KAL1L_MOUSE
ID KAL1L_MOUSE Reviewed; 991 AA.
AC Q5DTI6; B2KGC3; E9QLD1; Q3TC00; Q8BNM1; Q8C4R5;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 3.
DT 03-AUG-2022, entry version 105.
DE RecName: Full=KAT8 regulatory NSL complex subunit 1-like protein;
GN Name=Kansl1l; Synonyms=Kiaa4189;
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=Fetal brain;
RA Okazaki N., Kikuno R.F., Ohara R., Inamoto S., Nagase T., Ohara O.,
RA Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene. The
RT complete nucleotide sequences of mouse KIAA-homologous cDNAs identified by
RT screening of terminal sequences of cDNA clones randomly sampled from size-
RT fractionated libraries.";
RL Submitted (FEB-2005) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 4), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 311-991 (ISOFORM 5).
RC STRAIN=C57BL/6J, and NOD; TISSUE=Head;
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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-463, AND IDENTIFICATION BY
RP 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).
RN [5]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-863, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic fibroblast;
RX PubMed=23806337; DOI=10.1016/j.molcel.2013.06.001;
RA Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y.,
RA Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.;
RT "SIRT5-mediated lysine desuccinylation impacts diverse metabolic
RT pathways.";
RL Mol. Cell 50:919-930(2013).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q5DTI6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5DTI6-2; Sequence=VSP_031505, VSP_031506;
CC Name=3;
CC IsoId=Q5DTI6-3; Sequence=VSP_031507;
CC Name=4;
CC IsoId=Q5DTI6-4; Sequence=VSP_031502, VSP_031503;
CC Name=5;
CC IsoId=Q5DTI6-5; Sequence=VSP_031504;
CC -!- PTM: Acetylated on lysine residues by KAT8 upon ionizing radiation-
CC induced DNA damage; deacetylated by HDAC3. {ECO:0000250}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC38675.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAD90312.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK220534; BAD90312.1; ALT_INIT; mRNA.
DR EMBL; AK081413; BAC38212.1; -; mRNA.
DR EMBL; AK082897; BAC38675.1; ALT_INIT; mRNA.
DR EMBL; AK170981; BAE42157.1; -; mRNA.
DR EMBL; AC118589; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC124389; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CU329676; CAQ52187.1; -; Genomic_DNA.
DR EMBL; CU302198; CAQ52187.1; JOINED; Genomic_DNA.
DR EMBL; CU302198; CAQ52309.1; -; Genomic_DNA.
DR EMBL; CU329676; CAQ52309.1; JOINED; Genomic_DNA.
DR CCDS; CCDS35603.1; -. [Q5DTI6-3]
DR RefSeq; NP_001116210.1; NM_001122738.1. [Q5DTI6-5]
DR RefSeq; NP_808313.3; NM_177645.4. [Q5DTI6-3]
DR RefSeq; XP_006496304.1; XM_006496241.2. [Q5DTI6-1]
DR RefSeq; XP_006496309.1; XM_006496246.2.
DR RefSeq; XP_011236879.1; XM_011238577.2. [Q5DTI6-1]
DR AlphaFoldDB; Q5DTI6; -.
DR SMR; Q5DTI6; -.
DR STRING; 10090.ENSMUSP00000063843; -.
DR iPTMnet; Q5DTI6; -.
DR PhosphoSitePlus; Q5DTI6; -.
DR jPOST; Q5DTI6; -.
DR MaxQB; Q5DTI6; -.
DR PaxDb; Q5DTI6; -.
DR PRIDE; Q5DTI6; -.
DR ProteomicsDB; 301713; -. [Q5DTI6-1]
DR ProteomicsDB; 301714; -. [Q5DTI6-2]
DR ProteomicsDB; 301715; -. [Q5DTI6-3]
DR ProteomicsDB; 301716; -. [Q5DTI6-4]
DR ProteomicsDB; 301717; -. [Q5DTI6-5]
DR Antibodypedia; 63309; 34 antibodies from 13 providers.
DR DNASU; 68691; -.
DR Ensembl; ENSMUST00000068168; ENSMUSP00000063843; ENSMUSG00000026004. [Q5DTI6-3]
DR GeneID; 68691; -.
DR KEGG; mmu:68691; -.
DR UCSC; uc007bim.2; mouse. [Q5DTI6-5]
DR UCSC; uc007bin.2; mouse. [Q5DTI6-3]
DR UCSC; uc007bip.1; mouse. [Q5DTI6-2]
DR UCSC; uc007biq.2; mouse. [Q5DTI6-4]
DR CTD; 151050; -.
DR MGI; MGI:1915941; Kansl1l.
DR VEuPathDB; HostDB:ENSMUSG00000026004; -.
DR eggNOG; ENOG502QRI7; Eukaryota.
DR GeneTree; ENSGT00530000063688; -.
DR InParanoid; Q5DTI6; -.
DR OMA; WRVVDIQ; -.
DR OrthoDB; 191128at2759; -.
DR TreeFam; TF336511; -.
DR BioGRID-ORCS; 68691; 0 hits in 72 CRISPR screens.
DR ChiTaRS; Kansl1l; mouse.
DR PRO; PR:Q5DTI6; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q5DTI6; protein.
DR Bgee; ENSMUSG00000026004; Expressed in spermatocyte and 243 other tissues.
DR ExpressionAtlas; Q5DTI6; baseline and differential.
DR Genevisible; Q5DTI6; MM.
DR GO; GO:0044545; C:NSL complex; IBA:GO_Central.
DR GO; GO:0035035; F:histone acetyltransferase binding; IBA:GO_Central.
DR InterPro; IPR026180; NSL1.
DR InterPro; IPR029332; PEHE_dom.
DR PANTHER; PTHR22443; PTHR22443; 1.
DR Pfam; PF15275; PEHE; 1.
DR SMART; SM01300; PEHE; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Isopeptide bond; Phosphoprotein;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1..991
FT /note="KAT8 regulatory NSL complex subunit 1-like protein"
FT /id="PRO_0000319583"
FT REGION 443..462
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 749..770
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 749..767
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 463
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 863
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:23806337"
FT CROSSLNK 136
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:A0AUZ9"
FT VAR_SEQ 365..368
FT /note="NSST -> YAKR (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031502"
FT VAR_SEQ 369..991
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031503"
FT VAR_SEQ 412..446
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031504"
FT VAR_SEQ 412..417
FT /note="GIVILE -> VLLVFC (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031505"
FT VAR_SEQ 418..991
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_031506"
FT VAR_SEQ 677..720
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_031507"
FT CONFLICT 162
FT /note="A -> T (in Ref. 1; BAD90312, 2; BAE42157 and 3;
FT CAQ52309/CAQ52187)"
FT /evidence="ECO:0000305"
FT CONFLICT 204
FT /note="S -> T (in Ref. 2; BAC38212)"
FT /evidence="ECO:0000305"
FT CONFLICT 219
FT /note="Q -> E (in Ref. 1; BAD90312, 2; BAE42157 and 3;
FT CAQ52309/CAQ52187)"
FT /evidence="ECO:0000305"
FT CONFLICT 349
FT /note="S -> P (in Ref. 2; BAE42157)"
FT /evidence="ECO:0000305"
FT CONFLICT 353
FT /note="L -> V (in Ref. 1; BAD90312, 2; BAE42157 and 3;
FT CAQ52309/CAQ52187)"
FT /evidence="ECO:0000305"
FT CONFLICT 894
FT /note="P -> A (in Ref. 1; BAD90312 and 3; CAQ52309/
FT CAQ52187)"
FT /evidence="ECO:0000305"
FT CONFLICT 947
FT /note="T -> A (in Ref. 1; BAD90312 and 3; CAQ52309/
FT CAQ52187)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 991 AA; 112525 MW; 26065A4E837E0F28 CRC64;
MTPALKEATT KGICFSSLPN TMESDKMLCM ESPRTVDEKL KGGDTFSQML GFPTPEPTLN
TNFVNLKHFA SPQASKHFQT VLLMSSNSTL NKYNENYNQK KVMESNCSKL KNVLCNGSSI
QLSKICPSHS ENEFIKKELS DTTSQCMKDI QIVLDSNLTK DANVDRLHLQ NCKWYQKNAL
LDKFTDTKIK KGLLQCTQKK IGPSHSDVPT SSSAAEKEQE VNARLLHCVS KQKILLSQAR
RTQKHLQMLL AKHVVKHYGQ QMKFSMKHQL PTMKIFHEPT TVLSNSLLEH TEIKPEVNIL
ASENKFWDDT NNGFSQCTAA EIQRFALSAT GLLSHVEEGL DSDATDSSSD DELDEYTIRK
NVAVNSSTEW KWLVDRAQVG SRWTWLQAQI SELEYKIQQL TDIHRQIRAS KGIVILEECQ
LPKDILKKQI QFSNQAVSLN TSVNSQVPQR SEEPLPEHDF EMSPSSPTLL LRNIEKQSAQ
LTEIINSLIA PLNLSPTSSP LSSKSCSHKC LANGISRSAS ENLDELSSSS SWLLNQKHSK
KRRKDRTRLK SPSLAIMSTA ARTRPLQSFH KRKLYRLSPT FYWTPETLPS KEAFLSSTQT
PYTGSPFSWD NWEQSSRSHL LREQVSKLDS SFHPVLSLPS EIPLHLHFET LFKKTDMKGE
LAENQFVGDC LISPPPVQGT SSLNQWRNGY SPICKPQIRS QPSVQLLQGR KKRHLSETAL
AGERTRFEEF AFQRSEPGSH CNFTAVSNAN VTSRTQNPSS QNTSRRRLRS ESSYDIDNIV
IPMSLVAPAK LEKLQYKEIL TPRWRKVVLQ PLDEHNLNKE EIEDLSDDVF SLRHRKYEER
EQARWSLWEQ SKWHRRNNRA YSKNVEGQDL VLKEHSSELG SAQQGTAESP FELPAESHSL
CAQDSLSLND GQEDKSLRWE RRAFPLKDED TAALLCQDER KDQTGGTSTA FHDEVFCSTT
PESGHPPKMQ LDGMEEYKSF GIGVTNVKRN R
