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Protein

Polyubiquitin-C

Gene

Ubc

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score: -Experimental evidence at protein leveli

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 (By similarity).By similarity

Miscellaneous

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

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Binding sitei130Activating enzymeBy similarity1
Sitei144Essential for functionBy similarity1
Binding sitei148Activating enzymeBy similarity1

GO - Molecular functioni

  • protein tag Source: GO_Central
  • ubiquitin protein ligase binding Source: GO_Central

GO - Biological processi

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin-C
Cleaved into the following 2 chains:
Gene namesi
Name:Ubc
OrganismiRattus norvegicus (Rat)
Taxonomic identifieri10116 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
Proteomesi
  • UP000002494 Componenti: Unplaced

Organism-specific databases

RGDi621244 Ubc

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

Keywords - Cellular componenti

Cytoplasm, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_50001396881 – 76UbiquitinAdd BLAST76
ChainiPRO_500013968977 – 152UbiquitinAdd BLAST76
ChainiPRO_5000139690153 – 228UbiquitinAdd BLAST76
ChainiPRO_5000139691229 – 304UbiquitinAdd BLAST76
ChainiPRO_5000139692305 – 380UbiquitinAdd BLAST76
ChainiPRO_5000139693381 – 456UbiquitinAdd BLAST76
ChainiPRO_5000139694457 – 532UbiquitinAdd BLAST76
ChainiPRO_5000139695533 – 608UbiquitinAdd BLAST76
ChainiPRO_5000139696609 – 684UbiquitinAdd BLAST76
ChainiPRO_5000139697685 – 760UbiquitinAdd BLAST76
ChainiPRO_5000139698761 – 810Ubiquitin-relatedAdd BLAST50

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei65Phosphoserine; by PINK1By 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

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-riblosylated 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

PaxDbiQ63429
PRIDEiQ63429

PTM databases

iPTMnetiQ63429
PhosphoSitePlusiQ63429

Interactioni

GO - Molecular functioni

Protein-protein interaction databases

BioGridi248372, 817 interactors
IntActiQ63429, 1 interactor
MINTiQ63429
STRINGi10116.ENSRNOP00000043934

Structurei

3D structure databases

ProteinModelPortaliQ63429
SMRiQ63429
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
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

Sequence similaritiesi

Belongs to the ubiquitin family.Curated

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0001 Eukaryota
COG5272 LUCA
HOGENOMiHOG000233942
HOVERGENiHBG000057
InParanoidiQ63429
KOiK08770
PhylomeDBiQ63429

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

Sequence (1+)i

Sequence statusi: Complete.

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

Q63429-1 [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
760 770 780 790 800
LHLVLRLRGG MQIFVKTLTG KTITLEVEPS VNTKKVKQED TRTFLTTVSR
810
KSPSCACSWV
Length:810
Mass (Da):91,087
Last modified:November 1, 1996 - v1
Checksum:i4D4ADB697ADA3315
GO

Computationally mapped potential isoform sequencesi

There is 1 potential isoform mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
F1LML2F1LML2_RAT
Polyubiquitin-C
Ubc
810Annotation score:

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti776E → D in AAI03478 (PubMed:15489334).Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17296 mRNA Translation: BAA04129.1
BC103477 mRNA Translation: AAI03478.1
PIRiS45359
RefSeqiNP_059010.1, NM_017314.1
UniGeneiRn.3761

Genome annotation databases

GeneIDi50522
KEGGirno:50522
UCSCiRGD:621244 rat

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D17296 mRNA Translation: BAA04129.1
BC103477 mRNA Translation: AAI03478.1
PIRiS45359
RefSeqiNP_059010.1, NM_017314.1
UniGeneiRn.3761

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5L9Uelectron microscopy6.40S1-78[»]
ProteinModelPortaliQ63429
SMRiQ63429
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi248372, 817 interactors
IntActiQ63429, 1 interactor
MINTiQ63429
STRINGi10116.ENSRNOP00000043934

PTM databases

iPTMnetiQ63429
PhosphoSitePlusiQ63429

Proteomic databases

PaxDbiQ63429
PRIDEiQ63429

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi50522
KEGGirno:50522
UCSCiRGD:621244 rat

Organism-specific databases

CTDi7316
RGDi621244 Ubc

Phylogenomic databases

eggNOGiKOG0001 Eukaryota
COG5272 LUCA
HOGENOMiHOG000233942
HOVERGENiHBG000057
InParanoidiQ63429
KOiK08770
PhylomeDBiQ63429

Miscellaneous databases

PROiPR:Q63429

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
ProtoNetiSearch...

Entry informationi

Entry nameiUBC_RAT
AccessioniPrimary (citable) accession number: Q63429
Secondary accession number(s): Q3ZBA1
Entry historyiIntegrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: November 1, 1996
Last modified: November 7, 2018
This is version 106 of the entry and version 1 of the sequence. See complete history.
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

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

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
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