KANL1_MOUSE
ID KANL1_MOUSE Reviewed; 1036 AA.
AC Q80TG1; A2A5Y5; Q3TT88; Q3U5D8; Q3V3N3; Q7TMU3; Q80XP7; Q8R3L6; Q9D9G0;
DT 16-MAY-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2003, sequence version 1.
DT 03-AUG-2022, entry version 119.
DE RecName: Full=KAT8 regulatory NSL complex subunit 1;
DE AltName: Full=NSL complex protein NSL1;
DE AltName: Full=Non-specific lethal 1 homolog;
GN Name=Kansl1; Synonyms=Kiaa1267, Nsl1;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 4 AND 5).
RC STRAIN=C57BL/6J; TISSUE=Testis, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC STRAIN=C3H/He, C57BL/6J, and FVB/N;
RC TISSUE=Embryonic brain, Mammary gland, and Mesenchymal stem cell;
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 [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-249 AND SER-268, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Kidney, Liver, Lung, Pancreas, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: As part of the NSL complex it is involved in acetylation of
CC nucleosomal histone H4 on several lysine residues and therefore may be
CC involved in the regulation of transcription. {ECO:0000250}.
CC -!- SUBUNIT: Component of some MLL1/MLL complex, at least composed of the
CC core components KMT2A/MLL1, ASH2L, HCFC1, WDR5 and RBBP5, as well as
CC the facultative components BAP18, CHD8, E2F6, HSP70, INO80C, KANSL1,
CC LAS1L, MAX, MCRS1, MGA, KAT8/MOF, PELP1, PHF20, PRP31, RING2,
CC RUVB1/TIP49A, RUVB2/TIP49B, SENP3, TAF1, TAF4, TAF6, TAF7, TAF9 and
CC TEX10. Component of the NSL complex at least composed of MOF/KAT8,
CC KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1.
CC Interacts with KAT8; the interaction is direct (By similarity).
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q7Z3B3}.
CC Chromosome, centromere, kinetochore {ECO:0000250|UniProtKB:Q7Z3B3}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q80TG1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80TG1-2; Sequence=VSP_018363, VSP_018364;
CC Name=3;
CC IsoId=Q80TG1-3; Sequence=VSP_018362, VSP_018363, VSP_018364;
CC Name=4;
CC IsoId=Q80TG1-4; Sequence=VSP_018361;
CC Name=5;
CC IsoId=Q80TG1-5; Sequence=VSP_018360, VSP_018365;
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DR EMBL; AK122484; BAC65766.1; -; mRNA.
DR EMBL; AK006970; BAB24813.1; -; mRNA.
DR EMBL; AK037800; BAE20523.1; -; mRNA.
DR EMBL; AK153679; BAE32141.1; -; mRNA.
DR EMBL; AK161514; BAE36437.1; -; mRNA.
DR EMBL; AL593843; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC025052; AAH25052.1; -; mRNA.
DR EMBL; BC043121; AAH43121.2; -; mRNA.
DR EMBL; BC053389; AAH53389.2; -; mRNA.
DR EMBL; BC054752; AAH54752.2; -; mRNA.
DR EMBL; BC079594; AAH79594.1; -; mRNA.
DR CCDS; CCDS48953.1; -. [Q80TG1-1]
DR RefSeq; NP_001074514.1; NM_001081045.1. [Q80TG1-1]
DR RefSeq; XP_006534516.1; XM_006534453.3.
DR RefSeq; XP_011247610.1; XM_011249308.2.
DR RefSeq; XP_017170320.1; XM_017314831.1.
DR AlphaFoldDB; Q80TG1; -.
DR SMR; Q80TG1; -.
DR BioGRID; 218277; 1.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR IntAct; Q80TG1; 1.
DR MINT; Q80TG1; -.
DR STRING; 10090.ENSMUSP00000102585; -.
DR iPTMnet; Q80TG1; -.
DR PhosphoSitePlus; Q80TG1; -.
DR EPD; Q80TG1; -.
DR jPOST; Q80TG1; -.
DR MaxQB; Q80TG1; -.
DR PaxDb; Q80TG1; -.
DR PeptideAtlas; Q80TG1; -.
DR PRIDE; Q80TG1; -.
DR ProteomicsDB; 268951; -. [Q80TG1-1]
DR ProteomicsDB; 268952; -. [Q80TG1-2]
DR ProteomicsDB; 268953; -. [Q80TG1-3]
DR ProteomicsDB; 268954; -. [Q80TG1-4]
DR ProteomicsDB; 268955; -. [Q80TG1-5]
DR Antibodypedia; 2016; 78 antibodies from 15 providers.
DR Ensembl; ENSMUST00000018556; ENSMUSP00000018556; ENSMUSG00000018412. [Q80TG1-1]
DR Ensembl; ENSMUST00000106977; ENSMUSP00000102590; ENSMUSG00000018412. [Q80TG1-1]
DR GeneID; 76719; -.
DR KEGG; mmu:76719; -.
DR UCSC; uc007lwj.1; mouse. [Q80TG1-1]
DR UCSC; uc007lwm.1; mouse. [Q80TG1-3]
DR UCSC; uc007lwn.1; mouse. [Q80TG1-2]
DR UCSC; uc007lwo.1; mouse. [Q80TG1-4]
DR CTD; 284058; -.
DR MGI; MGI:1923969; Kansl1.
DR VEuPathDB; HostDB:ENSMUSG00000018412; -.
DR eggNOG; ENOG502QYK7; Eukaryota.
DR GeneTree; ENSGT00530000063688; -.
DR HOGENOM; CLU_011035_0_0_1; -.
DR InParanoid; Q80TG1; -.
DR OrthoDB; 191128at2759; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 76719; 25 hits in 59 CRISPR screens.
DR ChiTaRS; Kansl1; mouse.
DR PRO; PR:Q80TG1; -.
DR Proteomes; UP000000589; Chromosome 11.
DR RNAct; Q80TG1; protein.
DR Bgee; ENSMUSG00000018412; Expressed in embryonic post-anal tail and 242 other tissues.
DR ExpressionAtlas; Q80TG1; baseline and differential.
DR Genevisible; Q80TG1; MM.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0000776; C:kinetochore; IEA:UniProtKB-KW.
DR GO; GO:0071339; C:MLL1 complex; ISS:UniProtKB.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005634; C:nucleus; ISO:MGI.
DR GO; GO:0035035; F:histone acetyltransferase binding; IBA:GO_Central.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0043984; P:histone H4-K16 acetylation; ISS:UniProtKB.
DR GO; GO:0043981; P:histone H4-K5 acetylation; ISS:UniProtKB.
DR GO; GO:0043982; P:histone H4-K8 acetylation; ISS:UniProtKB.
DR GO; GO:0051571; P:positive regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0045893; P:positive regulation of transcription, DNA-templated; IC:ComplexPortal.
DR GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; IDA:ComplexPortal.
DR InterPro; IPR026180; NSL1.
DR InterPro; IPR029332; PEHE_dom.
DR PANTHER; PTHR22443; PTHR22443; 2.
DR Pfam; PF15275; PEHE; 1.
DR SMART; SM01300; PEHE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Centromere; Chromatin regulator;
KW Chromosome; Coiled coil; Isopeptide bond; Kinetochore; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1036
FT /note="KAT8 regulatory NSL complex subunit 1"
FT /id="PRO_0000234566"
FT REGION 145..211
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 226..257
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 399..423
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 739..787
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 781..813
FT /note="Required for activation of KAT8 histone
FT acetyltransferase activity"
FT /evidence="ECO:0000250"
FT REGION 814..1036
FT /note="Sufficient for interaction with KAT8"
FT /evidence="ECO:0000250"
FT REGION 869..931
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 989..1020
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 285..312
FT /evidence="ECO:0000255"
FT COMPBIAS 158..193
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 753..784
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 869..925
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 104
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3B3"
FT MOD_RES 249
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 268
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 922
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3B3"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3B3"
FT MOD_RES 934
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3B3"
FT MOD_RES 976
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3B3"
FT CROSSLNK 262
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3B3"
FT CROSSLNK 331
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q7Z3B3"
FT VAR_SEQ 1..770
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018360"
FT VAR_SEQ 431..1036
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018361"
FT VAR_SEQ 478..510
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_018362"
FT VAR_SEQ 615..643
FT /note="HRNVRSGCDVNPSCALCGSGSVNTMPPEI -> GAQRTGLRSALILSRVGEP
FT PSSPVNLQNY (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018363"
FT VAR_SEQ 644..1036
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_018364"
FT VAR_SEQ 771..779
FT /note="GSQVAASTS -> MCSLRSWNQ (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_018365"
FT CONFLICT 197
FT /note="D -> N (in Ref. 2; BAE36437)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1036 AA; 113179 MW; F619B60DEEE93A62 CRC64;
MAAMAPALTD AAAEAHHIRF KLAPPSSTLS PGSAENNGNA NILISANGTK RKAIAAEDPS
LDFRNNPTKE DLGKLQPLVA SYLCSDVTSV PAKESLKLQG VFSKQTVLKS HPLLSQSYEL
RAELLGRQPV LEFSLENLRT MNTSGQTALP QAPVNGLAKK LTKSSTHSDH DNSSSLNGGK
RSLTSSSLQG GEVGGPDSGN LKGGMTNCTL PHRSLDIQHT TLYSNNSTAN KSSVNSMDQP
ALQGSSRLSP STDSSSNLTN VKLEVKKSPL SSILFSALDS DTRITALLRR QADIEIRARR
LQKRLQVVQA KQVERHLQHQ LGGFLETTLS KLPNLESLRS RSQLMLTRKA EAALRKAASE
SATSEGLSNF LKSDSISEEL ERFTASGIAN LRCSEQAFDS DVTDSSSGGE SDIEEEELTR
ADPEQCHVPL KRRSEWRWAA DRAAIVSRWN WLQAHVSDLE YRIRQQTDIY KQIRANKGLI
VLGEAPFPDH TTDLLSLSSE VKTDHGRDKL IESVSQPSEN HGILVSNITE SLSTKSCGAP
RPVNGVVNSL QPVLADQVPG DSSDAEEQLH KKQRLNLVSS SDGTCVAART RPVLTCKKRR
LVRPSSIVPL SKKVHRNVRS GCDVNPSCAL CGSGSVNTMP PEIHYEAPLL ERLSQLDSCV
HPVLAFPDDV PTSLHFQSML KSQWQNKPFD KIKPTKKFSL KHRATMPCSL SDPVRKDRHK
LVNSFLTTAM LKHHTDMSSP SYLTATHHPP HSPLVRQLST SSDTSTPTSS GSQVAASTSQ
PVRRRRGESS FDINNIVIPM SVAATTRVEK LQYKEILTPS WREVDVQSLK GSPDEENEEI
EDLSDAAFAA LHAKCEEMER ARWLWTTSVP PQRRGSRSYR SSDGRTTPQL GSANPSTPQP
ASPDVSSSHS LSEFSHGQSP RSPISPELHS APLTPVARDS LRHLASEDTR CSTPELGLDE
QSVQPWERRT FPLAYSPQAE CEEQLDAQDT AARCTRRTSG SKTGREAEVA PTSPPVVPLK
SRHLAATVTA QRPAHR
