KANL2_MOUSE
ID KANL2_MOUSE Reviewed; 486 AA.
AC Q8BQR4; Q3TJH8; Q569W7; Q5XJH6; Q8C8F3; Q8C8I6; Q8CEY3; Q99LE5;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 03-AUG-2022, entry version 118.
DE RecName: Full=KAT8 regulatory NSL complex subunit 2;
DE AltName: Full=NSL complex protein NSL2;
DE AltName: Full=Non-specific lethal 2 homolog;
GN Name=Kansl2; Synonyms=Nsl2;
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] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Adipose tissue, Cerebellum, and Placenta;
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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 67-486 (ISOFORM 3).
RC STRAIN=C57BL/6J, Czech II, and FVB/N; TISSUE=Brain, and Mammary tumor;
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 [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-147 AND SER-149, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Testis;
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 Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q8BQR4-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8BQR4-2; Sequence=VSP_023275;
CC Name=3;
CC IsoId=Q8BQR4-4; Sequence=VSP_042532, VSP_042533;
CC -!- MISCELLANEOUS: [Isoform 3]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH03301.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAH92275.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
CC Sequence=BAC32935.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AK009662; BAC25264.1; -; mRNA.
DR EMBL; AK046649; BAC32821.1; -; mRNA.
DR EMBL; AK046983; BAC32935.1; ALT_FRAME; mRNA.
DR EMBL; AK047269; BAC33009.1; -; mRNA.
DR EMBL; AK167429; BAE39517.1; -; mRNA.
DR EMBL; BC003301; AAH03301.1; ALT_INIT; mRNA.
DR EMBL; BC083325; AAH83325.1; -; mRNA.
DR EMBL; BC092275; AAH92275.1; ALT_SEQ; mRNA.
DR EMBL; BC125633; AAI25634.1; -; mRNA.
DR EMBL; BC125631; AAI25632.1; -; mRNA.
DR CCDS; CCDS37190.1; -. [Q8BQR4-1]
DR CCDS; CCDS88832.1; -. [Q8BQR4-2]
DR RefSeq; NP_001276366.1; NM_001289437.1. [Q8BQR4-2]
DR RefSeq; NP_001276367.1; NM_001289438.1.
DR RefSeq; NP_001276368.1; NM_001289439.1.
DR RefSeq; NP_001276369.1; NM_001289440.1.
DR RefSeq; NP_598475.2; NM_133714.5. [Q8BQR4-1]
DR RefSeq; XP_006521423.1; XM_006521360.3.
DR AlphaFoldDB; Q8BQR4; -.
DR SMR; Q8BQR4; -.
DR BioGRID; 213571; 1.
DR ComplexPortal; CPX-875; NSL histone acetyltransferase complex.
DR STRING; 10090.ENSMUSP00000112101; -.
DR iPTMnet; Q8BQR4; -.
DR PhosphoSitePlus; Q8BQR4; -.
DR EPD; Q8BQR4; -.
DR MaxQB; Q8BQR4; -.
DR PaxDb; Q8BQR4; -.
DR PeptideAtlas; Q8BQR4; -.
DR PRIDE; Q8BQR4; -.
DR ProteomicsDB; 269174; -. [Q8BQR4-1]
DR ProteomicsDB; 269175; -. [Q8BQR4-2]
DR ProteomicsDB; 269176; -. [Q8BQR4-4]
DR Antibodypedia; 49479; 68 antibodies from 14 providers.
DR DNASU; 69612; -.
DR Ensembl; ENSMUST00000116400; ENSMUSP00000112101; ENSMUSG00000022992. [Q8BQR4-2]
DR Ensembl; ENSMUST00000230542; ENSMUSP00000155089; ENSMUSG00000022992. [Q8BQR4-1]
DR Ensembl; ENSMUST00000231066; ENSMUSP00000155461; ENSMUSG00000022992. [Q8BQR4-4]
DR GeneID; 69612; -.
DR KEGG; mmu:69612; -.
DR UCSC; uc007xmr.2; mouse. [Q8BQR4-1]
DR UCSC; uc007xms.2; mouse. [Q8BQR4-2]
DR CTD; 54934; -.
DR MGI; MGI:1916862; Kansl2.
DR VEuPathDB; HostDB:ENSMUSG00000022992; -.
DR eggNOG; ENOG502QTMA; Eukaryota.
DR GeneTree; ENSGT00940000155808; -.
DR HOGENOM; CLU_029808_3_0_1; -.
DR InParanoid; Q8BQR4; -.
DR OMA; GYNRAET; -.
DR OrthoDB; 172254at2759; -.
DR PhylomeDB; Q8BQR4; -.
DR TreeFam; TF324169; -.
DR Reactome; R-MMU-3214847; HATs acetylate histones.
DR BioGRID-ORCS; 69612; 21 hits in 74 CRISPR screens.
DR ChiTaRS; Kansl2; mouse.
DR PRO; PR:Q8BQR4; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q8BQR4; protein.
DR Bgee; ENSMUSG00000022992; Expressed in ventricular zone and 115 other tissues.
DR ExpressionAtlas; Q8BQR4; baseline and differential.
DR Genevisible; Q8BQR4; MM.
DR GO; GO:0015629; C:actin cytoskeleton; ISO:MGI.
DR GO; GO:0005829; C:cytosol; ISO:MGI.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR GO; GO:0044545; C:NSL complex; ISO:MGI.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; 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: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; IPR026316; NSL2.
DR InterPro; IPR025927; Potential_DNA-bd.
DR PANTHER; PTHR13453; PTHR13453; 1.
DR Pfam; PF13891; zf-C3Hc3H; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Chromatin regulator; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..486
FT /note="KAT8 regulatory NSL complex subunit 2"
FT /id="PRO_0000278293"
FT REGION 127..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 440..486
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 164..182
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 131
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9L4"
FT MOD_RES 147
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 168
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY70"
FT MOD_RES 172
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY70"
FT MOD_RES 175
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6AY70"
FT CROSSLNK 78
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q9H9L4"
FT VAR_SEQ 145..157
FT /note="EDSWSDGDQEPIT -> MLVSIQLKKWLLL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042532"
FT VAR_SEQ 158..486
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_042533"
FT VAR_SEQ 376..409
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:16141072"
FT /id="VSP_023275"
FT CONFLICT 80
FT /note="E -> K (in Ref. 1; BAE39517)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 486 AA; 54173 MW; DC789D0301E3F9C6 CRC64;
MNRIRIHVLP TNRGRITPVP RSQEPLSCSF THRPCSQPRL EGQEFCIKHI LEDKNAPFKQ
CSYVSTKNGK RCPSAAPKPE KKDGVSFCAE HARRNALALH AQMKKSNPGP MGETLLCQLS
SYAKTELGSQ TPESSRSEAS RILDEDSWSD GDQEPITVDQ TWRGDPDSEA DSIDSDQEDP
LKHAGVYTAE EVALIMREKL IRLQSLYIDQ FKRLQHLLKE KKRRYLHNRK VEHEALGSSL
LTGPEGLLAK ERENLKRLKC LRRYRQRYGV EALLHRQLKE RRMLATDGAA QQAHTTRSSQ
RCLAFVDDVR CSNQSLPMTR HCLTHICQDT NQVLFKCCQG SEEVPCNKPV PVSLSEDPCC
PLHFQLPPQM YKPEQVLSVP DDLEAGPMDL YLSAAELQPT ESLPLEFSDD LDVVGDGMPC
PPSPLLFDPS LTLEDHSVTE SAGDAGQMQA AGDGCRSQGA RSVEKAAFPQ RGLATANGKP
EPTSIS
