[»]
1ZGUNMR-B1-76[»]
1ZO6model-B/C1-76[»]
2AYOX-ray3.50B1-76[»]
2BGFNMR-A/B1-76[»]
2DENNMR-B1-76[»]
2FUHNMR-B1-76[»]
2G45X-ray1.99B/E1-76[»]
2GBJX-ray1.35A/B1-76[»]
2GBKX-ray1.99A/B/C/D10-76[»]
2GBMX-ray1.55A/B/C/D1-76[»]
2GBNX-ray1.60A1-76[»]
2GBRX-ray2.00A/B/C1-76[»]
2GMIX-ray2.50C1-76[»]
2HTHX-ray2.70A1-76[»]
2IBIX-ray2.20B1-75[»]
2J7QX-ray1.80B/D1-75[»]
2JF5X-ray1.95A/B1-76[»]
2JRINMR-B/C1-76[»]
2JY6NMR-A1-76[»]
2JZZNMR-A1-76[»]
2K25NMR-A1-75[»]
2K6DNMR-B1-75[»]
2K8BNMR-A1-76[»]
2K8CNMR-A1-76[»]
2KDFNMR-B/C1-76[»]
2KHWNMR-B1-76[»]
2KJHNMR-B1-75[»]
2KLGNMR-A1-76[»]
2KN5NMR-A1-76[»]
2KX0NMR-A74-151[»]
2L3ZNMR-A1-76[»]
2LD9NMR-A76-152[»]
2LVONMR-A1-76[»]
2LVPNMR-A/B1-76[»]
2LVQNMR-A/B1-76[»]
2LZ6NMR-A609-684[»]
2MBONMR-A/B609-684[»]
2MBQNMR-A/B609-684[»]
2MCNNMR-B609-684[»]
2MI8NMR-A609-684[»]
2MJ5NMR-A609-684[»]
2MORNMR-A609-684[»]
2MRENMR-A609-684[»]
2MWSNMR-A609-684[»]
2N2KNMR-A609-684[»]
B609-679[»]
2NR2NMR-A1-76[»]
2O6VX-ray2.20A/B/C/D/E/F/G/H1-76[»]
2OJRX-ray2.60A1-76[»]
2PE9NMR-A/B1-76[»]
2PEANMR-A/B1-76[»]
2RR9NMR-A/B1-76[»]
2RU6NMR-A609-684[»]
2W9NX-ray2.25A1-152[»]
2WDTX-ray2.30B/D1-75[»]
2XEWX-ray2.20A/B/C/D/E/F/G/H/I/J/K/L1-76[»]
2Y5BX-ray2.70B/F1-152[»]
2Z59NMR-B1-76[»]
2ZCBX-ray1.60A/B/C1-76[»]
2ZVNX-ray3.00A/C/E/G1-152[»]
2ZVOX-ray2.90A/G1-152[»]
3A33X-ray2.20B1-76[»]
3ALBX-ray1.85A/B/C/D1-76[»]
3AULX-ray2.39A/B1-76[»]
3B08X-ray1.70A/D/G/J1-152[»]
3B0AX-ray1.90A/D1-152[»]
3BY4X-ray1.55B1-75[»]
3C0RX-ray2.31B/D1-75[»]
3DVGX-ray2.60X/Y1-76[»]
3DVNX-ray2.70U/V/X/Y1-76[»]
3EECX-ray3.00A/B1-76[»]
3EFUX-ray1.84A1-76[»]
3EHVX-ray1.81A/B/C1-76[»]
3H7PX-ray1.90A/B1-76[»]
3H7SX-ray2.30A/B1-76[»]
3HM3X-ray1.96A/B/C/D1-76[»]
3I3TX-ray2.59B/D/F/H1-75[»]
3IFWX-ray2.40B1-75[»]
3IHPX-ray2.80C/D1-75[»]
3JSVX-ray2.70A/B1-76[»]
3JVZX-ray3.30X/Y1-76[»]
3JW0X-ray3.10X/Y1-76[»]
3K9OX-ray1.80B76-151[»]
3K9PX-ray2.80B1-76[»]
3KVFX-ray2.80B1-75[»]
3KW5X-ray2.83B1-75[»]
3LDZX-ray2.60E/F/G1-73[»]
3MHSX-ray1.89D1-76[»]
3MTNX-ray2.70B/D1-76[»]
3N30X-ray3.00A/B1-76[»]
3N32X-ray1.80A1-76[»]
3N3KX-ray2.60B5-76[»]
3NS8X-ray1.71A/B1-76[»]
3O65X-ray2.70B/D/F/H1-75[»]
3OFIX-ray2.35C/D1-76[»]
3OJ3X-ray2.50A/B/C/D/E/F/G/H1-76[»]
3OJ4X-ray3.40B/E1-76[»]
3ONSX-ray1.80A1-72[»]
3PRMX-ray2.30B/D1-75[»]
3PT2X-ray2.50B1-75[»]
3PTFX-ray2.70C/D1-76[»]
3Q3FX-ray2.17A2-76[»]
3RULX-ray2.50A/B/C/D1-75[»]
3TMPX-ray1.91B/D/F/H1-76[»]
3U30X-ray2.43A/D1-152[»]
3UGBX-ray2.35B1-76[»]
3V6CX-ray1.70B74-150[»]
3V6EX-ray2.10B74-150[»]
3VFKX-ray2.80A1-75[»]
3VUWX-ray1.95A/B/C1-76[»]
3VUXX-ray1.70A/B/C1-76[»]
3VUYX-ray1.98A/B/C1-76[»]
3WXEX-ray2.50B533-680[»]
3WXFX-ray2.30B/D533-680[»]
3ZLZX-ray2.90A/B1-76[»]
3ZNHX-ray2.30B1-75[»]
3ZNIX-ray2.21D/H/L/P1-76[»]
3ZNZX-ray1.90B1-152[»]
4AP4X-ray2.21C/F608-684[»]
4AUQX-ray2.18C/F1-76[»]
4BOSX-ray2.35C/E609-684[»]
F612-625[»]
4BOZX-ray3.03B/C/E1-76[»]
4BVUX-ray2.70C609-684[»]
4DDGX-ray3.30D/E/F/G/H/I/M/N/O/P/Q/R1-76[»]
4DDIX-ray3.80G/H/I/J/K/L1-76[»]
4DHJX-ray2.35B/F/J/M1-76[»]
D/H1-75[»]
4DHZX-ray3.11B1-76[»]
E1-75[»]
4FJVX-ray2.05B/D1-76[»]
4HK2X-ray1.40A/B/C/D1-76[»]
4HXDX-ray2.85A/C1-75[»]
4I6LX-ray2.49B77-150[»]
4I6NX-ray1.70B/D1-75[»]
4IG7X-ray2.00B1-75[»]
4IUMX-ray1.45B1-75[»]
4JQWX-ray2.90C609-684[»]
4K1RX-ray1.63B/D607-684[»]
4K7SX-ray1.76A/B/C1-76[»]
4K7UX-ray1.76A/B/C1-76[»]
4K7WX-ray1.76A/B/C1-76[»]
4KSKX-ray2.40C/D76-152[»]
4KSLX-ray2.83C/D/F/H/J/L/N/P/R/T/V/X76-228[»]
4LCDX-ray3.10E/F609-683[»]
4LDTX-ray1.90B/D609-684[»]
4MDKX-ray2.61E/F/G/H608-684[»]
4MM3X-ray2.75A609-684[»]
4MSMX-ray1.74B/D609-684[»]
4MSQX-ray1.95B/D609-684[»]
4NQKX-ray3.70E/F/G/H/I/J608-684[»]
4UN2X-ray1.51A609-684[»]
4V3KX-ray2.04B/E609-684[»]
4V3LX-ray1.53B/D609-684[»]
4WZPX-ray1.90A/B/C/D/E/F/G/H153-228[»]
4XOKX-ray2.20A/B/C1-76[»]
4XOLX-ray2.91A/B1-76[»]
4ZQSX-ray1.80A/B533-684[»]
5A5Belectron microscopy9.509609-684[»]
5AF4X-ray1.85A/B/C/D/E/F/G/H1-76[»]
5AF5X-ray1.68A1-73[»]
5AF6X-ray3.40A/B/C/D/E1-76[»]
5AITX-ray3.40C/F609-684[»]
5AIUX-ray2.21C/F609-684[»]
5B83X-ray2.69A/D1-304[»]
5C7JX-ray3.00C/D1-74[»]
5C7MX-ray3.03B/C1-75[»]
5E6JX-ray2.85B/E609-683[»]
5H07X-ray2.59A1-228[»]
5NL4X-ray1.32A/B/C1-76[»]
5NLFX-ray1.50A/B/C1-76[»]
5NLIX-ray1.53A/B/C1-76[»]
5NMCX-ray1.70A/B/C1-76[»]
5OE7X-ray2.95B1-146[»]
5OHVX-ray2.80A/C1-76[»]
5OXHX-ray1.60A1-76[»]
5OXIX-ray1.63A/B1-76[»]
5UDHX-ray3.24E1-76[»]
5WQ4X-ray3.00A/B1-152[»]
5ZQ3X-ray2.18C/D609-684[»]
5ZQ4X-ray2.22C/D609-684[»]
5ZQ5X-ray2.49B/D609-684[»]
5ZQ6X-ray3.01B/D609-684[»]
5ZQ7X-ray2.85B/D609-684[»]
6A43X-ray2.40A1-76[»]
6A44X-ray2.40A1-76[»]
6AQRX-ray2.10D609-684[»]
6B7MX-ray1.70B/C609-684[»]
6B7OX-ray1.85B/C609-684[»]
6EQIX-ray3.10A1-76[»]
ProteinModelPortaliP0CG48
SMRiP0CG48
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113164, 1618 interactors
IntActiP0CG48, 187 interactors
MINTiP0CG48
STRINGi9606.ENSP00000344818

Chemistry databases

DrugBankiDB04464 N-Formylmethionine

Protein family/group databases

MoonDBiP0CG48 Predicted

PTM databases

iPTMnetiP0CG48
PhosphoSitePlusiP0CG48
SwissPalmiP0CG48

Polymorphism and mutation databases

BioMutaiUBC
DMDMi391358178

Proteomic databases

EPDiP0CG48
jPOSTiP0CG48
MaxQBiP0CG48
PaxDbiP0CG48
PeptideAtlasiP0CG48
PRIDEiP0CG48
ProteomicsDBi52475
TopDownProteomicsiP0CG48

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000339647; ENSP00000344818; ENSG00000150991
ENST00000536769; ENSP00000441543; ENSG00000150991
GeneIDi7316
KEGGihsa:7316
UCSCiuc001ugs.5 human

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
7316
DisGeNETi7316
EuPathDBiHostDB:ENSG00000150991.14

GeneCards: human genes, protein and diseases

More...
GeneCardsi
UBC
HGNCiHGNC:12468 UBC
HPAiCAB000362
CAB005419
HPA041344
HPA049132
MIMi191340 gene
neXtProtiNX_P0CG48
OpenTargetsiENSG00000150991

GenAtlas: human gene database

More...
GenAtlasi
Search...

Phylogenomic databases

eggNOGiKOG0001 Eukaryota
COG5272 LUCA
GeneTreeiENSGT00940000163900
InParanoidiP0CG48
KOiK08770
OMAiMASEMQI
OrthoDBi1536766at2759
TreeFamiTF354256

Enzyme and pathway databases

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 Pink/Parkin 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 that don't undergo autocatalytic processing are degraded by ERAD
R-HSA-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-HSA-5607764 CLEC7A (Dectin-1) signaling
R-HSA-5610780 Degradation of GLI1 by the proteasome
R-HSA-5610783 Degradation of GLI2 by the proteasome
R-HSA-5610785 GLI3 is processed to GLI3R by the proteasome
R-HSA-5632684 Hedgehog 'on' state
R-HSA-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-69229 Ubiquitin-dependent degradation of Cyclin D1
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-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-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-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
SIGNORiP0CG48

Miscellaneous databases

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

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ChiTaRSi
UBC human
EvolutionaryTraceiP0CG48

The Gene Wiki collection of pages on human genes and proteins

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GeneWikii
Ubiquitin_C

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

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GenomeRNAii
7316

Protein Ontology

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PROi
PR:P0CG48

The Stanford Online Universal Resource for Clones and ESTs

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SOURCEi
Search...

Gene expression databases

BgeeiENSG00000150991 Expressed in 239 organ(s), highest expression level in Brodmann (1909) area 46
ExpressionAtlasiP0CG48 baseline and differential
GenevisibleiP0CG48 HS

Family and domain databases

InterProiView protein in InterPro
IPR019956 Ubiquitin
IPR029071 Ubiquitin-like_domsf
IPR019954 Ubiquitin_CS
IPR000626 Ubiquitin_dom
PfamiView protein in Pfam
PF00240 ubiquitin, 9 hits
PRINTSiPR00348 UBIQUITIN
SMARTiView protein in SMART
SM00213 UBQ, 9 hits
SUPFAMiSSF54236 SSF54236, 9 hits
PROSITEiView protein in PROSITE
PS00299 UBIQUITIN_1, 9 hits
PS50053 UBIQUITIN_2, 9 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
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 nameiUBC_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: P0CG48
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: June 13, 2012
Last modified: January 16, 2019
This is version 97 of the entry and version 3 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  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
UniProt is an ELIXIR core data resource
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