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Entry version 76 (18 Sep 2019)
Sequence version 1 (10 Aug 2010)
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Protein

Polyubiquitin

Gene

Ubi-p63E

Organism
Drosophila melanogaster (Fruit fly)
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>
-Protein inferred from homologyi <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-48-linked is involved in protein degradation via the proteasome. Linear polymer chains formed via attachment by the initiator Met lead to cell signaling. Ubiquitin is usually conjugated to Lys residues of target proteins, however, in rare cases, conjugation to Cys or Ser residues has been observed. When polyubiquitin is free (unanchored-polyubiquitin), it also has distinct roles, such as in activation of protein kinases, and in signaling (By similarity).By similarity

Miscellaneous

In Drosophila ubiquitin is encoded by 3 different genes. RpL40 and RpS27A genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. Ubi-p63E gene codes for a polyubiquitin precursor with 10 exact head to tail repeats.
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

GO - Biological processi

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-DME-110312 Translesion synthesis by REV1
R-DME-110314 Recognition of DNA damage by PCNA-containing replication complex
R-DME-110320 Translesion Synthesis by POLH
R-DME-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-DME-1253288 Downregulation of ERBB4 signaling
R-DME-1295596 Spry regulation of FGF signaling
R-DME-1358803 Downregulation of ERBB2:ERBB3 signaling
R-DME-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-DME-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-DME-174154 APC/C:Cdc20 mediated degradation of Securin
R-DME-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-DME-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-DME-179409 APC-Cdc20 mediated degradation of Nek2A
R-DME-182971 EGFR downregulation
R-DME-187577 SCF(Skp2)-mediated degradation of p27/p21
R-DME-195253 Degradation of beta-catenin by the destruction complex
R-DME-201681 TCF dependent signaling in response to WNT
R-DME-209360 Ubiquitination and proteolysis of phosphorylated CI
R-DME-209447 Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY
R-DME-209461 Ubiquitination and degradation of phosphorylated ARM
R-DME-209560 NF-kB is activated and signals survival
R-DME-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-DME-216167 Nuclear CI is degraded
R-DME-2173788 Downregulation of TGF-beta receptor signaling
R-DME-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-DME-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-DME-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-DME-2467813 Separation of Sister Chromatids
R-DME-2559580 Oxidative Stress Induced Senescence
R-DME-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-DME-2559585 Oncogene Induced Senescence
R-DME-3769402 Deactivation of the beta-catenin transactivating complex
R-DME-382556 ABC-family proteins mediated transport
R-DME-432395 Degradation of TIM
R-DME-432524 Degradation of PER
R-DME-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-DME-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-DME-4608870 Asymmetric localization of PCP proteins
R-DME-4641257 Degradation of AXIN
R-DME-4641258 Degradation of DVL
R-DME-5205685 Pink/Parkin Mediated Mitophagy
R-DME-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-DME-5358346 Hedgehog ligand biogenesis
R-DME-538864 Degradation of CRY
R-DME-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-DME-5610780 Degradation of GLI1 by the proteasome
R-DME-5610785 GLI3 is processed to GLI3R by the proteasome
R-DME-5632684 Hedgehog 'on' state
R-DME-5654726 Negative regulation of FGFR1 signaling
R-DME-5654727 Negative regulation of FGFR2 signaling
R-DME-5654732 Negative regulation of FGFR3 signaling
R-DME-5655862 Translesion synthesis by POLK
R-DME-5656121 Translesion synthesis by POLI
R-DME-5675482 Regulation of necroptotic cell death
R-DME-5676590 NIK-->noncanonical NF-kB signaling
R-DME-5689603 UCH proteinases
R-DME-5689877 Josephin domain DUBs
R-DME-5689880 Ub-specific processing proteases
R-DME-5689896 Ovarian tumor domain proteases
R-DME-5689901 Metalloprotease DUBs
R-DME-5696394 DNA Damage Recognition in GG-NER
R-DME-5696395 Formation of Incision Complex in GG-NER
R-DME-5696400 Dual Incision in GG-NER
R-DME-6781823 Formation of TC-NER Pre-Incision Complex
R-DME-6782135 Dual incision in TC-NER
R-DME-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-DME-6804756 Regulation of TP53 Activity through Phosphorylation
R-DME-6804757 Regulation of TP53 Degradation
R-DME-68827 CDT1 association with the CDC6:ORC:origin complex
R-DME-68949 Orc1 removal from chromatin
R-DME-69017 CDK-mediated phosphorylation and removal of Cdc6
R-DME-69231 Cyclin D associated events in G1
R-DME-69541 Stabilization of p53
R-DME-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-DME-75815 Ubiquitin-dependent degradation of Cyclin D
R-DME-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-DME-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-DME-8856825 Cargo recognition for clathrin-mediated endocytosis
R-DME-8856828 Clathrin-mediated endocytosis
R-DME-8863795 Downregulation of ERBB2 signaling
R-DME-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-DME-8866654 E3 ubiquitin ligases ubiquitinate target proteins
R-DME-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-DME-8939902 Regulation of RUNX2 expression and activity
R-DME-8941858 Regulation of RUNX3 expression and activity
R-DME-8948747 Regulation of PTEN localization
R-DME-8948751 Regulation of PTEN stability and activity
R-DME-8951664 Neddylation
R-DME-901032 ER Quality Control Compartment (ERQC)
R-DME-9010553 Regulation of expression of SLITs and ROBOs
R-DME-9020702 Interleukin-1 signaling
R-DME-9033241 Peroxisomal protein import
R-DME-912631 Regulation of signaling by CBL
R-DME-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-DME-917937 Iron uptake and transport
R-DME-937039 IRAK1 recruits IKK complex
R-DME-937042 IRAK2 mediated activation of TAK1 complex
R-DME-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-DME-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-DME-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-DME-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
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:Ubi-p63E
Synonyms:Ubi-m
ORF Names:CG11624
<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>OrganismiDrosophila melanogaster (Fruit fly)
<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 identifieri7227 [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 lineageiEukaryotaMetazoaEcdysozoaArthropodaHexapodaInsectaPterygotaNeopteraHolometabolaDipteraBrachyceraMuscomorphaEphydroideaDrosophilidaeDrosophilaSophophora
<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
  • UP000000803 <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 3L

Organism-specific databases

Drosophila genome database

More...
FlyBasei
FBgn0003943 Ubi-p63E

<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_00001148131 – 76UbiquitinAdd BLAST76
ChainiPRO_000039626077 – 152UbiquitinAdd BLAST76
ChainiPRO_0000396261153 – 228UbiquitinAdd BLAST76
ChainiPRO_0000396262229 – 304UbiquitinAdd BLAST76
ChainiPRO_0000396263305 – 380UbiquitinAdd BLAST76
ChainiPRO_0000396264381 – 456UbiquitinAdd BLAST76
ChainiPRO_0000396265457 – 532UbiquitinAdd BLAST76
ChainiPRO_0000396266533 – 608UbiquitinAdd BLAST76
ChainiPRO_0000396267609 – 684UbiquitinAdd BLAST76
ChainiPRO_0000396268685 – 760UbiquitinAdd 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_0000396269761 – 7633

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
Cross-linki76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)PROSITE-ProRule annotation

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

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

More...
PaxDbi
P0CG69

PRoteomics IDEntifications database

More...
PRIDEi
P0CG69

<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
FBgn0003943 Expressed in 32 organ(s), highest expression level in embryo

ExpressionAtlas, Differential and Baseline Expression

More...
ExpressionAtlasi
P0CG69 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
P0CG69 DM

<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

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
63944, 38 interactors

STRING: functional protein association networks

More...
STRINGi
7227.FBpp0073035

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

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

More...
SMRi
P0CG69

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_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
Domaini685 – 760Ubiquitin-like 10PROSITE-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

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InParanoidi
P0CG69

KEGG Orthology (KO)

More...
KOi
K08770

Identification of Orthologs from Complete Genome Data

More...
OMAi
RENMQIF

Database of Orthologous Groups

More...
OrthoDBi
1536766at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
P0CG69

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, 10 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, 10 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, 10 hits
PS50053 UBIQUITIN_2, 10 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

P0CG69-1 [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 TLTGKTITLE
710 720 730 740 750
VEPSDTIENV KAKIQDKEGI PPDQQRLIFA GKQLEDGRTL SDYNIQKEST
760
LHLVLRLRGG IQA
Length:763
Mass (Da):85,799
Last modified:August 10, 2010 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:i5693123AE7B186A7
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
A4V1F9A4V1F9_DROME
Ubiquitin-63E, isoform C
Ubi-p63E Dmel\CG11624, DmUb, DmUbi-p63E, magn, UB
763Annotation score:

Annotation score:3 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>

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

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DDBJi
Links Updated
AE014296 Genomic DNA Translation: AAF47806.3
M33013 Genomic DNA Translation: AAA28999.1
M33015 Genomic DNA Translation: AAA29001.1
M33122 Genomic DNA Translation: AAA29007.1
M22428 Genomic DNA Translation: AAA28997.1

Protein sequence database of the Protein Information Resource

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PIRi
A26087

NCBI Reference Sequences

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RefSeqi
NP_001261383.1, NM_001274454.1
NP_523909.2, NM_079185.4
NP_728908.1, NM_168043.3
NP_995994.1, NM_206272.1

Genome annotation databases

Ensembl metazoan genome annotation project

More...
EnsemblMetazoai
FBtr0073177; FBpp0073034; FBgn0003943
FBtr0073178; FBpp0073035; FBgn0003943
FBtr0073179; FBpp0089269; FBgn0003943
FBtr0333142; FBpp0305348; FBgn0003943

Database of genes from NCBI RefSeq genomes

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GeneIDi
38456

KEGG: Kyoto Encyclopedia of Genes and Genomes

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KEGGi
dme:Dmel_CG11624

<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
AE014296 Genomic DNA Translation: AAF47806.3
M33013 Genomic DNA Translation: AAA28999.1
M33015 Genomic DNA Translation: AAA29001.1
M33122 Genomic DNA Translation: AAA29007.1
M22428 Genomic DNA Translation: AAA28997.1
PIRiA26087
RefSeqiNP_001261383.1, NM_001274454.1
NP_523909.2, NM_079185.4
NP_728908.1, NM_168043.3
NP_995994.1, NM_206272.1

3D structure databases

SMRiP0CG69
ModBaseiSearch...

Protein-protein interaction databases

BioGridi63944, 38 interactors
STRINGi7227.FBpp0073035

Proteomic databases

PaxDbiP0CG69
PRIDEiP0CG69

Genome annotation databases

EnsemblMetazoaiFBtr0073177; FBpp0073034; FBgn0003943
FBtr0073178; FBpp0073035; FBgn0003943
FBtr0073179; FBpp0089269; FBgn0003943
FBtr0333142; FBpp0305348; FBgn0003943
GeneIDi38456
KEGGidme:Dmel_CG11624

Organism-specific databases

Comparative Toxicogenomics Database

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CTDi
38456
FlyBaseiFBgn0003943 Ubi-p63E

Phylogenomic databases

eggNOGiKOG0001 Eukaryota
COG5272 LUCA
GeneTreeiENSGT00940000163900
InParanoidiP0CG69
KOiK08770
OMAiRENMQIF
OrthoDBi1536766at2759
PhylomeDBiP0CG69

Enzyme and pathway databases

ReactomeiR-DME-110312 Translesion synthesis by REV1
R-DME-110314 Recognition of DNA damage by PCNA-containing replication complex
R-DME-110320 Translesion Synthesis by POLH
R-DME-1234176 Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha
R-DME-1253288 Downregulation of ERBB4 signaling
R-DME-1295596 Spry regulation of FGF signaling
R-DME-1358803 Downregulation of ERBB2:ERBB3 signaling
R-DME-174048 APC/C:Cdc20 mediated degradation of Cyclin B
R-DME-174084 Autodegradation of Cdh1 by Cdh1:APC/C
R-DME-174154 APC/C:Cdc20 mediated degradation of Securin
R-DME-174178 APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1
R-DME-174184 Cdc20:Phospho-APC/C mediated degradation of Cyclin A
R-DME-179409 APC-Cdc20 mediated degradation of Nek2A
R-DME-182971 EGFR downregulation
R-DME-187577 SCF(Skp2)-mediated degradation of p27/p21
R-DME-195253 Degradation of beta-catenin by the destruction complex
R-DME-201681 TCF dependent signaling in response to WNT
R-DME-209360 Ubiquitination and proteolysis of phosphorylated CI
R-DME-209447 Activation of the IkappaB kinase complex, KEY:IRD5 dimer:KEY
R-DME-209461 Ubiquitination and degradation of phosphorylated ARM
R-DME-209560 NF-kB is activated and signals survival
R-DME-2122948 Activated NOTCH1 Transmits Signal to the Nucleus
R-DME-216167 Nuclear CI is degraded
R-DME-2173788 Downregulation of TGF-beta receptor signaling
R-DME-2173791 TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition)
R-DME-2173795 Downregulation of SMAD2/3:SMAD4 transcriptional activity
R-DME-2173796 SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription
R-DME-2467813 Separation of Sister Chromatids
R-DME-2559580 Oxidative Stress Induced Senescence
R-DME-2559582 Senescence-Associated Secretory Phenotype (SASP)
R-DME-2559585 Oncogene Induced Senescence
R-DME-3769402 Deactivation of the beta-catenin transactivating complex
R-DME-382556 ABC-family proteins mediated transport
R-DME-432395 Degradation of TIM
R-DME-432524 Degradation of PER
R-DME-450321 JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1
R-DME-450408 AUF1 (hnRNP D0) binds and destabilizes mRNA
R-DME-4608870 Asymmetric localization of PCP proteins
R-DME-4641257 Degradation of AXIN
R-DME-4641258 Degradation of DVL
R-DME-5205685 Pink/Parkin Mediated Mitophagy
R-DME-532668 N-glycan trimming in the ER and Calnexin/Calreticulin cycle
R-DME-5358346 Hedgehog ligand biogenesis
R-DME-538864 Degradation of CRY
R-DME-5607761 Dectin-1 mediated noncanonical NF-kB signaling
R-DME-5610780 Degradation of GLI1 by the proteasome
R-DME-5610785 GLI3 is processed to GLI3R by the proteasome
R-DME-5632684 Hedgehog 'on' state
R-DME-5654726 Negative regulation of FGFR1 signaling
R-DME-5654727 Negative regulation of FGFR2 signaling
R-DME-5654732 Negative regulation of FGFR3 signaling
R-DME-5655862 Translesion synthesis by POLK
R-DME-5656121 Translesion synthesis by POLI
R-DME-5675482 Regulation of necroptotic cell death
R-DME-5676590 NIK-->noncanonical NF-kB signaling
R-DME-5689603 UCH proteinases
R-DME-5689877 Josephin domain DUBs
R-DME-5689880 Ub-specific processing proteases
R-DME-5689896 Ovarian tumor domain proteases
R-DME-5689901 Metalloprotease DUBs
R-DME-5696394 DNA Damage Recognition in GG-NER
R-DME-5696395 Formation of Incision Complex in GG-NER
R-DME-5696400 Dual Incision in GG-NER
R-DME-6781823 Formation of TC-NER Pre-Incision Complex
R-DME-6782135 Dual incision in TC-NER
R-DME-6782210 Gap-filling DNA repair synthesis and ligation in TC-NER
R-DME-6804756 Regulation of TP53 Activity through Phosphorylation
R-DME-6804757 Regulation of TP53 Degradation
R-DME-68827 CDT1 association with the CDC6:ORC:origin complex
R-DME-68949 Orc1 removal from chromatin
R-DME-69017 CDK-mediated phosphorylation and removal of Cdc6
R-DME-69231 Cyclin D associated events in G1
R-DME-69541 Stabilization of p53
R-DME-69601 Ubiquitin Mediated Degradation of Phosphorylated Cdc25A
R-DME-75815 Ubiquitin-dependent degradation of Cyclin D
R-DME-8849469 PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1
R-DME-8854050 FBXL7 down-regulates AURKA during mitotic entry and in early mitosis
R-DME-8856825 Cargo recognition for clathrin-mediated endocytosis
R-DME-8856828 Clathrin-mediated endocytosis
R-DME-8863795 Downregulation of ERBB2 signaling
R-DME-8866652 Synthesis of active ubiquitin: roles of E1 and E2 enzymes
R-DME-8866654 E3 ubiquitin ligases ubiquitinate target proteins
R-DME-8939236 RUNX1 regulates transcription of genes involved in differentiation of HSCs
R-DME-8939902 Regulation of RUNX2 expression and activity
R-DME-8941858 Regulation of RUNX3 expression and activity
R-DME-8948747 Regulation of PTEN localization
R-DME-8948751 Regulation of PTEN stability and activity
R-DME-8951664 Neddylation
R-DME-901032 ER Quality Control Compartment (ERQC)
R-DME-9010553 Regulation of expression of SLITs and ROBOs
R-DME-9020702 Interleukin-1 signaling
R-DME-9033241 Peroxisomal protein import
R-DME-912631 Regulation of signaling by CBL
R-DME-917729 Endosomal Sorting Complex Required For Transport (ESCRT)
R-DME-917937 Iron uptake and transport
R-DME-937039 IRAK1 recruits IKK complex
R-DME-937042 IRAK2 mediated activation of TAK1 complex
R-DME-937072 TRAF6-mediated induction of TAK1 complex within TLR4 complex
R-DME-975144 IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation
R-DME-975163 IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation
R-DME-983168 Antigen processing: Ubiquitination & Proteasome degradation

Miscellaneous databases

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

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GenomeRNAii
38456

Protein Ontology

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PROi
PR:P0CG69

Gene expression databases

BgeeiFBgn0003943 Expressed in 32 organ(s), highest expression level in embryo
ExpressionAtlasiP0CG69 baseline and differential
GenevisibleiP0CG69 DM

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, 10 hits
PRINTSiPR00348 UBIQUITIN
SMARTiView protein in SMART
SM00213 UBQ, 10 hits
SUPFAMiSSF54236 SSF54236, 10 hits
PROSITEiView protein in PROSITE
PS00299 UBIQUITIN_1, 10 hits
PS50053 UBIQUITIN_2, 10 hits

ProtoNet; Automatic hierarchical classification of proteins

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ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

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MobiDBi
Search...

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

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiUBIQP_DROME
<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: P0CG69
Secondary accession number(s): P68198
, Q0E8I1, Q9VKW6, Q9VQX7, Q9VZL4
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: September 18, 2019
This is version 76 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programDrosophila annotation project

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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. Drosophila
    Drosophila: entries, gene names and cross-references to FlyBase
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