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Protein

Polyubiquitin-C

Gene

UBC

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 - Molecular functioni

  • poly(A) RNA binding Source: UniProtKB
  • protease binding Source: UniProtKB

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-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-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-69481. G2/M Checkpoints.
R-HSA-69541. Stabilization of p53.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8849469. PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-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-977225. Amyloid fiber formation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Names & Taxonomyi

Protein namesi
Recommended name:
Polyubiquitin-C
Cleaved into the following chain:
Gene namesi
Name:UBC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 12

Organism-specific databases

HGNCiHGNC:12468. UBC.

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
  • myelin sheath Source: Ensembl
  • 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

Polymorphism and mutation databases

DMDMi391358178.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 7676UbiquitinPRO_0000396178Add
BLAST
Chaini77 – 15276UbiquitinPRO_0000396179Add
BLAST
Chaini153 – 22876UbiquitinPRO_0000396180Add
BLAST
Chaini229 – 30476UbiquitinPRO_0000396181Add
BLAST
Chaini305 – 38076UbiquitinPRO_0000396182Add
BLAST
Chaini381 – 45676UbiquitinPRO_0000396183Add
BLAST
Chaini457 – 53276UbiquitinPRO_0000396184Add
BLAST
Chaini533 – 60876UbiquitinPRO_0000396185Add
BLAST
Chaini609 – 68476UbiquitinPRO_0000396186Add
BLAST
Propeptidei685 – 6851PRO_0000396187

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-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

EPDiP0CG48.
PaxDbiP0CG48.
PeptideAtlasiP0CG48.
PRIDEiP0CG48.
TopDownProteomicsiP0CG48.

PTM databases

iPTMnetiP0CG48.
PhosphoSiteiP0CG48.
SwissPalmiP0CG48.

Expressioni

Gene expression databases

BgeeiP0CG48.
ExpressionAtlasiP0CG48. baseline and differential.
GenevisibleiP0CG48. HS.

Organism-specific databases

HPAiCAB000362.
CAB005419.
HPA041344.
HPA049132.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
ABCG2Q9UNQ02EBI-3390054,EBI-1569435
ADRBK1P250983EBI-3390054,EBI-3904795
ADRM1Q1618610EBI-3390054,EBI-954387
ASAP1Q9ULH12EBI-3390054,EBI-346622
ASAP2O431502EBI-3390054,EBI-310968
ATXN3P542522EBI-3390054,EBI-946046
BCL2L12Q9HB09-13EBI-3390054,EBI-6968951
BMI1P352262EBI-3390054,EBI-2341576
BUB1BO605663EBI-3390054,EBI-1001438
CDK1P064936EBI-3390054,EBI-444308
CSF3RQ990622EBI-3390054,EBI-7331284
DAXXQ9UER72EBI-3390054,EBI-77321
DDI1P400872EBI-3390054,EBI-5717From a different organism.
DENRO435833EBI-3390054,EBI-716083
DSK2P485102EBI-3390054,EBI-6174From a different organism.
DTX1Q86Y012EBI-3390054,EBI-1755174
ELAVL1Q157174EBI-3390054,EBI-374260
Fzd4Q610883EBI-3390054,EBI-7987880From a different organism.
IKBKGQ9Y6K94EBI-3390054,EBI-81279
IkbkgO885223EBI-3390054,EBI-998011From a different organism.
KLF5Q138872EBI-3390054,EBI-2696013
LCKP062392EBI-3390054,EBI-1348
LEPRP48357-32EBI-3390054,EBI-7886448
MALT1Q9UDY84EBI-3390054,EBI-1047372
MAP3K4Q9Y6R42EBI-3390054,EBI-448104
MAP3K7O433184EBI-3390054,EBI-358684
MARCH5Q9NX472EBI-3390054,EBI-2341610
MDM2Q009876EBI-3390054,EBI-389668
MYCP011065EBI-3390054,EBI-447544
NCK2O436392EBI-3390054,EBI-713635
NFATC4Q149343EBI-3390054,EBI-3905796
NFKBIAP259633EBI-3390054,EBI-307386
PARP1P098742EBI-3390054,EBI-355676
PCGF2P352272EBI-3390054,EBI-2129767
POLHQ9Y2534EBI-3390054,EBI-2827270
POLIQ9UNA44EBI-3390054,EBI-741774
PRKCAP172522EBI-3390054,EBI-1383528
PSMD4P550368EBI-3390054,EBI-359318
RAD23P326284EBI-3390054,EBI-14668From a different organism.
RAD23BP547274EBI-3390054,EBI-954531
RAD23CQ84L312EBI-3390054,EBI-4437395From a different organism.
RAP1BP612242EBI-3390054,EBI-358143
Rbck1Q629212EBI-3390054,EBI-7266339From a different organism.
RDH12Q96NR82EBI-3390054,EBI-3916363
RELAQ042066EBI-3390054,EBI-73886
revP043252EBI-3390054,EBI-7061954From a different organism.
RPN10P550342EBI-3390054,EBI-2620423From a different organism.
RPN13O487269EBI-3390054,EBI-7710745From a different organism.
RYBPQ8N4883EBI-3390054,EBI-752324
SENP3Q9H4L42EBI-3390054,EBI-2880236
SH3KBP1Q96B976EBI-3390054,EBI-346595
SNX9Q9Y5X12EBI-3390054,EBI-77848
SQSTM1Q135013EBI-3390054,EBI-307104
STAMQ927832EBI-3390054,EBI-752333
TAX1BP1Q86VP15EBI-3390054,EBI-529518
TP53P0463715EBI-3390054,EBI-366083
TRAF6Q9Y4K33EBI-3390054,EBI-359276
Trpv4Q9EPK83EBI-3390054,EBI-7091763From a different organism.
UBQLN1Q9UMX03EBI-3390054,EBI-741480
XIAPP981703EBI-3390054,EBI-517127
ZFAND5O760803EBI-3390054,EBI-8028844
ZRANB1Q9UGI02EBI-3390054,EBI-527853

GO - Molecular functioni

  • protease binding Source: UniProtKB

Protein-protein interaction databases

BioGridi113164. 1435 interactions.
IntActiP0CG48. 169 interactions.
MINTiMINT-97475.
STRINGi9606.ENSP00000344818.

Structurei

Secondary structure

1
685
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi534 – 5396Combined sources
Beta strandi540 – 5423Combined sources
Beta strandi544 – 5485Combined sources
Helixi555 – 56511Combined sources
Beta strandi568 – 5703Combined sources
Beta strandi573 – 5775Combined sources
Beta strandi579 – 5813Combined sources
Beta strandi586 – 5883Combined sources
Helixi589 – 5913Combined sources
Beta strandi598 – 6036Combined sources
Beta strandi610 – 6156Combined sources
Beta strandi616 – 6183Combined sources
Beta strandi620 – 6245Combined sources
Beta strandi627 – 6304Combined sources
Helixi631 – 64212Combined sources
Helixi646 – 6483Combined sources
Beta strandi649 – 6535Combined sources
Beta strandi654 – 6574Combined sources
Beta strandi660 – 6634Combined sources
Helixi664 – 6674Combined sources
Beta strandi674 – 6796Combined sources

3D structure databases

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

Miscellaneous databases

EvolutionaryTraceiP0CG48.

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
Domaini229 – 30476Ubiquitin-like 4PROSITE-ProRule annotationAdd
BLAST
Domaini305 – 38076Ubiquitin-like 5PROSITE-ProRule annotationAdd
BLAST
Domaini381 – 45676Ubiquitin-like 6PROSITE-ProRule annotationAdd
BLAST
Domaini457 – 53276Ubiquitin-like 7PROSITE-ProRule annotationAdd
BLAST
Domaini533 – 60876Ubiquitin-like 8PROSITE-ProRule annotationAdd
BLAST
Domaini609 – 68476Ubiquitin-like 9PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the ubiquitin family.Curated
Contains 9 ubiquitin-like domains.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00810000125435.
InParanoidiP0CG48.
KOiK08770.
OMAiTTINIKY.
OrthoDBiEOG7JDR1W.
TreeFamiTF354256.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 9 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 9 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 9 hits.
PROSITEiPS00299. UBIQUITIN_1. 9 hits.
PS50053. UBIQUITIN_2. 9 hits.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P0CG48-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL
60 70 80 90 100
EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE
110 120 130 140 150
NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR
160 170 180 190 200
GGMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK
210 220 230 240 250
QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT
260 270 280 290 300
IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR
310 320 330 340 350
LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA
360 370 380 390 400
GKQLEDGRTL SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS
410 420 430 440 450
DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV
460 470 480 490 500
LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
510 520 530 540 550
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE
560 570 580 590 600
PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH
610 620 630 640 650
LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR
660 670 680
LIFAGKQLED GRTLSDYNIQ KESTLHLVLR LRGGV
Length:685
Mass (Da):77,039
Last modified:June 13, 2012 - v3
Checksum:iB6E7BC06FEE77196
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti190 – 1901P → S in AC126309 (PubMed:16541075).Curated
Sequence conflicti397 – 3971V → G in BAA09860 (PubMed:8917096).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26880 mRNA. Translation: AAA36789.1.
AB009010 mRNA. Translation: BAA23632.1.
AB089613 Genomic DNA. Translation: BAC56951.1.
AC126309 Genomic DNA. No translation available.
BC039193 mRNA. Translation: AAH39193.1.
D63791 Genomic DNA. Translation: BAA09860.1.
AB003730 Genomic DNA. Translation: BAA23486.1.
M17597 mRNA. Translation: AAA36787.1.
CCDSiCCDS9260.1.
PIRiA02574. UQHU.
A22005. UQHUC.
A29526.
RefSeqiNP_066289.3. NM_021009.6.
UniGeneiHs.520348.
Hs.707528.
Hs.731841.

Genome annotation databases

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

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M26880 mRNA. Translation: AAA36789.1.
AB009010 mRNA. Translation: BAA23632.1.
AB089613 Genomic DNA. Translation: BAC56951.1.
AC126309 Genomic DNA. No translation available.
BC039193 mRNA. Translation: AAH39193.1.
D63791 Genomic DNA. Translation: BAA09860.1.
AB003730 Genomic DNA. Translation: BAA23486.1.
M17597 mRNA. Translation: AAA36787.1.
CCDSiCCDS9260.1.
PIRiA02574. UQHU.
A22005. UQHUC.
A29526.
RefSeqiNP_066289.3. NM_021009.6.
UniGeneiHs.520348.
Hs.707528.
Hs.731841.

3D structure databases

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

Protein-protein interaction databases

BioGridi113164. 1435 interactions.
IntActiP0CG48. 169 interactions.
MINTiMINT-97475.
STRINGi9606.ENSP00000344818.

PTM databases

iPTMnetiP0CG48.
PhosphoSiteiP0CG48.
SwissPalmiP0CG48.

Polymorphism and mutation databases

DMDMi391358178.

Proteomic databases

EPDiP0CG48.
PaxDbiP0CG48.
PeptideAtlasiP0CG48.
PRIDEiP0CG48.
TopDownProteomicsiP0CG48.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi7316.
GeneCardsiUBC.
HGNCiHGNC:12468. UBC.
HPAiCAB000362.
CAB005419.
HPA041344.
HPA049132.
MIMi191340. gene.
neXtProtiNX_P0CG48.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG0001. Eukaryota.
COG5272. LUCA.
GeneTreeiENSGT00810000125435.
InParanoidiP0CG48.
KOiK08770.
OMAiTTINIKY.
OrthoDBiEOG7JDR1W.
TreeFamiTF354256.

Enzyme and pathway databases

ReactomeiR-HSA-110312. Translesion synthesis by REV1.
R-HSA-110314. Recognition of DNA damage by PCNA-containing replication complex.
R-HSA-110320. Translesion Synthesis by POLH.
R-HSA-1169091. Activation of NF-kappaB in B cells.
R-HSA-1169408. ISG15 antiviral mechanism.
R-HSA-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-6804756. Regulation of TP53 Activity through Phosphorylation.
R-HSA-6804757. Regulation of TP53 Degradation.
R-HSA-6804760. Regulation of TP53 Activity through Methylation.
R-HSA-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-69481. G2/M Checkpoints.
R-HSA-69541. Stabilization of p53.
R-HSA-69601. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
R-HSA-8849469. PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
R-HSA-8852276. The role of GTSE1 in G2/M progression after G2 checkpoint.
R-HSA-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-977225. Amyloid fiber formation.
R-HSA-983168. Antigen processing: Ubiquitination & Proteasome degradation.

Miscellaneous databases

ChiTaRSiUBC. human.
EvolutionaryTraceiP0CG48.
GeneWikiiUbiquitin_C.
GenomeRNAii7316.
PROiP0CG48.
SOURCEiSearch...

Gene expression databases

BgeeiP0CG48.
ExpressionAtlasiP0CG48. baseline and differential.
GenevisibleiP0CG48. HS.

Family and domain databases

InterProiIPR019956. Ubiquitin.
IPR029071. Ubiquitin-rel_dom.
IPR019954. Ubiquitin_CS.
IPR000626. Ubiquitin_dom.
[Graphical view]
PfamiPF00240. ubiquitin. 9 hits.
[Graphical view]
PRINTSiPR00348. UBIQUITIN.
SMARTiSM00213. UBQ. 9 hits.
[Graphical view]
SUPFAMiSSF54236. SSF54236. 9 hits.
PROSITEiPS00299. UBIQUITIN_1. 9 hits.
PS50053. UBIQUITIN_2. 9 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human ubiquitin multigene family: some genes contain multiple directly repeated ubiquitin coding sequences."
    Wiborg O., Pedersen M.S., Wind A., Berglund L.E., Marcker K.A., Vuust J.
    EMBO J. 4:755-759(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human polyubiquitin cDNAs and a ubiquitin-binding assay involving its in vitro translation product."
    Kim N.S., Yamaguchi T., Sekine S., Saeki M., Iwamuro S., Kato S.
    J. Biochem. 124:35-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  3. "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].
  4. "The finished DNA sequence of human chromosome 12."
    Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y., Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C., Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C., Lewis L.R.
    , Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R., Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E., Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y., Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G., Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H., Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S., Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M., Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H., Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q., Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V., Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E., Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K., Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D., Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R., David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E., D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N., Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N., Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R., Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S., LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H., Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P., Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G., Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E., Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S., Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O., Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J., Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A., Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M., Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I., Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A., Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y., Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A., Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F., Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L., Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G., Gibbs R.A.
    Nature 440:346-351(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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, Lung and Placenta.
  6. "Heterogeneous structure of the polyubiquitin gene UbC of HeLa S3 cells."
    Nenoi M., Mita K., Ichimura S., Cartwright I.L., Takahashi E., Yamauchi M., Tsuji H.
    Gene 175:179-185(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-611.
  7. "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.
  8. 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.
  9. "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.
  10. "Higher frequency of concerted evolutionary events in rodents than in man at the polyubiquitin gene VNTR locus."
    Nenoi M., Mita K., Ichimura S., Kawano A.
    Genetics 148:867-876(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 77-685.
  11. "Cloning and sequence analysis of a cDNA encoding poly-ubiquitin in human ovarian granulosa cells."
    Einspanier R., Sharma H.S., Scheit K.H.
    Biochem. Biophys. Res. Commun. 147:581-587(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 417-685.
  12. "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.
  13. "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.
  14. "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.
  15. "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.
  16. "The emerging complexity of protein ubiquitination."
    Komander D.
    Biochem. Soc. Trans. 37:937-953(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: REVIEW, FUNCTION.
  17. Cited for: PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-65.
  18. "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.
  19. Cited for: PHOSPHORYLATION AT SER-65, MUTAGENESIS OF SER-65.
  20. "Structure of ubiquitin refined at 1.8-A resolution."
    Vijay-Kumar S., Bugg C.E., Cook W.J.
    J. Mol. Biol. 194:531-544(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  21. "Synthetic, structural and biological studies of the ubiquitin system: the total chemical synthesis of ubiquitin."
    Ramage R., Green J., Muir T.W., Ogunjobi O.M., Love S., Shaw K.
    Biochem. J. 299:151-158(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  22. "Structure of tetraubiquitin shows how multiubiquitin chains can be formed."
    Cook W.J., Jeffrey L.C., Kasperek E., Pickart C.M.
    J. Mol. Biol. 236:601-609(1994) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.8 ANGSTROMS).
  23. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
  24. "Crystal structure of a UBP-family deubiquitinating enzyme in isolation and in complex with ubiquitin aldehyde."
    Hu M., Li P., Li M., Li W., Yao T., Wu J.-W., Gu W., Cohen R.E., Shi Y.
    Cell 111:1041-1054(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP7.
  25. "Polyubiquitin binding and cross-reactivity in the USP domain deubiquitinase USP21."
    Ye Y., Akutsu M., Reyes-Turcu F., Enchev R.I., Wilkinson K.D., Komander D.
    EMBO Rep. 12:350-357(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.59 ANGSTROMS) OF 1-75 IN COMPLEX WITH USP21.
  26. "Lys11-linked ubiquitin chains adopt compact conformations and are preferentially hydrolyzed by the deubiquitinase Cezanne."
    Bremm A., Freund S.M., Komander D.
    Nat. Struct. Mol. Biol. 17:939-947(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 1-76.
  27. "OTU deubiquitinases reveal mechanisms of linkage specificity and enable ubiquitin chain restriction analysis."
    Mevissen T.E., Hospenthal M.K., Geurink P.P., Elliott P.R., Akutsu M., Arnaudo N., Ekkebus R., Kulathu Y., Wauer T., El Oualid F., Freund S.M., Ovaa H., Komander D.
    Cell 154:169-184(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-76 IN COMPLEX WITH YOD1.
  28. "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: X-RAY CRYSTALLOGRAPHY (1.90 ANGSTROMS) OF 153-228 PHOSPHORYLATED AT SER-65, PHOSPHORYLATION AT SER-65.

Entry informationi

Entry nameiUBC_HUMAN
AccessioniPrimary (citable) accession number: P0CG48
Secondary accession number(s): P02248
, P02249, P02250, P62988, Q29120, Q6LBL4, Q6LDU5, Q8WYN8, Q91887, Q91888, Q9BWD6, Q9BX98, Q9UEF2, Q9UEG1, Q9UEK8, Q9UPK7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 10, 2010
Last sequence update: June 13, 2012
Last modified: July 6, 2016
This is version 69 of the entry and version 3 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.
For the sake of clarity sequence features are annotated only for the first chain, and are not repeated for each of the following chains.

Keywords - Technical termi

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

Documents

  1. Human chromosome 12
    Human chromosome 12: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.