BUB3_HUMAN
ID BUB3_HUMAN Reviewed; 328 AA.
AC O43684; A6NJ42; B2R6E7; D3DRE9; O43685;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-1998, sequence version 1.
DT 03-AUG-2022, entry version 201.
DE RecName: Full=Mitotic checkpoint protein BUB3;
GN Name=BUB3;
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 [MRNA] (ISOFORMS 1 AND 2), FUNCTION, AND INTERACTION
RP WITH BUB1 AND MAD1L1.
RC TISSUE=Spleen, and Testis;
RX PubMed=10198256; DOI=10.1006/bbrc.1999.0514;
RA Seeley T.W., Wang L., Zhen J.Y.;
RT "Phosphorylation of human MAD1 by the BUB1 kinase in vitro.";
RL Biochem. Biophys. Res. Commun. 257:589-595(1999).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9660858; DOI=10.1083/jcb.142.1.1;
RA Taylor S.S., Ha E., McKeon F.;
RT "The human homologue of Bub3 is required for kinetochore localization of
RT Bub1 and a Mad3/Bub1-related protein kinase.";
RL J. Cell Biol. 142:1-11(1998).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Chan G.K.T., Yen T.J.;
RT "Human BUB3 is a kinetochore protein that interacts with hBUB1 and
RT hBUBR1.";
RL Submitted (AUG-1998) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Tongue;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Placenta;
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 [8]
RP FUNCTION, AND INTERACTION WITH BUB1.
RX PubMed=15525512; DOI=10.1016/j.molcel.2004.09.031;
RA Tang Z., Shu H., Oncel D., Chen S., Yu H.;
RT "Phosphorylation of Cdc20 by Bub1 provides a catalytic mechanism for APC/C
RT inhibition by the spindle checkpoint.";
RL Mol. Cell 16:387-397(2004).
RN [9]
RP FUNCTION.
RX PubMed=18199686; DOI=10.1091/mbc.e07-07-0633;
RA Logarinho E., Resende T., Torres C., Bousbaa H.;
RT "The human spindle assembly checkpoint protein Bub3 is required for the
RT establishment of efficient kinetochore-microtubule attachments.";
RL Mol. Biol. Cell 19:1798-1813(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-179, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP INTERACTION WITH ZNF207.
RX PubMed=24462186; DOI=10.1016/j.devcel.2013.12.013;
RA Jiang H., He X., Wang S., Jia J., Wan Y., Wang Y., Zeng R., Yates J. III,
RA Zhu X., Zheng Y.;
RT "A microtubule-associated zinc finger protein, BuGZ, regulates mitotic
RT chromosome alignment by ensuring Bub3 stability and kinetochore
RT targeting.";
RL Dev. Cell 28:268-281(2014).
RN [15]
RP INTERACTION WITH ZNF207.
RX PubMed=24462187; DOI=10.1016/j.devcel.2013.12.014;
RA Toledo C.M., Herman J.A., Olsen J.B., Ding Y., Corrin P., Girard E.J.,
RA Olson J.M., Emili A., Deluca J.G., Paddison P.J.;
RT "BuGZ is required for Bub3 stability, Bub1 kinetochore function, and
RT chromosome alignment.";
RL Dev. Cell 28:282-294(2014).
CC -!- FUNCTION: Has a dual function in spindle-assembly checkpoint signaling
CC and in promoting the establishment of correct kinetochore-microtubule
CC (K-MT) attachments. Promotes the formation of stable end-on bipolar
CC attachments. Necessary for kinetochore localization of BUB1. Regulates
CC chromosome segregation during oocyte meiosis. The BUB1/BUB3 complex
CC plays a role in the inhibition of anaphase-promoting complex or
CC cyclosome (APC/C) when spindle-assembly checkpoint is activated and
CC inhibits the ubiquitin ligase activity of APC/C by phosphorylating its
CC activator CDC20. This complex can also phosphorylate MAD1L1.
CC {ECO:0000269|PubMed:10198256, ECO:0000269|PubMed:15525512,
CC ECO:0000269|PubMed:18199686}.
CC -!- SUBUNIT: Interacts with BUB1 and BUBR1. The BUB1/BUB3 complex interacts
CC with MAD1L1. Interacts with ZNF207/BuGZ; leading to promote stability
CC and kinetochore loading of BUB3. {ECO:0000269|PubMed:10198256,
CC ECO:0000269|PubMed:15525512, ECO:0000269|PubMed:24462186,
CC ECO:0000269|PubMed:24462187}.
CC -!- INTERACTION:
CC O43684; P54253: ATXN1; NbExp=7; IntAct=EBI-1050987, EBI-930964;
CC O43684; O43683: BUB1; NbExp=5; IntAct=EBI-1050987, EBI-748936;
CC O43684; O60566: BUB1B; NbExp=10; IntAct=EBI-1050987, EBI-1001438;
CC O43684; O43586: PSTPIP1; NbExp=3; IntAct=EBI-1050987, EBI-1050964;
CC O43684; Q5XI90: Dynlt3; Xeno; NbExp=2; IntAct=EBI-1050987, EBI-1781818;
CC O43684; A0A0H3NF38: sspH2; Xeno; NbExp=3; IntAct=EBI-1050987, EBI-10689860;
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore
CC {ECO:0000250}. Note=Starts to localize at kinetochores in prometaphase
CC I (Pro-MI) stage and maintains the localization until the metaphase I-
CC anaphase I (MI-AI) transition. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O43684-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O43684-2; Sequence=VSP_038655;
CC -!- PTM: Poly-ADP-ribosylated by PARP1. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the WD repeat BUB3 family. {ECO:0000305}.
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DR EMBL; AF047472; AAC28438.1; -; mRNA.
DR EMBL; AF047473; AAC28439.1; -; mRNA.
DR EMBL; AF053304; AAC06258.1; -; mRNA.
DR EMBL; AF081496; AAC36307.1; -; mRNA.
DR EMBL; AK312546; BAG35444.1; -; mRNA.
DR EMBL; AC012391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471066; EAW49284.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49285.1; -; Genomic_DNA.
DR EMBL; CH471066; EAW49286.1; -; Genomic_DNA.
DR EMBL; BC005138; AAH05138.1; -; mRNA.
DR EMBL; BC022438; AAH22438.1; -; mRNA.
DR CCDS; CCDS31306.1; -. [O43684-2]
DR CCDS; CCDS7635.1; -. [O43684-1]
DR RefSeq; NP_001007794.1; NM_001007793.2. [O43684-2]
DR RefSeq; NP_004716.1; NM_004725.3. [O43684-1]
DR AlphaFoldDB; O43684; -.
DR SMR; O43684; -.
DR BioGRID; 114621; 198.
DR ComplexPortal; CPX-3946; Mitotic Checkpoint Complex.
DR CORUM; O43684; -.
DR DIP; DIP-24205N; -.
DR IntAct; O43684; 91.
DR MINT; O43684; -.
DR STRING; 9606.ENSP00000357858; -.
DR CarbonylDB; O43684; -.
DR GlyGen; O43684; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; O43684; -.
DR PhosphoSitePlus; O43684; -.
DR SwissPalm; O43684; -.
DR BioMuta; BUB3; -.
DR CPTAC; CPTAC-464; -.
DR CPTAC; CPTAC-465; -.
DR EPD; O43684; -.
DR jPOST; O43684; -.
DR MassIVE; O43684; -.
DR MaxQB; O43684; -.
DR PaxDb; O43684; -.
DR PeptideAtlas; O43684; -.
DR PRIDE; O43684; -.
DR ProteomicsDB; 49113; -. [O43684-1]
DR ProteomicsDB; 49114; -. [O43684-2]
DR TopDownProteomics; O43684-1; -. [O43684-1]
DR Antibodypedia; 1213; 388 antibodies from 41 providers.
DR DNASU; 9184; -.
DR Ensembl; ENST00000368858.9; ENSP00000357851.5; ENSG00000154473.18. [O43684-2]
DR Ensembl; ENST00000368865.9; ENSP00000357858.4; ENSG00000154473.18. [O43684-1]
DR GeneID; 9184; -.
DR KEGG; hsa:9184; -.
DR MANE-Select; ENST00000368865.9; ENSP00000357858.4; NM_004725.4; NP_004716.1.
DR UCSC; uc001lhd.3; human. [O43684-1]
DR CTD; 9184; -.
DR DisGeNET; 9184; -.
DR GeneCards; BUB3; -.
DR HGNC; HGNC:1151; BUB3.
DR HPA; ENSG00000154473; Low tissue specificity.
DR MalaCards; BUB3; -.
DR MIM; 603719; gene.
DR neXtProt; NX_O43684; -.
DR OpenTargets; ENSG00000154473; -.
DR Orphanet; 1052; Mosaic variegated aneuploidy syndrome.
DR PharmGKB; PA25467; -.
DR VEuPathDB; HostDB:ENSG00000154473; -.
DR eggNOG; KOG1036; Eukaryota.
DR GeneTree; ENSGT00950000183091; -.
DR HOGENOM; CLU_038526_0_1_1; -.
DR InParanoid; O43684; -.
DR OMA; WDPFNRK; -.
DR OrthoDB; 1048963at2759; -.
DR PhylomeDB; O43684; -.
DR TreeFam; TF105454; -.
DR PathwayCommons; O43684; -.
DR Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR Reactome; R-HSA-68877; Mitotic Prometaphase.
DR Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR SignaLink; O43684; -.
DR SIGNOR; O43684; -.
DR BioGRID-ORCS; 9184; 786 hits in 1088 CRISPR screens.
DR ChiTaRS; BUB3; human.
DR GeneWiki; BUB3; -.
DR GenomeRNAi; 9184; -.
DR Pharos; O43684; Tbio.
DR PRO; PR:O43684; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; O43684; protein.
DR Bgee; ENSG00000154473; Expressed in gingival epithelium and 209 other tissues.
DR ExpressionAtlas; O43684; baseline and differential.
DR Genevisible; O43684; HS.
DR GO; GO:1990298; C:bub1-bub3 complex; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0000776; C:kinetochore; IDA:UniProtKB.
DR GO; GO:0033597; C:mitotic checkpoint complex; IPI:ComplexPortal.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0043130; F:ubiquitin binding; IBA:GO_Central.
DR GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:UniProtKB.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0051321; P:meiotic cell cycle; IEA:UniProtKB-KW.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IEA:Ensembl.
DR GO; GO:0007094; P:mitotic spindle assembly checkpoint signaling; IBA:GO_Central.
DR GO; GO:0051444; P:negative regulation of ubiquitin-protein transferase activity; IDA:ComplexPortal.
DR GO; GO:0034501; P:protein localization to kinetochore; IPI:UniProtKB.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF00400; WD40; 3.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS50082; WD_REPEATS_2; 2.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW Acetylation; ADP-ribosylation; Alternative splicing; Cell cycle;
KW Cell division; Centromere; Chromosome; Chromosome partition;
KW Isopeptide bond; Kinetochore; Meiosis; Mitosis; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Ubl conjugation; WD repeat.
FT CHAIN 1..328
FT /note="Mitotic checkpoint protein BUB3"
FT /id="PRO_0000050891"
FT REPEAT 4..44
FT /note="WD 1"
FT REPEAT 47..84
FT /note="WD 2"
FT REPEAT 87..125
FT /note="WD 3"
FT REPEAT 129..164
FT /note="WD 4"
FT REPEAT 170..210
FT /note="WD 5"
FT REPEAT 217..263
FT /note="WD 6"
FT REPEAT 267..316
FT /note="WD 7"
FT MOD_RES 179
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 211
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT CROSSLNK 216
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT VAR_SEQ 326..328
FT /note="PCT -> T (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10198256"
FT /id="VSP_038655"
SQ SEQUENCE 328 AA; 37155 MW; 2915572A57368E5A CRC64;
MTGSNEFKLN QPPEDGISSV KFSPNTSQFL LVSSWDTSVR LYDVPANSMR LKYQHTGAVL
DCAFYDPTHA WSGGLDHQLK MHDLNTDQEN LVGTHDAPIR CVEYCPEVNV MVTGSWDQTV
KLWDPRTPCN AGTFSQPEKV YTLSVSGDRL IVGTAGRRVL VWDLRNMGYV QQRRESSLKY
QTRCIRAFPN KQGYVLSSIE GRVAVEYLDP SPEVQKKKYA FKCHRLKENN IEQIYPVNAI
SFHNIHNTFA TGGSDGFVNI WDPFNKKRLC QFHRYPTSIA SLAFSNDGTT LAIASSYMYE
MDDTEHPEDG IFIRQVTDAE TKPKSPCT
