CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-017061
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative Polycomb group protein ASXL1 
Protein Synonyms/Alias
 Additional sex combs-like protein 1 
Gene Name
 ASXL1 
Gene Synonyms/Alias
 KIAA0978 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
351EKKVEQWKEKFFEDYubiquitination[1, 2, 3]
353KVEQWKEKFFEDYYGubiquitination[3]
362FEDYYGQKLGLTKEEubiquitination[4, 5]
367GQKLGLTKEESLQQNubiquitination[1, 3]
1371VGSVKNEKTFVGGPLubiquitination[3]
1379TFVGGPLKANAENRKubiquitination[3]
1419KLPREPGKGLSEPLEubiquitination[1, 3]
1437LPSQLSIKQAFYGKLubiquitination[1, 2, 3]
1443IKQAFYGKLSKLQLSubiquitination[3]
1446AFYGKLSKLQLSSTSubiquitination[3]
Reference
 [1] 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]
 [2] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [3] 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]
 [4] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [5] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 
Functional Description
 Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator of RARA and RXRA through association with NCOA1. Acts as corepressor through recruitment of KDM1A and CBX5 to target genes in a cell-type specific manner; the function seems to involve differential recruitment of methylated histone H3 to respective promoters. Acts as corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity (By similarity). Non-catalytic component of the PR-DUB complex, a complex that specifically mediates deubiquitination of histone H2A monoubiquitinated at 'Lys-119' (H2AK119ub1). 
Sequence Annotation
 ZN_FING 1503 1540 PHD-type; atypical.
 REGION 170 174 Required for interaction with CBX5 (By
 REGION 175 370 Interaction with KDM1A (By similarity).
 REGION 300 658 Interaction with NCOA1 (By similarity).
 REGION 1107 1112 Required for interaction with RARA.
 MOTIF 160 164 Nuclear localization signal 1
 MOTIF 284 288 LXXLL motif.
 MOTIF 409 413 Nuclear localization signal 2
 MOD_RES 503 503 Phosphoserine (By similarity).  
Keyword
 Alternative splicing; Chromatin regulator; Complete proteome; Craniosynostosis; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repressor; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1541 AA 
Protein Sequence
MKDKQKKKKE RTWAEAARLV LENYSDAPMT PKQILQVIEA EGLKEMRSGT SPLACLNAML 60
HSNSRGGEGL FYKLPGRISL FTLKKDALQW SRHPATVEGE EPEDTADVES CGSNEASTVS 120
GENDVSLDET SSNASCSTES QSRPLSNPRD SYRASSQANK QKKKTGVMLP RVVLTPLKVN 180
GAHVESASGF SGCHADGESG SPSSSSSGSL ALGSAAIRGQ AEVTQDPAPL LRGFRKPATG 240
QMKRNRGEEI DFETPGSILV NTNLRALINS RTFHALPSHF QQQLLFLLPE VDRQVGTDGL 300
LRLSSSALNN EFFTHAAQSW RERLADGEFT HEMQVRIRQE MEKEKKVEQW KEKFFEDYYG 360
QKLGLTKEES LQQNVGQEEA EIKSGLCVPG ESVRIQRGPA TRQRDGHFKK RSRPDLRTRA 420
RRNLYKKQES EQAGVAKDAK SVASDVPLYK DGEAKTDPAG LSSPHLPGTS SAAPDLEGPE 480
FPVESVASRI QAEPDNLARA SASPDRIPSL PQETVDQEPK DQKRKSFEQA ASASFPEKKP 540
RLEDRQSFRN TIESVHTEKP QPTKEEPKVP PIRIQLSRIK PPWVVKGQPT YQICPRIIPT 600
TESSCRGWTG ARTLADIKAR ALQVRGARGH HCHREAATTA IGGGGGPGGG GGGATDEGGG 660
RGSSSGDGGE ACGHPEPRGG PSTPGKCTSD LQRTQLLPPY PLNGEHTQAG TAMSRARRED 720
LPSLRKEESC LLQRATVGLT DGLGDASQLP VAPTGDQPCQ ALPLLSSQTS VAERLVEQPQ 780
LHPDVRTECE SGTTSWESDD EEQGPTVPAD NGPILSLVGD DTLEKGTGQA LDSHPTMKDP 840
VNVTPSSTPE SSPTDCLQNR AFDDELGLGG SCPPMRESDT RQENLKTKAL VSNSSLHWIP 900
IPSNDEVVKQ PKPESREHIP SVEPQVGEEW EKAAPTPPAL PGDLTAEEGL DPLDSLTSLW 960
TVPSRGGSDS NGSYCQQVDI EKLKINGDSE ALSPHGESTD TASDFEGHLT EDSSEADTRE 1020
AAVTKGSSVD KDEKPNWNQS APLSKVNGDM RLVTRTDGMV APQSWVSRVC AVRQKIPDSL 1080
LLASTEYQPR AVCLSMPGSS VEATNPLVMQ LLQGSLPLEK VLPPAHDDSM SESPQVPLTK 1140
DQSHGSLRMG SLHGLGKNSG MVDGSSPSSL RALKEPLLPD SCETGTGLAR IEATQAPGAP 1200
QKNCKAVPSF DSLHPVTNPI TSSRKLEEMD SKEQFSSFSC EDQKEVRAMS QDSNSNAAPG 1260
KSPGDLTTSR TPRFSSPNVI SFGPEQTGRA LGDQSNVTGQ GKKLFGSGNV AATLQRPRPA 1320
DPMPLPAEIP PVFPSGKLGP STNSMSGGVQ TPREDWAPKP HAFVGSVKNE KTFVGGPLKA 1380
NAENRKATGH SPLELVGHLE GMPFVMDLPF WKLPREPGKG LSEPLEPSSL PSQLSIKQAF 1440
YGKLSKLQLS STSFNYSSSS PTFPKGLAGS VVQLSHKANF GASHSASLSL QMFTDSSTVE 1500
SISLQCACSL KAMIMCQGCG AFCHDDCIGP SKLCVLCLVV R 1541 
Gene Ontology
 GO:0000790; C:nuclear chromatin; ISS:UniProtKB.
 GO:0035517; C:PR-DUB complex; IDA:UniProtKB.
 GO:0003677; F:DNA binding; IEA:InterPro.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0042975; F:peroxisome proliferator activated receptor binding; ISS:UniProtKB.
 GO:0042974; F:retinoic acid receptor binding; ISS:UniProtKB.
 GO:0003713; F:transcription coactivator activity; ISS:UniProtKB.
 GO:0003714; F:transcription corepressor activity; ISS:UniProtKB.
 GO:0035522; P:monoubiquitinated histone H2A deubiquitination; IDA:UniProtKB.
 GO:0045599; P:negative regulation of fat cell differentiation; ISS:UniProtKB.
 GO:0035359; P:negative regulation of peroxisome proliferator activated receptor signaling pathway; ISS:UniProtKB.
 GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; ISS:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; ISS:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; ISS:UniProtKB.
 GO:0032526; P:response to retinoic acid; ISS:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR026905; ASX-like_PHD.
 IPR024811; ASX/ASX-like.
 IPR024815; ASXL1. 
Pfam
 PF13922; PHD_3 
SMART
  
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS