CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015900
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 KAT8 regulatory NSL complex subunit 1 
Protein Synonyms/Alias
 MLL1/MLL complex subunit KANSL1; MSL1 homolog 1; hMSL1v1; NSL complex protein NSL1; Non-specific lethal 1 homolog 
Gene Name
 KANSL1 
Gene Synonyms/Alias
 KIAA1267; MSL1V1; NSL1 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
69DFRNNPTKEDLGKLQubiquitination[1]
97VPSKESLKLQGVFSKubiquitination[1]
104KLQGVFSKQTVLKSHacetylation[2]
262SSNLGGVKLEGKKSPubiquitination[1]
311RLQVVQAKQVERHIQubiquitination[1]
331FLEKTLSKLPNLESLubiquitination[1]
372EGLSNFLKSNSISEEubiquitination[3]
601RPVLSCKKRRLVRPNacetylation[4]
735SSFLTTAKLSHHQTRacetylation[5]
785VHDPNHSKMRLRDHSacetylation[5]
Reference
 [1] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [2] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [3] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [4] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786]
 [5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302
Functional Description
 As part of the NSL complex it is involved in acetylation of nucleosomal histone H4 on several lysine residues and therefore may be involved in the regulation of transcription. 
Sequence Annotation
 REGION 883 1105 Sufficient for interaction with KAT8.
 MOD_RES 104 104 N6-acetyllysine.
 MOD_RES 249 249 Phosphoserine.
 MOD_RES 268 268 Phosphoserine.
 MOD_RES 991 991 Phosphoserine.
 MOD_RES 1003 1003 Phosphothreonine.
 MOD_RES 1045 1045 Phosphoserine.  
Keyword
 Acetylation; Alternative splicing; Chromatin regulator; Coiled coil; Complete proteome; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1105 AA 
Protein Sequence
MAAMAPALTD AAAEAHHIRF KLAPPSSTLS PGSAENNGNA NILIAANGTK RKAIAAEDPS 60
LDFRNNPTKE DLGKLQPLVA SYLCSDVTSV PSKESLKLQG VFSKQTVLKS HPLLSQSYEL 120
RAELLGRQPV LEFSLENLRT MNTSGQTALP QAPVNGLAKK LTKSSTHSDH DNSTSLNGGK 180
RALTSSALHG GEMGGSESGD LKGGMTNCTL PHRSLDVEHT TLYSNNSTAN KSSVNSMEQP 240
ALQGSSRLSP GTDSSSNLGG VKLEGKKSPL SSILFSALDS DTRITALLRR QADIESRARR 300
LQKRLQVVQA KQVERHIQHQ LGGFLEKTLS KLPNLESLRP RSQLMLTRKA EAALRKAASE 360
TTTSEGLSNF LKSNSISEEL ERFTASGIAN LRCSEQAFDS DVTDSSSGGE SDIEEEELTR 420
ADPEQRHVPL RRRSEWKWAA DRAAIVSRWN WLQAHVSDLE YRIRQQTDIY KQIRANKGLI 480
VLGEVPPPEH TTDLFLPLSS EVKTDHGTDK LIESVSQPLE NHGARIIGHI SESLSTKSCG 540
ALRPVNGVIN TLQPVLADHI PGDSSDAEEQ LHKKQRLNLV SSSSDGTCVA ARTRPVLSCK 600
KRRLVRPNSI VPLSKKVHRN STIRPGCDVN PSCALCGSGS INTMPPEIHY EAPLLERLSQ 660
LDSCVHPVLA FPDDVPTSLH FQSMLKSQWQ NKPFDKIKPP KKLSLKHRAP MPGSLPDSAR 720
KDRHKLVSSF LTTAKLSHHQ TRPDRTHRQH LDDVGAVPMV ERVTAPKAER LLNPPPPVHD 780
PNHSKMRLRD HSSERSEVLK HHTDMSSSSY LAATHHPPHS PLVRQLSTSS DSPAPASSSS 840
QVTASTSQQP VRRRRGESSF DINNIVIPMS VAATTRVEKL QYKEILTPSW REVDLQSLKG 900
SPDEENEEIE DLSDAAFAAL HAKCEEMERA RWLWTTSVPP QRRGSRSYRS SDGRTTPQLG 960
SANPSTPQPA SPDVSSSHSL SEYSHGQSPR SPISPELHSA PLTPVARDTP RHLASEDTRC 1020
STPELGLDEQ SVQPWERRTF PLAHSPQAEC EDQLDAQERA ARCTRRTSGS KTGRETEAAP 1080
TSPPIVPLKS RHLVAAATAQ RPTHR 1105 
Gene Ontology
 GO:0000123; C:histone acetyltransferase complex; IDA:UniProtKB.
 GO:0071339; C:MLL1 complex; IDA:UniProtKB.
 GO:0043984; P:histone H4-K16 acetylation; IDA:UniProtKB.
 GO:0043981; P:histone H4-K5 acetylation; IDA:UniProtKB.
 GO:0043982; P:histone H4-K8 acetylation; IDA:UniProtKB. 
Interpro
 IPR026180; NSL1. 
Pfam
  
SMART
  
PROSITE
  
PRINTS