KANL2_CAPHI
ID KANL2_CAPHI Reviewed; 492 AA.
AC Q861R7; Q861R9; Q861T1; Q861T2; Q864R6;
DT 20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT 20-FEB-2007, sequence version 2.
DT 25-MAY-2022, entry version 45.
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 Capra hircus (Goat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Laurasiatheria; Artiodactyla; Ruminantia; Pecora; Bovidae;
OC Caprinae; Capra.
OX NCBI_TaxID=9925;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 1; 2; 3; 4 AND 5), AND
RP TISSUE SPECIFICITY.
RX PubMed=14637001; DOI=10.1016/j.gene.2003.08.004;
RA Mata X., Taourit S., Le Provost F.;
RT "Putative FLJ20436 gene characterisation in goat. Observed ubiquitous
RT expression in goat and transgenic mice allowed to restrict the location of
RT an hypothesised insulator element.";
RL Gene 321:137-144(2003).
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=5;
CC Comment=Additional isoforms seem to exist.;
CC Name=1;
CC IsoId=Q861R7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q861R7-2; Sequence=VSP_023267;
CC Name=3;
CC IsoId=Q861R7-3; Sequence=VSP_023266;
CC Name=4;
CC IsoId=Q861R7-4; Sequence=VSP_023266, VSP_023267;
CC Name=5;
CC IsoId=Q861R7-5; Sequence=VSP_023268, VSP_023269;
CC -!- TISSUE SPECIFICITY: Ubiquitously expressed.
CC {ECO:0000269|PubMed:14637001}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAO47890.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO47891.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO47893.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAO47894.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAO47896.1; Type=Erroneous gene model prediction; Evidence={ECO:0000305};
CC Sequence=AAP04353.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAP04354.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY214590; AAO47890.1; ALT_INIT; mRNA.
DR EMBL; AY214591; AAO47891.1; ALT_INIT; mRNA.
DR EMBL; AY214592; AAO47892.1; -; mRNA.
DR EMBL; AY214593; AAO47893.1; ALT_INIT; mRNA.
DR EMBL; AY245697; AAP04353.1; ALT_INIT; mRNA.
DR EMBL; AY245698; AAP04354.1; ALT_INIT; mRNA.
DR EMBL; AY214597; AAO47894.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY214595; AAO47894.1; JOINED; Genomic_DNA.
DR EMBL; AY214596; AAO47894.1; JOINED; Genomic_DNA.
DR EMBL; AY214599; AAO47895.1; -; Genomic_DNA.
DR EMBL; AY214595; AAO47895.1; JOINED; Genomic_DNA.
DR EMBL; AY214596; AAO47895.1; JOINED; Genomic_DNA.
DR EMBL; AY214598; AAO47895.1; JOINED; Genomic_DNA.
DR EMBL; AY214599; AAO47896.1; ALT_SEQ; Genomic_DNA.
DR EMBL; AY214595; AAO47896.1; JOINED; Genomic_DNA.
DR EMBL; AY214596; AAO47896.1; JOINED; Genomic_DNA.
DR EMBL; AY214598; AAO47896.1; JOINED; Genomic_DNA.
DR EMBL; AY214599; AAO47897.1; -; Genomic_DNA.
DR EMBL; AY214595; AAO47897.1; JOINED; Genomic_DNA.
DR EMBL; AY214596; AAO47897.1; JOINED; Genomic_DNA.
DR EMBL; AY214598; AAO47897.1; JOINED; Genomic_DNA.
DR RefSeq; NP_001273955.1; NM_001287026.1.
DR RefSeq; NP_001273956.1; NM_001287027.1.
DR AlphaFoldDB; Q861R7; -.
DR SMR; Q861R7; -.
DR STRING; 9925.ENSCHIP00000032011; -.
DR GeneID; 100860885; -.
DR KEGG; chx:100860885; -.
DR CTD; 54934; -.
DR OrthoDB; 172254at2759; -.
DR Proteomes; UP000291000; Unassembled WGS sequence.
DR GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
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 InterPro; IPR026316; NSL2.
DR InterPro; IPR025927; Potential_DNA-bd.
DR PANTHER; PTHR13453; PTHR13453; 1.
DR Pfam; PF13891; zf-C3Hc3H; 2.
PE 2: Evidence at transcript level;
KW Alternative splicing; Chromatin regulator; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..492
FT /note="KAT8 regulatory NSL complex subunit 2"
FT /id="PRO_0000278291"
FT REGION 126..182
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 453..492
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 COMPBIAS 468..492
FT /note="Polar 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:0000250|UniProtKB:Q9H9L4"
FT MOD_RES 149
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9H9L4"
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 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 1..195
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14637001"
FT /id="VSP_023266"
FT VAR_SEQ 325..347
FT /note="HICQDTNRVLFKCCQGSEEVPCN -> QKDATAIGDLLTLYSGLMERALD
FT (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14637001"
FT /id="VSP_023268"
FT VAR_SEQ 348..492
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14637001"
FT /id="VSP_023269"
FT VAR_SEQ 376..409
FT /note="Missing (in isoform 2 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:14637001"
FT /id="VSP_023267"
SQ SEQUENCE 492 AA; 54984 MW; 9DA3EBB7DC0DC1C5 CRC64;
MNRIRIHVLP TNRGRITPVP RSQEPLSCSF THRPCSQPRL EGQEFCIKHI LEDKNAPFKQ
CSYISTKNGK RCPSAAPKPE KKDGVSFCAE HARRNALALH AQMKKTNPGP VGETLLCQLS
SYAKTELGSQ TPESSRSEAS RILDEDSWSD GEQEPITVDQ TWRGDPDSEA DSIDRDQEDP
LKHAGVYTAE EVALIMREKL IRLQSLDIDQ VKRLQHLLKE KKRRYLHNRK VEHEALGSSL
LTGPEGLLAR ERENLKRLKC LRRYRQRYGV KALLHRQLKE RRMLATDGAA QQAHTTRSSQ
RCLAFVDDVR CSNQSLPMTR HCLTHICQDT NRVLFKCCQG SEEVPCNKPV PVSLSEDPCC
PLHFQLPPQM YKPEQVLSVP DDLEAGPMDL YLSAAELQPT ESLPLEFSDD LDVVGDSMQC
PPSPLLFDPS LTLEDHPVKE IAEGPVDILG QMQMAGDGCR SQGPRNSEKA PAPLSQSGIA
TANGKPEPTS VS
