UBB_HUMAN
ID UBB_HUMAN Reviewed; 229 AA.
AC P0CG47; P02248; P02249; P02250; P62988; Q29120; Q6LBL4; Q6LDU5; Q8WYN8;
AC Q91887; Q91888; Q9BWD6; Q9BX98; Q9UEF2; Q9UEG1; Q9UEK8; Q9UPK7;
DT 10-AUG-2010, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 1.
DT 03-AUG-2022, entry version 115.
DE RecName: Full=Polyubiquitin-B;
DE Contains:
DE RecName: Full=Ubiquitin;
DE Flags: Precursor;
GN Name=UBB;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RC TISSUE=Blood;
RX PubMed=3029682; DOI=10.1093/nar/15.2.443;
RA Baker R.T., Board P.G.;
RT "The human ubiquitin gene family: structure of a gene and pseudogenes from
RT the Ub B subfamily.";
RL Nucleic Acids Res. 15:443-463(1987).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=14745543; DOI=10.1007/s00239-003-2532-4;
RA Tachikui H., Saitou N., Nakajima T., Hayasaka I., Ishida T., Inoue I.;
RT "Lineage-specific homogenization of the polyubiquitin gene among human and
RT great apes.";
RL J. Mol. Evol. 57:737-744(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, Liver, and Lung;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP PROTEIN SEQUENCE OF 1-27; 30-42 AND 55-72, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Fetal brain cortex;
RA Lubec G., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [6]
RP PROTEIN SEQUENCE OF 1-74.
RX PubMed=1128706; DOI=10.1038/255423a0;
RA Schlesinger D.H., Goldstein G.;
RT "Molecular conservation of 74 amino acid sequence of ubiquitin between
RT cattle and man.";
RL Nature 255:423-424(1975).
RN [7]
RP PROTEIN SEQUENCE OF 1-27 AND 43-54, UBIQUITINATION AT LYS-6; LYS-11 AND
RP LYS-48, AND IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16443603; DOI=10.1074/jbc.m512786200;
RA Cripps D., Thomas S.N., Jeng Y., Yang F., Davies P., Yang A.J.;
RT "Alzheimer disease-specific conformation of hyperphosphorylated paired
RT helical filament-tau is polyubiquitinated through Lys-48, Lys-11, and Lys-6
RT ubiquitin conjugation.";
RL J. Biol. Chem. 281:10825-10838(2006).
RN [8]
RP FUNCTION, UBIQUITINATION AT LYS-11; LYS-29; LYS-48 AND LYS-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RX PubMed=16543144; DOI=10.1016/j.molcel.2006.02.018;
RA Huang F., Kirkpatrick D., Jiang X., Gygi S.P., Sorkin A.;
RT "Differential regulation of EGF receptor internalization and degradation by
RT multiubiquitination within the kinase domain.";
RL Mol. Cell 21:737-748(2006).
RN [9]
RP UBIQUITINATION AT LYS-27.
RX PubMed=15466860; DOI=10.1074/jbc.m402916200;
RA Okumura F., Hatakeyama S., Matsumoto M., Kamura T., Nakayama K.;
RT "Functional regulation of FEZ1 by the U-box-type ubiquitin ligase E4B
RT contributes to neuritogenesis.";
RL J. Biol. Chem. 279:53533-53543(2004).
RN [10]
RP UBIQUITINATION AT LYS-63, AND MUTAGENESIS OF LYS-48 AND LYS-63.
RX PubMed=18719106; DOI=10.1073/pnas.0805685105;
RA Motegi A., Liaw H.-J., Lee K.-Y., Roest H.P., Maas A., Wu X., Moinova H.,
RA Markowitz S.D., Ding H., Hoeijmakers J.H.J., Myung K.;
RT "Polyubiquitination of proliferating cell nuclear antigen by HLTF and SHPRH
RT prevents genomic instability from stalled replication forks.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:12411-12416(2008).
RN [11]
RP REVIEW, AND FUNCTION.
RX PubMed=19754430; DOI=10.1042/bst0370937;
RA Komander D.;
RT "The emerging complexity of protein ubiquitination.";
RL Biochem. Soc. Trans. 37:937-953(2009).
RN [12]
RP CLEAVAGE BY UCHL3 (VARIANT UBB(+1)).
RX PubMed=21762696; DOI=10.1016/j.febslet.2011.06.037;
RA Dennissen F.J., Kholod N., Hermes D.J., Kemmerling N., Steinbusch H.W.,
RA Dantuma N.P., van Leeuwen F.W.;
RT "Mutant ubiquitin (UBB(+1)) associated with neurodegenerative disorders is
RT hydrolyzed by ubiquitin C-terminal hydrolase L3 (UCH-L3).";
RL FEBS Lett. 585:2568-2574(2011).
RN [13]
RP IDENTIFICATION OF VARIANT UBB(+1).
RX PubMed=9422699; DOI=10.1126/science.279.5348.242;
RA van Leeuwen F.W., de Kleijn D.P., van den Hurk H.H., Neubauer A.,
RA Sonnemans M.A., Sluijs J.A., Koycu S., Ramdjielal R.D., Salehi A.,
RA Martens G.J., Grosveld F.G., Peter J., Burbach H., Hol E.M.;
RT "Frameshift mutants of beta amyloid precursor protein and ubiquitin-B in
RT Alzheimer's and Down patients.";
RL Science 279:242-247(1998).
RN [14]
RP TISSUE SPECIFICITY (VARIANT UBB(+1)).
RX PubMed=14597671; DOI=10.1096/fj.03-0205com;
RA Fischer D.F., De Vos R.A., Van Dijk R., De Vrij F.M., Proper E.A.,
RA Sonnemans M.A., Verhage M.C., Sluijs J.A., Hobo B., Zouambia M.,
RA Steur E.N., Kamphorst W., Hol E.M., Van Leeuwen F.W.;
RT "Disease-specific accumulation of mutant ubiquitin as a marker for
RT proteasomal dysfunction in the brain.";
RL FASEB J. 17:2014-2024(2003).
RN [15]
RP PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX PubMed=24660806; DOI=10.1042/bj20140334;
RA Kazlauskaite A., Kondapalli C., Gourlay R., Campbell D.G., Ritorto M.S.,
RA Hofmann K., Alessi D.R., Knebel A., Trost M., Muqit M.M.;
RT "Parkin is activated by PINK1-dependent phosphorylation of ubiquitin at
RT Ser65.";
RL Biochem. J. 460:127-139(2014).
RN [16]
RP SUBCELLULAR LOCATION, PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX PubMed=24751536; DOI=10.1083/jcb.201402104;
RA Kane L.A., Lazarou M., Fogel A.I., Li Y., Yamano K., Sarraf S.A.,
RA Banerjee S., Youle R.J.;
RT "PINK1 phosphorylates ubiquitin to activate Parkin E3 ubiquitin ligase
RT activity.";
RL J. Cell Biol. 205:143-153(2014).
RN [17]
RP PHOSPHORYLATION AT SER-65, AND MUTAGENESIS OF SER-65.
RX PubMed=24784582; DOI=10.1038/nature13392;
RA Koyano F., Okatsu K., Kosako H., Tamura Y., Go E., Kimura M., Kimura Y.,
RA Tsuchiya H., Yoshihara H., Hirokawa T., Endo T., Fon E.A., Trempe J.F.,
RA Saeki Y., Tanaka K., Matsuda N.;
RT "Ubiquitin is phosphorylated by PINK1 to activate parkin.";
RL Nature 510:162-166(2014).
RN [18]
RP PHOSPHORYLATION AT SER-65.
RX PubMed=25527291; DOI=10.15252/embj.201489847;
RA Wauer T., Swatek K.N., Wagstaff J.L., Gladkova C., Pruneda J.N.,
RA Michel M.A., Gersch M., Johnson C.M., Freund S.M., Komander D.;
RT "Ubiquitin Ser65 phosphorylation affects ubiquitin structure, chain
RT assembly and hydrolysis.";
RL EMBO J. 34:307-325(2015).
RN [19]
RP ADP-RIBOSYLATION AT GLY-76, AND MUTAGENESIS OF HIS-68; ARG-72; ARG-74 AND
RP GLY-76.
RX PubMed=28525742; DOI=10.1016/j.molcel.2017.04.028;
RA Yang C.S., Jividen K., Spencer A., Dworak N., Ni L., Oostdyk L.T.,
RA Chatterjee M., Kusmider B., Reon B., Parlak M., Gorbunova V., Abbas T.,
RA Jeffery E., Sherman N.E., Paschal B.M.;
RT "Ubiquitin Modification by the E3 Ligase/ADP-Ribosyltransferase
RT Dtx3L/Parp9.";
RL Mol. Cell 66:503-516(2017).
RN [20]
RP FUNCTION (UBIQUITIN), AND UBIQUITINATION AT LYS-29.
RX PubMed=34239127; DOI=10.1038/s41589-021-00823-5;
RA Yu Y., Zheng Q., Erramilli S.K., Pan M., Park S., Xie Y., Li J., Fei J.,
RA Kossiakoff A.A., Liu L., Zhao M.;
RT "K29-linked ubiquitin signaling regulates proteotoxic stress response and
RT cell cycle.";
RL Nat. Chem. Biol. 17:896-905(2021).
RN [21] {ECO:0007744|PDB:6BYH, ECO:0007744|PDB:6C16}
RP X-RAY CRYSTALLOGRAPHY (2.61 ANGSTROMS) OF 152-228 IN COMPLEX WITH SKP1;
RP KMD2A AND KMD2B, AND INTERACTION WITH SKP1-KDM2A AND SKP1-KDM2B COMPLEXES.
RX PubMed=30033217; DOI=10.1016/j.str.2018.06.004;
RA Gorelik M., Manczyk N., Pavlenco A., Kurinov I., Sidhu S.S., Sicheri F.;
RT "A Structure-Based Strategy for Engineering Selective Ubiquitin Variant
RT Inhibitors of Skp1-Cul1-F-Box Ubiquitin Ligases.";
RL Structure 26:1226-1236.E3(2018).
RN [22]
RP X-RAY CRYSTALLOGRAPHY (3.03 ANGSTROMS) OF 1-76 IN COMPLEX WITH ZRANB1, AND
RP UBIQUITINATION AT LYS-29.
RX PubMed=25752573; DOI=10.1016/j.molcel.2015.01.041;
RA Kristariyanto Y.A., Abdul Rehman S.A., Campbell D.G., Morrice N.A.,
RA Johnson C., Toth R., Kulathu Y.;
RT "K29-selective ubiquitin binding domain reveals structural basis of
RT specificity and heterotypic nature of K29 polyubiquitin.";
RL Mol. Cell 58:83-94(2015).
RN [23]
RP X-RAY CRYSTALLOGRAPHY (1.68 ANGSTROMS) OF 1-76 IN COMPLEX WITH ZRANB1, AND
RP UBIQUITINATION AT LYS-29 AND LYS-33.
RX PubMed=25752577; DOI=10.1016/j.molcel.2015.01.042;
RA Michel M.A., Elliott P.R., Swatek K.N., Simicek M., Pruneda J.N.,
RA Wagstaff J.L., Freund S.M., Komander D.;
RT "Assembly and specific recognition of K29- and K33-linked polyubiquitin.";
RL Mol. Cell 58:95-109(2015).
RN [24] {ECO:0007744|PDB:5CAW}
RP X-RAY CRYSTALLOGRAPHY (2.62 ANGSTROMS) OF 153-228, AND PHOSPHORYLATION AT
RP SER-65.
RX PubMed=26161729; DOI=10.1038/nature14879;
RA Wauer T., Simicek M., Schubert A., Komander D.;
RT "Mechanism of phospho-ubiquitin-induced PARKIN activation.";
RL Nature 524:370-374(2015).
RN [25]
RP ERRATUM OF PUBMED:26161729.
RX PubMed=26416742; DOI=10.1038/nature15531;
RA Wauer T., Simicek M., Schubert A., Komander D.;
RL Nature 526:728-728(2015).
CC -!- FUNCTION: [Ubiquitin]: Exists either covalently attached to another
CC protein, or free (unanchored). When covalently bound, it is conjugated
CC to target proteins via an isopeptide bond either as a monomer
CC (monoubiquitin), a polymer linked via different Lys residues of the
CC ubiquitin (polyubiquitin chains) or a linear polymer linked via the
CC initiator Met of the ubiquitin (linear polyubiquitin chains).
CC Polyubiquitin chains, when attached to a target protein, have different
CC functions depending on the Lys residue of the ubiquitin that is linked:
CC Lys-6-linked may be involved in DNA repair; Lys-11-linked is involved
CC in ERAD (endoplasmic reticulum-associated degradation) and in cell-
CC cycle regulation; Lys-29-linked is involved in proteotoxic stress
CC response and cell cycle; Lys-33-linked is involved in kinase
CC modification; Lys-48-linked is involved in protein degradation via the
CC proteasome; Lys-63-linked is involved in endocytosis, DNA-damage
CC responses as well as in signaling processes leading to activation of
CC the transcription factor NF-kappa-B. Linear polymer chains formed via
CC attachment by the initiator Met lead to cell signaling. Ubiquitin is
CC usually conjugated to Lys residues of target proteins, however, in rare
CC cases, conjugation to Cys or Ser residues has been observed. When
CC polyubiquitin is free (unanchored-polyubiquitin), it also has distinct
CC roles, such as in activation of protein kinases, and in signaling.
CC {ECO:0000269|PubMed:16543144, ECO:0000269|PubMed:34239127,
CC ECO:0000303|PubMed:19754430}.
CC -!- SUBUNIT: Interacts with SKP1-KMD2A and SKP1-KMD2B complexes.
CC {ECO:0000269|PubMed:30033217}.
CC -!- INTERACTION:
CC P0CG47; P05067: APP; NbExp=3; IntAct=EBI-413034, EBI-77613;
CC P0CG47; Q8IVM0: CCDC50; NbExp=2; IntAct=EBI-413034, EBI-723996;
CC P0CG47; Q9H305: CDIP1; NbExp=3; IntAct=EBI-413034, EBI-2876678;
CC P0CG47; Q15038: DAZAP2; NbExp=7; IntAct=EBI-413034, EBI-724310;
CC P0CG47; Q6ICB0: DESI1; NbExp=3; IntAct=EBI-413034, EBI-2806959;
CC P0CG47; P28562: DUSP1; NbExp=2; IntAct=EBI-413034, EBI-975493;
CC P0CG47; Q9UJY5: GGA1; NbExp=3; IntAct=EBI-413034, EBI-447141;
CC P0CG47; Q9NZ52: GGA3; NbExp=2; IntAct=EBI-413034, EBI-447404;
CC P0CG47; P33993: MCM7; NbExp=2; IntAct=EBI-413034, EBI-355924;
CC P0CG47; Q8N3F0: MTURN; NbExp=3; IntAct=EBI-413034, EBI-11980301;
CC P0CG47; P46934: NEDD4; NbExp=2; IntAct=EBI-413034, EBI-726944;
CC P0CG47; Q96FW1: OTUB1; NbExp=3; IntAct=EBI-413034, EBI-1058491;
CC P0CG47; Q6GQQ9-2: OTUD7B; NbExp=3; IntAct=EBI-413034, EBI-25830200;
CC P0CG47; Q96CS7: PLEKHB2; NbExp=3; IntAct=EBI-413034, EBI-373552;
CC P0CG47; Q9NRQ2: PLSCR4; NbExp=3; IntAct=EBI-413034, EBI-769257;
CC P0CG47; O60260-5: PRKN; NbExp=6; IntAct=EBI-413034, EBI-21251460;
CC P0CG47; Q9UJ41: RABGEF1; NbExp=6; IntAct=EBI-413034, EBI-913954;
CC P0CG47; P54727: RAD23B; NbExp=5; IntAct=EBI-413034, EBI-954531;
CC P0CG47; Q9Y3C5: RNF11; NbExp=3; IntAct=EBI-413034, EBI-396669;
CC P0CG47; Q68DV7: RNF43; NbExp=2; IntAct=EBI-413034, EBI-1647060;
CC P0CG47; Q8N488: RYBP; NbExp=3; IntAct=EBI-413034, EBI-752324;
CC P0CG47; O00560: SDCBP; NbExp=3; IntAct=EBI-413034, EBI-727004;
CC P0CG47; Q9HAU4: SMURF2; NbExp=4; IntAct=EBI-413034, EBI-396727;
CC P0CG47; P00441: SOD1; NbExp=3; IntAct=EBI-413034, EBI-990792;
CC P0CG47; O75886: STAM2; NbExp=3; IntAct=EBI-413034, EBI-373258;
CC P0CG47; O95630: STAMBP; NbExp=4; IntAct=EBI-413034, EBI-396676;
CC P0CG47; Q86VP1: TAX1BP1; NbExp=3; IntAct=EBI-413034, EBI-529518;
CC P0CG47; Q9BSL1: UBAC1; NbExp=4; IntAct=EBI-413034, EBI-749370;
CC P0CG47; Q9UHD9: UBQLN2; NbExp=3; IntAct=EBI-413034, EBI-947187;
CC P0CG47; P45974-2: USP5; NbExp=3; IntAct=EBI-413034, EBI-12072186;
CC P0CG47; Q8NA23-2: WDR31; NbExp=3; IntAct=EBI-413034, EBI-25835937;
CC P0CG47; Q60592: Mast2; Xeno; NbExp=2; IntAct=EBI-413034, EBI-493888;
CC P0CG47; Q9DLK6: NP; Xeno; NbExp=2; IntAct=EBI-413034, EBI-8433218;
CC P0CG47; P24610: Pax3; Xeno; NbExp=2; IntAct=EBI-413034, EBI-1208116;
CC -!- SUBCELLULAR LOCATION: [Ubiquitin]: Cytoplasm {ECO:0000250}. Nucleus
CC {ECO:0000250}. Mitochondrion outer membrane
CC {ECO:0000269|PubMed:24751536}; Peripheral membrane protein
CC {ECO:0000305|PubMed:24751536}.
CC -!- PTM: [Ubiquitin]: Phosphorylated at Ser-65 by PINK1 during mitophagy
CC (PubMed:24660806, PubMed:24751536, PubMed:24784582, PubMed:25527291,
CC PubMed:26161729). Phosphorylated ubiquitin specifically binds and
CC activates parkin (PRKN), triggering mitophagy (PubMed:24660806,
CC PubMed:24751536, PubMed:24784582, PubMed:25527291, PubMed:26161729).
CC Phosphorylation does not affect E1-mediated E2 charging of ubiquitin
CC but affects discharging of E2 enzymes to form polyubiquitin chains. It
CC also affects deubiquitination by deubiquitinase enzymes such as USP30
CC (PubMed:25527291). {ECO:0000269|PubMed:24660806,
CC ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582,
CC ECO:0000269|PubMed:25527291, ECO:0000269|PubMed:26161729}.
CC -!- PTM: [Ubiquitin]: Mono-ADP-ribosylated at the C-terminus by PARP9, a
CC component of the PPAR9-DTX3L complex. ADP-ribosylation requires
CC processing by E1 and E2 enzymes and prevents ubiquitin conjugation to
CC substrates such as histones. {ECO:0000269|PubMed:28525742}.
CC -!- MISCELLANEOUS: Ubiquitin is encoded by 4 different genes. UBA52 and
CC RPS27A genes code for a single copy of ubiquitin fused to the ribosomal
CC proteins L40 and S27a, respectively. UBB and UBC genes code for a
CC polyubiquitin precursor with exact head to tail repeats, the number of
CC repeats differ between species and strains.
CC -!- MISCELLANEOUS: The mRNA encoding variant UBB(+1) is produced by an
CC unknown mechanism involving the deletion of a GT dinucleotide in the
CC close proximity of a GAGAG motif (PubMed:9422699). This variant mRNA is
CC found in normal brain, but the encoded protein accumulates only in
CC brain neurofibrillary tangles and neuritic plaques in Alzheimer disease
CC and other tauopathies, as well as polyglutaminopathies
CC (PubMed:14597671). UBB(+1) variant cannot be used for
CC polyubiquitination, is not effectively degraded by the proteasome when
CC ubiquitinated and ubiquitinated UBB(+1) is refractory to disassembly by
CC deubiquitinating enzymes (DUBs). In healthy brain, UBB(+1) C-terminus
CC can be cleaved by UCHL3 (PubMed:21762696).
CC {ECO:0000305|PubMed:14597671, ECO:0000305|PubMed:21762696,
CC ECO:0000305|PubMed:9422699}.
CC -!- MISCELLANEOUS: For a better understanding, features related to
CC ubiquitin are only indicated for the first chain.
CC -!- SIMILARITY: Belongs to the ubiquitin family. {ECO:0000305}.
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DR EMBL; X04803; CAA28495.1; -; Genomic_DNA.
DR EMBL; AB089617; BAC56955.1; -; Genomic_DNA.
DR EMBL; AC093484; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC000379; AAH00379.1; -; mRNA.
DR EMBL; BC009301; AAH09301.1; -; mRNA.
DR EMBL; BC015127; AAH15127.1; -; mRNA.
DR EMBL; BC026301; AAH26301.1; -; mRNA.
DR EMBL; BC031027; AAH31027.1; -; mRNA.
DR EMBL; BC046123; AAH46123.1; -; mRNA.
DR CCDS; CCDS11177.1; -.
DR PIR; A26437; UQHUB.
DR RefSeq; NP_001268645.1; NM_001281716.1.
DR RefSeq; NP_001268646.1; NM_001281717.1.
DR RefSeq; NP_001268647.1; NM_001281718.1.
DR RefSeq; NP_001268648.1; NM_001281719.1.
DR RefSeq; NP_001268649.1; NM_001281720.1.
DR RefSeq; NP_061828.1; NM_018955.3.
DR PDB; 2KHW; NMR; -; B=153-228.
DR PDB; 2MBB; NMR; -; B=153-228.
DR PDB; 2MRO; NMR; -; A=153-228.
DR PDB; 2MSG; NMR; -; A=153-224.
DR PDB; 2N13; NMR; -; B=153-228, C=153-229.
DR PDB; 4UEL; X-ray; 2.30 A; B=153-228.
DR PDB; 4UF6; X-ray; 3.69 A; B/E/H/K=153-227.
DR PDB; 4WHV; X-ray; 8.30 A; A/F/G/L=153-228.
DR PDB; 4WLR; X-ray; 2.00 A; C=153-228.
DR PDB; 4WUR; X-ray; 3.16 A; B=153-228.
DR PDB; 4XOF; X-ray; 1.15 A; A=153-228.
DR PDB; 4ZFR; X-ray; 1.72 A; B=153-228.
DR PDB; 4ZFT; X-ray; 2.30 A; B/D=153-228.
DR PDB; 4ZPZ; X-ray; 1.54 A; A/B=153-225.
DR PDB; 4ZUX; X-ray; 3.82 A; X/c/h/m=153-228.
DR PDB; 5BNB; X-ray; 2.49 A; E/F/G/I=153-229.
DR PDB; 5CAW; X-ray; 2.62 A; B/D=153-228.
DR PDB; 5CRA; X-ray; 2.64 A; C/D=153-227.
DR PDB; 5CVM; X-ray; 1.90 A; B=153-211.
DR PDB; 5CVN; X-ray; 3.36 A; D=153-228.
DR PDB; 5CVO; X-ray; 3.88 A; C/F=153-228.
DR PDB; 5D0K; X-ray; 2.65 A; B/E/H/K=153-228.
DR PDB; 5D0M; X-ray; 1.91 A; B=153-228.
DR PDB; 5DFL; X-ray; 2.10 A; B=153-228.
DR PDB; 5DK8; X-ray; 1.32 A; A/B=154-227.
DR PDB; 5E6J; X-ray; 2.85 A; C/F=153-227.
DR PDB; 5EDV; X-ray; 3.48 A; E/F/G/H=153-228.
DR PDB; 5EMZ; X-ray; 1.66 A; A/B/C/D/E/F=1-76.
DR PDB; 5EYA; X-ray; 2.40 A; C/D=153-228.
DR PDB; 5GJQ; EM; 4.50 A; y=153-228.
DR PDB; 5GO7; X-ray; 1.80 A; A=1-76.
DR PDB; 5GO8; X-ray; 2.21 A; A=1-76.
DR PDB; 5GOB; X-ray; 1.15 A; A=1-76.
DR PDB; 5GOC; X-ray; 1.73 A; A=1-76.
DR PDB; 5GOD; X-ray; 1.15 A; A/B=1-76.
DR PDB; 5GOG; X-ray; 1.98 A; A=1-76.
DR PDB; 5GOH; X-ray; 1.95 A; A=1-76.
DR PDB; 5GOI; X-ray; 1.59 A; A/B=1-76.
DR PDB; 5GOJ; X-ray; 1.55 A; A=1-76.
DR PDB; 5GOK; X-ray; 1.84 A; A=1-76.
DR PDB; 5H7S; X-ray; 3.49 A; E/F=1-76.
DR PDB; 5IBK; X-ray; 2.50 A; C/F=151-226.
DR PDB; 5IFR; X-ray; 2.20 A; B=153-227.
DR PDB; 5JBY; X-ray; 1.99 A; A/C/E=153-228.
DR PDB; 5JG6; X-ray; 2.00 A; B/C=76-153.
DR PDB; 5JP3; X-ray; 2.90 A; B/D/F/H=153-227.
DR PDB; 5JTJ; X-ray; 3.32 A; B=153-228.
DR PDB; 5JTV; X-ray; 3.31 A; B/D/F/H=1-76.
DR PDB; 5K9P; X-ray; 1.55 A; A=153-228.
DR PDB; 5KGF; EM; 4.54 A; M/O=153-228.
DR PDB; 5KHY; X-ray; 3.50 A; A=153-225, B=153-227.
DR PDB; 5KYC; X-ray; 1.43 A; C=153-228.
DR PDB; 5KYD; X-ray; 1.62 A; D=153-228.
DR PDB; 5KYE; X-ray; 1.97 A; C/D=153-228.
DR PDB; 5KYF; X-ray; 1.45 A; C=153-228.
DR PDB; 5L8H; X-ray; 1.85 A; B=1-76.
DR PDB; 5L8W; X-ray; 2.79 A; C=1-75.
DR PDB; 5L9T; EM; 6.40 A; S=1-73.
DR PDB; 5LN1; X-ray; 3.14 A; U=1-76.
DR PDB; 5LRV; X-ray; 2.80 A; B=1-76, C=1-75.
DR PDB; 5LRW; X-ray; 2.00 A; B/D=1-75.
DR PDB; 5LRX; X-ray; 2.85 A; B/D=1-76.
DR PDB; 5M93; X-ray; 1.79 A; A/B/C=1-76.
DR PDB; 5MNJ; X-ray; 2.16 A; B/F=1-76.
DR PDB; 5N2W; X-ray; 2.68 A; B=1-76.
DR PDB; 5N38; X-ray; 2.60 A; B=1-76.
DR PDB; 5NL5; X-ray; 1.96 A; A/B/C=1-76.
DR PDB; 5NLJ; X-ray; 1.53 A; A/B/C=1-76.
DR PDB; 5NVG; X-ray; 1.07 A; A=1-76.
DR PDB; 5O44; X-ray; 3.14 A; B/C=1-74, D/F=1-76.
DR PDB; 5O6T; X-ray; 1.57 A; C/D=1-76.
DR PDB; 5OHK; X-ray; 2.34 A; B=1-76.
DR PDB; 5OHL; X-ray; 2.50 A; I/J/K/L/M/N/O/P=1-76.
DR PDB; 5OHN; X-ray; 3.60 A; B/D=1-76.
DR PDB; 5OHP; X-ray; 2.80 A; B/C=1-76.
DR PDB; 5TOF; X-ray; 1.12 A; A=1-76.
DR PDB; 5TOG; X-ray; 1.08 A; A=1-76.
DR PDB; 5TUT; X-ray; 2.60 A; B=1-76.
DR PDB; 5TXK; X-ray; 1.84 A; B=1-76.
DR PDB; 5UJL; NMR; -; A/B=1-76.
DR PDB; 5UJN; NMR; -; A/B=1-76.
DR PDB; 5ULF; X-ray; 1.80 A; B/D=1-76.
DR PDB; 5ULH; X-ray; 1.95 A; B=1-76.
DR PDB; 5ULK; X-ray; 2.38 A; B=1-76.
DR PDB; 5V1Y; X-ray; 1.42 A; C/D=1-76.
DR PDB; 5V1Z; X-ray; 2.00 A; C/D=1-76.
DR PDB; 5VEY; NMR; -; B=1-76.
DR PDB; 5VF0; NMR; -; A=1-76.
DR PDB; 5VNZ; X-ray; 3.41 A; C/F=1-76.
DR PDB; 5VO0; X-ray; 3.90 A; C/F=1-76.
DR PDB; 5VZM; NMR; -; A=153-228.
DR PDB; 5VZW; X-ray; 2.28 A; C/D=153-228.
DR PDB; 5W46; X-ray; 1.18 A; A/B=153-228.
DR PDB; 5WFI; X-ray; 1.85 A; C/D=1-76.
DR PDB; 5X3M; X-ray; 1.82 A; A=1-76.
DR PDB; 5X3N; X-ray; 1.65 A; A=1-76.
DR PDB; 5X3O; X-ray; 2.19 A; A=1-76.
DR PDB; 5XBO; NMR; -; A=1-76.
DR PDB; 5XDP; X-ray; 2.38 A; A=1-76.
DR PDB; 5XK4; NMR; -; A=153-228.
DR PDB; 5XK5; NMR; -; A=153-228.
DR PDB; 5XPK; X-ray; 2.27 A; A=153-228.
DR PDB; 5YDR; X-ray; 2.00 A; A/D=153-225.
DR PDB; 5YIJ; X-ray; 3.18 A; C/D/G=153-228.
DR PDB; 5YIK; X-ray; 3.10 A; C/D/F=153-228.
DR PDB; 5YMY; NMR; -; A/B=1-76.
DR PDB; 5YT6; X-ray; 1.50 A; A/C/E/G=1-76.
DR PDB; 5ZBU; X-ray; 3.20 A; E=1-76.
DR PDB; 5ZD0; NMR; -; A=153-228.
DR PDB; 6ASR; X-ray; 2.36 A; A/C=153-228.
DR PDB; 6BVA; X-ray; 2.66 A; A/B=76-152.
DR PDB; 6BYH; X-ray; 2.61 A; C/D/H=76-152.
DR PDB; 6C16; X-ray; 3.27 A; D/H=77-152.
DR PDB; 6CP2; X-ray; 2.90 A; C=75-152.
DR PDB; 6DGF; X-ray; 2.34 A; B=1-74.
DR PDB; 6EI1; X-ray; 1.73 A; B=153-227.
DR PDB; 6FDK; X-ray; 1.60 A; B=1-76.
DR PDB; 6FGE; X-ray; 1.74 A; C=153-227.
DR PDB; 6FTX; EM; 4.50 A; N/O=1-76.
DR PDB; 6FX4; X-ray; 2.50 A; B/D=1-76.
DR PDB; 6FYH; X-ray; 2.91 A; B=1-76.
DR PDB; 6GLC; X-ray; 1.80 A; B=153-228.
DR PDB; 6GZS; X-ray; 1.90 A; B=1-75.
DR PDB; 6H4H; X-ray; 3.50 A; C/D=1-75.
DR PDB; 6HEI; X-ray; 1.64 A; B=1-75.
DR PDB; 6HEK; X-ray; 3.03 A; B/D=1-76.
DR PDB; 6IF1; X-ray; 2.47 A; C/D=1-76.
DR PDB; 6ISU; X-ray; 1.87 A; B/C=1-76.
DR PDB; 6JB6; X-ray; 2.70 A; B=1-76.
DR PDB; 6JB7; X-ray; 2.10 A; B=1-76.
DR PDB; 6JMA; EM; 6.80 A; Y=1-76.
DR PDB; 6K4I; NMR; -; A=1-76.
DR PDB; 6K9P; X-ray; 2.05 A; G=1-76.
DR PDB; 6KOW; NMR; -; A=1-76.
DR PDB; 6KOX; NMR; -; A=1-76.
DR PDB; 6LP2; X-ray; 2.48 A; C=1-75.
DR PDB; 6MSB; EM; 3.00 A; u/w=1-76.
DR PDB; 6MSD; EM; 3.20 A; u/w=1-76.
DR PDB; 6MSE; EM; 3.30 A; u=1-76.
DR PDB; 6MSG; EM; 3.50 A; u=1-76.
DR PDB; 6N13; NMR; -; D=1-76.
DR PDB; 6NJ9; EM; 2.96 A; L/N=1-76.
DR PDB; 6NJG; X-ray; 2.35 A; A=1-78.
DR PDB; 6O96; EM; 3.50 A; L=1-76.
DR PDB; 6OAM; X-ray; 2.50 A; C/D=1-75.
DR PDB; 6PGV; X-ray; 2.30 A; B=1-75.
DR PDB; 6PZV; X-ray; 3.01 A; A/B/E/F=1-76.
DR PDB; 6QF8; NMR; -; A=1-76.
DR PDB; 6QK9; X-ray; 2.23 A; A/B/C/D/E/F/G/H/I/J/K/L=1-74.
DR PDB; 6QML; X-ray; 2.10 A; B/E=1-76.
DR PDB; 6TBM; EM; 20.00 A; R=153-227.
DR PDB; 6UH5; EM; 3.50 A; Q=1-76.
DR PDB; 6XAA; X-ray; 2.70 A; B=1-76.
DR PDB; 6XQC; NMR; -; A=1-76.
DR PDB; 6XZ1; X-ray; 2.30 A; C/D=1-75.
DR PDB; 7AY2; X-ray; 3.20 A; C/F=1-75.
DR PDB; 7BBD; X-ray; 2.20 A; B=1-74.
DR PDB; 7BU0; X-ray; 2.43 A; C/D=1-75.
DR PDB; 7CAP; X-ray; 1.33 A; A/B/C=1-76.
DR PDB; 7DNI; EM; 3.20 A; E/F/G/H/I/J/K/L=1-76.
DR PDB; 7DNJ; EM; 3.30 A; E/F/G/H/I/J/K/L=1-76.
DR PDB; 7E8I; EM; 3.10 A; L=153-228.
DR PDB; 7JMS; X-ray; 2.78 A; B/D/F/H=1-75.
DR PDB; 7LYC; EM; 2.94 A; K=1-76.
DR PDB; 7M2K; X-ray; 2.47 A; B/D/F/H=1-76.
DR PDB; 7MC9; X-ray; 3.10 A; B/D/F/H/J/L/N/P=1-76.
DR PDB; 7MEY; EM; 3.67 A; C/D=1-75.
DR PDB; 7MYF; X-ray; 3.00 A; B=1-75.
DR PDB; 7MYH; X-ray; 2.39 A; B=1-75.
DR PDB; 7OJE; X-ray; 2.05 A; B/D=1-76.
DR PDB; 7OJX; X-ray; 2.40 A; C/D/E=1-76.
DR PDB; 7RBR; X-ray; 1.88 A; B=1-77.
DR PDBsum; 2KHW; -.
DR PDBsum; 2MBB; -.
DR PDBsum; 2MRO; -.
DR PDBsum; 2MSG; -.
DR PDBsum; 2N13; -.
DR PDBsum; 4UEL; -.
DR PDBsum; 4UF6; -.
DR PDBsum; 4WHV; -.
DR PDBsum; 4WLR; -.
DR PDBsum; 4WUR; -.
DR PDBsum; 4XOF; -.
DR PDBsum; 4ZFR; -.
DR PDBsum; 4ZFT; -.
DR PDBsum; 4ZPZ; -.
DR PDBsum; 4ZUX; -.
DR PDBsum; 5BNB; -.
DR PDBsum; 5CAW; -.
DR PDBsum; 5CRA; -.
DR PDBsum; 5CVM; -.
DR PDBsum; 5CVN; -.
DR PDBsum; 5CVO; -.
DR PDBsum; 5D0K; -.
DR PDBsum; 5D0M; -.
DR PDBsum; 5DFL; -.
DR PDBsum; 5DK8; -.
DR PDBsum; 5E6J; -.
DR PDBsum; 5EDV; -.
DR PDBsum; 5EMZ; -.
DR PDBsum; 5EYA; -.
DR PDBsum; 5GJQ; -.
DR PDBsum; 5GO7; -.
DR PDBsum; 5GO8; -.
DR PDBsum; 5GOB; -.
DR PDBsum; 5GOC; -.
DR PDBsum; 5GOD; -.
DR PDBsum; 5GOG; -.
DR PDBsum; 5GOH; -.
DR PDBsum; 5GOI; -.
DR PDBsum; 5GOJ; -.
DR PDBsum; 5GOK; -.
DR PDBsum; 5H7S; -.
DR PDBsum; 5IBK; -.
DR PDBsum; 5IFR; -.
DR PDBsum; 5JBY; -.
DR PDBsum; 5JG6; -.
DR PDBsum; 5JP3; -.
DR PDBsum; 5JTJ; -.
DR PDBsum; 5JTV; -.
DR PDBsum; 5K9P; -.
DR PDBsum; 5KGF; -.
DR PDBsum; 5KHY; -.
DR PDBsum; 5KYC; -.
DR PDBsum; 5KYD; -.
DR PDBsum; 5KYE; -.
DR PDBsum; 5KYF; -.
DR PDBsum; 5L8H; -.
DR PDBsum; 5L8W; -.
DR PDBsum; 5L9T; -.
DR PDBsum; 5LN1; -.
DR PDBsum; 5LRV; -.
DR PDBsum; 5LRW; -.
DR PDBsum; 5LRX; -.
DR PDBsum; 5M93; -.
DR PDBsum; 5MNJ; -.
DR PDBsum; 5N2W; -.
DR PDBsum; 5N38; -.
DR PDBsum; 5NL5; -.
DR PDBsum; 5NLJ; -.
DR PDBsum; 5NVG; -.
DR PDBsum; 5O44; -.
DR PDBsum; 5O6T; -.
DR PDBsum; 5OHK; -.
DR PDBsum; 5OHL; -.
DR PDBsum; 5OHN; -.
DR PDBsum; 5OHP; -.
DR PDBsum; 5TOF; -.
DR PDBsum; 5TOG; -.
DR PDBsum; 5TUT; -.
DR PDBsum; 5TXK; -.
DR PDBsum; 5UJL; -.
DR PDBsum; 5UJN; -.
DR PDBsum; 5ULF; -.
DR PDBsum; 5ULH; -.
DR PDBsum; 5ULK; -.
DR PDBsum; 5V1Y; -.
DR PDBsum; 5V1Z; -.
DR PDBsum; 5VEY; -.
DR PDBsum; 5VF0; -.
DR PDBsum; 5VNZ; -.
DR PDBsum; 5VO0; -.
DR PDBsum; 5VZM; -.
DR PDBsum; 5VZW; -.
DR PDBsum; 5W46; -.
DR PDBsum; 5WFI; -.
DR PDBsum; 5X3M; -.
DR PDBsum; 5X3N; -.
DR PDBsum; 5X3O; -.
DR PDBsum; 5XBO; -.
DR PDBsum; 5XDP; -.
DR PDBsum; 5XK4; -.
DR PDBsum; 5XK5; -.
DR PDBsum; 5XPK; -.
DR PDBsum; 5YDR; -.
DR PDBsum; 5YIJ; -.
DR PDBsum; 5YIK; -.
DR PDBsum; 5YMY; -.
DR PDBsum; 5YT6; -.
DR PDBsum; 5ZBU; -.
DR PDBsum; 5ZD0; -.
DR PDBsum; 6ASR; -.
DR PDBsum; 6BVA; -.
DR PDBsum; 6BYH; -.
DR PDBsum; 6C16; -.
DR PDBsum; 6CP2; -.
DR PDBsum; 6DGF; -.
DR PDBsum; 6EI1; -.
DR PDBsum; 6FDK; -.
DR PDBsum; 6FGE; -.
DR PDBsum; 6FTX; -.
DR PDBsum; 6FX4; -.
DR PDBsum; 6FYH; -.
DR PDBsum; 6GLC; -.
DR PDBsum; 6GZS; -.
DR PDBsum; 6H4H; -.
DR PDBsum; 6HEI; -.
DR PDBsum; 6HEK; -.
DR PDBsum; 6IF1; -.
DR PDBsum; 6ISU; -.
DR PDBsum; 6JB6; -.
DR PDBsum; 6JB7; -.
DR PDBsum; 6JMA; -.
DR PDBsum; 6K4I; -.
DR PDBsum; 6K9P; -.
DR PDBsum; 6KOW; -.
DR PDBsum; 6KOX; -.
DR PDBsum; 6LP2; -.
DR PDBsum; 6MSB; -.
DR PDBsum; 6MSD; -.
DR PDBsum; 6MSE; -.
DR PDBsum; 6MSG; -.
DR PDBsum; 6N13; -.
DR PDBsum; 6NJ9; -.
DR PDBsum; 6NJG; -.
DR PDBsum; 6O96; -.
DR PDBsum; 6OAM; -.
DR PDBsum; 6PGV; -.
DR PDBsum; 6PZV; -.
DR PDBsum; 6QF8; -.
DR PDBsum; 6QK9; -.
DR PDBsum; 6QML; -.
DR PDBsum; 6TBM; -.
DR PDBsum; 6UH5; -.
DR PDBsum; 6XAA; -.
DR PDBsum; 6XQC; -.
DR PDBsum; 6XZ1; -.
DR PDBsum; 7AY2; -.
DR PDBsum; 7BBD; -.
DR PDBsum; 7BU0; -.
DR PDBsum; 7CAP; -.
DR PDBsum; 7DNI; -.
DR PDBsum; 7DNJ; -.
DR PDBsum; 7E8I; -.
DR PDBsum; 7JMS; -.
DR PDBsum; 7LYC; -.
DR PDBsum; 7M2K; -.
DR PDBsum; 7MC9; -.
DR PDBsum; 7MEY; -.
DR PDBsum; 7MYF; -.
DR PDBsum; 7MYH; -.
DR PDBsum; 7OJE; -.
DR PDBsum; 7OJX; -.
DR PDBsum; 7RBR; -.
DR AlphaFoldDB; P0CG47; -.
DR BMRB; P0CG47; -.
DR SASBDB; P0CG47; -.
DR SMR; P0CG47; -.
DR BioGRID; 113162; 362.
DR IntAct; P0CG47; 217.
DR MINT; P0CG47; -.
DR STRING; 9606.ENSP00000304697; -.
DR ChEMBL; CHEMBL4523178; -.
DR DrugBank; DB02542; (4s)-5-Fluoro-L-Leucine.
DR MoonDB; P0CG47; Predicted.
DR GlyGen; P0CG47; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P0CG47; -.
DR MetOSite; P0CG47; -.
DR PhosphoSitePlus; P0CG47; -.
DR SwissPalm; P0CG47; -.
DR BioMuta; UBB; -.
DR DMDM; 302595875; -.
DR EPD; P0CG47; -.
DR jPOST; P0CG47; -.
DR MassIVE; P0CG47; -.
DR PaxDb; P0CG47; -.
DR PeptideAtlas; P0CG47; -.
DR PRIDE; P0CG47; -.
DR TopDownProteomics; P0CG47; -.
DR Antibodypedia; 4579; 650 antibodies from 42 providers.
DR DNASU; 7314; -.
DR Ensembl; ENST00000302182.8; ENSP00000304697.3; ENSG00000170315.14.
DR Ensembl; ENST00000395837.1; ENSP00000379178.1; ENSG00000170315.14.
DR Ensembl; ENST00000395839.5; ENSP00000379180.1; ENSG00000170315.14.
DR Ensembl; ENST00000614404.1; ENSP00000478771.1; ENSG00000170315.14.
DR GeneID; 7314; -.
DR KEGG; hsa:7314; -.
DR MANE-Select; ENST00000302182.8; ENSP00000304697.3; NM_018955.4; NP_061828.1.
DR CTD; 7314; -.
DR DisGeNET; 7314; -.
DR GeneCards; UBB; -.
DR HGNC; HGNC:12463; UBB.
DR HPA; ENSG00000170315; Low tissue specificity.
DR MalaCards; UBB; -.
DR MIM; 191339; gene.
DR neXtProt; NX_P0CG47; -.
DR OpenTargets; ENSG00000170315; -.
DR Orphanet; 99771; Bifid uvula.
DR Orphanet; 101023; Cleft hard palate.
DR Orphanet; 99772; Cleft velum.
DR Orphanet; 155878; Submucosal cleft palate.
DR VEuPathDB; HostDB:ENSG00000170315; -.
DR eggNOG; KOG0001; Eukaryota.
DR GeneTree; ENSGT00940000162439; -.
DR InParanoid; P0CG47; -.
DR OMA; CAQVEQV; -.
DR OrthoDB; 1536766at2759; -.
DR PhylomeDB; P0CG47; -.
DR TreeFam; TF300820; -.
DR BioCyc; MetaCyc:ENSG00000170315-MON; -.
DR PathwayCommons; P0CG47; -.
DR Reactome; R-HSA-110312; Translesion synthesis by REV1.
DR Reactome; R-HSA-110314; Recognition of DNA damage by PCNA-containing replication complex.
DR Reactome; R-HSA-110320; Translesion Synthesis by POLH.
DR Reactome; R-HSA-1169091; Activation of NF-kappaB in B cells.
DR Reactome; R-HSA-1169408; ISG15 antiviral mechanism.
DR Reactome; R-HSA-1234176; Oxygen-dependent proline hydroxylation of Hypoxia-inducible Factor Alpha.
DR Reactome; R-HSA-1236382; Constitutive Signaling by Ligand-Responsive EGFR Cancer Variants.
DR Reactome; R-HSA-1236974; ER-Phagosome pathway.
DR Reactome; R-HSA-1253288; Downregulation of ERBB4 signaling.
DR Reactome; R-HSA-1295596; Spry regulation of FGF signaling.
DR Reactome; R-HSA-1358803; Downregulation of ERBB2:ERBB3 signaling.
DR Reactome; R-HSA-162588; Budding and maturation of HIV virion.
DR Reactome; R-HSA-168638; NOD1/2 Signaling Pathway.
DR Reactome; R-HSA-168927; TICAM1, RIP1-mediated IKK complex recruitment.
DR Reactome; R-HSA-168928; DDX58/IFIH1-mediated induction of interferon-alpha/beta.
DR Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR Reactome; R-HSA-174113; SCF-beta-TrCP mediated degradation of Emi1.
DR Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-174490; Membrane binding and targetting of GAG proteins.
DR Reactome; R-HSA-175474; Assembly Of The HIV Virion.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-180534; Vpu mediated degradation of CD4.
DR Reactome; R-HSA-180585; Vif-mediated degradation of APOBEC3G.
DR Reactome; R-HSA-182971; EGFR downregulation.
DR Reactome; R-HSA-187577; SCF(Skp2)-mediated degradation of p27/p21.
DR Reactome; R-HSA-195253; Degradation of beta-catenin by the destruction complex.
DR Reactome; R-HSA-201681; TCF dependent signaling in response to WNT.
DR Reactome; R-HSA-202424; Downstream TCR signaling.
DR Reactome; R-HSA-205043; NRIF signals cell death from the nucleus.
DR Reactome; R-HSA-209543; p75NTR recruits signalling complexes.
DR Reactome; R-HSA-209560; NF-kB is activated and signals survival.
DR Reactome; R-HSA-211733; Regulation of activated PAK-2p34 by proteasome mediated degradation.
DR Reactome; R-HSA-2122947; NOTCH1 Intracellular Domain Regulates Transcription.
DR Reactome; R-HSA-2122948; Activated NOTCH1 Transmits Signal to the Nucleus.
DR Reactome; R-HSA-2173788; Downregulation of TGF-beta receptor signaling.
DR Reactome; R-HSA-2173791; TGF-beta receptor signaling in EMT (epithelial to mesenchymal transition).
DR Reactome; R-HSA-2173795; Downregulation of SMAD2/3:SMAD4 transcriptional activity.
DR Reactome; R-HSA-2173796; SMAD2/SMAD3:SMAD4 heterotrimer regulates transcription.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR Reactome; R-HSA-2559585; Oncogene Induced Senescence.
DR Reactome; R-HSA-2565942; Regulation of PLK1 Activity at G2/M Transition.
DR Reactome; R-HSA-2644606; Constitutive Signaling by NOTCH1 PEST Domain Mutants.
DR Reactome; R-HSA-2672351; Stimuli-sensing channels.
DR Reactome; R-HSA-2691232; Constitutive Signaling by NOTCH1 HD Domain Mutants.
DR Reactome; R-HSA-2871837; FCERI mediated NF-kB activation.
DR Reactome; R-HSA-2894862; Constitutive Signaling by NOTCH1 HD+PEST Domain Mutants.
DR Reactome; R-HSA-2979096; NOTCH2 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-3134975; Regulation of innate immune responses to cytosolic DNA.
DR Reactome; R-HSA-3322077; Glycogen synthesis.
DR Reactome; R-HSA-349425; Autodegradation of the E3 ubiquitin ligase COP1.
DR Reactome; R-HSA-3769402; Deactivation of the beta-catenin transactivating complex.
DR Reactome; R-HSA-3785653; Myoclonic epilepsy of Lafora.
DR Reactome; R-HSA-382556; ABC-family proteins mediated transport.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-445989; TAK1-dependent IKK and NF-kappa-B activation.
DR Reactome; R-HSA-450302; activated TAK1 mediates p38 MAPK activation.
DR Reactome; R-HSA-450321; JNK (c-Jun kinases) phosphorylation and activation mediated by activated human TAK1.
DR Reactome; R-HSA-450408; AUF1 (hnRNP D0) binds and destabilizes mRNA.
DR Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
DR Reactome; R-HSA-4641257; Degradation of AXIN.
DR Reactome; R-HSA-4641258; Degradation of DVL.
DR Reactome; R-HSA-4641263; Regulation of FZD by ubiquitination.
DR Reactome; R-HSA-5205685; PINK1-PRKN Mediated Mitophagy.
DR Reactome; R-HSA-532668; N-glycan trimming in the ER and Calnexin/Calreticulin cycle.
DR Reactome; R-HSA-5357905; Regulation of TNFR1 signaling.
DR Reactome; R-HSA-5357956; TNFR1-induced NFkappaB signaling pathway.
DR Reactome; R-HSA-5358346; Hedgehog ligand biogenesis.
DR Reactome; R-HSA-5362768; Hh mutants are degraded by ERAD.
DR Reactome; R-HSA-5607761; Dectin-1 mediated noncanonical NF-kB signaling.
DR Reactome; R-HSA-5607764; CLEC7A (Dectin-1) signaling.
DR Reactome; R-HSA-5610780; Degradation of GLI1 by the proteasome.
DR Reactome; R-HSA-5610783; Degradation of GLI2 by the proteasome.
DR Reactome; R-HSA-5610785; GLI3 is processed to GLI3R by the proteasome.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR Reactome; R-HSA-5654726; Negative regulation of FGFR1 signaling.
DR Reactome; R-HSA-5654727; Negative regulation of FGFR2 signaling.
DR Reactome; R-HSA-5654732; Negative regulation of FGFR3 signaling.
DR Reactome; R-HSA-5654733; Negative regulation of FGFR4 signaling.
DR Reactome; R-HSA-5655862; Translesion synthesis by POLK.
DR Reactome; R-HSA-5656121; Translesion synthesis by POLI.
DR Reactome; R-HSA-5656169; Termination of translesion DNA synthesis.
DR Reactome; R-HSA-5658442; Regulation of RAS by GAPs.
DR Reactome; R-HSA-5668541; TNFR2 non-canonical NF-kB pathway.
DR Reactome; R-HSA-5675221; Negative regulation of MAPK pathway.
DR Reactome; R-HSA-5675482; Regulation of necroptotic cell death.
DR Reactome; R-HSA-5676590; NIK-->noncanonical NF-kB signaling.
DR Reactome; R-HSA-5678895; Defective CFTR causes cystic fibrosis.
DR Reactome; R-HSA-5684264; MAP3K8 (TPL2)-dependent MAPK1/3 activation.
DR Reactome; R-HSA-5685942; HDR through Homologous Recombination (HRR).
DR Reactome; R-HSA-5687128; MAPK6/MAPK4 signaling.
DR Reactome; R-HSA-5689603; UCH proteinases.
DR Reactome; R-HSA-5689877; Josephin domain DUBs.
DR Reactome; R-HSA-5689880; Ub-specific processing proteases.
DR Reactome; R-HSA-5689896; Ovarian tumor domain proteases.
DR Reactome; R-HSA-5689901; Metalloprotease DUBs.
DR Reactome; R-HSA-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR Reactome; R-HSA-5693607; Processing of DNA double-strand break ends.
DR Reactome; R-HSA-5696394; DNA Damage Recognition in GG-NER.
DR Reactome; R-HSA-5696395; Formation of Incision Complex in GG-NER.
DR Reactome; R-HSA-5696397; Gap-filling DNA repair synthesis and ligation in GG-NER.
DR Reactome; R-HSA-5696400; Dual Incision in GG-NER.
DR Reactome; R-HSA-6781823; Formation of TC-NER Pre-Incision Complex.
DR Reactome; R-HSA-6781827; Transcription-Coupled Nucleotide Excision Repair (TC-NER).
DR Reactome; R-HSA-6782135; Dual incision in TC-NER.
DR Reactome; R-HSA-6782210; Gap-filling DNA repair synthesis and ligation in TC-NER.
DR Reactome; R-HSA-6783310; Fanconi Anemia Pathway.
DR Reactome; R-HSA-6804756; Regulation of TP53 Activity through Phosphorylation.
DR Reactome; R-HSA-6804757; Regulation of TP53 Degradation.
DR Reactome; R-HSA-6804760; Regulation of TP53 Activity through Methylation.
DR Reactome; R-HSA-6807004; Negative regulation of MET activity.
DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR Reactome; R-HSA-68949; Orc1 removal from chromatin.
DR Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR Reactome; R-HSA-69231; Cyclin D associated events in G1.
DR Reactome; R-HSA-69481; G2/M Checkpoints.
DR Reactome; R-HSA-69541; Stabilization of p53.
DR Reactome; R-HSA-69601; Ubiquitin Mediated Degradation of Phosphorylated Cdc25A.
DR Reactome; R-HSA-75815; Ubiquitin-dependent degradation of Cyclin D.
DR Reactome; R-HSA-8849469; PTK6 Regulates RTKs and Their Effectors AKT1 and DOK1.
DR Reactome; R-HSA-8852276; The role of GTSE1 in G2/M progression after G2 checkpoint.
DR Reactome; R-HSA-8854050; FBXL7 down-regulates AURKA during mitotic entry and in early mitosis.
DR Reactome; R-HSA-8856825; Cargo recognition for clathrin-mediated endocytosis.
DR Reactome; R-HSA-8856828; Clathrin-mediated endocytosis.
DR Reactome; R-HSA-8863795; Downregulation of ERBB2 signaling.
DR Reactome; R-HSA-8866427; VLDLR internalisation and degradation.
DR Reactome; R-HSA-8866652; Synthesis of active ubiquitin: roles of E1 and E2 enzymes.
DR Reactome; R-HSA-8866654; E3 ubiquitin ligases ubiquitinate target proteins.
DR Reactome; R-HSA-8875360; InlB-mediated entry of Listeria monocytogenes into host cell.
DR Reactome; R-HSA-8876493; InlA-mediated entry of Listeria monocytogenes into host cells.
DR Reactome; R-HSA-8939236; RUNX1 regulates transcription of genes involved in differentiation of HSCs.
DR Reactome; R-HSA-8939902; Regulation of RUNX2 expression and activity.
DR Reactome; R-HSA-8941858; Regulation of RUNX3 expression and activity.
DR Reactome; R-HSA-8948747; Regulation of PTEN localization.
DR Reactome; R-HSA-8948751; Regulation of PTEN stability and activity.
DR Reactome; R-HSA-8951664; Neddylation.
DR Reactome; R-HSA-901032; ER Quality Control Compartment (ERQC).
DR Reactome; R-HSA-9010553; Regulation of expression of SLITs and ROBOs.
DR Reactome; R-HSA-9013507; NOTCH3 Activation and Transmission of Signal to the Nucleus.
DR Reactome; R-HSA-9013973; TICAM1-dependent activation of IRF3/IRF7.
DR Reactome; R-HSA-9014325; TICAM1,TRAF6-dependent induction of TAK1 complex.
DR Reactome; R-HSA-9020702; Interleukin-1 signaling.
DR Reactome; R-HSA-9033241; Peroxisomal protein import.
DR Reactome; R-HSA-912631; Regulation of signaling by CBL.
DR Reactome; R-HSA-917729; Endosomal Sorting Complex Required For Transport (ESCRT).
DR Reactome; R-HSA-917937; Iron uptake and transport.
DR Reactome; R-HSA-936440; Negative regulators of DDX58/IFIH1 signaling.
DR Reactome; R-HSA-936964; Activation of IRF3/IRF7 mediated by TBK1/IKK epsilon.
DR Reactome; R-HSA-937039; IRAK1 recruits IKK complex.
DR Reactome; R-HSA-937041; IKK complex recruitment mediated by RIP1.
DR Reactome; R-HSA-937042; IRAK2 mediated activation of TAK1 complex.
DR Reactome; R-HSA-937072; TRAF6-mediated induction of TAK1 complex within TLR4 complex.
DR Reactome; R-HSA-9604323; Negative regulation of NOTCH4 signaling.
DR Reactome; R-HSA-9613829; Chaperone Mediated Autophagy.
DR Reactome; R-HSA-9615710; Late endosomal microautophagy.
DR Reactome; R-HSA-9636383; Prevention of phagosomal-lysosomal fusion.
DR Reactome; R-HSA-9637628; Modulation by Mtb of host immune system.
DR Reactome; R-HSA-9645460; Alpha-protein kinase 1 signaling pathway.
DR Reactome; R-HSA-9646399; Aggrephagy.
DR Reactome; R-HSA-9648002; RAS processing.
DR Reactome; R-HSA-9664873; Pexophagy.
DR Reactome; R-HSA-9683683; Maturation of protein E.
DR Reactome; R-HSA-9694493; Maturation of protein E.
DR Reactome; R-HSA-9705462; Inactivation of CSF3 (G-CSF) signaling.
DR Reactome; R-HSA-9705671; SARS-CoV-2 activates/modulates innate and adaptive immune responses.
DR Reactome; R-HSA-9706369; Negative regulation of FLT3.
DR Reactome; R-HSA-9706377; FLT3 signaling by CBL mutants.
DR Reactome; R-HSA-9708530; Regulation of BACH1 activity.
DR Reactome; R-HSA-975110; TRAF6 mediated IRF7 activation in TLR7/8 or 9 signaling.
DR Reactome; R-HSA-975144; IRAK1 recruits IKK complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-HSA-975163; IRAK2 mediated activation of TAK1 complex upon TLR7/8 or 9 stimulation.
DR Reactome; R-HSA-9755511; KEAP1-NFE2L2 pathway.
DR Reactome; R-HSA-9762114; GSK3B and BTRC:CUL1-mediated-degradation of NFE2L2.
DR Reactome; R-HSA-977225; Amyloid fiber formation.
DR Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR SignaLink; P0CG47; -.
DR BioGRID-ORCS; 7314; 371 hits in 1005 CRISPR screens.
DR ChiTaRS; UBB; human.
DR GeneWiki; Ubiquitin_B; -.
DR GenomeRNAi; 7314; -.
DR Pharos; P0CG47; Tbio.
DR PRO; PR:P0CG47; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; P0CG47; protein.
DR Bgee; ENSG00000170315; Expressed in adult organism and 212 other tissues.
DR ExpressionAtlas; P0CG47; baseline and differential.
DR Genevisible; P0CG47; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0030666; C:endocytic vesicle membrane; TAS:Reactome.
DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome.
DR GO; GO:0010008; C:endosome membrane; TAS:Reactome.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0031315; C:extrinsic component of mitochondrial outer membrane; IDA:UniProtKB.
DR GO; GO:0005741; C:mitochondrial outer membrane; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IDA:MGI.
DR GO; GO:0043005; C:neuron projection; IDA:MGI.
DR GO; GO:0043025; C:neuronal cell body; IDA:MGI.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; HDA:UniProtKB.
DR GO; GO:0005886; C:plasma membrane; TAS:Reactome.
DR GO; GO:0031982; C:vesicle; HDA:UniProtKB.
DR GO; GO:0031386; F:protein tag; IBA:GO_Central.
DR GO; GO:0031625; F:ubiquitin protein ligase binding; IBA:GO_Central.
DR GO; GO:0097009; P:energy homeostasis; IEA:Ensembl.
DR GO; GO:0060613; P:fat pad development; IEA:Ensembl.
DR GO; GO:0008585; P:female gonad development; IEA:Ensembl.
DR GO; GO:0007144; P:female meiosis I; IEA:Ensembl.
DR GO; GO:0021888; P:hypothalamus gonadotrophin-releasing hormone neuron development; IEA:Ensembl.
DR GO; GO:0007141; P:male meiosis I; IEA:Ensembl.
DR GO; GO:0047497; P:mitochondrion transport along microtubule; IDA:MGI.
DR GO; GO:0019941; P:modification-dependent protein catabolic process; IBA:GO_Central.
DR GO; GO:0048812; P:neuron projection morphogenesis; IMP:MGI.
DR GO; GO:1902255; P:positive regulation of intrinsic apoptotic signaling pathway by p53 class mediator; IDA:MGI.
DR GO; GO:1902527; P:positive regulation of protein monoubiquitination; IMP:ParkinsonsUK-UCL.
DR GO; GO:0031398; P:positive regulation of protein ubiquitination; IDA:ParkinsonsUK-UCL.
DR GO; GO:0016567; P:protein ubiquitination; IBA:GO_Central.
DR GO; GO:0051881; P:regulation of mitochondrial membrane potential; IDA:MGI.
DR GO; GO:1901214; P:regulation of neuron death; IDA:MGI.
DR GO; GO:0061136; P:regulation of proteasomal protein catabolic process; IDA:MGI.
DR GO; GO:0072520; P:seminiferous tubule development; IEA:Ensembl.
DR InterPro; IPR000626; Ubiquitin-like_dom.
DR InterPro; IPR029071; Ubiquitin-like_domsf.
DR InterPro; IPR019954; Ubiquitin_CS.
DR InterPro; IPR019956; Ubiquitin_dom.
DR Pfam; PF00240; ubiquitin; 3.
DR PRINTS; PR00348; UBIQUITIN.
DR SMART; SM00213; UBQ; 3.
DR SUPFAM; SSF54236; SSF54236; 3.
DR PROSITE; PS00299; UBIQUITIN_1; 3.
DR PROSITE; PS50053; UBIQUITIN_2; 3.
PE 1: Evidence at protein level;
KW 3D-structure; ADP-ribosylation; Cytoplasm; Direct protein sequencing;
KW Isopeptide bond; Membrane; Mitochondrion; Mitochondrion outer membrane;
KW Nucleus; Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
FT CHAIN 1..76
FT /note="Ubiquitin"
FT /id="PRO_0000396174"
FT CHAIN 77..152
FT /note="Ubiquitin"
FT /id="PRO_0000396175"
FT CHAIN 153..228
FT /note="Ubiquitin"
FT /id="PRO_0000396176"
FT PROPEP 229
FT /id="PRO_0000396177"
FT DOMAIN 1..76
FT /note="Ubiquitin-like 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 77..152
FT /note="Ubiquitin-like 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT DOMAIN 153..228
FT /note="Ubiquitin-like 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00214"
FT SITE 54
FT /note="Interacts with activating enzyme"
FT SITE 68
FT /note="Essential for function"
FT SITE 72
FT /note="Interacts with activating enzyme"
FT MOD_RES 65
FT /note="Phosphoserine; by PINK1"
FT /evidence="ECO:0000269|PubMed:24660806,
FT ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582,
FT ECO:0000269|PubMed:25527291"
FT MOD_RES 76
FT /note="ADP-ribosylglycine"
FT /evidence="ECO:0000269|PubMed:28525742"
FT CROSSLNK 6
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16443603"
FT CROSSLNK 11
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16443603,
FT ECO:0000269|PubMed:16543144"
FT CROSSLNK 27
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000305|PubMed:15466860"
FT CROSSLNK 29
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144,
FT ECO:0000269|PubMed:25752573, ECO:0000269|PubMed:25752577,
FT ECO:0000269|PubMed:34239127"
FT CROSSLNK 33
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:25752577"
FT CROSSLNK 48
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16443603,
FT ECO:0000269|PubMed:16543144"
FT CROSSLNK 63
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000269|PubMed:16543144,
FT ECO:0000269|PubMed:18719106"
FT CROSSLNK 76
FT /note="Glycyl lysine isopeptide (Gly-Lys) (interchain with
FT K-? in acceptor proteins)"
FT VARIANT 76..229
FT /note="GMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKEGIPPDQQRLIFAGKQLE
FT DGRTLSDYNIQKESTLHLVLRLRGGMQIFVKTLTGKTITLEVEPSDTIENVKAKIQDKE
FT GIPPDQQRLIFAGKQLEDGRTLSDYNIQKESTLHLVLRLRGGC -> YADLREDPDRQD
FT HHPGSGAQ (in UBB(+1); loss of polyubiquitination; impairs
FT the ubiquitin-proteasome pathway; refractory to disassembly
FT by DUBs; slow degradation by UCHL3)"
FT /id="VAR_066248"
FT MUTAGEN 48
FT /note="K->R: No effect on HLTF-mediated polyubiquitination
FT of PCNA."
FT /evidence="ECO:0000269|PubMed:18719106"
FT MUTAGEN 63
FT /note="K->R: Abolishes HLTF-mediated polyubiquitination of
FT PCNA."
FT /evidence="ECO:0000269|PubMed:18719106"
FT MUTAGEN 65
FT /note="S->A: Prevents phosphorylation in case of mitophagy.
FT Decreased localization of PRKN to mitochondria."
FT /evidence="ECO:0000269|PubMed:24660806,
FT ECO:0000269|PubMed:24751536, ECO:0000269|PubMed:24784582"
FT MUTAGEN 65
FT /note="S->D: Phosphomimetic mutant that binds and activates
FT PRKN."
FT /evidence="ECO:0000269|PubMed:24751536"
FT MUTAGEN 65
FT /note="S->E: Phosphomimetic mutant that binds and activates
FT PRKN."
FT /evidence="ECO:0000269|PubMed:24751536"
FT MUTAGEN 68
FT /note="H->G: Loss of DTX3L-mediated polyubiquitination of
FT histone H3 and H4."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 72
FT /note="R->G: No effect on ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 72
FT /note="R->K: No effect on ADP-ribosylation, when associated
FT with K-74."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 74
FT /note="R->G: No effect on ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 74
FT /note="R->K: No effect on ADP-ribosylation, when associated
FT with K-72."
FT /evidence="ECO:0000269|PubMed:28525742"
FT MUTAGEN 76
FT /note="G->A: Loss of ADP-ribosylation."
FT /evidence="ECO:0000269|PubMed:28525742"
FT STRAND 78..82
FT /evidence="ECO:0007829|PDB:7RBR"
FT STRAND 84..86
FT /evidence="ECO:0007829|PDB:7MYH"
FT STRAND 88..92
FT /evidence="ECO:0007829|PDB:7RBR"
FT HELIX 99..110
FT /evidence="ECO:0007829|PDB:7RBR"
FT HELIX 114..116
FT /evidence="ECO:0007829|PDB:7RBR"
FT STRAND 117..121
FT /evidence="ECO:0007829|PDB:7RBR"
FT HELIX 133..135
FT /evidence="ECO:0007829|PDB:7RBR"
FT STRAND 142..147
FT /evidence="ECO:0007829|PDB:7RBR"
FT STRAND 154..159
FT /evidence="ECO:0007829|PDB:5NVG"
FT STRAND 160..162
FT /evidence="ECO:0007829|PDB:4ZFR"
FT STRAND 164..168
FT /evidence="ECO:0007829|PDB:5NVG"
FT STRAND 171..174
FT /evidence="ECO:0007829|PDB:5XPK"
FT HELIX 175..186
FT /evidence="ECO:0007829|PDB:5NVG"
FT HELIX 190..192
FT /evidence="ECO:0007829|PDB:5NVG"
FT STRAND 193..197
FT /evidence="ECO:0007829|PDB:5NVG"
FT STRAND 200..202
FT /evidence="ECO:0007829|PDB:5YIJ"
FT STRAND 206..208
FT /evidence="ECO:0007829|PDB:5GO7"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:5NVG"
FT STRAND 218..223
FT /evidence="ECO:0007829|PDB:5NVG"
FT STRAND 226..228
FT /evidence="ECO:0007829|PDB:6CP2"
SQ SEQUENCE 229 AA; 25762 MW; 33011162F1C48BB1 CRC64;
MQIFVKTLTG KTITLEVEPS DTIENVKAKI QDKEGIPPDQ QRLIFAGKQL EDGRTLSDYN
IQKESTLHLV LRLRGGMQIF VKTLTGKTIT LEVEPSDTIE NVKAKIQDKE GIPPDQQRLI
FAGKQLEDGR TLSDYNIQKE STLHLVLRLR GGMQIFVKTL TGKTITLEVE PSDTIENVKA
KIQDKEGIPP DQQRLIFAGK QLEDGRTLSD YNIQKESTLH LVLRLRGGC
