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 27-MAR-2024, entry version 85. 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, RC Pancreas, 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}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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 GlyGen; E9Q6J5; 1 site, 1 O-linked glycan (1 site). DR iPTMnet; E9Q6J5; -. DR PhosphoSitePlus; E9Q6J5; -. DR SwissPalm; E9Q6J5; -. DR EPD; E9Q6J5; -. DR jPOST; E9Q6J5; -. DR MaxQB; E9Q6J5; -. DR PaxDb; 10090-ENSMUSP00000058618; -. DR PeptideAtlas; E9Q6J5; -. DR ProteomicsDB; 265203; -. [E9Q6J5-1] DR ProteomicsDB; 265204; -. [E9Q6J5-2] DR ProteomicsDB; 265205; -. [E9Q6J5-3] DR Pumba; E9Q6J5; -. DR Antibodypedia; 50158; 43 antibodies from 14 providers. DR Ensembl; ENSMUST00000050556.11; ENSMUSP00000058618.8; ENSMUSG00000061755.11. [E9Q6J5-1] DR Ensembl; ENSMUST00000202908.2; ENSMUSP00000144359.2; ENSMUSG00000061755.11. [E9Q6J5-2] DR GeneID; 665775; -. DR KEGG; mmu:665775; -. DR UCSC; uc008xhd.3; mouse. [E9Q6J5-1] DR UCSC; uc008xhg.1; mouse. DR AGR; MGI:2444804; -. 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; IKFYPVD; -. DR OrthoDB; 5321057at2759; -. DR PhylomeDB; E9Q6J5; -. DR TreeFam; TF335808; -. DR Reactome; R-MMU-9772755; Formation of WDR5-containing histone-modifying complexes. DR BioGRID-ORCS; 665775; 20 hits in 116 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 260 other cell types or tissues. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; ISO:MGI. DR GO; GO:0048188; C:Set1C/COMPASS complex; ISO:MGI. DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW. DR GO; GO:0006974; P:DNA damage response; ISS:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0031297; P:replication fork processing; ISS:UniProtKB. DR InterPro; IPR043244; BOD1L1. DR PANTHER; PTHR47391; BIORIENTATION OF CHROMOSOMES IN CELL DIVISION 1 LIKE 1; 1. DR PANTHER; PTHR47391:SF1; BIORIENTATION OF CHROMOSOMES IN CELL DIVISION 1 LIKE 1; 1. DR Pfam; PF05205; COMPASS-Shg1; 1. DR Genevisible; E9Q6J5; MM. 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 //