CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012798
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Centrosome-associated zinc finger protein CP190 
Protein Synonyms/Alias
 Protein enhancer of mod(mdg4)4-1; dMAP190 
Gene Name
 Cp190 
Gene Synonyms/Alias
 E(mod)4-1; CG6384 
Created Date
 July 27, 2013 
Organism
 Drosophila melanogaster (Fruit fly) 
NCBI Taxa ID
 7227 
Lysine Modification
Position
Peptide
Type
References
402KKLHVSFKADKSTPLacetylation[1]
794PRDDISEKLKELTGDacetylation[1]
Reference
 [1] Proteome-wide mapping of the Drosophila acetylome demonstrates a high degree of conservation of lysine acetylation.
 Weinert BT, Wagner SA, Horn H, Henriksen P, Liu WR, Olsen JV, Jensen LJ, Choudhary C.
 Sci Signal. 2011 Jul 26;4(183):ra48. [PMID: 21791702] 
Functional Description
 Component of the gypsy chromatin insulator complex which is required for the function of the gypsy chromatin insulator and other endogenous chromatin insulators. Chromatin insulators are regulatory elements which establish independent domains of transcriptional activity within eukaryotic genomes. Insulators have two defining properties; they can block the communication between an enhancer and a promoter when placed between them and can also buffer transgenes from position effect variegation (PEV). Insulators are proposed to structure the chromatin fiber into independent domains of differing transcriptional potential by promoting the formation of distinct chromatin loops. This chromatin looping may involve the formation of insulator bodies, where homotypic interactions between individual subunits of the insulator complex could promote the clustering of widely spaced insulators at the nuclear periphery. Within the gypsy insulator complex, this protein may directly bind to insulator DNA at sites distinct from those recognized by su(Hw). Required during embryogenesis for axial expansion, an actin/myosin dependent process that distributes the dividing nuclei along the anterior- posterior axis of the syncytial embryo. Does not appear to play a crucial role in organizing centrosomal microtubules during mitosis. 
Sequence Annotation
 DOMAIN 30 97 BTB.
 ZN_FING 538 561 C2H2-type 1.
 ZN_FING 567 590 C2H2-type 2.
 REGION 207 271 Nuclear localization.
 REGION 385 508 Centrosomal localization and interaction
 MOD_RES 197 197 Phosphoserine.
 MOD_RES 211 211 Phosphoserine.
 MOD_RES 229 229 Phosphothreonine.
 MOD_RES 233 233 Phosphoserine.
 MOD_RES 298 298 Phosphoserine.
 MOD_RES 319 319 Phosphoserine.
 MOD_RES 603 603 Phosphothreonine.
 MOD_RES 610 610 Phosphoserine.
 MOD_RES 708 708 Phosphoserine.
 MOD_RES 723 723 Phosphoserine.
 MOD_RES 727 727 Phosphothreonine.
 MOD_RES 745 745 Phosphoserine.
 MOD_RES 748 748 Phosphoserine.
 MOD_RES 757 757 Phosphoserine.
 MOD_RES 760 760 Phosphoserine.
 MOD_RES 817 817 Phosphothreonine.
 MOD_RES 920 920 Phosphoserine.
 MOD_RES 925 925 Phosphoserine.
 MOD_RES 927 927 Phosphoserine.
 MOD_RES 936 936 Phosphothreonine.
 MOD_RES 938 938 Phosphoserine.
 MOD_RES 1071 1071 Phosphoserine.
 MOD_RES 1074 1074 Phosphoserine.  
Keyword
 Chromatin regulator; Chromosome; Complete proteome; Cytoplasm; Cytoskeleton; DNA-binding; Metal-binding; Microtubule; Nucleus; Phosphoprotein; Reference proteome; Repeat; Transcription; Transcription regulation; Zinc; Zinc-finger. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1096 AA 
Protein Sequence
MGEVKSVKVD NWGVFFLQKL QNFFNKTDYC DLTLQFRDNS QLKVHRLVLS ACTDYFNVLE 60
QTCEIVDDAL IMPNEFQADV VVPIVNFMYT GTLEFELKMY GKLLRTAKEM NMTVLLKLLE 120
AHRRTMENVN RQQRPPSPKG IRRRTVGQPS SGLPQQRVLG PSPQSRNVAT PIAQRANTQR 180
GSTGNTMSRT SGGSNRSPYG DSSNVKQEPT SPFEQLRKGY NNNKRPAQTS LLSPPSKKPS 240
LEEVKEFAEQ QRMRKQIAAE YGDNDPEYDG GMLYDDVHAG DDDDDDMPPQ PSTSKQQSPQ 300
GTQTQLEHGS TTIILKQDSP SQTPTIIVKD SSNAKLNHTK IIAEVLRQYP HIVKGHKNIK 360
LKIMPNTPAA PTEKSAPATV KPPANQSSAT TSPHKKLHVS FKADKSTPLI TAQQKAASSQ 420
QKSGTSQTTG NQGTGANPPA NTAAAQKRRI DSKTMHALIA QGAENTTGPW LCLRCGVNGR 480
PISIPSYRGF RRHLINTHKE TIDPALCEHC GWRSVNNREL HFHMYMEHQT KSLLYTFAEC 540
ALCNQSYRTK GELEAHINEV HTDDNKQQCI YCNKVFEQEL QLYRHMKSYH KEQALEDGII 600
DETDEEFLGS QDEEEEAEGD EEQEPEQTGK VRILSDISLP ATSAITVQQA QQEQLQEEDV 660
EQVQQEVKFV GADGNEVELT DEQRKEILSQ LNQQQAGATA GGVVMVLSEP EAEHVKQETD 720
EKSLAGTEEE YDDSQIYSEL GAADSVESAK KNIADESKES IDNLEWAENL IAESEEQSNK 780
EPKSDKPRDD ISEKLKELTG DWTEDENDDD VDDKPATAEL ASELANKDPE PTVHEEEDDI 840
DLALQSLHKG PEEATEEKAS EESVTSADDA VDAVPNINSQ PEKMDVDSEA ADEKASKAEV 900
QIKKEAELEN DQEEFIKEDS PIPHSDSVAE LREAVTASEG EDDVHLEADN IRKELLDELI 960
AEAEKPDQEK DIVQSEENAT TEALDRSVTD EDDLVPPTQV STEQMEIDEP AAEKAAENNE 1020
DTRTADEKEA VEDKPNQTQD VTTAEKPTLE SAKAGDEATS GEAASVDKVK SLISEWGDDD 1080
EDEDENGVSA AAKEEL 1096 
Gene Ontology
 GO:0005813; C:centrosome; IDA:UniProtKB.
 GO:0005737; C:cytoplasm; IEA:UniProtKB-KW.
 GO:0005874; C:microtubule; IEA:UniProtKB-KW.
 GO:0005875; C:microtubule associated complex; IDA:FlyBase.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0005700; C:polytene chromosome; IDA:UniProtKB.
 GO:0043035; F:chromatin insulator sequence binding; IDA:FlyBase.
 GO:0008017; F:microtubule binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:InterPro.
 GO:0016568; P:chromatin modification; IEA:UniProtKB-KW.
 GO:0007017; P:microtubule-based process; ISS:FlyBase.
 GO:0035191; P:nuclear axial expansion; IMP:FlyBase.
 GO:0051493; P:regulation of cytoskeleton organization; IMP:UniProtKB.
 GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW.
 GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. 
Interpro
 IPR000210; BTB/POZ-like.
 IPR011333; BTB/POZ_fold.
 IPR013069; BTB_POZ.
 IPR007087; Znf_C2H2.
 IPR015880; Znf_C2H2-like. 
Pfam
 PF00651; BTB 
SMART
 SM00225; BTB
 SM00355; ZnF_C2H2 
PROSITE
 PS50097; BTB
 PS00028; ZINC_FINGER_C2H2_1
 PS50157; ZINC_FINGER_C2H2_2 
PRINTS