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UniProtKB - P0CG50 (UBC_MOUSE)

Entry version 85 (18 Sep 2019)
Sequence version 2 (27 Jul 2011)
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Protein

Polyubiquitin-C

Gene

Ubc

Organism
Mus musculus (Mouse)
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.1 Publication

Miscellaneous

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

Sites

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

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

Complete GO annotation on QuickGO ...

GO - Biological processi

Complete GO annotation on QuickGO ...

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-MMU-110312 Translesion synthesis by REV1
R-MMU-110314 Recognition of DNA damage by PCNA-containing replication complex
R-MMU-110320 Translesion Synthesis by POLH
R-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1253288 Downregulation of ERBB4 signaling
R-MMU-1295596 Spry regulation of FGF signaling
R-MMU-1358803 Downregulation of ERBB2:ERBB3 signaling
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-MMU-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174154 APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-182971 EGFR downregulation
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-201681 TCF dependent signaling in response to WNT
R-MMU-202424 Downstream TCR signaling
R-MMU-205043 NRIF signals cell death from the nucleus
R-MMU-209543 p75NTR recruits signalling complexes
R-MMU-209560 NF-kB is activated and signals survival
R-MMU-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-MMU-2173788 Downregulation of TGF-beta receptor signaling
R-MMU-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-MMU-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-MMU-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-2559585 Oncogene Induced Senescence
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-2672351 Stimuli-sensing channels
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-3134975 Regulation of innate immune responses to cytosolic DNA
R-MMU-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-3769402 Deactivation of the beta-catenin transactivating complex
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-MMU-4608870 Asymmetric localization of PCP proteins
R-MMU-4641257 Degradation of AXIN
R-MMU-4641258 Degradation of DVL
R-MMU-4641263 Regulation of FZD by ubiquitination
R-MMU-5205685 Pink/Parkin Mediated Mitophagy
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-5357905 Regulation of TNFR1 signaling
R-MMU-5357956 TNFR1-induced NFkappaB signaling pathway
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome
R-MMU-5632684 Hedgehog 'on' state
R-MMU-5654726 Negative regulation of FGFR1 signaling
R-MMU-5654727 Negative regulation of FGFR2 signaling
R-MMU-5654732 Negative regulation of FGFR3 signaling
R-MMU-5654733 Negative regulation of FGFR4 signaling
R-MMU-5655862 Translesion synthesis by POLK
R-MMU-5656121 Translesion synthesis by POLI
R-MMU-5656169 Termination of translesion DNA synthesis
R-MMU-5658442 Regulation of RAS by GAPs
R-MMU-5668541 TNFR2 non-canonical NF-kB pathway
R-MMU-5675221 Negative regulation of MAPK pathway
R-MMU-5675482 Regulation of necroptotic cell death
R-MMU-5676590 NIK-->noncanonical NF-kB signaling
R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-5685942 HDR through Homologous Recombination (HRR)
R-MMU-5687128 MAPK6/MAPK4 signaling
R-MMU-5689603 UCH proteinases
R-MMU-5689877 Josephin domain DUBs
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-5689901 Metalloprotease DUBs
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-MMU-5696400 Dual Incision in GG-NER
R-MMU-6781823 Formation of TC-NER Pre-Incision Complex
R-MMU-6782135 Dual incision in TC-NER
R-MMU-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-6783310 Fanconi Anemia Pathway
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-6804760 Regulation of TP53 Activity through Methylation
R-MMU-6807004 Negative regulation of MET activity
R-MMU-68827 CDT1 association with the CDC6:ORC:origin complex
R-MMU-68949 Orc1 removal from chromatin
R-MMU-69017 CDK-mediated phosphorylation and removal of Cdc6
R-MMU-69231 Cyclin D associated events in G1
R-MMU-69481 G2/M Checkpoints
R-MMU-69541 Stabilization of p53
R-MMU-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-75815 Ubiquitin-dependent degradation of Cyclin D
R-MMU-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8863795 Downregulation of ERBB2 signaling
R-MMU-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-MMU-8866654 E3 ubiquitin ligases ubiquitinate target proteins
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8941858 Regulation of RUNX3 expression and activity
R-MMU-8948747 Regulation of PTEN localization
R-MMU-8948751 Regulation of PTEN stability and activity
R-MMU-8951664 Neddylation
R-MMU-901032 ER Quality Control Compartment (ERQC)
R-MMU-9010553 Regulation of expression of SLITs and ROBOs
R-MMU-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
R-MMU-9020702 Interleukin-1 signaling
R-MMU-9033241 Peroxisomal protein import
R-MMU-912631 Regulation of signaling by CBL
R-MMU-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-MMU-917937 Iron uptake and transport
R-MMU-936440 Negative regulators of DDX58/IFIH1 signaling
R-MMU-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-MMU-937041 IKK complex recruitment mediated by RIP1
R-MMU-937042 IRAK2 mediated activation of TAK1 complex
R-MMU-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-MMU-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

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

<p>This subsection of the <a href="http://www.uniprot.org/help/names_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 3 chains:
Ubiquitin
Ubiquitin-related 1
Ubiquitin-related 2
<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>OrganismiMus musculus (Mouse)
<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 identifieri10090 [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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Mus › Mus
<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
  • UP000000589 <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 5

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...MGIi		MGI:98889 Ubc

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywords - Cellular componenti

Cytoplasm, Nucleus

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

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00003961921 – 76UbiquitinAdd BLAST76
ChainiPRO_000039619377 – 152UbiquitinAdd BLAST76
ChainiPRO_0000396194153 – 228UbiquitinAdd BLAST76
ChainiPRO_0000396195229 – 304Ubiquitin-related 1Add BLAST76
ChainiPRO_0000396196305 – 380UbiquitinAdd BLAST76
ChainiPRO_0000396197381 – 456UbiquitinAdd BLAST76
ChainiPRO_0000396198457 – 532UbiquitinAdd BLAST76
ChainiPRO_0000396199533 – 608UbiquitinAdd BLAST76
ChainiPRO_0000396200609 – 684UbiquitinAdd BLAST76
ChainiPRO_0000396201685 – 734Ubiquitin-related 2Add BLAST50

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-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei65Phosphoserine; by PINK1By similarity1
Modified residuei76ADP-ribosylglycineBy similarity1
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation
Cross-linki82Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki87Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki103Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki105Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki124Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki139Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei141PhosphoserineBy similarity1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_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. Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30.By similarity
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.By similarity

Keywords - PTMi

ADP-ribosylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P0CG50

MaxQB - The MaxQuant DataBase

More...MaxQBi		P0CG50

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

More...PaxDbi		P0CG50

PRoteomics IDEntifications database

More...PRIDEi		P0CG50

2D gel databases

REPRODUCTION-2DPAGE

More...REPRODUCTION-2DPAGEi		P62991

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P0CG50

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

More...PhosphoSitePlusi		P0CG50

SwissPalm database of S-palmitoylation events

More...SwissPalmi		P0CG50

<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

More...Bgeei		ENSMUSG00000008348 Expressed in 302 organ(s), highest expression level in hypothalamus

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P0CG50 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P0CG50 MM

<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

GO - Molecular functioni

Complete GO annotation on QuickGO ...

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		204403, 459 interactors

Protein interaction database and analysis system

More...IntActi		P0CG50, 2 interactors

STRING: functional protein association networks

More...STRINGi		10090.ENSMUSP00000115578

<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

1734
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

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

More...SMRi		P0CG50

Database of comparative protein structure models

More...ModBasei		Search...

Miscellaneous databases

Relative evolutionary importance of amino acids within a protein sequence

More...EvolutionaryTracei		P0CG50

<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		P0CG50

KEGG Orthology (KO)

More...KOi		K08770

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, 10 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>. 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 1 potential isoform that is computationally mapped.Show allAlign All

P0CG50-1 [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        690        700
LIFAGKQLED GRTLSDYNIQ KESTLHLVLR LRGGMQIFVK TLTGKTITLD 
       710        720        730 
VEPSVTTKKV KQEDRRTFLT TVSKKSPPCA CSWV
Length:734
Mass (Da):82,550
Last modified:July 27, 2011 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iEDD9B8556FF81D5B
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
E9Q5F6E9Q5F6_MOUSE
Polyubiquitin-C
Ubc
201Annotation 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 conflicti75G → GGMQIFVKTLTGKTITLEVE PSDTIENVKAKIQDKEGIPP DQQRLIFAGKQLEDGRTLSD YNIQKESTLHLVLRLRGGMQ IFVKTLTGKTITLEVEPSDT IENVKAKIQDKEGIPPDQQR LIFAGKQLEGGRTLSDYNIQ KESTLHLVLRLRG in AAG00513 (PubMed:12107596).Curated1
Sequence conflicti265P → S in AAG00512 (PubMed:12107596).Curated1
Sequence conflicti265P → S in AAG00513 (PubMed:12107596).Curated1

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
AF285161 Genomic DNA Translation: AAG00512.1
AF285162 Genomic DNA Translation: AAG00513.1
AC138613 Genomic DNA No translation available.
D50527 mRNA Translation: BAA09096.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS19684.2

Protein sequence database of the Protein Information Resource

More...PIRi		A49007
S11296

NCBI Reference Sequences

More...RefSeqi		NP_062613.3, NM_019639.4

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENSMUST00000136312; ENSMUSP00000114180; ENSMUSG00000008348
ENSMUST00000156249; ENSMUSP00000115578; ENSMUSG00000008348

Database of genes from NCBI RefSeq genomes

More...GeneIDi		22190

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		mmu:22190

UCSC genome browser

More...UCSCi		uc008zri.2 mouse

<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
AF285161 Genomic DNA Translation: AAG00512.1
AF285162 Genomic DNA Translation: AAG00513.1
AC138613 Genomic DNA No translation available.
D50527 mRNA Translation: BAA09096.1
CCDSiCCDS19684.2
PIRiA49007
S11296
RefSeqiNP_062613.3, NM_019639.4

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
2ZNVX-ray1.60B/C/E/F1-76[»]
3A1QX-ray2.20A/B/D/E1-76[»]
3A9JX-ray1.18A/B1-76[»]
3A9KX-ray1.40A/B1-76[»]
3VHTX-ray2.40C1-76[»]
3WWQX-ray1.90A/B/D/E/G/H/J/K609-684[»]
3WXGX-ray3.10B/E609-684[»]
C/F609-680[»]
4NQLX-ray2.30B/C609-684[»]
6N5MX-ray3.01A1-76[»]
SMRiP0CG50
ModBaseiSearch...

Protein-protein interaction databases

BioGridi204403, 459 interactors
IntActiP0CG50, 2 interactors
STRINGi10090.ENSMUSP00000115578

PTM databases

iPTMnetiP0CG50
PhosphoSitePlusiP0CG50
SwissPalmiP0CG50

2D gel databases

REPRODUCTION-2DPAGEiP62991

Proteomic databases

jPOSTiP0CG50
MaxQBiP0CG50
PaxDbiP0CG50
PRIDEiP0CG50

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000136312; ENSMUSP00000114180; ENSMUSG00000008348
ENSMUST00000156249; ENSMUSP00000115578; ENSMUSG00000008348
GeneIDi22190
KEGGimmu:22190
UCSCiuc008zri.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		7316
MGIiMGI:98889 Ubc

Phylogenomic databases

eggNOGiKOG0001 Eukaryota
COG5272 LUCA
GeneTreeiENSGT00940000163900
InParanoidiP0CG50
KOiK08770
OrthoDBi1536766at2759
TreeFamiTF354256

Enzyme and pathway databases

ReactomeiR-MMU-110312 Translesion synthesis by REV1
R-MMU-110314 Recognition of DNA damage by PCNA-containing replication complex
R-MMU-110320 Translesion Synthesis by POLH
R-MMU-1169091 Activation of NF-kappaB in B cells
R-MMU-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-MMU-1253288 Downregulation of ERBB4 signaling
R-MMU-1295596 Spry regulation of FGF signaling
R-MMU-1358803 Downregulation of ERBB2:ERBB3 signaling
R-MMU-168638 NOD1/2 Signaling Pathway
R-MMU-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-MMU-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-MMU-174154 APC/C:Cdc20 mediated degradation of Securin
R-MMU-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-MMU-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-MMU-179409 APC-Cdc20 mediated degradation of Nek2A
R-MMU-182971 EGFR downregulation
R-MMU-187577 SCF(Skp2)-mediated degradation of p27/p21
R-MMU-195253 Degradation of beta-catenin by the destruction complex
R-MMU-201681 TCF dependent signaling in response to WNT
R-MMU-202424 Downstream TCR signaling
R-MMU-205043 NRIF signals cell death from the nucleus
R-MMU-209543 p75NTR recruits signalling complexes
R-MMU-209560 NF-kB is activated and signals survival
R-MMU-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-MMU-2173788 Downregulation of TGF-beta receptor signaling
R-MMU-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-MMU-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-MMU-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-MMU-2467813 Separation of Sister Chromatids
R-MMU-2559580 Oxidative Stress Induced Senescence
R-MMU-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-MMU-2559585 Oncogene Induced Senescence
R-MMU-2565942 Regulation of PLK1 Activity at G2/M Transition
R-MMU-2672351 Stimuli-sensing channels
R-MMU-2871837 FCERI mediated NF-kB activation
R-MMU-3134975 Regulation of innate immune responses to cytosolic DNA
R-MMU-349425 Autodegradation of the E3 ubiquitin ligase COP1
R-MMU-3769402 Deactivation of the beta-catenin transactivating complex
R-MMU-382556 ABC-family proteins mediated transport
R-MMU-445989 TAK1 activates NFkB by phosphorylation and activation of IKKs complex
R-MMU-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-MMU-4608870 Asymmetric localization of PCP proteins
R-MMU-4641257 Degradation of AXIN
R-MMU-4641258 Degradation of DVL
R-MMU-4641263 Regulation of FZD by ubiquitination
R-MMU-5205685 Pink/Parkin Mediated Mitophagy
R-MMU-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-MMU-5357905 Regulation of TNFR1 signaling
R-MMU-5357956 TNFR1-induced NFkappaB signaling pathway
R-MMU-5358346 Hedgehog ligand biogenesis
R-MMU-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-MMU-5607764 CLEC7A (Dectin-1) signaling
R-MMU-5610780 Degradation of GLI1 by the proteasome
R-MMU-5610785 GLI3 is processed to GLI3R by the proteasome
R-MMU-5632684 Hedgehog 'on' state
R-MMU-5654726 Negative regulation of FGFR1 signaling
R-MMU-5654727 Negative regulation of FGFR2 signaling
R-MMU-5654732 Negative regulation of FGFR3 signaling
R-MMU-5654733 Negative regulation of FGFR4 signaling
R-MMU-5655862 Translesion synthesis by POLK
R-MMU-5656121 Translesion synthesis by POLI
R-MMU-5656169 Termination of translesion DNA synthesis
R-MMU-5658442 Regulation of RAS by GAPs
R-MMU-5668541 TNFR2 non-canonical NF-kB pathway
R-MMU-5675221 Negative regulation of MAPK pathway
R-MMU-5675482 Regulation of necroptotic cell death
R-MMU-5676590 NIK-->noncanonical NF-kB signaling
R-MMU-5684264 MAP3K8 (TPL2)-dependent MAPK1/3 activation
R-MMU-5685942 HDR through Homologous Recombination (HRR)
R-MMU-5687128 MAPK6/MAPK4 signaling
R-MMU-5689603 UCH proteinases
R-MMU-5689877 Josephin domain DUBs
R-MMU-5689880 Ub-specific processing proteases
R-MMU-5689896 Ovarian tumor domain proteases
R-MMU-5689901 Metalloprotease DUBs
R-MMU-5693565 Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks
R-MMU-5693607 Processing of DNA double-strand break ends
R-MMU-5696394 DNA Damage Recognition in GG-NER
R-MMU-5696395 Formation of Incision Complex in GG-NER
R-MMU-5696397 Gap-filling DNA repair synthesis and ligation in GG-NER
R-MMU-5696400 Dual Incision in GG-NER
R-MMU-6781823 Formation of TC-NER Pre-Incision Complex
R-MMU-6782135 Dual incision in TC-NER
R-MMU-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-MMU-6783310 Fanconi Anemia Pathway
R-MMU-6804756 Regulation of TP53 Activity through Phosphorylation
R-MMU-6804757 Regulation of TP53 Degradation
R-MMU-6804760 Regulation of TP53 Activity through Methylation
R-MMU-6807004 Negative regulation of MET activity
R-MMU-68827 CDT1 association with the CDC6:ORC:origin complex
R-MMU-68949 Orc1 removal from chromatin
R-MMU-69017 CDK-mediated phosphorylation and removal of Cdc6
R-MMU-69231 Cyclin D associated events in G1
R-MMU-69481 G2/M Checkpoints
R-MMU-69541 Stabilization of p53
R-MMU-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-MMU-75815 Ubiquitin-dependent degradation of Cyclin D
R-MMU-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-MMU-8852276 The role of GTSE1 in G2/M progression after G2 checkpoint
R-MMU-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-MMU-8856825 Cargo recognition for clathrin-mediated endocytosis
R-MMU-8856828 Clathrin-mediated endocytosis
R-MMU-8863795 Downregulation of ERBB2 signaling
R-MMU-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-MMU-8866654 E3 ubiquitin ligases ubiquitinate target proteins
R-MMU-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-MMU-8939902 Regulation of RUNX2 expression and activity
R-MMU-8941858 Regulation of RUNX3 expression and activity
R-MMU-8948747 Regulation of PTEN localization
R-MMU-8948751 Regulation of PTEN stability and activity
R-MMU-8951664 Neddylation
R-MMU-901032 ER Quality Control Compartment (ERQC)
R-MMU-9010553 Regulation of expression of SLITs and ROBOs
R-MMU-9013507 NOTCH3 Activation and Transmission of Signal to the Nucleus
R-MMU-9020702 Interleukin-1 signaling
R-MMU-9033241 Peroxisomal protein import
R-MMU-912631 Regulation of signaling by CBL
R-MMU-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-MMU-917937 Iron uptake and transport
R-MMU-936440 Negative regulators of DDX58/IFIH1 signaling
R-MMU-936964 Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon
R-MMU-937041 IKK complex recruitment mediated by RIP1
R-MMU-937042 IRAK2 mediated activation of TAK1 complex
R-MMU-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-MMU-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-MMU-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

EvolutionaryTraceiP0CG50

Protein Ontology

More...PROi		PR:P0CG50

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSMUSG00000008348 Expressed in 302 organ(s), highest expression level in hypothalamus
ExpressionAtlasiP0CG50 baseline and differential
GenevisibleiP0CG50 MM

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, 10 hits
PROSITEiView protein in PROSITE
PS00299 UBIQUITIN_1, 9 hits
PS50053 UBIQUITIN_2, 9 hits

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiUBC_MOUSE
<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: P0CG50
Secondary accession number(s): E9QKI0
, P02248, P02249, P02250, P62991, Q29120, Q62317, Q64223, Q8VCH1, Q91887, Q91888, Q9CXY4, Q9CZM0, Q9D1R5, Q9D8D9, Q9ET23, Q9ET24, Q9Z0H9
<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: July 27, 2011
Last modified: September 18, 2019
This is version 85 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  2. SIMILARITY comments
    Index of protein domains and families
  3. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
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