KANL3_MOUSE
ID KANL3_MOUSE Reviewed; 903 AA.
AC A2RSY1; Q6ZPU0; Q8C0P9;
DT 15-MAY-2007, integrated into UniProtKB/Swiss-Prot.
DT 06-MAR-2007, sequence version 1.
DT 03-AUG-2022, entry version 102.
DE RecName: Full=KAT8 regulatory NSL complex subunit 3;
DE AltName: Full=NSL complex protein NSL3;
DE AltName: Full=Non-specific lethal 3 homolog;
GN Name=Kansl3; Synonyms=Kiaa1310, Nsl3;
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 3).
RC TISSUE=Embryonic tail;
RX PubMed=14621295; DOI=10.1093/dnares/10.4.167;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: III.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:167-180(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J; TISSUE=Testis;
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 MRNA] (ISOFORM 1).
RC TISSUE=Brain;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-536 AND SER-540, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, 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 the NSL complex at least composed of MOF/KAT8,
CC KANSL1, KANSL2, KANSL3, MCRS1, PHF20, OGT1/OGT, WDR5 and HCFC1.
CC {ECO:0000250}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=A2RSY1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=A2RSY1-2; Sequence=VSP_025335;
CC Name=3;
CC IsoId=A2RSY1-3; Sequence=VSP_025334, VSP_025335;
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC98139.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK129329; BAC98139.1; ALT_INIT; mRNA.
DR EMBL; AK030079; BAC26771.1; -; mRNA.
DR EMBL; BC132293; AAI32294.1; -; mRNA.
DR CCDS; CCDS14877.1; -. [A2RSY1-2]
DR CCDS; CCDS78561.1; -. [A2RSY1-1]
DR RefSeq; NP_001297442.1; NM_001310513.1. [A2RSY1-1]
DR RefSeq; NP_766240.1; NM_172652.3. [A2RSY1-2]
DR AlphaFoldDB; A2RSY1; -.
DR SMR; A2RSY1; -.
DR BioGRID; 230578; 2.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR IntAct; A2RSY1; 1.
DR STRING; 10090.ENSMUSP00000010597; -.
DR ESTHER; mouse-Kansl3; NLS3-Tex30.
DR iPTMnet; A2RSY1; -.
DR PhosphoSitePlus; A2RSY1; -.
DR EPD; A2RSY1; -.
DR jPOST; A2RSY1; -.
DR MaxQB; A2RSY1; -.
DR PaxDb; A2RSY1; -.
DR PeptideAtlas; A2RSY1; -.
DR PRIDE; A2RSY1; -.
DR ProteomicsDB; 269060; -. [A2RSY1-1]
DR ProteomicsDB; 269061; -. [A2RSY1-2]
DR ProteomicsDB; 269062; -. [A2RSY1-3]
DR Antibodypedia; 32468; 119 antibodies from 21 providers.
DR Ensembl; ENSMUST00000010597; ENSMUSP00000010597; ENSMUSG00000010453. [A2RSY1-2]
DR Ensembl; ENSMUST00000185912; ENSMUSP00000140547; ENSMUSG00000010453. [A2RSY1-3]
DR Ensembl; ENSMUST00000186470; ENSMUSP00000140597; ENSMUSG00000010453. [A2RSY1-1]
DR GeneID; 226976; -.
DR KEGG; mmu:226976; -.
DR UCSC; uc007apz.1; mouse. [A2RSY1-1]
DR UCSC; uc007aqa.1; mouse. [A2RSY1-2]
DR UCSC; uc011wjj.1; mouse. [A2RSY1-3]
DR CTD; 55683; -.
DR MGI; MGI:1918055; Kansl3.
DR VEuPathDB; HostDB:ENSMUSG00000010453; -.
DR eggNOG; KOG3253; Eukaryota.
DR GeneTree; ENSGT00390000007636; -.
DR HOGENOM; CLU_009783_0_0_1; -.
DR InParanoid; A2RSY1; -.
DR OMA; GADDNLX; -.
DR OrthoDB; 316190at2759; -.
DR PhylomeDB; A2RSY1; -.
DR TreeFam; TF323466; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 226976; 23 hits in 75 CRISPR screens.
DR ChiTaRS; Kansl3; mouse.
DR PRO; PR:A2RSY1; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; A2RSY1; protein.
DR Bgee; ENSMUSG00000010453; Expressed in spermatocyte and 224 other tissues.
DR ExpressionAtlas; A2RSY1; baseline and differential.
DR Genevisible; A2RSY1; MM.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0043231; C:intracellular membrane-bounded organelle; ISO:MGI.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
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:0045944; P:positive regulation of transcription by RNA polymerase II; IBA:GO_Central.
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 Gene3D; 3.40.50.1820; -; 1.
DR InterPro; IPR029058; AB_hydrolase.
DR InterPro; IPR026555; NSL3/Tex30.
DR PANTHER; PTHR13136; PTHR13136; 1.
DR SUPFAM; SSF53474; SSF53474; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Nucleus; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..903
FT /note="KAT8 regulatory NSL complex subunit 3"
FT /id="PRO_0000287138"
FT REGION 478..562
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 626..645
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 657..678
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 696..720
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 761..781
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 868..903
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 478..507
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 518..562
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 868..897
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2N6"
FT MOD_RES 536
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 540
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 772
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9P2N6"
FT VAR_SEQ 1..99
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295"
FT /id="VSP_025334"
FT VAR_SEQ 581..606
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14621295,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_025335"
SQ SEQUENCE 903 AA; 96135 MW; 68D32C689768DB7D CRC64;
MAHRGGERDF QTSARRMGTS LLFQLSVHER ELDLVFLDHS YAKPWSAHPD ASSARPTRML
FVTPRRQQEN TIESDVPIDV ETVTATPVPL YDNQKARSVM NECERHVIFA RTDADAPPPP
EDWEEHVNRT GWTVAQNKLF NKILKALQSD RLARLANEGA CNEPVLRRVA VDKCARRVRQ
ALASVSWDTK LTQWLHTTLV ETLSLPMLAA YLDALQTLKG KIPTLIDRML VSSNTKTGAA
GAEALSLLLK RPWDPAVGVL SHNKPSKLPG SPLILIVSSG PSSSVFPASR RHRFWQSQLS
CLGKVIPVAT HLLNNGSGVG VLQCLEHMIG AVRSKVLEIH SHFPHKPIIL IGWNTGALVA
CHVSVMEYVT AVVCLGFPLL TVDGPRGDVD DPLLDMKTPV LFVIGQNSLQ CHPEAMEDFR
EKIRAENSLV VVGGADDNLR ISKAKKKSEG LTQSMVDRCI QDEIVDFLTG VLTRAEGHVG
SEPRDQDAEK KKKPRDLTRR DLAFEIPERG SRPASPAARL PTSPSGSEDL SSVSSSPTSS
PKTKVTTVTS TQKSSQIGTS QLLKRHVQRT EAVLTHRQAQ AQFAAFLKQN MLVRKAFPPG
TSSCLFVPIS SESVEDIEKE ELRVQLKRHH SSSPLPGAKP SKRPKIKVSL ISQGDTVGGP
CTLSQGGTPE AAGGKPITMT LGASAGAKEL TGLLTTAKSS SSEGGGTAST TPSVASSSAT
PNAIHTLQSR LVATSPGSSL PGTASASSLL QGLSFSLQDI SSKTSGLPGS PSPGPAPQAT
SVKLPTPMQS LGAITTGTST IVRTIPVATT LSSLGATPGG KPTAIHQLLT NGSLAKLASS
LPGLAQISNQ ASGLKVPTTI TLTLRGQPSR ITTLSPMGSG ATPSEEPNSQ MLPSSSQRLP
PAP
