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Database: UniProt
Entry: Q8NG31
LinkDB: Q8NG31
Original site: Q8NG31 
ID   KNL1_HUMAN              Reviewed;        2342 AA.
AC   Q8NG31; Q8NHE1; Q8WXA6; Q9HCK2; Q9NR92;
DT   24-MAY-2005, integrated into UniProtKB/Swiss-Prot.
DT   10-FEB-2009, sequence version 3.
DT   29-SEP-2021, entry version 158.
DE   RecName: Full=Kinetochore scaffold 1;
DE   AltName: Full=ALL1-fused gene from chromosome 15q14 protein;
DE            Short=AF15q14;
DE   AltName: Full=Bub-linking kinetochore protein;
DE            Short=Blinkin;
DE   AltName: Full=Cancer susceptibility candidate gene 5 protein;
DE   AltName: Full=Cancer/testis antigen 29;
DE            Short=CT29;
DE   AltName: Full=Kinetochore-null protein 1;
DE   AltName: Full=Protein CASC5;
DE   AltName: Full=Protein D40/AF15q14;
GN   Name=KNL1 {ECO:0000312|HGNC:HGNC:24054}; Synonyms=CASC5, KIAA1570;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 2 AND 4), CHROMOSOMAL TRANSLOCATION
RP   WITH KMT2A/MLL1, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND VARIANTS
RP   SER-486; THR-598; GLY-936; GLU-1285 AND ALA-1473.
RX   PubMed=10980622; DOI=10.1038/sj.onc.1203789;
RA   Hayette S., Tigaud I., Vanier A., Martel S., Corbo L., Charrin C.,
RA   Beillard E., Deleage G., Magaud J.-P., Rimokh R.;
RT   "AF15q14, a novel partner gene fused to the MLL gene in an acute myeloid
RT   leukaemia with a t(11;15)(q23;q14).";
RL   Oncogene 19:4446-4450(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), TISSUE SPECIFICITY, AND VARIANTS
RP   THR-43; ALA-113; SER-486; THR-598 AND GLY-936.
RC   TISSUE=Testis;
RX   PubMed=12087463; DOI=10.1038/sj.bjc.6600328;
RA   Takimoto M., Wei G., Dosaka-Akita H., Mao P., Kondo S., Sakuragi N.,
RA   Chiba I., Miura T., Itoh N., Sasao T., Koya R.C., Tsukamoto T.,
RA   Fujimoto S., Kato H., Kuzumaki N.;
RT   "Frequent expression of new cancer/testis gene D40/AF15q14 in lung cancer
RT   of smokers.";
RL   Br. J. Cancer 86:1757-1762(2002).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHROMOSOMAL TRANSLOCATION WITH
RP   KMT2A/MLL1, TISSUE SPECIFICITY, AND VARIANTS THR-598 AND GLY-936.
RX   PubMed=12618768; DOI=10.1038/sj.onc.1206272;
RA   Kuefer M.U., Chinwalla V., Zeleznik-Le N.J., Behm F.G., Naeve C.W.,
RA   Rakestraw K.M., Mukatira S.T., Raimondi S.C., Morris S.W.;
RT   "Characterization of the MLL partner gene AF15q14 involved in
RT   t(11;15)(q23;q14).";
RL   Oncogene 22:1418-1424(2003).
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 983-2342.
RC   TISSUE=Brain;
RX   PubMed=10997877; DOI=10.1093/dnares/7.4.271;
RA   Nagase T., Kikuno R., Nakayama M., Hirosawa M., Ohara O.;
RT   "Prediction of the coding sequences of unidentified human genes. XVIII. The
RT   complete sequences of 100 new cDNA clones from brain which code for large
RT   proteins in vitro.";
RL   DNA Res. 7:273-281(2000).
RN   [6]
RP   CHROMOSOMAL TRANSLOCATION WITH KMT2A.
RX   PubMed=12618766; DOI=10.1038/sj.onc.1206273;
RA   Chinwalla V., Chien A., Odero M., Neilly M.B., Zeleznik-Le N.J.,
RA   Rowley J.D.;
RT   "A t(11;15) fuses MLL to two different genes, AF15q14 and a novel gene
RT   MPFYVE on chromosome 15.";
RL   Oncogene 22:1400-1410(2003).
RN   [7]
RP   INTERACTION WITH DSN1 AND MIS12, IDENTIFICATION BY MASS SPECTROMETRY, AND
RP   FUNCTION.
RX   PubMed=15502821; DOI=10.1038/ncb1187;
RA   Obuse C., Iwasaki O., Kiyomitsu T., Goshima G., Toyoda Y., Yanagida M.;
RT   "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and
RT   outer kinetochore protein Zwint-1.";
RL   Nat. Cell Biol. 6:1135-1141(2004).
RN   [8]
RP   SUBCELLULAR LOCATION.
RX   PubMed=15579588; DOI=10.1530/rep.1.00312;
RA   Sasao T., Itoh N., Takano H., Watanabe S., Wei G., Tsukamoto T.,
RA   Kuzumaki N., Takimoto M.;
RT   "The protein encoded by cancer/testis gene D40/AF15q14 is localized in
RT   spermatocytes, acrosomes of spermatids and ejaculated spermatozoa.";
RL   Reproduction 128:709-716(2004).
RN   [9]
RP   FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH BUB1; BUB1B; NSL1;
RP   DSN1 AND ZWINT.
RX   PubMed=17981135; DOI=10.1016/j.devcel.2007.09.005;
RA   Kiyomitsu T., Obuse C., Yanagida M.;
RT   "Human Blinkin/AF15q14 is required for chromosome alignment and the mitotic
RT   checkpoint through direct interaction with Bub1 and BubR1.";
RL   Dev. Cell 13:663-676(2007).
RN   [10]
RP   FUNCTION, AND SUBCELLULAR LOCATION.
RX   PubMed=18045986; DOI=10.1091/mbc.e07-10-1051;
RA   Cheeseman I.M., Hori T., Fukagawa T., Desai A.;
RT   "KNL1 and the CENP-H/I/K complex coordinately direct kinetochore assembly
RT   in vertebrates.";
RL   Mol. Biol. Cell 19:587-594(2008).
RN   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076, AND IDENTIFICATION BY
RP   MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA   Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA   Greff Z., Keri G., Stemmann O., Mann M.;
RT   "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT   kinome across the cell cycle.";
RL   Mol. Cell 31:438-448(2008).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-60; SER-1076;
RP   SER-1773 AND SER-1845, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   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   SUBCELLULAR LOCATION.
RX   PubMed=19450515; DOI=10.1016/j.cell.2009.03.035;
RA   Wan X., O'Quinn R.P., Pierce H.L., Joglekar A.P., Gall W.E., DeLuca J.G.,
RA   Carroll C.W., Liu S.-T., Yen T.J., McEwen B.F., Stukenberg P.T., Desai A.,
RA   Salmon E.D.;
RT   "Protein architecture of the human kinetochore microtubule attachment
RT   site.";
RL   Cell 137:672-684(2009).
RN   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1076, AND IDENTIFICATION BY
RP   MASS 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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-539; SER-956; SER-1076 AND
RP   SER-1831, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE 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   [16]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-32; SER-60; THR-539; SER-578;
RP   SER-584; THR-586; SER-767; SER-956; SER-1039; SER-1076; SER-1088; SER-1448;
RP   SER-1675; SER-1845 AND SER-1860, AND IDENTIFICATION BY MASS SPECTROMETRY
RP   [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   [17]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-598.
RX   PubMed=18987736; DOI=10.1038/nature07485;
RA   Ley T.J., Mardis E.R., Ding L., Fulton B., McLellan M.D., Chen K.,
RA   Dooling D., Dunford-Shore B.H., McGrath S., Hickenbotham M., Cook L.,
RA   Abbott R., Larson D.E., Koboldt D.C., Pohl C., Smith S., Hawkins A.,
RA   Abbott S., Locke D., Hillier L.W., Miner T., Fulton L., Magrini V.,
RA   Wylie T., Glasscock J., Conyers J., Sander N., Shi X., Osborne J.R.,
RA   Minx P., Gordon D., Chinwalla A., Zhao Y., Ries R.E., Payton J.E.,
RA   Westervelt P., Tomasson M.H., Watson M., Baty J., Ivanovich J., Heath S.,
RA   Shannon W.D., Nagarajan R., Walter M.J., Link D.C., Graubert T.A.,
RA   DiPersio J.F., Wilson R.K.;
RT   "DNA sequencing of a cytogenetically normal acute myeloid leukaemia
RT   genome.";
RL   Nature 456:66-72(2008).
RN   [18]
RP   VARIANT MCPH4 ILE-2041.
RX   PubMed=22983954; DOI=10.1093/hmg/dds386;
RA   Genin A., Desir J., Lambert N., Biervliet M., Van Der Aa N., Pierquin G.,
RA   Killian A., Tosi M., Urbina M., Lefort A., Libert F., Pirson I.,
RA   Abramowicz M.;
RT   "Kinetochore KMN network gene CASC5 mutated in primary microcephaly.";
RL   Hum. Mol. Genet. 21:5306-5317(2012).
RN   [19]
RP   VARIANT MCPH4 ILE-2041.
RX   PubMed=26626498; DOI=10.1007/s10048-015-0468-7;
RA   Saadi A., Verny F., Siquier-Pernet K., Bole-Feysot C., Nitschke P.,
RA   Munnich A., Abada-Dendib M., Chaouch M., Abramowicz M., Colleaux L.;
RT   "Refining the phenotype associated with CASC5 mutation.";
RL   Neurogenetics 17:71-78(2016).
CC   -!- FUNCTION: Performs two crucial functions during mitosis: it is
CC       essential for spindle-assembly checkpoint signaling and for correct
CC       chromosome alignment. Required for attachment of the kinetochores to
CC       the spindle microtubules. Directly links BUB1 and BUB1B to
CC       kinetochores. Part of the MIS12 complex, which may be fundamental for
CC       kinetochore formation and proper chromosome segregation during mitosis.
CC       Acts in coordination with CENPK to recruit the NDC80 complex to the
CC       outer kinetochore. {ECO:0000269|PubMed:15502821,
CC       ECO:0000269|PubMed:17981135, ECO:0000269|PubMed:18045986}.
CC   -!- SUBUNIT: Interacts with DSN1, MIS12, BUB1, BUB1B, NSL1 and ZWINT.
CC       {ECO:0000269|PubMed:15502821, ECO:0000269|PubMed:17981135}.
CC   -!- INTERACTION:
CC       Q8NG31; O43683: BUB1; NbExp=2; IntAct=EBI-1001161, EBI-748936;
CC       Q8NG31; P62136: PPP1CA; NbExp=2; IntAct=EBI-1001161, EBI-357253;
CC       Q8NG31-2; O43683: BUB1; NbExp=3; IntAct=EBI-10973816, EBI-748936;
CC       Q8NG31-2; O60566: BUB1B; NbExp=10; IntAct=EBI-10973816, EBI-1001438;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Chromosome, centromere, kinetochore.
CC       Note=Weakly expressed in interphase nuclei. Expression increases from
CC       prophase to late anaphase, but greatly diminishes from the telophase
CC       and cytokinesis to early G1 phase of cell cycle.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=4;
CC       Name=1;
CC         IsoId=Q8NG31-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q8NG31-2; Sequence=VSP_013795;
CC       Name=3;
CC         IsoId=Q8NG31-3; Sequence=VSP_013795, VSP_013796, VSP_013797;
CC       Name=4;
CC         IsoId=Q8NG31-4; Sequence=VSP_013795, VSP_018524, VSP_018525;
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis, where it is localized
CC       in germ cells, in particular in spermatocytes and in the pre-acrosome
CC       of round spermatids. Detected in the acrosome of ejaculated
CC       spermatozoa. Detected in adult thymus, bone marrow, colon, small
CC       intestine, appendix and placenta, and in fetal liver and thymus.
CC       {ECO:0000269|PubMed:10980622, ECO:0000269|PubMed:12087463,
CC       ECO:0000269|PubMed:12618768}.
CC   -!- DISEASE: Note=A chromosomal aberration involving KNL1 is associated
CC       with acute myeloblastic leukemia (AML). Translocation t(11;15)(q23;q14)
CC       with KMT2A. May give rise to a KMT2A-KNL1 fusion protein.
CC       {ECO:0000269|PubMed:12618766}.
CC   -!- DISEASE: Microcephaly 4, primary, autosomal recessive (MCPH4)
CC       [MIM:604321]: A disease defined as a head circumference more than 3
CC       standard deviations below the age-related mean. Brain weight is
CC       markedly reduced and the cerebral cortex is disproportionately small.
CC       Despite this marked reduction in size, the gyral pattern is relatively
CC       well preserved, with no major abnormality in cortical architecture.
CC       Affected individuals are mentally retarded. Primary microcephaly is
CC       further defined by the absence of other syndromic features or
CC       significant neurological deficits due to degenerative brain disorder.
CC       {ECO:0000269|PubMed:22983954, ECO:0000269|PubMed:26626498}. Note=The
CC       disease is caused by variants affecting the gene represented in this
CC       entry.
CC   -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC       Haematology;
CC       URL="http://atlasgeneticsoncology.org/Genes/AF15q14ID318.html";
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DR   EMBL; AF248041; AAF97513.1; -; mRNA.
DR   EMBL; AF461041; AAL67803.1; -; mRNA.
DR   EMBL; AB022190; BAC05691.1; -; mRNA.
DR   EMBL; AF173994; AAM45143.1; -; mRNA.
DR   EMBL; AC022405; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AB046790; BAB13396.1; -; mRNA.
DR   CCDS; CCDS42023.1; -. [Q8NG31-1]
DR   CCDS; CCDS42024.1; -. [Q8NG31-2]
DR   RefSeq; NP_653091.3; NM_144508.4. [Q8NG31-2]
DR   RefSeq; NP_733468.3; NM_170589.4. [Q8NG31-1]
DR   PDB; 3SI5; X-ray; 2.20 A; X/Y=234-252.
DR   PDB; 4A1G; X-ray; 2.60 A; E/F/G/H=176-226.
DR   PDB; 4NF9; X-ray; 2.80 A; A/B=2117-2337.
DR   PDB; 4NFA; X-ray; 2.50 A; A=2131-2337.
DR   PDBsum; 3SI5; -.
DR   PDBsum; 4A1G; -.
DR   PDBsum; 4NF9; -.
DR   PDBsum; 4NFA; -.
DR   BMRB; Q8NG31; -.
DR   SMR; Q8NG31; -.
DR   BioGRID; 121354; 69.
DR   ComplexPortal; CPX-5644; Kinetochore KNL1 complex.
DR   CORUM; Q8NG31; -.
DR   DIP; DIP-36474N; -.
DR   ELM; Q8NG31; -.
DR   IntAct; Q8NG31; 57.
DR   MINT; Q8NG31; -.
DR   STRING; 9606.ENSP00000335463; -.
DR   GlyGen; Q8NG31; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q8NG31; -.
DR   PhosphoSitePlus; Q8NG31; -.
DR   BioMuta; KNL1; -.
DR   DMDM; 223590239; -.
DR   EPD; Q8NG31; -.
DR   jPOST; Q8NG31; -.
DR   MassIVE; Q8NG31; -.
DR   MaxQB; Q8NG31; -.
DR   PaxDb; Q8NG31; -.
DR   PeptideAtlas; Q8NG31; -.
DR   PRIDE; Q8NG31; -.
DR   ProteomicsDB; 73413; -. [Q8NG31-1]
DR   ProteomicsDB; 73414; -. [Q8NG31-2]
DR   ProteomicsDB; 73415; -. [Q8NG31-3]
DR   ProteomicsDB; 73416; -. [Q8NG31-4]
DR   Antibodypedia; 23122; 112 antibodies.
DR   CPTC; Q8NG31; 1 antibody.
DR   DNASU; 57082; -.
DR   Ensembl; ENST00000346991; ENSP00000335463; ENSG00000137812. [Q8NG31-1]
DR   Ensembl; ENST00000399668; ENSP00000382576; ENSG00000137812. [Q8NG31-2]
DR   GeneID; 57082; -.
DR   KEGG; hsa:57082; -.
DR   UCSC; uc010bbs.2; human. [Q8NG31-1]
DR   CTD; 57082; -.
DR   DisGeNET; 57082; -.
DR   GeneCards; KNL1; -.
DR   HGNC; HGNC:24054; KNL1.
DR   HPA; ENSG00000137812; Group enriched (lymphoid tissue, testis).
DR   MalaCards; KNL1; -.
DR   MIM; 604321; phenotype.
DR   MIM; 609173; gene.
DR   neXtProt; NX_Q8NG31; -.
DR   OpenTargets; ENSG00000137812; -.
DR   Orphanet; 2512; Autosomal recessive primary microcephaly.
DR   PharmGKB; PA142672201; -.
DR   VEuPathDB; HostDB:ENSG00000137812; -.
DR   eggNOG; ENOG502QW5H; Eukaryota.
DR   GeneTree; ENSGT00410000025918; -.
DR   InParanoid; Q8NG31; -.
DR   OMA; DINRNLW; -.
DR   OrthoDB; 1249457at2759; -.
DR   PhylomeDB; Q8NG31; -.
DR   TreeFam; TF335517; -.
DR   PathwayCommons; Q8NG31; -.
DR   Reactome; R-HSA-141444; Amplification of signal from unattached kinetochores via a MAD2 inhibitory signal.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2500257; Resolution of Sister Chromatid Cohesion.
DR   Reactome; R-HSA-5663220; RHO GTPases Activate Formins.
DR   Reactome; R-HSA-606279; Deposition of new CENPA-containing nucleosomes at the centromere.
DR   Reactome; R-HSA-68877; Mitotic Prometaphase.
DR   Reactome; R-HSA-9648025; EML4 and NUDC in mitotic spindle formation.
DR   SIGNOR; Q8NG31; -.
DR   BioGRID-ORCS; 57082; 569 hits in 1026 CRISPR screens.
DR   ChiTaRS; KNL1; human.
DR   EvolutionaryTrace; Q8NG31; -.
DR   GeneWiki; CASC5; -.
DR   GenomeRNAi; 57082; -.
DR   Pharos; Q8NG31; Tbio.
DR   PRO; PR:Q8NG31; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; Q8NG31; protein.
DR   Bgee; ENSG00000137812; Expressed in testis and 142 other tissues.
DR   ExpressionAtlas; Q8NG31; baseline and differential.
DR   Genevisible; Q8NG31; HS.
DR   GO; GO:0001669; C:acrosomal vesicle; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0000776; C:kinetochore; IDA:WormBase.
DR   GO; GO:0016604; C:nuclear body; IDA:HPA.
DR   GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR   GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR   GO; GO:0001675; P:acrosome assembly; NAS:UniProtKB.
DR   GO; GO:0008608; P:attachment of spindle microtubules to kinetochore; IDA:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0034501; P:protein localization to kinetochore; IDA:MGI.
DR   DisProt; DP01269; -.
DR   IDEAL; IID00417; -.
DR   InterPro; IPR037388; Blinkin.
DR   InterPro; IPR043651; KNL1_MELT_rep.
DR   InterPro; IPR040850; Knl1_RWD_C.
DR   PANTHER; PTHR16520; PTHR16520; 1.
DR   Pfam; PF18210; Knl1_RWD_C; 1.
DR   Pfam; PF19221; MELT; 12.
PE   1: Evidence at protein level;
KW   3D-structure; Alternative splicing; Cell cycle; Cell division; Centromere;
KW   Chromosomal rearrangement; Chromosome; Chromosome partition; Coiled coil;
KW   Disease variant; Kinetochore; Mental retardation; Mitosis; Nucleus;
KW   Phosphoprotein; Primary microcephaly; Reference proteome; Repeat.
FT   CHAIN           1..2342
FT                   /note="Kinetochore scaffold 1"
FT                   /id="PRO_0000089327"
FT   REPEAT          885..989
FT                   /note="1"
FT   REPEAT          1099..1201
FT                   /note="2"
FT   REGION          1..728
FT                   /note="Interaction with BUB1 and BUB1B"
FT                   /evidence="ECO:0000269|PubMed:17981135"
FT   REGION          1..56
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          620..646
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          855..1201
FT                   /note="2 X 104 AA approximate repeats"
FT   REGION          1639..1662
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1834..2316
FT                   /note="Necessary for kinetochore localization and for
FT                   interaction with NSL1 and DSN1"
FT                   /evidence="ECO:0000269|PubMed:17981135"
FT   COILED          1942..2133
FT                   /evidence="ECO:0000255"
FT   MOTIF           1789..1803
FT                   /note="Nuclear localization signal"
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        632..646
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   SITE            1818..1819
FT                   /note="Breakpoint for translocation to form KMT2A-KNL1"
FT                   /evidence="ECO:0000269|PubMed:12618766"
FT   MOD_RES         32
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         60
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         539
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         578
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         584
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         586
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         767
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         956
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1039
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1076
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         1088
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1448
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1675
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   MOD_RES         1773
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1831
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231"
FT   MOD_RES         1845
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         1860
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   VAR_SEQ         84..109
FT                   /note="Missing (in isoform 2, isoform 3 and isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10980622,
FT                   ECO:0000303|PubMed:12087463"
FT                   /id="VSP_013795"
FT   VAR_SEQ         1764..1772
FT                   /note="LIETYQKEI -> VGTRRRRYS (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12087463"
FT                   /id="VSP_013796"
FT   VAR_SEQ         1773..2342
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:12087463"
FT                   /id="VSP_013797"
FT   VAR_SEQ         1819..1859
FT                   /note="IFDHHTEEDIDKSANSVLIKNLSRTPSSCSSSLDSIKADGT -> VSSVLNQ
FT                   RMFLNFGFCFVFLNCGYSQILILVSGRQKIIIST (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10980622"
FT                   /id="VSP_018524"
FT   VAR_SEQ         1860..2342
FT                   /note="Missing (in isoform 4)"
FT                   /evidence="ECO:0000303|PubMed:10980622"
FT                   /id="VSP_018525"
FT   VARIANT         43
FT                   /note="R -> T (in dbSNP:rs7177192)"
FT                   /evidence="ECO:0000269|PubMed:12087463"
FT                   /id="VAR_026428"
FT   VARIANT         70
FT                   /note="T -> A (in dbSNP:rs16970874)"
FT                   /id="VAR_026429"
FT   VARIANT         113
FT                   /note="T -> A (in dbSNP:rs12911738)"
FT                   /evidence="ECO:0000269|PubMed:12087463"
FT                   /id="VAR_026430"
FT   VARIANT         177
FT                   /note="M -> V (in dbSNP:rs35146555)"
FT                   /id="VAR_061568"
FT   VARIANT         486
FT                   /note="A -> S (in dbSNP:rs2412541)"
FT                   /evidence="ECO:0000269|PubMed:10980622,
FT                   ECO:0000269|PubMed:12087463"
FT                   /id="VAR_026431"
FT   VARIANT         598
FT                   /note="M -> T (in dbSNP:rs11858113)"
FT                   /evidence="ECO:0000269|PubMed:10980622,
FT                   ECO:0000269|PubMed:12087463, ECO:0000269|PubMed:12618768,
FT                   ECO:0000269|PubMed:18987736"
FT                   /id="VAR_054342"
FT   VARIANT         936
FT                   /note="R -> G (in dbSNP:rs8040502)"
FT                   /evidence="ECO:0000269|PubMed:10980622,
FT                   ECO:0000269|PubMed:12087463, ECO:0000269|PubMed:12618768"
FT                   /id="VAR_026432"
FT   VARIANT         1190
FT                   /note="L -> V (in dbSNP:rs58614880)"
FT                   /id="VAR_061569"
FT   VARIANT         1285
FT                   /note="K -> E (in dbSNP:rs17747633)"
FT                   /evidence="ECO:0000269|PubMed:10980622"
FT                   /id="VAR_026433"
FT   VARIANT         1473
FT                   /note="T -> A (in dbSNP:rs16970911)"
FT                   /evidence="ECO:0000269|PubMed:10980622"
FT                   /id="VAR_026434"
FT   VARIANT         2041
FT                   /note="M -> I (in MCPH4; may inactivate an exonic splicing
FT                   enhancer and result in abnormal splicing;
FT                   dbSNP:rs763915472)"
FT                   /evidence="ECO:0000269|PubMed:22983954,
FT                   ECO:0000269|PubMed:26626498"
FT                   /id="VAR_069085"
FT   VARIANT         2338
FT                   /note="C -> Y (in dbSNP:rs61164860)"
FT                   /id="VAR_061570"
FT   CONFLICT        37
FT                   /note="L -> H (in Ref. 3; AAM45143)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1332
FT                   /note="P -> A (in Ref. 2; BAC05691)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1357
FT                   /note="N -> H (in Ref. 2; BAC05691)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1756
FT                   /note="N -> Y (in Ref. 2; BAC05691)"
FT                   /evidence="ECO:0000305"
FT   HELIX           205..211
FT                   /evidence="ECO:0007829|PDB:4A1G"
FT   HELIX           241..250
FT                   /evidence="ECO:0007829|PDB:3SI5"
FT   HELIX           2123..2130
FT                   /evidence="ECO:0007829|PDB:4NF9"
FT   STRAND          2136..2140
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   STRAND          2146..2151
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   STRAND          2154..2162
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   TURN            2168..2170
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   HELIX           2172..2174
FT                   /evidence="ECO:0007829|PDB:4NF9"
FT   STRAND          2177..2184
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   TURN            2188..2190
FT                   /evidence="ECO:0007829|PDB:4NF9"
FT   HELIX           2193..2210
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   TURN            2213..2215
FT                   /evidence="ECO:0007829|PDB:4NF9"
FT   HELIX           2219..2221
FT                   /evidence="ECO:0007829|PDB:4NF9"
FT   HELIX           2222..2249
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   HELIX           2250..2253
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   STRAND          2255..2261
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   STRAND          2264..2271
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   TURN            2272..2275
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   STRAND          2276..2283
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   TURN            2286..2289
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   STRAND          2295..2302
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   HELIX           2306..2315
FT                   /evidence="ECO:0007829|PDB:4NFA"
FT   HELIX           2322..2334
FT                   /evidence="ECO:0007829|PDB:4NFA"
SQ   SEQUENCE   2342 AA;  265391 MW;  8E29150CA4F5B5C1 CRC64;
     MDGVSSEANE ENDNIERPVR RRHSSILKPP RSPLQDLRGG NERVQESNAL RNKKNSRRVS
     FADTIKVFQT ESHMKIVRKS EMEGCSAMVP SQLQLLPPGF KRFSCLSLPE TETGENLLLI
     QNKKLEDNYC EITGMNTLLS APIHTQMQQK EFSIIEHTRE RKHANDQTVI FSDENQMDLT
     SSHTVMITKG LLDNPISEKS TKIDTTSFLA NLKLHTEDSR MKKEVNFSVD QNTSSENKID
     FNDFIKRLKT GKCSAFPDVP DKENFEIPIY SKEPNSASST HQMHVSLKED ENNSNITRLF
     REKDDGMNFT QCHTANIQTL IPTSSETNSR ESKGNDITIY GNDFMDLTFN HTLQILPATG
     NFSEIENQTQ NAMDVTTGYG TKASGNKTVF KSKQNTAFQD LSINSADKIH ITRSHIMGAE
     THIVSQTCNQ DARILAMTPE SIYSNPSIQG CKTVFYSSCN DAMEMTKCLS NMREEKNLLK
     HDSNYAKMYC NPDAMSSLTE KTIYSGEENM DITKSHTVAI DNQIFKQDQS NVQIAAAPTP
     EKEMMLQNLM TTSEDGKMNV NCNSVPHVSK ERIQQSLSNP LSISLTDRKT ELLSGENMDL
     TESHTSNLGS QVPLAAYNLA PESTSESHSQ SKSSSDECEE ITKSRNEPFQ RSDIIAKNSL
     TDTWNKDKDW VLKILPYLDK DSPQSADCNQ EIATSHNIVY CGGVLDKQIT NRNTVSWEQS
     LFSTTKPLFS SGQFSMKNHD TAISSHTVKS VLGQNSKLAE PLRKSLSNPT PDYCHDKMII
     CSEEEQNMDL TKSHTVVIGF GPSELQELGK TNLEHTTGQL TTMNRQIAVK VEKCGKSPIE
     KSGVLKSNCI MDVLEDESVQ KPKFPKEKQN VKIWGRKSVG GPKIDKTIVF SEDDKNDMDI
     TKSYTIEINH RPLLEKRDCH LVPLAGTSET ILYTCRQDDM EITRSHTTAL ECKTVSPDEI
     TTRPMDKTVV FVDNHVELEM TESHTVFIDY QEKERTDRPN FELSQRKSLG TPTVICTPTE
     ESVFFPGNGE SDRLVANDSQ LTPLEEWSNN RGPVEVADNM ELSKSATCKN IKDVQSPGFL
     NEPLSSKSQR RKSLKLKNDK TIVFSENHKN DMDITQSCMV EIDNESALED KEDFHLAGAS
     KTILYSCGQD DMEITRSHTT ALECKTLLPN EIAIRPMDKT VLFTDNYSDL EVTDSHTVFI
     DCQATEKILE ENPKFGIGKG KNLGVSFPKD NSCVQEIAEK QALAVGNKIV LHTEQKQQLF
     AATNRTTNEI IKFHSAAMDE KVIGKVVDQA CTLEKAQVES CQLNNRDRRN VDFTSSHATA
     VCGSSDNYSC LPNVISCTDN LEGSAMLLCD KDEEKANYCP VQNDLAYAND FASEYYLESE
     GQPLSAPCPL LEKEEVIQTS TKGQLDCVIT LHKDQDLIKD PRNLLANQTL VYSQDLGEMT
     KLNSKRVSFK LPKDQMKVYV DDIYVIPQPH FSTDQPPLPK KGQSSINKEE VILSKAGNKS
     LNIIENSSAP ICENKPKILN SEEWFAAACK KELKENIQTT NYNTALDFHS NSDVTKQVIQ
     THVNAGEAPD PVITSNVPCF HSIKPNLNNL NGKTGEFLAF QTVHLPPLPE QLLELGNKAH
     NDMHIVQATE IHNINIISSN AKDSRDEENK KSHNGAETTS LPPKTVFKDK VRRCSLGIFL
     PRLPNKRNCS VTGIDDLEQI PADTTDINHL ETQPVSSKDS GIGSVAGKLN LSPSQYINEE
     NLPVYPDEIN SSDSINIETE EKALIETYQK EISPYENKMG KTCNSQKRTW VQEEEDIHKE
     KKIRKNEIKF SDTTQDREIF DHHTEEDIDK SANSVLIKNL SRTPSSCSSS LDSIKADGTS
     LDFSTYRSSQ MESQFLRDTI CEESLREKLQ DGRITIREFF ILLQVHILIQ KPRQSNLPGN
     FTVNTPPTPE DLMLSQYVYR PKIQIYREDC EARRQKIEEL KLSASNQDKL LVDINKNLWE
     KMRHCSDKEL KAFGIYLNKI KSCFTKMTKV FTHQGKVALY GKLVQSAQNE REKLQIKIDE
     MDKILKKIDN CLTEMETETK NLEDEEKNNP VEEWDSEMRA AEKELEQLKT EEEELQRNLL
     ELEVQKEQTL AQIDFMQKQR NRTEELLDQL SLSEWDVVEW SDDQAVFTFV YDTIQLTITF
     EESVVGFPFL DKRYRKIVDV NFQSLLDEDQ APPSSLLVHK LIFQYVEEKE SWKKTCTTQH
     QLPKMLEEFS LVVHHCRLLG EEIEYLKRWG PNYNLMNIDI NNNELRLLFS SSAAFAKFEI
     TLFLSAYYPS VPLPSTIQNH VGNTSQDDIA TILSKVPLEN NYLKNVVKQI YQDLFQDCHF
     YH
//
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