BD1L1_HUMAN
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 03-AUG-2022, entry version 144.
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};
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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; 101.
DR ComplexPortal; CPX-7111; Histone-lysine N-methyltransferase complex, SET1B variant.
DR CORUM; Q8NFC6; -.
DR IntAct; Q8NFC6; 39.
DR MINT; Q8NFC6; -.
DR STRING; 9606.ENSP00000040738; -.
DR GlyGen; Q8NFC6; 1 site, 1 O-linked glycan (1 site).
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; Q8NFC6; -.
DR PeptideAtlas; Q8NFC6; -.
DR PRIDE; Q8NFC6; -.
DR ProteomicsDB; 73286; -.
DR Antibodypedia; 50158; 40 antibodies from 13 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 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; NMKQKTS; -.
DR OrthoDB; 1333373at2759; -.
DR PhylomeDB; Q8NFC6; -.
DR TreeFam; TF335808; -.
DR PathwayCommons; Q8NFC6; -.
DR SignaLink; Q8NFC6; -.
DR BioGRID-ORCS; 259282; 90 hits in 1079 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 185 other tissues.
DR ExpressionAtlas; Q8NFC6; baseline and differential.
DR Genevisible; Q8NFC6; HS.
DR GO; GO:0005813; C:centrosome; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000940; C:outer kinetochore; IBA:GO_Central.
DR GO; GO:0048188; C:Set1C/COMPASS complex; IPI:ComplexPortal.
DR GO; GO:0005876; C:spindle microtubule; IBA:GO_Central.
DR GO; GO:0000922; C:spindle pole; IBA:GO_Central.
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; IDA:UniProtKB.
DR GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
DR GO; GO:0051568; P:histone H3-K4 methylation; IC:ComplexPortal.
DR GO; GO:0032515; P:negative regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR GO; GO:0031297; P:replication fork processing; IDA:UniProtKB.
DR InterPro; IPR043244; BOD1L1.
DR PANTHER; PTHR47391; PTHR47391; 2.
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
