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KANL2_RAT
ID   KANL2_RAT               Reviewed;         488 AA.
AC   Q6AY70; G3V7H0;
DT   20-FEB-2007, integrated into UniProtKB/Swiss-Prot.
DT   21-MAR-2012, sequence version 2.
DT   03-AUG-2022, entry version 90.
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   Rattus norvegicus (Rat).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Rattus.
OX   NCBI_TaxID=10116;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=Brown Norway;
RA   Mural R.J., Adams M.D., Myers E.W., Smith H.O., Venter J.C.;
RL   Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC   TISSUE=Kidney;
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; SER-149; SER-168;
RP   SER-172 AND SER-175, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP   ANALYSIS].
RX   PubMed=22673903; DOI=10.1038/ncomms1871;
RA   Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA   Olsen J.V.;
RT   "Quantitative maps of protein phosphorylation sites across 14 different rat
RT   organs and tissues.";
RL   Nat. Commun. 3:876-876(2012).
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=2;
CC       Name=1;
CC         IsoId=Q6AY70-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=Q6AY70-2; Sequence=VSP_042534, VSP_042535;
CC   -!- MISCELLANEOUS: [Isoform 2]: 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=AAH79169.1; Type=Erroneous translation; Note=Wrong choice of CDS.; Evidence={ECO:0000305};
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DR   EMBL; CH474035; EDL87055.1; -; Genomic_DNA.
DR   EMBL; BC079169; AAH79169.1; ALT_SEQ; mRNA.
DR   RefSeq; NP_001004244.2; NM_001004244.2. [Q6AY70-1]
DR   RefSeq; XP_008763913.1; XM_008765691.1. [Q6AY70-1]
DR   RefSeq; XP_008763914.1; XM_008765692.2. [Q6AY70-1]
DR   RefSeq; XP_008763915.1; XM_008765693.2. [Q6AY70-1]
DR   RefSeq; XP_008763916.1; XM_008765694.2.
DR   RefSeq; XP_008764075.1; XM_008765853.2. [Q6AY70-1]
DR   RefSeq; XP_008764076.1; XM_008765854.2. [Q6AY70-1]
DR   RefSeq; XP_008764077.1; XM_008765855.2. [Q6AY70-1]
DR   RefSeq; XP_008764078.1; XM_008765856.2.
DR   RefSeq; XP_008764079.1; XM_008765857.1.
DR   AlphaFoldDB; Q6AY70; -.
DR   SMR; Q6AY70; -.
DR   STRING; 10116.ENSRNOP00000014875; -.
DR   iPTMnet; Q6AY70; -.
DR   PhosphoSitePlus; Q6AY70; -.
DR   PaxDb; Q6AY70; -.
DR   PRIDE; Q6AY70; -.
DR   Ensembl; ENSRNOT00000086886; ENSRNOP00000073779; ENSRNOG00000060185. [Q6AY70-1]
DR   Ensembl; ENSRNOT00000090730; ENSRNOP00000072729; ENSRNOG00000060185. [Q6AY70-2]
DR   GeneID; 300206; -.
DR   KEGG; rno:300206; -.
DR   UCSC; RGD:1303127; rat. [Q6AY70-1]
DR   CTD; 54934; -.
DR   RGD; 1303127; Kansl2.
DR   eggNOG; ENOG502QTMA; Eukaryota.
DR   GeneTree; ENSGT00940000155808; -.
DR   InParanoid; Q6AY70; -.
DR   OrthoDB; 172254at2759; -.
DR   TreeFam; TF324169; -.
DR   Reactome; R-RNO-3214847; HATs acetylate histones.
DR   PRO; PR:Q6AY70; -.
DR   Proteomes; UP000002494; Chromosome 7.
DR   Proteomes; UP000234681; Chromosome 7.
DR   GO; GO:0000123; C:histone acetyltransferase complex; ISS:UniProtKB.
DR   GO; GO:0044545; C:NSL complex; ISO:RGD.
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:RGD.
DR   GO; GO:1900095; P:regulation of dosage compensation by inactivation of X chromosome; ISO:RGD.
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..488
FT                   /note="KAT8 regulatory NSL complex subunit 2"
FT                   /id="PRO_0000278295"
FT   REGION          127..182
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:22673903"
FT   MOD_RES         149
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         168
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         172
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
FT   MOD_RES         175
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:22673903"
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 -> MRVSIQPRRWLLS (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042534"
FT   VAR_SEQ         158..488
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_042535"
SQ   SEQUENCE   488 AA;  54378 MW;  AA9563622D63842E CRC64;
     MNRIRIHVLP TNRGRITPVP RSQEPLSCSF THRPCSQPRL EGQEFCLKHI LEDKNAPFKQ
     CSYISTKNGK RCPSAAPKPE KKDGVSFCAE HARRNALALH AQMKKSNPGP MGETLLCQLS
     SYAKTELGSQ TPESSRSEAS RILDEDSWSD GDQEPITVDQ TWRGDPDSEA DSIDSDQEDP
     LKHAGVYTAE EVALIMREKL IRLQSLYIDQ FKRLQHLLKE KKRRYLHNRK VEHEALGSSL
     LTGPEGLLAK ERENLKRLKC LRRYRQRYGV EALLHRQLKE RRMLATEGAA QQAHTTRSSQ
     RCLAFVDDVR CSNQSLPMTR HCLTHICQDT NQVLFKCCQG SEEVPCNKPV PVSLSEDPCC
     PLHFQLPPQM YKPEQVLSVP DGLEAGPMDL YLSAAELQPT ESLPLELSDD LDVVGDGMPC
     PPSPLLFDPS LTLEDHSVTE IAGGPGQIQV AGDGCRSQGP HNVEKTCAPF PQRGLATANG
     KPEPTSIS
 
 
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