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Protein

Polyubiquitin-B

Gene

UBB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei54 – 541Activating enzyme
Sitei68 – 681Essential for function
Binding sitei72 – 721Activating enzyme

GO - Biological processi

Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-110320. Translesion Synthesis by POLH.
R-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-1227986. Signaling by ERBB2.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236382. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1253288. Downregulation of ERBB4 signaling.
R-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-168928. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-174490. Membrane binding and targetting of GAG proteins.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-182971. EGFR downregulation.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-202424. Downstream TCR signaling.
R-HSA-205043. NRIF signals cell death from the nucleus.
R-HSA-209543. p75NTR recruits signalling complexes.
R-HSA-209560. NF-kB is activated and signals survival.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2672351. Stimuli-sensing channels.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-3322077. Glycogen synthesis.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-3785653. Myoclonic epilepsy of Lafora.
R-HSA-400253. Circadian Clock.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-4641263. Regulation of FZD by ubiquitination.
R-HSA-5205685. Pink/Parkin Mediated Mitophagy.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5654733. Negative regulation of FGFR4 signaling.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-5675482. Regulation of necroptotic cell death.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6783310. Fanconi Anemia Pathway.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69298. Association of licensing factors with the pre-replicative complex.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-912631. Regulation of signaling by CBL.
R-HSA-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
R-HSA-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-HSA-937039. IRAK1 recruits IKK complex.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
R-HSA-937042. IRAK2 mediated activation of TAK1 complex.
R-HSA-937072. TRAF6 mediated induction of TAK1 complex.
R-HSA-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-HSA-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
R-HSA-975163. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin-B
Cleaved into the following chain:
Gene namesi
Name:UBB
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:12463. UBB.

Subcellular locationi

Ubiquitin :

GO - Cellular componenti

  • cytosol Source: Reactome
  • endocytic vesicle membrane Source: Reactome
  • endosome membrane Source: Reactome
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • mitochondrion Source: MGI
  • myelin sheath Source: Ensembl
  • neuronal cell body Source: MGI
  • neuron projection Source: MGI
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • plasma membrane Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi48 – 481K → R: No effect on HLTF-mediated polyubiquitination of PCNA. 1 Publication
Mutagenesisi63 – 631K → R: Abolishes HLTF-mediated polyubiquitination of PCNA. 1 Publication
Mutagenesisi65 – 651S → A: Prevents phosphorylation in case of mitophagy. 3 Publications
Mutagenesisi65 – 651S → D: Phosphomimetic mutant that binds and activates PARK2. 1 Publication

Organism-specific databases

MalaCardsiUBB.

Polymorphism and mutation databases

DMDMi302595875.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396174Add
BLAST
Chaini77 – 15276UbiquitinPRO_0000396175Add
BLAST
Chaini153 – 22876UbiquitinPRO_0000396176Add
BLAST
Propeptidei229 – 2291PRO_0000396177

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki11 – 11Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Cross-linki27 – 27Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki29 – 29Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Cross-linki33 – 33Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Cross-linki48 – 48Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)3 Publications
Cross-linki63 – 63Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)2 Publications
Modified residuei65 – 651Phosphoserine; by PINK14 Publications
Cross-linki76 – 76Glycyl lysine isopeptide (Gly-Lys) (interchain with K-? in acceptor proteins)

Post-translational modificationi

Ubiquitin: Phosphorylated at Ser-65 by PINK1 during mitophagy. Phosphorylated ubiquitin specifically binds and activates parkin (PARK2), triggering mitophagy (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291). Phosphorylation does not affect E1-mediated E2 charging of ubiquitin but affects discharging of E2 enzymes to form polyubiquitin chains. It also affects deubiquitination by deubiquitinase enzymes such as USP30 (PubMed:25527291).4 Publications

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP0CG47.
PaxDbiP0CG47.
PRIDEiP0CG47.
TopDownProteomicsiP0CG47.

PTM databases

iPTMnetiP0CG47.
PhosphoSiteiP0CG47.
SwissPalmiP0CG47.

Expressioni

Gene expression databases

BgeeiP0CG47.
ExpressionAtlasiP0CG47. baseline and differential.
GenevisibleiP0CG47. HS.

Organism-specific databases

HPAiCAB013048.
HPA041344.
HPA049132.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC50Q8IVM02EBI-413034,EBI-723996
DUSP1P285622EBI-413034,EBI-975493
GGA1Q9UJY53EBI-413034,EBI-447141
GGA3Q9NZ522EBI-413034,EBI-447404
MAP3K3Q997592EBI-413034,EBI-307281
Mast2Q605922EBI-413034,EBI-493888From a different organism.
MCM7P339932EBI-413034,EBI-355924
NPQ9DLK62EBI-413034,EBI-8433218From a different organism.
Pax3P246102EBI-413034,EBI-1208116From a different organism.
RABGEF1Q9UJ416EBI-413034,EBI-913954
RNF11Q9Y3C52EBI-413034,EBI-396669
RNF43Q68DV72EBI-413034,EBI-1647060
SMURF2Q9HAU44EBI-413034,EBI-396727

Protein-protein interaction databases

BioGridi113162. 158 interactions.
IntActiP0CG47. 86 interactions.
MINTiMINT-8084593.
STRINGi9606.ENSP00000304697.

Structurei

Secondary structure

1
229
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi154 – 1596Combined sources
Beta strandi160 – 1623Combined sources
Beta strandi164 – 1685Combined sources
Beta strandi171 – 1744Combined sources
Helixi175 – 18612Combined sources
Helixi190 – 1923Combined sources
Beta strandi193 – 1975Combined sources
Beta strandi206 – 2083Combined sources
Helixi209 – 2113Combined sources
Beta strandi218 – 2236Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KHWNMR-B153-228[»]
2MBBNMR-B153-228[»]
2MRONMR-A153-228[»]
2MSGNMR-A153-224[»]
4UELX-ray2.30B153-228[»]
4UF6X-ray3.69B/E/H/K153-227[»]
4WHVX-ray8.30A/F/G/L153-228[»]
4WLRX-ray2.00C153-228[»]
4WURX-ray3.16B153-228[»]
4XOFX-ray1.15A153-228[»]
4ZFRX-ray1.72B153-228[»]
4ZFTX-ray2.30B/D153-228[»]
4ZPZX-ray1.54A/B153-225[»]
4ZUXX-ray3.82X/c/h/m153-228[»]
5BNBX-ray2.49E/F/G/I153-229[»]
5CAWX-ray2.62B/D153-228[»]
5CRAX-ray2.64C/D153-227[»]
5CVMX-ray1.90B153-211[»]
5CVNX-ray3.36D153-228[»]
5CVOX-ray3.88C/F153-228[»]
5D0KX-ray2.65B/E/H/K153-228[»]
5D0MX-ray1.91B153-228[»]
5DFLX-ray2.10B153-228[»]
5DK8X-ray1.32A/B154-227[»]
5EDVX-ray3.48E/F/G/H153-228[»]
ProteinModelPortaliP0CG47.
SMRiP0CG47. Positions 1-227.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1 – 7676Ubiquitin-like 1PROSITE-ProRule annotationAdd
BLAST
Domaini77 – 15276Ubiquitin-like 2PROSITE-ProRule annotationAdd
BLAST
Domaini153 – 22876Ubiquitin-like 3PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family.Curated
Contains 3 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
InParanoidiP0CG47.
KOiK04551.
OMAiCPMERIM.
PhylomeDBiP0CG47.
TreeFamiTF300820.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 3 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 3 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 3 hits.
PROSITEiPS00299. UBIQUITIN_1. 3 hits.
PS50053. UBIQUITIN_2. 3 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P0CG47-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
110 120 130 140 150
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR
160 170 180 190 200
GGMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK
210 220
QLEDGRTLSD YNIQKESTLH LVLRLRGGC
Length:229
Mass (Da):25,762
Last modified:August 10, 2010 - v1
Checksum:i33011162F1C48BB1
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti76 – 229154GMQIF…LRGGC → YADLREDPDRQDHHPGSGAQ in UBB(+1); loss of polyubiquitination; impairs the ubiquitin-proteasome pathway; refractory to disassembly by DUBs; slow degradation by UCHL3.
VAR_066248Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04803 Genomic DNA. Translation: CAA28495.1.
AB089617 Genomic DNA. Translation: BAC56955.1.
AC093484 Genomic DNA. No translation available.
BC000379 mRNA. Translation: AAH00379.1.
BC009301 mRNA. Translation: AAH09301.1.
BC015127 mRNA. Translation: AAH15127.1.
BC026301 mRNA. Translation: AAH26301.1.
BC031027 mRNA. Translation: AAH31027.1.
BC046123 mRNA. Translation: AAH46123.1.
CCDSiCCDS11177.1.
PIRiA26437. UQHUB.
RefSeqiNP_001268645.1. NM_001281716.1.
NP_001268646.1. NM_001281717.1.
NP_001268647.1. NM_001281718.1.
NP_001268648.1. NM_001281719.1.
NP_001268649.1. NM_001281720.1.
NP_061828.1. NM_018955.3.
UniGeneiHs.356190.
Hs.730603.
Hs.741549.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X04803 Genomic DNA. Translation: CAA28495.1.
AB089617 Genomic DNA. Translation: BAC56955.1.
AC093484 Genomic DNA. No translation available.
BC000379 mRNA. Translation: AAH00379.1.
BC009301 mRNA. Translation: AAH09301.1.
BC015127 mRNA. Translation: AAH15127.1.
BC026301 mRNA. Translation: AAH26301.1.
BC031027 mRNA. Translation: AAH31027.1.
BC046123 mRNA. Translation: AAH46123.1.
CCDSiCCDS11177.1.
PIRiA26437. UQHUB.
RefSeqiNP_001268645.1. NM_001281716.1.
NP_001268646.1. NM_001281717.1.
NP_001268647.1. NM_001281718.1.
NP_001268648.1. NM_001281719.1.
NP_001268649.1. NM_001281720.1.
NP_061828.1. NM_018955.3.
UniGeneiHs.356190.
Hs.730603.
Hs.741549.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2KHWNMR-B153-228[»]
2MBBNMR-B153-228[»]
2MRONMR-A153-228[»]
2MSGNMR-A153-224[»]
4UELX-ray2.30B153-228[»]
4UF6X-ray3.69B/E/H/K153-227[»]
4WHVX-ray8.30A/F/G/L153-228[»]
4WLRX-ray2.00C153-228[»]
4WURX-ray3.16B153-228[»]
4XOFX-ray1.15A153-228[»]
4ZFRX-ray1.72B153-228[»]
4ZFTX-ray2.30B/D153-228[»]
4ZPZX-ray1.54A/B153-225[»]
4ZUXX-ray3.82X/c/h/m153-228[»]
5BNBX-ray2.49E/F/G/I153-229[»]
5CAWX-ray2.62B/D153-228[»]
5CRAX-ray2.64C/D153-227[»]
5CVMX-ray1.90B153-211[»]
5CVNX-ray3.36D153-228[»]
5CVOX-ray3.88C/F153-228[»]
5D0KX-ray2.65B/E/H/K153-228[»]
5D0MX-ray1.91B153-228[»]
5DFLX-ray2.10B153-228[»]
5DK8X-ray1.32A/B154-227[»]
5EDVX-ray3.48E/F/G/H153-228[»]
ProteinModelPortaliP0CG47.
SMRiP0CG47. Positions 1-227.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113162. 158 interactions.
IntActiP0CG47. 86 interactions.
MINTiMINT-8084593.
STRINGi9606.ENSP00000304697.

PTM databases

iPTMnetiP0CG47.
PhosphoSiteiP0CG47.
SwissPalmiP0CG47.

Polymorphism and mutation databases

DMDMi302595875.

Proteomic databases

EPDiP0CG47.
PaxDbiP0CG47.
PRIDEiP0CG47.
TopDownProteomicsiP0CG47.

Protocols and materials databases

DNASUi7314.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7314.
GeneCardsiUBB.
HGNCiHGNC:12463. UBB.
HPAiCAB013048.
HPA041344.
HPA049132.
MalaCardsiUBB.
MIMi191339. gene.
neXtProtiNX_P0CG47.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
InParanoidiP0CG47.
KOiK04551.
OMAiCPMERIM.
PhylomeDBiP0CG47.
TreeFamiTF300820.

Enzyme and pathway databases

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-110320. Translesion Synthesis by POLH.
R-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-1227986. Signaling by ERBB2.
R-HSA-1234176. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
R-HSA-1236382. Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
R-HSA-1236974. ER-Phagosome pathway.
R-HSA-1253288. Downregulation of ERBB4 signaling.
R-HSA-1295596. Spry regulation of FGF signaling.
R-HSA-1358803. Downregulation of ERBB2:ERBB3 signaling.
R-HSA-162588. Budding and maturation of HIV virion.
R-HSA-168638. NOD1/2 Signaling Pathway.
R-HSA-168928. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
R-HSA-174048. APC/C:Cdc20 mediated degradation of Cyclin B.
R-HSA-174084. Autodegradation of Cdh1 by Cdh1:APC/C.
R-HSA-174113. SCF-beta-TrCP mediated degradation of Emi1.
R-HSA-174154. APC/C:Cdc20 mediated degradation of Securin.
R-HSA-174178. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
R-HSA-174184. Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
R-HSA-174490. Membrane binding and targetting of GAG proteins.
R-HSA-175474. Assembly Of The HIV Virion.
R-HSA-179409. APC-Cdc20 mediated degradation of Nek2A.
R-HSA-180534. Vpu mediated degradation of CD4.
R-HSA-180585. Vif-mediated degradation of APOBEC3G.
R-HSA-182971. EGFR downregulation.
R-HSA-187577. SCF(Skp2)-mediated degradation of p27/p21.
R-HSA-195253. Degradation of beta-catenin by the destruction complex.
R-HSA-201681. TCF dependent signaling in response to WNT.
R-HSA-202424. Downstream TCR signaling.
R-HSA-205043. NRIF signals cell death from the nucleus.
R-HSA-209543. p75NTR recruits signalling complexes.
R-HSA-209560. NF-kB is activated and signals survival.
R-HSA-211733. Regulation of activated PAK-2p34 by proteasome mediated degradation.
R-HSA-2122947. NOTCH1 Intracellular Domain Regulates Transcription.
R-HSA-2122948. Activated NOTCH1 Transmits Signal to the Nucleus.
R-HSA-2173788. Downregulation of TGF-beta receptor signaling.
R-HSA-2173791. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
R-HSA-2173795. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
R-HSA-2173796. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
R-HSA-2467813. Separation of Sister Chromatids.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559582. Senescence-Associated Secretory Phenotype (SASP).
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-2565942. Regulation of PLK1 Activity at G2/M Transition.
R-HSA-2644606. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
R-HSA-2672351. Stimuli-sensing channels.
R-HSA-2691232. Constitutive Signaling by NOTCH1 HD Domain Mutants.
R-HSA-2871837. FCERI mediated NF-kB activation.
R-HSA-2894862. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
R-HSA-2979096. NOTCH2 Activation and Transmission of Signal to the Nucleus.
R-HSA-3134975. Regulation of innate immune responses to cytosolic DNA.
R-HSA-3322077. Glycogen synthesis.
R-HSA-349425. Autodegradation of the E3 ubiquitin ligase COP1.
R-HSA-3769402. Deactivation of the beta-catenin transactivating complex.
R-HSA-3785653. Myoclonic epilepsy of Lafora.
R-HSA-400253. Circadian Clock.
R-HSA-445989. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
R-HSA-446652. Interleukin-1 signaling.
R-HSA-450302. activated TAK1 mediates p38 MAPK activation.
R-HSA-450321. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
R-HSA-450408. AUF1 (hnRNP D0) binds and destabilizes mRNA.
R-HSA-4608870. Asymmetric localization of PCP proteins.
R-HSA-4641257. Degradation of AXIN.
R-HSA-4641258. Degradation of DVL.
R-HSA-4641263. Regulation of FZD by ubiquitination.
R-HSA-5205685. Pink/Parkin Mediated Mitophagy.
R-HSA-5357905. Regulation of TNFR1 signaling.
R-HSA-5357956. TNFR1-induced NFkappaB signaling pathway.
R-HSA-5358346. Hedgehog ligand biogenesis.
R-HSA-5362768. Hh mutants that don't undergo autocatalytic processing are degraded by ERAD.
R-HSA-5607761. Dectin-1 mediated noncanonical NF-kB signaling.
R-HSA-5607764. CLEC7A (Dectin-1) signaling.
R-HSA-5610780. Degradation of GLI1 by the proteasome.
R-HSA-5610783. Degradation of GLI2 by the proteasome.
R-HSA-5610785. GLI3 is processed to GLI3R by the proteasome.
R-HSA-5632684. Hedgehog 'on' state.
R-HSA-5654726. Negative regulation of FGFR1 signaling.
R-HSA-5654727. Negative regulation of FGFR2 signaling.
R-HSA-5654732. Negative regulation of FGFR3 signaling.
R-HSA-5654733. Negative regulation of FGFR4 signaling.
R-HSA-5655862. Translesion synthesis by POLK.
R-HSA-5656121. Translesion synthesis by POLI.
R-HSA-5656169. Termination of translesion DNA synthesis.
R-HSA-5658442. Regulation of RAS by GAPs.
R-HSA-5668541. TNFR2 non-canonical NF-kB pathway.
R-HSA-5675221. Negative regulation of MAPK pathway.
R-HSA-5675482. Regulation of necroptotic cell death.
R-HSA-5676590. NIK-->noncanonical NF-kB signaling.
R-HSA-5684264. MAP3K8 (TPL2)-dependent MAPK1/3 activation.
R-HSA-5685942. HDR through Homologous Recombination (HRR).
R-HSA-5687128. MAPK6/MAPK4 signaling.
R-HSA-5693565. Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
R-HSA-5693607. Processing of DNA double-strand break ends.
R-HSA-5696394. DNA Damage Recognition in GG-NER.
R-HSA-5696395. Formation of Incision Complex in GG-NER.
R-HSA-5696397. Gap-filling DNA repair synthesis and ligation in GG-NER.
R-HSA-5696400. Dual Incision in GG-NER.
R-HSA-6781823. Formation of TC-NER Pre-Incision Complex.
R-HSA-6781827. Transcription-Coupled Nucleotide Excision Repair (TC-NER).
R-HSA-6782135. Dual incision in TC-NER.
R-HSA-6782210. Gap-filling DNA repair synthesis and ligation in TC-NER.
R-HSA-6783310. Fanconi Anemia Pathway.
R-HSA-68827. CDT1 association with the CDC6:ORC:origin complex.
R-HSA-68949. Orc1 removal from chromatin.
R-HSA-69017. CDK-mediated phosphorylation and removal of Cdc6.
R-HSA-69229. Ubiquitin-dependent degradation of Cyclin D1.
R-HSA-69231. Cyclin D associated events in G1.
R-HSA-69298. Association of licensing factors with the pre-replicative complex.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-912631. Regulation of signaling by CBL.
R-HSA-917729. Endosomal Sorting Complex Required For Transport (ESCRT).
R-HSA-936440. Negative regulators of RIG-I/MDA5 signaling.
R-HSA-936964. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
R-HSA-937039. IRAK1 recruits IKK complex.
R-HSA-937041. IKK complex recruitment mediated by RIP1.
R-HSA-937042. IRAK2 mediated activation of TAK1 complex.
R-HSA-937072. TRAF6 mediated induction of TAK1 complex.
R-HSA-975110. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
R-HSA-975144. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
R-HSA-975163. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiUBB. human.
GeneWikiiUbiquitin_B.
GenomeRNAii7314.
NextBioi28592.
PROiP0CG47.
SOURCEiSearch...

Gene expression databases

BgeeiP0CG47.
ExpressionAtlasiP0CG47. baseline and differential.
GenevisibleiP0CG47. HS.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 3 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 3 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 3 hits.
PROSITEiPS00299. UBIQUITIN_1. 3 hits.
PS50053. UBIQUITIN_2. 3 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human ubiquitin gene family: structure of a gene and pseudogenes from the Ub B subfamily."
    Baker R.T., Board P.G.
    Nucleic Acids Res. 15:443-463(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Blood.
  2. "Lineage-specific homogenization of the polyubiquitin gene among human and great apes."
    Tachikui H., Saitou N., Nakajima T., Hayasaka I., Ishida T., Inoue I.
    J. Mol. Evol. 57:737-744(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
    Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
    , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
    Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain, Liver and Lung.
  5. Lubec G., Chen W.-Q., Sun Y.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Fetal brain cortex.
  6. "Molecular conservation of 74 amino acid sequence of ubiquitin between cattle and man."
    Schlesinger D.H., Goldstein G.
    Nature 255:423-424(1975) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-74.
  7. "Alzheimer disease-specific conformation of hyperphosphorylated paired helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6 ubiquitin conjugation."
    Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.
    J. Biol. Chem. 281:10825-10838(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND LYS-48, IDENTIFICATION BY MASS SPECTROMETRY.
  8. "Differential regulation of EGF receptor internalization and degradation by multiubiquitination within the kinase domain."
    Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.
    Mol. Cell 21:737-748(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, IDENTIFICATION BY MASS SPECTROMETRY.
  9. "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B contributes to neuritogenesis."
    Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.
    J. Biol. Chem. 279:53533-53543(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-27.
  10. "The proteomic reactor facilitates the analysis of affinity-purified proteins by mass spectrometry: application for identifying ubiquitinated proteins in human cells."
    Vasilescu J., Zweitzig D.R., Denis N.J., Smith J.C., Ethier M., Haines D.S., Figeys D.
    J. Proteome Res. 6:298-305(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-48.
    Tissue: Lung adenocarcinoma.
  11. "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH prevents genomic instability from stalled replication forks."
    Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H., Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.
    Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-63, MUTAGENESIS OF LYS-48 AND LYS-63.
  12. "The emerging complexity of protein ubiquitination."
    Komander D.
    Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.
  13. "Mutant ubiquitin (UBB(+1)) associated with neurodegenerative disorders is hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3)."
    Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N., Steinbusch H.W., Dantuma N.P., van Leeuwen F.W.
    FEBS Lett. 585:2568-2574(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CLEAVAGE BY UCHL3 (VARIANT UBB(+1)).
  14. Cited for: IDENTIFICATION OF VARIANT UBB(+1).
  15. "Disease-specific accumulation of mutant ubiquitin as a marker for proteasomal dysfunction in the brain."
    Fischer D.F., De Vos R.A., Van Dijk R., De Vrij F.M., Proper E.A., Sonnemans M.A., Verhage M.C., Sluijs J.A., Hobo B., Zouambia M., Steur E.N., Kamphorst W., Hol E.M., Van Leeuwen F.W.
    FASEB J. 17:2014-2024(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY (VARIANT UBB(+1)).
  16. Cited for: PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-65.
  17. "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase activity."
    Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A., Banerjee S., Youle R.J.
    J. Cell Biol. 205:143-153(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-65.
  18. Cited for: PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-65.
  19. "Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain assembly and hydrolysis."
    Wauer T., Swatek K.N., Wagstaff J.L., Gladkova C., Pruneda J.N., Michel M.A., Gersch M., Johnson C.M., Freund S.M., Komander D.
    EMBO J. 34:307-325(2015) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-65.

Entry informationi

Entry nameiUBB_HUMAN
AccessioniPrimary (citable) accession number: P0CG47
Secondary accession number(s): P02248
, P02249, P02250, P62988, Q29120, Q6LBL4, Q6LDU5, Q8WYN8, Q91887, Q91888, Q9BWD6, Q9BX98, Q9UEF2, Q9UEG1, Q9UEK8, Q9UPK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: August 10, 2010
Last modified: April 13, 2016
This is version 64 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

Ubiquitin is encoded by 4 different genes. UBA52 and RPS27A genes code for a single copy of ubiquitin fused to the ribosomal proteins L40 and S27a, respectively. UBB and UBC genes code for a polyubiquitin precursor with exact head to tail repeats, the number of repeats differ between species and strains.
The mRNA encoding variant UBB(+1) is produced by an unknown mechanism involving the deletion of a GT dinucleotide in the close proximity of a GAGAG motif (PubMed:9422699). This variant mRNA is found in normal brain, but the encoded protein accumulates only in brain neurofibrillary tangles and neuritic plaques in Alzheimer disease and other tauopathies, as well as polyglutaminopathies (PubMed:14597671). UBB(+1) variant cannot be used for polyubiquitination, is not effectively degraded by the proteasome when ubiquitinated and ubiquitinated UBB(+1) is refractory to disassembly by deubiquitinating enzymes (DUBs). In healthy brain, UBB(+1) C-terminus can be cleaved by UCHL3 (PubMed:21762696).3 Publications
For a better understanding, features related to ubiquitin are only indicated for the first chain.

Keywords - Technical termi

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

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.