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P0CG48

- UBC_HUMAN

UniProt

P0CG48 - UBC_HUMAN

Protein

Polyubiquitin-C

Gene

UBC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 48 (01 Oct 2014)
      Sequence version 3 (13 Jun 2012)
      Previous versions | rss
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    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

    1. poly(A) RNA binding Source: UniProtKB
    2. protease binding Source: UniProtKB
    3. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of MAPK activity Source: Reactome
    2. anaphase-promoting complex-dependent proteasomal ubiquitin-dependent protein catabolic process Source: Reactome
    3. antigen processing and presentation of exogenous peptide antigen via MHC class I Source: Reactome
    4. antigen processing and presentation of exogenous peptide antigen via MHC class I, TAP-dependent Source: Reactome
    5. antigen processing and presentation of peptide antigen via MHC class I Source: Reactome
    6. apoptotic process Source: Reactome
    7. apoptotic signaling pathway Source: Reactome
    8. carbohydrate metabolic process Source: Reactome
    9. cellular response to hypoxia Source: Reactome
    10. cytokine-mediated signaling pathway Source: Reactome
    11. DNA damage response, signal transduction by p53 class mediator resulting in cell cycle arrest Source: Reactome
    12. DNA repair Source: Reactome
    13. endosomal transport Source: Reactome
    14. epidermal growth factor receptor signaling pathway Source: Reactome
    15. Fc-epsilon receptor signaling pathway Source: Reactome
    16. fibroblast growth factor receptor signaling pathway Source: Reactome
    17. G1/S transition of mitotic cell cycle Source: Reactome
    18. G2/M transition of mitotic cell cycle Source: Reactome
    19. gene expression Source: Reactome
    20. glucose metabolic process Source: Reactome
    21. glycogen biosynthetic process Source: Reactome
    22. I-kappaB kinase/NF-kappaB signaling Source: Reactome
    23. innate immune response Source: Reactome
    24. intracellular transport of virus Source: Reactome
    25. ion transmembrane transport Source: Reactome
    26. JNK cascade Source: Reactome
    27. membrane organization Source: Reactome
    28. mitotic cell cycle Source: Reactome
    29. mRNA metabolic process Source: Reactome
    30. MyD88-dependent toll-like receptor signaling pathway Source: Reactome
    31. MyD88-independent toll-like receptor signaling pathway Source: Reactome
    32. negative regulation of apoptotic process Source: Reactome
    33. negative regulation of epidermal growth factor receptor signaling pathway Source: Reactome
    34. negative regulation of transcription from RNA polymerase II promoter Source: Reactome
    35. negative regulation of transforming growth factor beta receptor signaling pathway Source: Reactome
    36. negative regulation of type I interferon production Source: Reactome
    37. negative regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    38. neurotrophin TRK receptor signaling pathway Source: Reactome
    39. Notch receptor processing Source: Reactome
    40. Notch signaling pathway Source: Reactome
    41. nucleotide-binding domain, leucine rich repeat containing receptor signaling pathway Source: Reactome
    42. nucleotide-binding oligomerization domain containing signaling pathway Source: Reactome
    43. positive regulation of apoptotic process Source: Reactome
    44. positive regulation of I-kappaB kinase/NF-kappaB signaling Source: Reactome
    45. positive regulation of NF-kappaB transcription factor activity Source: Reactome
    46. positive regulation of transcription from RNA polymerase II promoter Source: Reactome
    47. positive regulation of type I interferon production Source: Reactome
    48. positive regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    49. protein polyubiquitination Source: Reactome
    50. regulation of apoptotic process Source: Reactome
    51. regulation of transcription from RNA polymerase II promoter in response to hypoxia Source: Reactome
    52. regulation of type I interferon production Source: Reactome
    53. regulation of ubiquitin-protein ligase activity involved in mitotic cell cycle Source: Reactome
    54. RNA metabolic process Source: Reactome
    55. small molecule metabolic process Source: Reactome
    56. stress-activated MAPK cascade Source: Reactome
    57. T cell receptor signaling pathway Source: Reactome
    58. toll-like receptor 10 signaling pathway Source: Reactome
    59. toll-like receptor 2 signaling pathway Source: Reactome
    60. toll-like receptor 3 signaling pathway Source: Reactome
    61. toll-like receptor 4 signaling pathway Source: Reactome
    62. toll-like receptor 5 signaling pathway Source: Reactome
    63. toll-like receptor 9 signaling pathway Source: Reactome
    64. toll-like receptor signaling pathway Source: Reactome
    65. toll-like receptor TLR1:TLR2 signaling pathway Source: Reactome
    66. toll-like receptor TLR6:TLR2 signaling pathway Source: Reactome
    67. transcription, DNA-templated Source: Reactome
    68. transcription initiation from RNA polymerase II promoter Source: Reactome
    69. transforming growth factor beta receptor signaling pathway Source: Reactome
    70. transmembrane transport Source: Reactome
    71. TRIF-dependent toll-like receptor signaling pathway Source: Reactome
    72. viral life cycle Source: Reactome
    73. viral process Source: Reactome
    74. viral protein processing Source: Reactome
    75. virion assembly Source: Reactome

    Enzyme and pathway databases

    ReactomeiREACT_111080. Spry regulation of FGF signaling.
    REACT_111178. ER-Phagosome pathway.
    REACT_111184. Negative regulation of FGFR signaling.
    REACT_1156. Orc1 removal from chromatin.
    REACT_115662. Downregulation of ERBB2:ERBB3 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115828. Downregulation of ERBB4 signaling.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_115893. Membrane binding and targetting of GAG proteins.
    REACT_1181. Association of licensing factors with the pre-replicative complex.
    REACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_12484. EGFR downregulation.
    REACT_12555. Downstream TCR signaling.
    REACT_13415. p75NTR recruits signalling complexes.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_150471. Separation of Sister Chromatids.
    REACT_160089. Constitutive Signaling by NOTCH1 HD Domain Mutants.
    REACT_160189. Stimuli-sensing channels.
    REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_163977. Regulation of innate immune responses to cytosolic DNA.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169208. Glycogen synthesis.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_18265. Regulation of the Fanconi anemia pathway.
    REACT_18410. Fanconi Anemia pathway.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_200716. regulation of FZD by ubiquitination.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200766. degradation of AXIN.
    REACT_200777. TCF dependent signaling in response to WNT.
    REACT_200783. Myoclonic epilepsy of Lafora.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    REACT_22442. Interleukin-1 signaling.
    REACT_225574. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_23787. Regulation of signaling by CBL.
    REACT_24918. IRAK1 recruits IKK complex.
    REACT_24941. Circadian Clock.
    REACT_25018. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_25351. TRAF6 mediated induction of TAK1 complex.
    REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_25380. IRAK2 mediated activation of TAK1 complex.
    REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6359. Budding and maturation of HIV virion.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6818. Assembly Of The HIV Virion.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75776. NOD1/2 Signaling Pathway.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_821. Cyclin D associated events in G1.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    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
    ProteomesiUP000005640: Chromosome 12

    Organism-specific databases

    HGNCiHGNC:12468. UBC.

    Subcellular locationi

    Chain Ubiquitin : Cytoplasm By similarity. Nucleus By similarity

    GO - Cellular componenti

    1. cytosol Source: Reactome
    2. endocytic vesicle membrane Source: Reactome
    3. endosome membrane Source: Reactome
    4. nucleoplasm Source: Reactome
    5. plasma membrane Source: Reactome

    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. 1 Publication

    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-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 PINK11 Publication
    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.6 Publications

    Keywords - PTMi

    Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    PRIDEiP0CG48.

    PTM databases

    PhosphoSiteiP0CG48.

    Expressioni

    Gene expression databases

    ArrayExpressiP0CG48.
    BgeeiP0CG48.

    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

    Protein-protein interaction databases

    BioGridi113164. 10150 interactions.
    IntActiP0CG48. 161 interactions.
    MINTiMINT-97475.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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[»]
    3ZLZX-ray2.90A/B1-76[»]
    3ZNHX-ray2.30B1-75[»]
    3ZNIX-ray2.21D/H/L/P1-76[»]
    3ZNZX-ray1.90B1-152[»]
    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[»]
    4MSMX-ray1.74B/D609-684[»]
    4MSQX-ray1.95B/D609-684[»]
    4NQKX-ray3.70E/F/G/H/I/J608-684[»]
    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

    OrthoDBiEOG7JDR1W.
    TreeFamiTF354256.

    Family and domain databases

    InterProiIPR019956. Ubiquitin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR019954. Ubiquitin_CS.
    [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

    MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL    50
    EDGRTLSDYN IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE 100
    NVKAKIQDKE GIPPDQQRLI FAGKQLEDGR TLSDYNIQKE STLHLVLRLR 150
    GGMQIFVKTL TGKTITLEVE PSDTIENVKA KIQDKEGIPP DQQRLIFAGK 200
    QLEDGRTLSD YNIQKESTLH LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT 250
    IENVKAKIQD KEGIPPDQQR LIFAGKQLED GRTLSDYNIQ KESTLHLVLR 300
    LRGGMQIFVK TLTGKTITLE VEPSDTIENV KAKIQDKEGI PPDQQRLIFA 350
    GKQLEDGRTL SDYNIQKEST LHLVLRLRGG MQIFVKTLTG KTITLEVEPS 400
    DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN IQKESTLHLV 450
    LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI 500
    FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE 550
    PSDTIENVKA KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH 600
    LVLRLRGGMQ IFVKTLTGKT ITLEVEPSDT IENVKAKIQD KEGIPPDQQR 650
    LIFAGKQLED GRTLSDYNIQ KESTLHLVLR LRGGV 685
    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:
    EMBL
    GenBank
    DDBJ
    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.

    Genome annotation databases

    EnsembliENST00000339647; ENSP00000344818; ENSG00000150991.
    ENST00000536769; ENSP00000441543; ENSG00000150991.
    GeneIDi7316.
    UCSCiuc001ugs.4. human.

    Polymorphism databases

    DMDMi391358178.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS9260.1.
    PIRi A02574. UQHU.
    A22005. UQHUC.
    A29526.
    RefSeqi NP_066289.3. NM_021009.6.
    UniGenei Hs.520348.
    Hs.707528.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1C3T NMR - A 1-76 [» ]
    1CMX X-ray 2.25 B/D 1-76 [» ]
    1D3Z NMR - A 1-76 [» ]
    1F9J X-ray 2.70 A/B 1-76 [» ]
    1FXT NMR - B 1-76 [» ]
    1G6J NMR - A 1-76 [» ]
    1GJZ NMR - A/B 1-51 [» ]
    1NBF X-ray 2.30 C/D 1-76 [» ]
    1OGW X-ray 1.32 A 1-76 [» ]
    1Q5W NMR - B 1-76 [» ]
    1S1Q X-ray 2.00 B/D 1-76 [» ]
    1SIF X-ray 2.18 A 6-76 [» ]
    1TBE X-ray 2.40 A/B 1-76 [» ]
    1UBI X-ray 1.80 A 1-76 [» ]
    1UBQ X-ray 1.80 A 1-76 [» ]
    1UD7 NMR - A 1-76 [» ]
    1XD3 X-ray 1.45 B/D 1-75 [» ]
    1XQQ NMR - A 1-76 [» ]
    1YX5 NMR - B 1-76 [» ]
    1YX6 NMR - B 1-76 [» ]
    1ZGU NMR - B 1-76 [» ]
    1ZO6 model - B/C 1-76 [» ]
    2AYO X-ray 3.50 B 1-76 [» ]
    2BGF NMR - A/B 1-76 [» ]
    2DEN NMR - B 1-76 [» ]
    2FUH NMR - B 1-76 [» ]
    2G45 X-ray 1.99 B/E 1-76 [» ]
    2GBJ X-ray 1.35 A/B 1-76 [» ]
    2GBK X-ray 1.99 A/B/C/D 10-76 [» ]
    2GBM X-ray 1.55 A/B/C/D 1-76 [» ]
    2GBN X-ray 1.60 A 1-76 [» ]
    2GBR X-ray 2.00 A/B/C 1-76 [» ]
    2GMI X-ray 2.50 C 1-76 [» ]
    2HTH X-ray 2.70 A 1-76 [» ]
    2IBI X-ray 2.20 B 1-75 [» ]
    2J7Q X-ray 1.80 B/D 1-75 [» ]
    2JF5 X-ray 1.95 A/B 1-76 [» ]
    2JRI NMR - B/C 1-76 [» ]
    2JY6 NMR - A 1-76 [» ]
    2JZZ NMR - A 1-76 [» ]
    2K25 NMR - A 1-75 [» ]
    2K6D NMR - B 1-75 [» ]
    2K8B NMR - A 1-76 [» ]
    2K8C NMR - A 1-76 [» ]
    2KDF NMR - B/C 1-76 [» ]
    2KHW NMR - B 1-76 [» ]
    2KJH NMR - B 1-75 [» ]
    2KLG NMR - A 1-76 [» ]
    2KN5 NMR - A 1-76 [» ]
    2KX0 NMR - A 74-151 [» ]
    2L3Z NMR - A 1-76 [» ]
    2LD9 NMR - A 76-152 [» ]
    2LVO NMR - A 1-76 [» ]
    2LVP NMR - A/B 1-76 [» ]
    2LVQ NMR - A/B 1-76 [» ]
    2LZ6 NMR - A 609-684 [» ]
    2MBO NMR - A/B 609-684 [» ]
    2MBQ NMR - A/B 609-684 [» ]
    2MCN NMR - B 609-684 [» ]
    2MI8 NMR - A 609-684 [» ]
    2MJ5 NMR - A 609-684 [» ]
    2NR2 NMR - A 1-76 [» ]
    2O6V X-ray 2.20 A/B/C/D/E/F/G/H 1-76 [» ]
    2OJR X-ray 2.60 A 1-76 [» ]
    2PE9 NMR - A/B 1-76 [» ]
    2PEA NMR - A/B 1-76 [» ]
    2RR9 NMR - A/B 1-76 [» ]
    2RU6 NMR - A 609-684 [» ]
    2W9N X-ray 2.25 A 1-152 [» ]
    2WDT X-ray 2.30 B/D 1-75 [» ]
    2XEW X-ray 2.20 A/B/C/D/E/F/G/H/I/J/K/L 1-76 [» ]
    2Y5B X-ray 2.70 B/F 1-152 [» ]
    2Z59 NMR - B 1-76 [» ]
    2ZCB X-ray 1.60 A/B/C 1-76 [» ]
    2ZVN X-ray 3.00 A/C/E/G 1-152 [» ]
    2ZVO X-ray 2.90 A/G 1-152 [» ]
    3A33 X-ray 2.20 B 1-76 [» ]
    3ALB X-ray 1.85 A/B/C/D 1-76 [» ]
    3AUL X-ray 2.39 A/B 1-76 [» ]
    3B08 X-ray 1.70 A/D/G/J 1-152 [» ]
    3B0A X-ray 1.90 A/D 1-152 [» ]
    3BY4 X-ray 1.55 B 1-75 [» ]
    3C0R X-ray 2.31 B/D 1-75 [» ]
    3DVG X-ray 2.60 X/Y 1-76 [» ]
    3DVN X-ray 2.70 U/V/X/Y 1-76 [» ]
    3EEC X-ray 3.00 A/B 1-76 [» ]
    3EFU X-ray 1.84 A 1-76 [» ]
    3EHV X-ray 1.81 A/B/C 1-76 [» ]
    3H7P X-ray 1.90 A/B 1-76 [» ]
    3H7S X-ray 2.30 A/B 1-76 [» ]
    3HM3 X-ray 1.96 A/B/C/D 1-76 [» ]
    3I3T X-ray 2.59 B/D/F/H 1-75 [» ]
    3IFW X-ray 2.40 B 1-75 [» ]
    3IHP X-ray 2.80 C/D 1-75 [» ]
    3JSV X-ray 2.70 A/B 1-76 [» ]
    3JVZ X-ray 3.30 X/Y 1-76 [» ]
    3JW0 X-ray 3.10 X/Y 1-76 [» ]
    3K9O X-ray 1.80 B 76-151 [» ]
    3K9P X-ray 2.80 B 1-76 [» ]
    3KVF X-ray 2.80 B 1-75 [» ]
    3KW5 X-ray 2.83 B 1-75 [» ]
    3LDZ X-ray 2.60 E/F/G 1-73 [» ]
    3MHS X-ray 1.89 D 1-76 [» ]
    3MTN X-ray 2.70 B/D 1-76 [» ]
    3N30 X-ray 3.00 A/B 1-76 [» ]
    3N32 X-ray 1.80 A 1-76 [» ]
    3N3K X-ray 2.60 B 5-76 [» ]
    3NS8 X-ray 1.71 A/B 1-76 [» ]
    3O65 X-ray 2.70 B/D/F/H 1-75 [» ]
    3OFI X-ray 2.35 C/D 1-76 [» ]
    3OJ3 X-ray 2.50 A/B/C/D/E/F/G/H 1-76 [» ]
    3OJ4 X-ray 3.40 B/E 1-76 [» ]
    3ONS X-ray 1.80 A 1-72 [» ]
    3PRM X-ray 2.30 B/D 1-75 [» ]
    3PT2 X-ray 2.50 B 1-75 [» ]
    3PTF X-ray 2.70 C/D 1-76 [» ]
    3Q3F X-ray 2.17 A 2-76 [» ]
    3RUL X-ray 2.50 A/B/C/D 1-75 [» ]
    3TMP X-ray 1.91 B/D/F/H 1-76 [» ]
    3U30 X-ray 2.43 A/D 1-152 [» ]
    3UGB X-ray 2.35 B 1-76 [» ]
    3V6C X-ray 1.70 B 74-150 [» ]
    3V6E X-ray 2.10 B 74-150 [» ]
    3VFK X-ray 2.80 A 1-75 [» ]
    3VUW X-ray 1.95 A/B/C 1-76 [» ]
    3VUX X-ray 1.70 A/B/C 1-76 [» ]
    3VUY X-ray 1.98 A/B/C 1-76 [» ]
    3ZLZ X-ray 2.90 A/B 1-76 [» ]
    3ZNH X-ray 2.30 B 1-75 [» ]
    3ZNI X-ray 2.21 D/H/L/P 1-76 [» ]
    3ZNZ X-ray 1.90 B 1-152 [» ]
    4AUQ X-ray 2.18 C/F 1-76 [» ]
    4BOS X-ray 2.35 C/E 609-684 [» ]
    F 612-625 [» ]
    4BOZ X-ray 3.03 B/C/E 1-76 [» ]
    4BVU X-ray 2.70 C 609-684 [» ]
    4DDG X-ray 3.30 D/E/F/G/H/I/M/N/O/P/Q/R 1-76 [» ]
    4DDI X-ray 3.80 G/H/I/J/K/L 1-76 [» ]
    4DHJ X-ray 2.35 B/F/J/M 1-76 [» ]
    D/H 1-75 [» ]
    4DHZ X-ray 3.11 B 1-76 [» ]
    E 1-75 [» ]
    4FJV X-ray 2.05 B/D 1-76 [» ]
    4HK2 X-ray 1.40 A/B/C/D 1-76 [» ]
    4HXD X-ray 2.85 A/C 1-75 [» ]
    4I6L X-ray 2.49 B 77-150 [» ]
    4I6N X-ray 1.70 B/D 1-75 [» ]
    4IG7 X-ray 2.00 B 1-75 [» ]
    4IUM X-ray 1.45 B 1-75 [» ]
    4JQW X-ray 2.90 C 609-684 [» ]
    4K1R X-ray 1.63 B/D 607-684 [» ]
    4K7S X-ray 1.76 A/B/C 1-76 [» ]
    4K7U X-ray 1.76 A/B/C 1-76 [» ]
    4K7W X-ray 1.76 A/B/C 1-76 [» ]
    4KSK X-ray 2.40 C/D 76-152 [» ]
    4KSL X-ray 2.83 C/D/F/H/J/L/N/P/R/T/V/X 76-228 [» ]
    4LCD X-ray 3.10 E/F 609-683 [» ]
    4LDT X-ray 1.90 B/D 609-684 [» ]
    4MDK X-ray 2.61 E/F/G/H 608-684 [» ]
    4MSM X-ray 1.74 B/D 609-684 [» ]
    4MSQ X-ray 1.95 B/D 609-684 [» ]
    4NQK X-ray 3.70 E/F/G/H/I/J 608-684 [» ]
    ProteinModelPortali P0CG48.
    SMRi P0CG48. Positions 1-683.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113164. 10150 interactions.
    IntActi P0CG48. 161 interactions.
    MINTi MINT-97475.

    PTM databases

    PhosphoSitei P0CG48.

    Polymorphism databases

    DMDMi 391358178.

    Proteomic databases

    PRIDEi P0CG48.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000339647 ; ENSP00000344818 ; ENSG00000150991 .
    ENST00000536769 ; ENSP00000441543 ; ENSG00000150991 .
    GeneIDi 7316.
    UCSCi uc001ugs.4. human.

    Organism-specific databases

    CTDi 7316.
    GeneCardsi GC12M125396.
    HGNCi HGNC:12468. UBC.
    HPAi CAB000362.
    CAB005419.
    HPA041344.
    HPA049132.
    MIMi 191340. gene.
    neXtProti NX_P0CG48.
    GenAtlasi Search...

    Phylogenomic databases

    OrthoDBi EOG7JDR1W.
    TreeFami TF354256.

    Enzyme and pathway databases

    Reactomei REACT_111080. Spry regulation of FGF signaling.
    REACT_111178. ER-Phagosome pathway.
    REACT_111184. Negative regulation of FGFR signaling.
    REACT_1156. Orc1 removal from chromatin.
    REACT_115662. Downregulation of ERBB2:ERBB3 signaling.
    REACT_115755. Signaling by ERBB2.
    REACT_115828. Downregulation of ERBB4 signaling.
    REACT_115831. ISG15 antiviral mechanism.
    REACT_115852. Signaling by constitutively active EGFR.
    REACT_115893. Membrane binding and targetting of GAG proteins.
    REACT_1181. Association of licensing factors with the pre-replicative complex.
    REACT_118614. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_118656. Activation of NF-kappaB in B cells.
    REACT_118780. NOTCH1 Intracellular Domain Regulates Transcription.
    REACT_120726. TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
    REACT_120727. Downregulation of TGF-beta receptor signaling.
    REACT_120734. SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
    REACT_120916. Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
    REACT_121111. Downregulation of SMAD2/3:SMAD4 transcriptional activity.
    REACT_1221. CDK-mediated phosphorylation and removal of Cdc6.
    REACT_12484. EGFR downregulation.
    REACT_12555. Downstream TCR signaling.
    REACT_13415. p75NTR recruits signalling complexes.
    REACT_13464. Regulation of activated PAK-2p34 by proteasome mediated degradation.
    REACT_13643. NRIF signals cell death from the nucleus.
    REACT_13696. NF-kB is activated and signals survival.
    REACT_150471. Separation of Sister Chromatids.
    REACT_160089. Constitutive Signaling by NOTCH1 HD Domain Mutants.
    REACT_160189. Stimuli-sensing channels.
    REACT_160205. NOTCH2 Activation and Transmission of Signal to the Nucleus.
    REACT_160243. Constitutive Signaling by NOTCH1 PEST Domain Mutants.
    REACT_160254. Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
    REACT_160315. Regulation of PLK1 Activity at G2/M Transition.
    REACT_1614. Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
    REACT_163977. Regulation of innate immune responses to cytosolic DNA.
    REACT_163994. FCERI mediated NF-kB activation.
    REACT_169168. Senescence-Associated Secretory Phenotype (SASP).
    REACT_169208. Glycogen synthesis.
    REACT_169325. Oncogene Induced Senescence.
    REACT_169436. Oxidative Stress Induced Senescence.
    REACT_172638. Asymmetric localization of PCP proteins.
    REACT_18265. Regulation of the Fanconi anemia pathway.
    REACT_18410. Fanconi Anemia pathway.
    REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
    REACT_199384. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_200716. regulation of FZD by ubiquitination.
    REACT_200731. deactivation of the beta-catenin transactivating complex.
    REACT_200766. degradation of AXIN.
    REACT_200777. TCF dependent signaling in response to WNT.
    REACT_200783. Myoclonic epilepsy of Lafora.
    REACT_200841. degradation of DVL.
    REACT_20549. Autodegradation of the E3 ubiquitin ligase COP1.
    REACT_21281. TAK1 activates NFkB by phosphorylation and activation of IKKs complex.
    REACT_21368. JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
    REACT_21399. activated TAK1 mediates p38 MAPK activation.
    REACT_22442. Interleukin-1 signaling.
    REACT_225574. Activated NOTCH1 Transmits Signal to the Nucleus.
    REACT_23787. Regulation of signaling by CBL.
    REACT_24918. IRAK1 recruits IKK complex.
    REACT_24941. Circadian Clock.
    REACT_25018. IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
    REACT_25120. TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
    REACT_25148. Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
    REACT_25271. Negative regulators of RIG-I/MDA5 signaling.
    REACT_25325. AUF1 (hnRNP D0) destabilizes mRNA.
    REACT_25351. TRAF6 mediated induction of TAK1 complex.
    REACT_25354. IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
    REACT_25359. RIG-I/MDA5 mediated induction of IFN-alpha/beta pathways.
    REACT_25374. IKK complex recruitment mediated by RIP1.
    REACT_25380. IRAK2 mediated activation of TAK1 complex.
    REACT_27258. Endosomal Sorting Complex Required For Transport (ESCRT).
    REACT_4. Ubiquitin-dependent degradation of Cyclin D1.
    REACT_6359. Budding and maturation of HIV virion.
    REACT_6761. APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
    REACT_6785. Autodegradation of Cdh1 by Cdh1:APC/C.
    REACT_6818. Assembly Of The HIV Virion.
    REACT_6820. APC/C:Cdc20 mediated degradation of Cyclin B.
    REACT_6821. SCF-beta-TrCP mediated degradation of Emi1.
    REACT_6871. APC/C:Cdc20 mediated degradation of Securin.
    REACT_75776. NOD1/2 Signaling Pathway.
    REACT_75842. Antigen processing: Ubiquitination & Proteasome degradation.
    REACT_821. Cyclin D associated events in G1.
    REACT_9003. SCF(Skp2)-mediated degradation of p27/p21.
    REACT_9031. Vpu mediated degradation of CD4.
    REACT_9453. Vif-mediated degradation of APOBEC3G.

    Miscellaneous databases

    ChiTaRSi UBC. human.
    EvolutionaryTracei P0CG48.
    GeneWikii Ubiquitin_C.
    NextBioi 33412565.
    PROi P0CG48.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P0CG48.
    Bgeei P0CG48.

    Family and domain databases

    InterProi IPR019956. Ubiquitin.
    IPR000626. Ubiquitin-like.
    IPR029071. Ubiquitin-rel_dom.
    IPR019954. Ubiquitin_CS.
    [Graphical view ]
    Pfami PF00240. ubiquitin. 9 hits.
    [Graphical view ]
    PRINTSi PR00348. UBIQUITIN.
    SMARTi SM00213. UBQ. 9 hits.
    [Graphical view ]
    SUPFAMi SSF54236. SSF54236. 9 hits.
    PROSITEi PS00299. UBIQUITIN_1. 9 hits.
    PS50053. UBIQUITIN_2. 9 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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).
    19. "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).
    20. "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).
    21. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS).
    22. "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.
    23. "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.
    24. "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.
    25. "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.

    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: October 1, 2014
    This is version 48 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

    External Data

    Dasty 3