CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-015666
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Putative Polycomb group protein ASXL2 
Protein Synonyms/Alias
 Additional sex combs-like protein 2 
Gene Name
 ASXL2 
Gene Synonyms/Alias
 ASXH2; KIAA1685 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
365QEIEKEKKVEPWKEQubiquitination[1, 2]
370EKKVEPWKEQFFESYubiquitination[1, 2, 3, 4]
1245NEQTTLSKENYLFTRubiquitination[1, 4]
1259RGQTFDEKTLARDLIubiquitination[4]
1271DLIQAAQKQMAHAVRubiquitination[4]
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] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
 Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
 Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
 [3] 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]
 [4] 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] 
Functional Description
 Putative Polycomb group (PcG) protein. PcG proteins act by forming multiprotein complexes, which are required to maintain the transcriptionally repressive state of homeotic genes throughout development. PcG proteins are not required to initiate repression, but to maintain it during later stages of development. They probably act via methylation of histones, rendering chromatin heritably changed in its expressibility (By similarity). Involved in transcriptional regulation mediated by ligand-bound nuclear hormone receptors, such as peroxisome proliferator-activated receptor gamma (PPARG). Acts as coactivator for PPARG and enhances its adipocyte differentiation-inducing activity; the function seems to involve differential recruitment of acetylated and methylated histone H3. 
Sequence Annotation
 ZN_FING 1397 1434 PHD-type; atypical.
 MOTIF 174 178 Nuclear localization signal (Potential).
 MOTIF 303 307 LXXLL motif 1.
 MOTIF 887 891 LXXLL motif 2.
 MOD_RES 146 146 Phosphoserine.  
Keyword
 Alternative splicing; Chromosomal rearrangement; Complete proteome; Metal-binding; Nucleus; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1435 AA 
Protein Sequence
MREKGRRKKG RTWAEAAKTV LEKYPNTPMS HKEILQVIQR EGLKEIRSGT SPLACLNAML 60
HTNSRGEEGI FYKVPGRMGV YTLKKDVPDG VKELSEGSEE SSDGQSDSQS SENSSSSSDG 120
GSNKEGKKSR WKRKVSSSSP QSGCPSPTIP AGKVISPSQK HSKKALKQAL KQQQQKKQQQ 180
QCRPSISISS NQHLSLKTVK AASDSVPAKP ATWEGKQSDG QTGSPQNSNS SFSSSVKVEN 240
TLLGLGKKSF QRSERLHTRQ MKRTKCADID VETPDSILVN TNLRALINKH TFSVLPGDCQ 300
QRLLLLLPEV DRQVGPDGLM KLNGSALNNE FFTSAAQGWK ERLSEGEFTP EMQVRIRQEI 360
EKEKKVEPWK EQFFESYYGQ SSGLSLEDSK KLTASPSDPK VKKTPAEQPK SMPVSEASLI 420
RIVPVVSQSE CKEEALQMSS PGRKEECESQ GEVQPNFSTS SEPLLSSALN THELSSILPI 480
KCPKDEDLLE QKPVTSAEQE SEKNHLTTAS NYNKSESQES LVTSPSKPKS PGVEKPIVKP 540
TAGAGPQETN MKEPLATLVD QSPESLKRKS SLTQEEAPVS WEKRPRVTEN RQHQQPFQVS 600
PQPFLNRGDR IQVRKVPPLK IPVSRISPMP FHPSQVSPRA RFPVSITSPN RTGARTLADI 660
KAKAQLVKAQ RAAAAAAAAA AAAASVGGTI PGPGPGGGQG PGEGGEGQTA RGGSPGSDRV 720
SETGKGPTLE LAGTGSRGGT RELLPCGPET QPQSETKTTP SQAQPHSVSG AQLQQTPPVP 780
PTPAVSGACT SVPSPAHIEK LDNEKLNPTR ATATVASVSH PQGPSSCRQE KAPSPTGPAL 840
ISGASPVHCA ADGTVELKAG PSKNIPNPSA SSKTDASVPV AVTPSPLTSL LTTATLEKLP 900
VPQVSATTAP AGSAPPSSTL PAASSLKTPG TSLNMNGPTL RPTSSIPANN PLVTQLLQGK 960
DVPMEQILPK PLTKVEMKTV PLTAKEERGM GALIATNTTE NSTREEVNER QSHPATQQQL 1020
GKTLQSKQLP QVPRPLQLFS AKELRDSSID THQYHEGLSK ATQDQILQTL IQRVRRQNLL 1080
SVVPPSQFNF AHSGFQLEDI STSQRFMLGF AGRRTSKPAM AGHYLLNIST YGRGSESFRR 1140
THSVNPEDRF CLSSPTEALK MGYTDCKNAT GESSSSKEDD TDEESTGDEQ ESVTVKEEPQ 1200
VSQSAGKGDT SSGPHSRETL STSDCLASKN VKAEIPLNEQ TTLSKENYLF TRGQTFDEKT 1260
LARDLIQAAQ KQMAHAVRGK AIRSSPELFS STVLPLPADS PTHQPLLLPP LQTPKLYGSP 1320
TQIGPSYRGM INVSTSSDMD HNSAVPGSQV SSNVGDVMSF SVTVTTIPAS QAMNPSSHGQ 1380
TIPVQAFSEE NSIEGTPSKC YCRLKAMIMC KGCGAFCHDD CIGPSKLCVS CLVVR 1435 
Gene Ontology
 GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
 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:0045600; P:positive regulation of fat cell differentiation; IDA:UniProtKB.
 GO:0035360; P:positive regulation of peroxisome proliferator activated receptor signaling pathway; IDA:UniProtKB.
 GO:0045944; P:positive regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR026905; ASX-like_PHD.
 IPR024811; ASX/ASX-like.
 IPR024817; ASXL2. 
Pfam
 PF13922; PHD_3 
SMART
  
PROSITE
 PS01359; ZF_PHD_1
 PS50016; ZF_PHD_2 
PRINTS