BD1L1_MOUSE
ID BD1L1_MOUSE Reviewed; 3032 AA.
AC E9Q6J5; O35243; Q3TR39; Q3USW6; Q80TF0; Q8BHG7;
DT 14-OCT-2015, integrated into UniProtKB/Swiss-Prot.
DT 05-APR-2011, sequence version 1.
DT 03-AUG-2022, entry version 76.
DE RecName: Full=Biorientation of chromosomes in cell division protein 1-like 1 {ECO:0000305};
GN Name=Bod1l {ECO:0000312|MGI:MGI:2444804};
GN Synonyms=Kiaa1327 {ECO:0000303|PubMed:12693553};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-327; 724-1707 AND 2256-2668.
RC STRAIN=C57BL/6J;
RC TISSUE=Aorta, Corpora quadrigemina, Hypothalamus, and Vein;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1466-3032.
RX PubMed=8686505; DOI=10.1002/jbmr.5650101010;
RA Benayahu D., Efrati M., Wientroub S.;
RT "Monoclonal antibodies recognize antigen expressed by osteoblasts.";
RL J. Bone Miner. Res. 10:1496-1503(1995).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1571-2985 (ISOFORM 2).
RC TISSUE=Brain {ECO:0000312|EMBL:BAC65777.1};
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482 AND SER-2001, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=19131326; DOI=10.1074/mcp.m800451-mcp200;
RA Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.;
RT "Large scale localization of protein phosphorylation by use of electron
RT capture dissociation mass spectrometry.";
RL Mol. Cell. Proteomics 8:904-912(2009).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-480; SER-482; SER-656;
RP THR-657; SER-1364; SER-1676; SER-1685; SER-1989; SER-2001; SER-2554;
RP SER-2681; SER-2841 AND SER-2888, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [8]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-534, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
RN [9]
RP SUBCELLULAR LOCATION.
RX PubMed=26166705; DOI=10.1016/j.molcel.2015.06.007;
RA Higgs M.R., Reynolds J.J., Winczura A., Blackford A.N., Borel V.,
RA Miller E.S., Zlatanou A., Nieminuszczy J., Ryan E.L., Davies N.J.,
RA Stankovic T., Boulton S.J., Niedzwiedz W., Stewart G.S.;
RT "BOD1L is required to suppress deleterious resection of stressed
RT replication forks.";
RL Mol. Cell 59:462-477(2015).
CC -!- FUNCTION: Component of the fork protection machinery required to
CC protect stalled/damaged replication forks from uncontrolled DNA2-
CC dependent resection. Acts by stabilizing RAD51 at stalled replication
CC forks and protecting RAD51 nucleofilaments from the antirecombinogenic
CC activities of FBH1 and BLM. Does not regulate spindle orientation.
CC {ECO:0000250|UniProtKB:Q8NFC6}.
CC -!- SUBUNIT: Interacts (via COMPASS-Shg1 domain) with SETD1A at stalled
CC replication forks; this interaction mediates FANCD2-dependent
CC nucleosome remodeling at reversed forks protecting them from
CC nucleolytic degradation. {ECO:0000250|UniProtKB:Q8NFC6}.
CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|PubMed:26166705}.
CC Note=Localizes at replication forks: following DNA damage, localizes to
CC damaged replication forks undergoing resection.
CC {ECO:0000250|UniProtKB:Q8NFC6}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=E9Q6J5-1; Sequence=Displayed;
CC Name=2;
CC IsoId=E9Q6J5-2; Sequence=VSP_057903;
CC Name=3;
CC IsoId=E9Q6J5-3; Sequence=VSP_057902;
CC -!- SIMILARITY: Belongs to the BOD1 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAB69856.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE24214.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAE37191.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AC102858; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC157932; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK046296; BAC32675.1; -; mRNA.
DR EMBL; AK079548; BAC37680.1; -; mRNA.
DR EMBL; AK140021; BAE24214.1; ALT_INIT; mRNA.
DR EMBL; AK163093; BAE37191.1; ALT_INIT; mRNA.
DR EMBL; AF013969; AAB69856.1; ALT_INIT; mRNA.
DR EMBL; AK122495; BAC65777.1; -; mRNA.
DR CCDS; CCDS39079.1; -. [E9Q6J5-1]
DR CCDS; CCDS80273.1; -. [E9Q6J5-2]
DR PIR; T03730; T03730.
DR RefSeq; NP_001074891.1; NM_001081422.3. [E9Q6J5-1]
DR RefSeq; NP_001297530.1; NM_001310601.1. [E9Q6J5-2]
DR IntAct; E9Q6J5; 1.
DR MINT; E9Q6J5; -.
DR STRING; 10090.ENSMUSP00000058618; -.
DR iPTMnet; E9Q6J5; -.
DR PhosphoSitePlus; E9Q6J5; -.
DR EPD; E9Q6J5; -.
DR jPOST; E9Q6J5; -.
DR MaxQB; E9Q6J5; -.
DR PaxDb; E9Q6J5; -.
DR PeptideAtlas; E9Q6J5; -.
DR PRIDE; E9Q6J5; -.
DR ProteomicsDB; 265203; -. [E9Q6J5-1]
DR ProteomicsDB; 265204; -. [E9Q6J5-2]
DR ProteomicsDB; 265205; -. [E9Q6J5-3]
DR Antibodypedia; 50158; 40 antibodies from 13 providers.
DR Ensembl; ENSMUST00000050556; ENSMUSP00000058618; ENSMUSG00000061755. [E9Q6J5-1]
DR Ensembl; ENSMUST00000202908; ENSMUSP00000144359; ENSMUSG00000061755. [E9Q6J5-2]
DR GeneID; 665775; -.
DR KEGG; mmu:665775; -.
DR UCSC; uc008xhd.3; mouse. [E9Q6J5-1]
DR UCSC; uc008xhg.1; mouse.
DR CTD; 665775; -.
DR MGI; MGI:2444804; Bod1l.
DR VEuPathDB; HostDB:ENSMUSG00000061755; -.
DR eggNOG; ENOG502QTHP; Eukaryota.
DR GeneTree; ENSGT00940000156198; -.
DR HOGENOM; CLU_000519_0_0_1; -.
DR InParanoid; E9Q6J5; -.
DR OMA; NMKQKTS; -.
DR OrthoDB; 1333373at2759; -.
DR PhylomeDB; E9Q6J5; -.
DR TreeFam; TF335808; -.
DR BioGRID-ORCS; 665775; 19 hits in 111 CRISPR screens.
DR ChiTaRS; Bod1l; mouse.
DR PRO; PR:E9Q6J5; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; E9Q6J5; protein.
DR Bgee; ENSMUSG00000061755; Expressed in embryonic post-anal tail and 258 other tissues.
DR Genevisible; E9Q6J5; MM.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0000940; C:outer kinetochore; IBA:GO_Central.
DR GO; GO:0048188; C:Set1C/COMPASS complex; ISO:MGI.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0051721; F:protein phosphatase 2A binding; IBA:GO_Central.
DR GO; GO:0004864; F:protein phosphatase inhibitor activity; IBA:GO_Central.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; ISS:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB.
DR InterPro; IPR043244; BOD1L1.
DR PANTHER; PTHR47391; PTHR47391; 2.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; DNA damage; DNA repair;
KW DNA-binding; Isopeptide bond; Phosphoprotein; Reference proteome;
KW Ubl conjugation.
FT CHAIN 1..3032
FT /note="Biorientation of chromosomes in cell division
FT protein 1-like 1"
FT /id="PRO_0000434111"
FT DNA_BIND 2807..2819
FT /note="A.T hook"
FT /evidence="ECO:0000255"
FT REGION 1..48
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 164..195
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 214..397
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 409..465
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 480..1153
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1296
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1309..1366
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1424..1491
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1675..1701
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1740..1858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1934..1978
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2082..2101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2303..2322
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2370..2469
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2536..2559
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2575..2596
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 2682..3032
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..34
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 214..244
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 245..264
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 308..375
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 381..395
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 417..437
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 482..529
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 541..656
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 665..848
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 861..875
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 882..907
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 908..930
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 931..963
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 964..979
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 980..1076
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1084..1111
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1123..1143
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1236..1253
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1254..1296
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1311..1333
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1429..1465
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1741..1800
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2303..2318
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2402..2416
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2539..2553
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2700..2717
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2735..2754
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2768..2807
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2815..2833
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2834..2849
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2850..2879
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2886..2914
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 2915..2932
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 264
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 471
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 480
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 482
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 534
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT MOD_RES 632
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 656
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 657
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1071
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 1138
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 1315
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 1364
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1676
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1685
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1989
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2001
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 2092
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2166
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2417
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2443
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2554
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2681
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2840
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2841
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2888
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 2890
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2892
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2898
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2907
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 2920
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT MOD_RES 3000
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT CROSSLNK 2915
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT CROSSLNK 2916
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q8NFC6"
FT VAR_SEQ 2588..2589
FT /note="GN -> VLLGS (in isoform 3)"
FT /id="VSP_057902"
FT VAR_SEQ 2947..2993
FT /note="Missing (in isoform 2)"
FT /id="VSP_057903"
FT CONFLICT 864
FT /note="S -> R (in Ref. 2; BAE24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 887
FT /note="P -> H (in Ref. 2; BAE24214)"
FT /evidence="ECO:0000305"
FT CONFLICT 1811..1812
FT /note="DI -> AL (in Ref. 3; AAB69856)"
FT /evidence="ECO:0000305"
FT CONFLICT 2017
FT /note="S -> G (in Ref. 3; AAB69856)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 3032 AA; 327453 MW; 095613921911B8D5 CRC64;
MATNPQPQPP PPAPPPPPPQ PQPPPPPPGP GAGPGASGPG SAGAGAGDPQ LVAMIVNHLK
SQGLFDQFRR DCLADVDTKP AYQNLRQRVD NFVANHLATH TWSPHLNKNQ LRNNIRQQVL
KSGMLESGID RIISQVVDPK INHTFRPQVE KAVHEFLATL NHKEEAAGST APDDEKPESS
VITQGAPAPG PSANVASDAM SILETITSLN QEANAARAST EMSNAKVSER TSRKLSSQPS
TDVSTDKERG SEDATEREKA TSDSGGDGLE AALKSEEPSD LPCPVEETKN HMKENNSLLL
LSKDAQQEST DPKIKSMDKG EKKPDGNEKG ERKKEKKEKT EKKIDHSKRN EDTQKVKDER
QAKDKEVEST KLPSEKSNSR ARAAEGTKED CSLLDSDVDG LTDITVSSVH TSDLSSFEED
TEEEVVVSES MEEGEITSED EEKNKQNKAK VQPGDSSDGK ARGVRHAYVH KPYLYSKYYS
DSDDELTVEQ RRQSIAKEKE ERLLRRRINR EKLEEKRKQK AEKTKSSKVK SQGKSTVDLE
DSSAKTLEPK APRIKEVLKE RKVLEKKVAL SKRRRKDSRN VDENSKKKPQ AEEESKEALK
TTEYCEKEKA SSKDLRHTHG KGEPSRPARR LSESLHSADE NKTESKVERE YKRRTSTPVI
LEGAQEETDT RDGKKQPERS ETNVEETQKQ KSTLKNEKYQ KKDDPETHGK GLPKKEAKSA
KERPEKEKAQ SEDKPSSKHK HKGDSVHKMS DETELHSSEK GETEESVRKQ GQQTKLSSDD
RTERKSKHKS ERRLSVLGRD GKPVSEYTIK TDEHARKDNK KEKHLSSEKS KAEHKSRRSS
DSKLQKDALS SKQHSVTSQK RSESCSEDKC ETDSTNADSS FKPEELPHKE RRRTKSLLED
KVVSKSKSKG QSKQTKAAET EAQEGVTRQV TTPKPDKEKN TEDNDTERQR KFKLEDRTSE
ETVTDPALEN TVSSAHSAQK DSGHRAKLAS IKEKHKTDKD STSSKLERKV SDGHRSRSLK
HSNKDMKKKE ENKPDDKNGK EVDSSHEKGR GNGPVTEKKL SRRLCENRRG STSQEMAKED
KLVANMSGTT SSSSLQRPKK STETTSIPEQ EPMEIDSEAA VENVSELSKT EDISSNSSQQ
DTDFENVTKH KATAGVLKDE FRTSMVDSKP AAAVTCKSGR GLAVTSISER HADHKSTLTK
KVHSQGNPSK AAPREREPIQ RGAQEVSVDS EVSRKALSRA PSENEKGQKN LKGMSKTTEE
CGTHRNASLE YSTDSDLLSS SGSVTVVPQK ESHNSNTIPV IDREAISEGG RASTSLANHS
DVPNQYSTVK KSEVHKTNGS KEGNDGFTVD MPTKANGGSK RHLSEDSQAT LLYSKESKIS
IPLADKSMSV TGDNKNINKQ RSLMGTAKRE SDLKVNPDIK QDSAAGEHVV DLSTRKEAET
VRRKHNKEIP TDVERKTENS EVDTSARRDS APVPQQRHGK MERGAAGSGR RDKAFIATST
EGTDKGIMLN TVKTGDATTT SSEVGEKGTA LPCTSIEADE GFMMGACPKK HPLQVGAEAS
ECTVFAAAEE GKGVVTEGFA ESEILLTSSK EGESGECAVA ESEDRVAGPL AAHTVQAEAN
VNSITTEEKD DAVTSAGSEE KCGGSACTVE GTATFIGEVE SDGAVTSAGT EIRAGSLSSE
DVDGSQENRI QVGPKKETEG TVTCTETKGR NDNFICLVTR VETQEQRVVT GADVVQVNAA
KPQEANANQG DGSGTDGAEG ESAVTSTGIT EEDGEASANC TGSEDNREGC AISSETEESA
ESAMDSTEAK DITNAPLVAA GPCDDEGIVT STGAKEEDDE DEGVVTSTGR GNEPGHASAC
TGIEESEGMM VCESGEGGAQ IGPTIDHVNA EAGAATVNTN DSNVDSMSGA EKEIKDTNIC
SSAKGIVESS VTSALAGNSD RPPVLCGSEG PMASASSHHS DSQLTRKETV EDTTISTGLV
KGSDDVLVSG EVPECEVGHM SPRKNEECDG LMASTASCDV SNKDSLAGSK SQGNGLMIST
STNACTPQIS AVIDVRGGHL STLSTEEIRD GVRVHREGFE APMPSAVSGE NSQLTASRSE
EKDECAMIST SIGEEFELPI SSAVTVTCAE RQQPVAAVEE STTGPALVST EDFEVPMPSA
PTEAESPLAS TSKEEKDECA LISTSIAEEC EASVFGVSRN APSVTDGNAV ISTSSVEDCE
GSVSSAVPQE SVCPSVIPVE ETGDTAMIST STSEGREAVM VGTIPTDDDQ ATTVRGEDLS
DAAIISTSTA ECVLTCTSLS RHEENQQATH NPEGNGGHLA TKQSKCELPM PSLVAERNCK
CPGPFRMGKG VGPLMAVGTR GEHDRLPVCE PSVGQGQPGT ALCLGEEESH GMDCPGQDLN
AKERNTLLSS VQRESKSAEA EAAGDSSTAR RTVRKDSERN ANSLSETNCL REPEQKPAED
TSGSTHCLTA VNPGAEADGM LPITHAALEY PDHQEPESNL KTTTKCITGQ ESQMPSSHTG
VLSAVCHVAP CASEQEGGLP TKSDHSGTWT SEGSPEKMGH VAGARQSFHR EGNLDVTLPP
EDNGCGVGNE ESPPKGIGGL ELSTGLTTEI SVSSEEDTSH GVVAAPENPC VGRRRGAAEL
QMEALLMRES LNVEKSESRI NEEIHFESQN KEEICCGRKG STEALSGCSV EADPEEVEEE
EKQISQRNRK PDYSSSEEEL DDSPDVLDSR IETAQRQYSE TEPHDTKEEN SGDVEEFSSV
TSKTNSSTGL EDRDEFSSSE GTGEKTEPNE DDGSIKSQED DHPIIIKRRR GRPRKYPAET
AFKSKEDSKT ETDITTVEQS SPSGKLKVSQ ADESNKEIAN LEEKSTSNDD SEEKTASMRL
RGRKPKRSLT SSDDAESSEP ERKRQKSVSE TSEDKKDEES DEEEEEEEEE EPLGATTRSA
TRSEAQRKNH SKPSTRATSK LGIPETISPR NRQKLAKEKL STSEKVSKSP PLGRSKAQLS
PSVKRKREVS PPGARTRGQQ KVDENPLKKA KR
