CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-009171
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
 Mus musculus (Mouse) 
NCBI Taxa ID
 10090 
Lysine Modification
Position
Peptide
Type
References
351EKKVEQWKEKFFEDYubiquitination[1, 2]
353KVEQWKEKFFEDYYGubiquitination[2]
Reference
 [1] Proteomic analyses reveal divergent ubiquitylation site patterns in murine tissues.
 Wagner SA, Beli P, Weinert BT, Schölz C, Kelstrup CD, Young C, Nielsen ML, Olsen JV, Brakebusch C, Choudhary C.
 Mol Cell Proteomics. 2012 Dec;11(12):1578-85. [PMID: 22790023]
 [2] BTB-ZF factors recruit the E3 ligase cullin 3 to regulate lymphoid effector programs.
 Mathew R, Seiler MP, Scanlon ST, Mao AP, Constantinides MG, Bertozzi-Villa C, Singer JD, Bendelac A.
 Nature. 2012 Nov 22;491(7425):618-21. [PMID: 23086144] 
Functional Description
 Probable Polycomb group (PcG) protein involved in transcriptional regulation mediated by ligand-bound retinoic acid receptors (RARs) and peroxisome proliferator-activated receptor gamma (PPARG). Acts as a coactivator of RARA and RXRA through association with NCOA1. Acts as a 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 a corepressor for PPARG and suppresses its adipocyte differentiation-inducing activity. 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 1476 1513 PHD-type; atypical.
 REGION 170 174 Required for interaction with CBX5.
 REGION 175 370 Interaction with KDM1A.
 REGION 300 655 Interaction with NCOA1.
 REGION 1082 1087 Required for interaction with RARA (By
 MOTIF 284 288 LXXLL motif 1.
 MOTIF 409 413 Nuclear localization signal (Potential).
 MOTIF 808 812 LXXLL motif 2.
 MOD_RES 500 500 Phosphoserine.  
Keyword
 Chromatin regulator; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Ubl conjugation pathway; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1514 AA 
Protein Sequence
MKDKQKRKKE RTWAEAARLV LENYSDAPMT PKQILQVIEA EGLKEMRSGT SPLACLNAML 60
HSNSRGGEGL FYKLPGRISL FTLKKDAVQW SRNAATVDGD EPEDSADVES CGSNEASTVS 120
GENDVSLDET SSNASCSTES QSRPLSNPRD SHRASSQANK QKKRTGVMLP RVVLTPLKVN 180
GAHVEPASGF SGRHADGESG SPSSSSSGSL ALGNSAIRGQ AEVTRDPAPL LRGFRKPATG 240
QMKRNRGEEV DFETPGSILV NTNLRALINS RTFHALPLHF QQQLLLLLPE VDRQVGTDGL 300
LRLSGSALNN EFFTHAAQSW RERLADGEFT HEMQVRLRQE MEKEKKVEQW KEKFFEDYYG 360
QKLGLTKEES LQQKEVQEEA KVKSGLCVSG ESVRPQRGPN TRQRDGHFKK RSRPDLRTRS 420
RRNIYKKQEP EQAGVAKDAS AAPDVSLSKD TKTDLAGVNS TPGPDVSSAT SGQEGPKCPS 480
EPVASQIQAE RDNLACASAS PDRIPTLPQD TVDQETKDQK RKSFEQEASA SFPEKKPRLE 540
DRQSFRNTIE SVHTEKPQPT KEEPKVPPIR IQLSRIKPPW VAKGRPTYQI CPRIVPITES 600
SCRGWTGART LADIKARALQ ARGARGYHCN RETATTAIGG GGGPGGGGSG AIDEGGGRDS 660
SSGDGSEACG HPEPRGAPST SGESASDLQR TQLLPPCPLN GEHTPAEAAM PRARREDSAS 720
LRKEESCLLK RVPGVLTSGL EDASQPPIAP TGDQPCQALP PLSSQTPVAE MLTEQPKLLL 780
DDRTECESSR EDQGPTIPSE SSSGRFPLGD LLGGGSDQAF DNMKEPVSMT PTFISELSLA 840
NYLQDRPDDD GLGLGATGLL IRESSRQEAL TEAFASGSPT SWVPILSNYE VIKTSDPESR 900
ENIPCPEPQD EKEWERAVPL IAATESVPQP ESCISHWTPP PAAVGSTGSD SEQVDLERLE 960
MNGISEAPSP HSESTDTASD SEGHLSEDSS EVDASEVTVV KGSLGGDEKQ DWDPSASLSK 1020
VNNDLSVLTR TGGVAASQSW VSRVCSVPHK IPDSLLLSST ECQPRSVCPL RPGSSVEVTN 1080
PLVMHLLHGN LPLEKVLPPG HRSSRLESSQ LPLREQSQDR GTLQGTGENN RLAARINPGS 1140
AQTLKESILA QSYGASAGLV RAMASKAPAM SQKIAKMVTS LDSQHPETEL TPSSGNLEEI 1200
DSKEHLSSFL CEEQKEGHSL SQGSDPGAAP GQCLGDHTTS KVPCFSSTNV SLSFGSEQTD 1260
GTLSDQNNAG GHEKKLFGPG NTVTTLQCPR SEEQTPLPAE VPPVFPSRKI EPSKNSVSGG 1320
VQTTRENRMP KPPPVSADSI KTEQTFLRDP IKADAENRKA AGYSSLELVG HLQGMPFVVD 1380
LPFWKLPREP GKGFSQPLEP SSIPSQLNIK QALYGKLSKL QLSPTSFNYS SSSATFPKGL 1440
AGGVVQLSHK ASFGTGHTAS LSLQMFADSS AVESISLQCA CSLKAMIMCQ GCGAFCHDDC 1500
IGPSKLCVLC LVVR 1514 
Gene Ontology
 GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
 GO:0035517; C:PR-DUB complex; ISS: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; IDA:UniProtKB.
 GO:0042974; F:retinoic acid receptor binding; IDA:UniProtKB.
 GO:0003713; F:transcription coactivator activity; IDA:UniProtKB.
 GO:0003714; F:transcription corepressor activity; IDA:UniProtKB.
 GO:0060348; P:bone development; IMP:MGI.
 GO:0035522; P:monoubiquitinated histone H2A deubiquitination; ISS:UniProtKB.
 GO:0045599; P:negative regulation of fat cell differentiation; IDA:UniProtKB.
 GO:0035359; P:negative regulation of peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
 GO:0048387; P:negative regulation of retinoic acid receptor signaling pathway; IDA:UniProtKB.
 GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0048386; P:positive regulation of retinoic acid receptor signaling pathway; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0032526; P:response to retinoic acid; IDA: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