ID BD1L1_HUMAN Reviewed; 3051 AA. AC Q8NFC6; Q6P0M8; Q96AL1; Q9H6G0; Q9NTD6; Q9P2L9; DT 22-NOV-2005, integrated into UniProtKB/Swiss-Prot. DT 02-OCT-2007, sequence version 2. DT 27-MAR-2024, entry version 153. DE RecName: Full=Biorientation of chromosomes in cell division protein 1-like 1 {ECO:0000305}; GN Name=BOD1L1 {ECO:0000312|HGNC:HGNC:31792}; GN Synonyms=BOD1L, FAM44A, KIAA1327 {ECO:0000303|PubMed:10718198}; 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 [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-502. RC TISSUE=Ovary; RA Guo J.H., Yu L.; RL Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases. RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-338 AND 2649-3051. RC TISSUE=Duodenum, Skin, and Uterus; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1207-1861. 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 MRNA] OF 1248-3051, AND VARIANT LEU-2396. RC TISSUE=Brain; RX PubMed=10718198; DOI=10.1093/dnares/7.1.65; RA Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.; RT "Prediction of the coding sequences of unidentified human genes. XVI. The RT complete sequences of 150 new cDNA clones from brain which code for large RT proteins in vitro."; RL DNA Res. 7:65-73(2000). RN [6] RP SEQUENCE REVISION. RX PubMed=12168954; DOI=10.1093/dnares/9.3.99; RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.; RT "Construction of expression-ready cDNA clones for KIAA genes: manual RT curation of 330 KIAA cDNA clones."; RL DNA Res. 9:99-106(2002). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2444-2874. RC TISSUE=Testis; RX PubMed=17974005; DOI=10.1186/1471-2164-8-399; RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., RA Wiemann S., Schupp I.; RT "The full-ORF clone resource of the German cDNA consortium."; RL BMC Genomics 8:399-399(2007). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026; RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-1354, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=16964243; DOI=10.1038/nbt1240; RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; RT "A probability-based approach for high-throughput protein phosphorylation RT analysis and site localization."; RL Nat. Biotechnol. 24:1285-1292(2006). RN [10] RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-2981 AND LYS-2982, AND RP IDENTIFICATION BY MASS SPECTROMETRY. RC TISSUE=Mammary cancer; RX PubMed=17370265; DOI=10.1002/pmic.200600410; RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.; RT "Tryptic digestion of ubiquitin standards reveals an improved strategy for RT identifying ubiquitinated proteins by mass spectrometry."; RL Proteomics 7:868-874(2007). RN [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1145 AND SER-1710, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Embryonic kidney; RX PubMed=17525332; DOI=10.1126/science.1140321; RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., RA Gygi S.P., Elledge S.J.; RT "ATM and ATR substrate analysis reveals extensive protein networks RT responsive to DNA damage."; RL Science 316:1160-1166(2007). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482; SER-484; THR-1354; RP SER-1531; SER-2954 AND SER-2986, AND IDENTIFICATION BY MASS SPECTROMETRY RP [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 [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19413330; DOI=10.1021/ac9004309; RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.; RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a RT refined SCX-based approach."; RL Anal. Chem. 81:4493-4501(2009). RN [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-482; SER-484; RP SER-2907; THR-2956; SER-2958 AND SER-2964, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [15] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-473, 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 [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-482; SER-484; SER-635; RP SER-1531 AND SER-2501, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [17] 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 [18] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-482; SER-484; RP SER-1531; SER-2905; SER-2973 AND SER-2986, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [19] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-266; SER-482; SER-484; RP SER-635; SER-659; THR-660; THR-733; SER-1077; SER-1318; THR-1354; SER-1531; RP SER-1701; SER-2128; SER-2475; SER-2501; SER-2905; THR-2956; SER-2986 AND RP SER-3019, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and 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 [20] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2203, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [21] RP VARIANT [LARGE SCALE ANALYSIS] ILE-246. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). RN [22] RP FUNCTION, AND 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). RN [23] RP FUNCTION, AND INTERACTION WITH SETD1A. RX PubMed=29937342; DOI=10.1016/j.molcel.2018.05.018; RA Higgs M.R., Sato K., Reynolds J.J., Begum S., Bayley R., Goula A., RA Vernet A., Paquin K.L., Skalnik D.G., Kobayashi W., Takata M., RA Howlett N.G., Kurumizaka H., Kimura H., Stewart G.S.; RT "Histone Methylation by SETD1A Protects Nascent DNA through the Nucleosome RT Chaperone Activity of FANCD2."; RL Mol. Cell 71:25-41(2018). 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 (PubMed:26166705, PubMed:29937342). Does not CC regulate spindle orientation (PubMed:26166705). CC {ECO:0000269|PubMed:26166705, ECO:0000269|PubMed:29937342}. 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:0000269|PubMed:29937342}. CC -!- INTERACTION: CC Q8NFC6; P61964: WDR5; NbExp=4; IntAct=EBI-2654318, EBI-540834; CC -!- SUBCELLULAR LOCATION: Chromosome {ECO:0000269|Ref.2}. Note=Localizes at CC replication forks: following DNA damage, localizes to damaged CC replication forks undergoing resection. {ECO:0000269|Ref.2}. CC -!- SIMILARITY: Belongs to the BOD1 family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAH16987.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAB15299.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305}; CC Sequence=CAB70705.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; 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; AC006445; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF528529; AAM94279.1; -; mRNA. DR EMBL; BC016987; AAH16987.1; ALT_INIT; mRNA. DR EMBL; BC065546; AAH65546.1; -; mRNA. DR EMBL; BC087835; AAH87835.1; -; mRNA. DR EMBL; AK025965; BAB15299.1; ALT_TERM; mRNA. DR EMBL; AB037748; BAA92565.2; -; mRNA. DR EMBL; AL137350; CAB70705.1; ALT_TERM; mRNA. DR CCDS; CCDS3411.2; -. DR PIR; T46424; T46424. DR RefSeq; NP_683692.2; NM_148894.2. DR BioGRID; 129238; 135. DR ComplexPortal; CPX-7111; Histone-lysine N-methyltransferase complex, SET1B variant. DR CORUM; Q8NFC6; -. DR IntAct; Q8NFC6; 42. DR MINT; Q8NFC6; -. DR STRING; 9606.ENSP00000040738; -. DR GlyCosmos; Q8NFC6; 1 site, 1 glycan. DR GlyGen; Q8NFC6; 6 sites, 1 O-linked glycan (6 sites). DR iPTMnet; Q8NFC6; -. DR PhosphoSitePlus; Q8NFC6; -. DR BioMuta; BOD1L1; -. DR DMDM; 158931124; -. DR EPD; Q8NFC6; -. DR jPOST; Q8NFC6; -. DR MassIVE; Q8NFC6; -. DR MaxQB; Q8NFC6; -. DR PaxDb; 9606-ENSP00000040738; -. DR PeptideAtlas; Q8NFC6; -. DR ProteomicsDB; 73286; -. DR Pumba; Q8NFC6; -. DR Antibodypedia; 50158; 43 antibodies from 14 providers. DR DNASU; 259282; -. DR Ensembl; ENST00000040738.10; ENSP00000040738.5; ENSG00000038219.13. DR GeneID; 259282; -. DR KEGG; hsa:259282; -. DR MANE-Select; ENST00000040738.10; ENSP00000040738.5; NM_148894.3; NP_683692.2. DR UCSC; uc003gmz.2; human. DR AGR; HGNC:31792; -. DR CTD; 259282; -. DR DisGeNET; 259282; -. DR GeneCards; BOD1L1; -. DR HGNC; HGNC:31792; BOD1L1. DR HPA; ENSG00000038219; Low tissue specificity. DR MIM; 616746; gene. DR neXtProt; NX_Q8NFC6; -. DR OpenTargets; ENSG00000038219; -. DR PharmGKB; PA164716652; -. DR VEuPathDB; HostDB:ENSG00000038219; -. DR eggNOG; ENOG502QTHP; Eukaryota. DR GeneTree; ENSGT00940000156198; -. DR HOGENOM; CLU_000519_0_0_1; -. DR InParanoid; Q8NFC6; -. DR OMA; IKFYPVD; -. DR OrthoDB; 5321057at2759; -. DR PhylomeDB; Q8NFC6; -. DR TreeFam; TF335808; -. DR PathwayCommons; Q8NFC6; -. DR Reactome; R-HSA-9772755; Formation of WDR5-containing histone-modifying complexes. DR SignaLink; Q8NFC6; -. DR BioGRID-ORCS; 259282; 97 hits in 1157 CRISPR screens. DR ChiTaRS; BOD1L1; human. DR GenomeRNAi; 259282; -. DR Pharos; Q8NFC6; Tdark. DR PRO; PR:Q8NFC6; -. DR Proteomes; UP000005640; Chromosome 4. DR RNAct; Q8NFC6; Protein. DR Bgee; ENSG00000038219; Expressed in sural nerve and 187 other cell types or tissues. DR ExpressionAtlas; Q8NFC6; baseline and differential. DR GO; GO:0005694; C:chromosome; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0048188; C:Set1C/COMPASS complex; IPI:ComplexPortal. DR GO; GO:0006974; P:DNA damage response; IDA:UniProtKB. DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW. DR GO; GO:0031297; P:replication fork processing; IDA: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; Q8NFC6; HS. PE 1: Evidence at protein level; KW Acetylation; Chromosome; DNA damage; DNA repair; Isopeptide bond; KW Phosphoprotein; Reference proteome; Ubl conjugation. FT CHAIN 1..3051 FT /note="Biorientation of chromosomes in cell division FT protein 1-like 1" FT /id="PRO_0000187027" FT DNA_BIND 2872..2884 FT /note="A.T hook" FT REGION 1..47 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 164..197 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 215..288 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 301..393 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 411..469 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 497..1203 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1456..1550 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1700..1725 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1760..1890 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2189..2210 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2258..2285 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2403..2447 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2472..2519 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2615..2635 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 2717..3051 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1..35 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 175..197 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 215..246 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 247..266 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 310..377 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 419..439 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 497..531 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 543..660 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 668..770 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 781..854 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 867..881 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 888..913 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 937..969 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 986..1082 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1091..1107 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1131..1167 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1456..1481 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1482..1504 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1534..1550 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1768..1835 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2426..2440 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2472..2495 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2504..2519 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2618..2632 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2724..2783 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2799..2823 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2833..2872 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2880..2897 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2898..2930 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2953..2981 FT /note="Basic and acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 2982..2998 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 3002..3018 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 266 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 473 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 482 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 484 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 635 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 659 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 660 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 733 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1077 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1145 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 1318 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1354 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:16964243, FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:23186163" FT MOD_RES 1531 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 1701 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 1710 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17525332" FT MOD_RES 2013 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:E9Q6J5" FT MOD_RES 2025 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:E9Q6J5" FT MOD_RES 2128 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2203 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:24275569" FT MOD_RES 2475 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 2501 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2618 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:E9Q6J5" FT MOD_RES 2905 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2907 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 2954 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 2956 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:19690332, FT ECO:0007744|PubMed:23186163" FT MOD_RES 2958 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 2964 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 2973 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:21406692" FT MOD_RES 2986 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163" FT MOD_RES 3019 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT CROSSLNK 2981 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17370265" FT CROSSLNK 2982 FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with FT G-Cter in ubiquitin)" FT /evidence="ECO:0000269|PubMed:17370265" FT VARIANT 246 FT /note="S -> I (in a breast cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036124" FT VARIANT 429 FT /note="T -> M (in dbSNP:rs2035820)" FT /id="VAR_035220" FT VARIANT 650 FT /note="L -> I (in dbSNP:rs1971278)" FT /id="VAR_035221" FT VARIANT 1369 FT /note="A -> G (in dbSNP:rs17745712)" FT /id="VAR_035222" FT VARIANT 1448 FT /note="T -> A (in dbSNP:rs17745676)" FT /id="VAR_035223" FT VARIANT 1515 FT /note="T -> A (in dbSNP:rs16888885)" FT /id="VAR_035224" FT VARIANT 1645 FT /note="V -> I (in dbSNP:rs17807493)" FT /id="VAR_035225" FT VARIANT 2361 FT /note="G -> S (in dbSNP:rs3822227)" FT /id="VAR_035226" FT VARIANT 2396 FT /note="P -> L (in dbSNP:rs3733557)" FT /evidence="ECO:0000269|PubMed:10718198" FT /id="VAR_035227" FT VARIANT 2944 FT /note="V -> M (in dbSNP:rs28538279)" FT /id="VAR_061166" FT CONFLICT 337 FT /note="E -> K (in Ref. 3; AAH65546/AAH87835)" FT /evidence="ECO:0000305" FT CONFLICT 498..502 FT /note="AKEKE -> GILWF (in Ref. 2; AAM94279)" FT /evidence="ECO:0000305" FT CONFLICT 1417 FT /note="N -> S (in Ref. 4; BAB15299)" FT /evidence="ECO:0000305" FT CONFLICT 1438 FT /note="I -> V (in Ref. 4; BAB15299)" FT /evidence="ECO:0000305" FT CONFLICT 1740 FT /note="V -> M (in Ref. 4; BAB15299)" FT /evidence="ECO:0000305" SQ SEQUENCE 3051 AA; 330466 MW; 44AD19BDDFDCE560 CRC64; MATNPQPQPP PPAPPPPPPQ PQPQPPPPPP GPGAGPGAGG AGGAGAGAGD PQLVAMIVNH LKSQGLFDQF RRDCLADVDT KPAYQNLRQR VDNFVANHLA THTWSPHLNK NQLRNNIRQQ VLKSGMLESG IDRIISQVVD PKINHTFRPQ VEKAVHEFLA TLNHKEEGSG NTAPDDEKPD TSLITQGVPT PGPSANVAND AMSILETITS LNQEASAARA STETSNAKTS ERASKKLPSQ PTTDTSTDKE RTSEDMADKE KSTADSGGEG LETAPKSEEF SDLPCPVEEI KNYTKEHNNL ILLNKDVQQE SSEQKNKSTD KGEKKPDSNE KGERKKEKKE KTEKKFDHSK KSEDTQKVKD EKQAKEKEVE SLKLPSEKNS NKAKTVEGTK EDFSLIDSDV DGLTDITVSS VHTSDLSSFE EDTEEEVVTS DSMEEGEITS DDEEKNKQNK TKTQTSDSSE GKTKSVRHAY VHKPYLYSKY YSDSDDELTV EQRRQSIAKE KEERLLRRQI NREKLEEKRK QKAEKTKSSK TKGQGRSSVD LEESSTKSLE PKAARIKEVL KERKVLEKKV ALSKKRKKDS RNVEENSKKK QQYEEDSKET LKTSEHCEKE KISSSKELKH VHAKSEPSKP ARRLSESLHV VDENKNESKL EREHKRRTST PVIMEGVQEE TDTRDVKRQV ERSEICTEEP QKQKSTLKNE KHLKKDDSET PHLKSLLKKE VKSSKEKPER EKTPSEDKLS VKHKYKGDCM HKTGDETELH SSEKGLKVEE NIQKQSQQTK LSSDDKTERK SKHRNERKLS VLGKDGKPVS EYIIKTDENV RKENNKKERR LSAEKTKAEH KSRRSSDSKI QKDSLGSKQH GITLQRRSES YSEDKCDMDS TNMDSNLKPE EVVHKEKRRT KSLLEEKLVL KSKSKTQGKQ VKVVETELQE GATKQATTPK PDKEKNTEEN DSEKQRKSKV EDKPFEETGV EPVLETASSS AHSTQKDSSH RAKLPLAKEK YKSDKDSTST RLERKLSDGH KSRSLKHSSK DIKKKDENKS DDKDGKEVDS SHEKARGNSS LMEKKLSRRL CENRRGSLSQ EMAKGEEKLA ANTLSTPSGS SLQRPKKSGD MTLIPEQEPM EIDSEPGVEN VFEVSKTQDN RNNNSQQDID SENMKQKTSA TVQKDELRTC TADSKATAPA YKPGRGTGVN SNSEKHADHR STLTKKMHIQ SAVSKMNPGE KEPIHRGTTE VNIDSETVHR MLLSAPSEND RVQKNLKNTA AEEHVAQGDA TLEHSTNLDS SPSLSSVTVV PLRESYDPDV IPLFDKRTVL EGSTASTSPA DHSALPNQSL TVRESEVLKT SDSKEGGEGF TVDTPAKASI TSKRHIPEAH QATLLDGKQG KVIMPLGSKL TGVIVENENI TKEGGLVDMA KKENDLNAEP NLKQTIKATV ENGKKDGIAV DHVVGLNTEK YAETVKLKHK RSPGKVKDIS IDVERRNENS EVDTSAGSGS APSVLHQRNG QTEDVATGPR RAEKTSVATS TEGKDKDVTL SPVKAGPATT TSSETRQSEV ALPCTSIEAD EGLIIGTHSR NNPLHVGAEA SECTVFAAAE EGGAVVTEGF AESETFLTST KEGESGECAV AESEDRAADL LAVHAVKIEA NVNSVVTEEK DDAVTSAGSE EKCDGSLSRD SEIVEGTITF ISEVESDGAV TSAGTEIRAG SISSEEVDGS QGNMMRMGPK KETEGTVTCT GAEGRSDNFV ICSVTGAGPR EERMVTGAGV VLGDNDAPPG TSASQEGDGS VNDGTEGESA VTSTGITEDG EGPASCTGSE DSSEGFAISS ESEENGESAM DSTVAKEGTN VPLVAAGPCD DEGIVTSTGA KEEDEEGEDV VTSTGRGNEI GHASTCTGLG EESEGVLICE SAEGDSQIGT VVEHVEAEAG AAIMNANENN VDSMSGTEKG SKDTDICSSA KGIVESSVTS AVSGKDEVTP VPGGCEGPMT SAASDQSDSQ LEKVEDTTIS TGLVGGSYDV LVSGEVPECE VAHTSPSEKE DEDIITSVEN EECDGLMATT ASGDITNQNS LAGGKNQGKV LIISTSTTND YTPQVSAITD VEGGLSDALR TEENMEGTRV TTEEFEAPMP SAVSGDDSQL TASRSEEKDE CAMISTSIGE EFELPISSAT TIKCAESLQP VAAAVEERAT GPVLISTADF EGPMPSAPPE AESPLASTSK EEKDECALIS TSIAEECEAS VSGVVVESEN ERAGTVMEEK DGSGIISTSS VEDCEGPVSS AVPQEEGDPS VTPAEEMGDT AMISTSTSEG CEAVMIGAVL QDEDRLTITR VEDLSDAAII STSTAECMPI SASIDRHEEN QLTADNPEGN GDLSATEVSK HKVPMPSLIA ENNCRCPGPV RGGKEPGPVL AVSTEEGHNG PSVHKPSAGQ GHPSAVCAEK EEKHGKECPE IGPFAGRGQK ESTLHLINAE EKNVLLNSLQ KEDKSPETGT AGGSSTASYS AGRGLEGNAN SPAHLRGPEQ TSGQTAKDPS VSIRYLAAVN TGAIKADDMP PVQGTVAEHS FLPAEQQGSE DNLKTSTTKC ITGQESKIAP SHTMIPPATY SVALLAPKCE QDLTIKNDYS GKWTDQASAE KTGDDNSTRK SFPEEGDIMV TVSSEENVCD IGNEESPLNV LGGLKLKANL KMEAYVPSEE EKNGEILAPP ESLCGGKPSG IAELQREPLL VNESLNVENS GFRTNEEIHS ESYNKGEISS GRKDNAEAIS GHSVEADPKE VEEEERHMPK RKRKQHYLSS EDEPDDNPDV LDSRIETAQR QCPETEPHDT KEENSRDLEE LPKTSSETNS TTSRVMEEKD EYSSSETTGE KPEQNDDDTI KSQEEDQPII IKRKRGRPRK YPVETTLKMK DDSKTDTGIV TVEQSPSSSK LKVMQTDESN KETANLQERS ISNDDGEEKI VTSVRRRGRK PKRSLTVSDD AESSEPERKR QKSVSDPVED KKEQESDEEE EEEEEDEPSG ATTRSTTRSE AQRSKTQLSP SIKRKREVSP PGARTRGQQR VEEAPVKKAK R //