CP190_DROME - dbPTM
CP190_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CP190_DROME
UniProt AC Q24478
Protein Name Centrosome-associated zinc finger protein CP190
Gene Name Cp190
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1096
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton. Chromosome. Nucleus in interphase. Colocalizes with other elements of the gypsy chromatin insulator complex at multiple sites on polytene chromosomes and at nuclear insulator bodies.
Protein 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..
Protein Sequence MGEVKSVKVDNWGVFFLQKLQNFFNKTDYCDLTLQFRDNSQLKVHRLVLSACTDYFNVLEQTCEIVDDALIMPNEFQADVVVPIVNFMYTGTLEFELKMYGKLLRTAKEMNMTVLLKLLEAHRRTMENVNRQQRPPSPKGIRRRTVGQPSSGLPQQRVLGPSPQSRNVATPIAQRANTQRGSTGNTMSRTSGGSNRSPYGDSSNVKQEPTSPFEQLRKGYNNNKRPAQTSLLSPPSKKPSLEEVKEFAEQQRMRKQIAAEYGDNDPEYDGGMLYDDVHAGDDDDDDMPPQPSTSKQQSPQGTQTQLEHGSTTIILKQDSPSQTPTIIVKDSSNAKLNHTKIIAEVLRQYPHIVKGHKNIKLKIMPNTPAAPTEKSAPATVKPPANQSSATTSPHKKLHVSFKADKSTPLITAQQKAASSQQKSGTSQTTGNQGTGANPPANTAAAQKRRIDSKTMHALIAQGAENTTGPWLCLRCGVNGRPISIPSYRGFRRHLINTHKETIDPALCEHCGWRSVNNRELHFHMYMEHQTKSLLYTFAECALCNQSYRTKGELEAHINEVHTDDNKQQCIYCNKVFEQELQLYRHMKSYHKEQALEDGIIDETDEEFLGSQDEEEEAEGDEEQEPEQTGKVRILSDISLPATSAITVQQAQQEQLQEEDVEQVQQEVKFVGADGNEVELTDEQRKEILSQLNQQQAGATAGGVVMVLSEPEAEHVKQETDEKSLAGTEEEYDDSQIYSELGAADSVESAKKNIADESKESIDNLEWAENLIAESEEQSNKEPKSDKPRDDISEKLKELTGDWTEDENDDDVDDKPATAELASELANKDPEPTVHEEEDDIDLALQSLHKGPEEATEEKASEESVTSADDAVDAVPNINSQPEKMDVDSEAADEKASKAEVQIKKEAELENDQEEFIKEDSPIPHSDSVAELREAVTASEGEDDVHLEADNIRKELLDELIAEAEKPDQEKDIVQSEENATTEALDRSVTDEDDLVPPTQVSTEQMEIDEPAAEKAAENNEDTRTADEKEAVEDKPNQTQDVTTAEKPTLESAKAGDEATSGEAASVDKVKSLISEWGDDDEDEDENGVSAAAKEEL
Overview of Protein Modification Sites with Functional and Structural Information
Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations Modification Substrate Peptides
&
Secondary Structure		 ASA (%) Reference Orthologous
Protein Cluster
137PhosphorylationNRQQRPPSPKGIRRR
CHHCCCCCCCCCCCC		41.7625749252
145PhosphorylationPKGIRRRTVGQPSSG
CCCCCCCCCCCCCCC		27.4622817900
162PhosphorylationQQRVLGPSPQSRNVA
CCCCCCCCCCCCCCC		33.5019429919
165PhosphorylationVLGPSPQSRNVATPI
CCCCCCCCCCCCCHH		29.2527626673
170PhosphorylationPQSRNVATPIAQRAN
CCCCCCCCHHHHHHH		15.7925749252
182PhosphorylationRANTQRGSTGNTMSR
HHHCCCCCCCCCCCC		35.0227626673
194PhosphorylationMSRTSGGSNRSPYGD
CCCCCCCCCCCCCCC		32.3721082442
197PhosphorylationTSGGSNRSPYGDSSN
CCCCCCCCCCCCCCC		27.0719429919
199PhosphorylationGGSNRSPYGDSSNVK
CCCCCCCCCCCCCCC		34.5129892262
210PhosphorylationSNVKQEPTSPFEQLR
CCCCCCCCCHHHHHH		48.5619429919
211PhosphorylationNVKQEPTSPFEQLRK
CCCCCCCCHHHHHHH		38.0019429919
229PhosphorylationNNKRPAQTSLLSPPS
CCCCCCCCCCCCCCC		24.3718327897
233PhosphorylationPAQTSLLSPPSKKPS
CCCCCCCCCCCCCCC		39.8119429919
236PhosphorylationTSLLSPPSKKPSLEE
CCCCCCCCCCCCHHH		57.6119429919
240PhosphorylationSPPSKKPSLEEVKEF
CCCCCCCCHHHHHHH		58.2419429919
298PhosphorylationPSTSKQQSPQGTQTQ
CCCCCCCCCCCCCEE		19.3919429919
302PhosphorylationKQQSPQGTQTQLEHG
CCCCCCCCCEEECCC		24.1622817900
310PhosphorylationQTQLEHGSTTIILKQ
CEEECCCCEEEEEEC		25.0422817900
319PhosphorylationTIILKQDSPSQTPTI
EEEEECCCCCCCCEE		24.7721082442
321PhosphorylationILKQDSPSQTPTIIV
EEECCCCCCCCEEEE		51.1119429919
323PhosphorylationKQDSPSQTPTIIVKD
ECCCCCCCCEEEEEC		27.0819429919
325PhosphorylationDSPSQTPTIIVKDSS
CCCCCCCEEEEECCC		27.0719429919
372PhosphorylationPNTPAAPTEKSAPAT
CCCCCCCCCCCCCCC		51.8523607784
375PhosphorylationPAAPTEKSAPATVKP
CCCCCCCCCCCCCCC		33.0023607784
379PhosphorylationTEKSAPATVKPPANQ
CCCCCCCCCCCCCCC		28.1823607784
387PhosphorylationVKPPANQSSATTSPH
CCCCCCCCCCCCCCC		23.0319429919
388PhosphorylationKPPANQSSATTSPHK
CCCCCCCCCCCCCCC		21.6319429919
390PhosphorylationPANQSSATTSPHKKL
CCCCCCCCCCCCCEE		29.7419429919
391PhosphorylationANQSSATTSPHKKLH
CCCCCCCCCCCCEEE		39.7219429919
392PhosphorylationNQSSATTSPHKKLHV
CCCCCCCCCCCEEEE		22.2019429919
400PhosphorylationPHKKLHVSFKADKST
CCCEEEEEEECCCCC		15.4122817900
402AcetylationKKLHVSFKADKSTPL
CEEEEEEECCCCCCE		48.4421791702
603PhosphorylationEDGIIDETDEEFLGS
HHCCCCCCCHHHHCC		44.9922817900
610PhosphorylationTDEEFLGSQDEEEEA
CCHHHHCCCCHHHHH		36.2822817900
708PhosphorylationGGVVMVLSEPEAEHV
CCEEEECCCHHHHHH		39.4322817900
723PhosphorylationKQETDEKSLAGTEEE
CHHCCCCCCCCCHHH		22.7719429919
727PhosphorylationDEKSLAGTEEEYDDS
CCCCCCCCHHHCCHH		34.3219429919
731PhosphorylationLAGTEEEYDDSQIYS
CCCCHHHCCHHHHHH		28.4719429919
734PhosphorylationTEEEYDDSQIYSELG
CHHHCCHHHHHHHHC		18.6419429919
737PhosphorylationEYDDSQIYSELGAAD
HCCHHHHHHHHCCHH		6.6119429919
745PhosphorylationSELGAADSVESAKKN
HHHCCHHHHHHHHHH		24.0622817900
748PhosphorylationGAADSVESAKKNIAD
CCHHHHHHHHHHCCH		43.1422817900
757PhosphorylationKKNIADESKESIDNL
HHHCCHHHHHHHHHH		42.1219429919
760PhosphorylationIADESKESIDNLEWA
CCHHHHHHHHHHHHH		38.6919429919
792PhosphorylationDKPRDDISEKLKELT
CCCCCHHHHHHHHHH		35.3619429919
794AcetylationPRDDISEKLKELTGD
CCCHHHHHHHHHHCC		59.0521791702
803PhosphorylationKELTGDWTEDENDDD
HHHHCCCCCCCCCCC		37.9919429919
817PhosphorylationDVDDKPATAELASEL
CCCCCHHHHHHHHHH		29.2318327897
860PhosphorylationEATEEKASEESVTSA
HHCHHHHCHHHCCCH		53.6219429919
863PhosphorylationEEKASEESVTSADDA
HHHHCHHHCCCHHHH		27.0019429919
865PhosphorylationKASEESVTSADDAVD
HHCHHHCCCHHHHHH		27.7219429919
866PhosphorylationASEESVTSADDAVDA
HCHHHCCCHHHHHHC		27.7819429919
879PhosphorylationDAVPNINSQPEKMDV
HCCCCCCCCCHHCCC		43.2322668510
888PhosphorylationPEKMDVDSEAADEKA
CHHCCCCHHHHHHHH		29.0519429919
920PhosphorylationEEFIKEDSPIPHSDS
HHHHHCCCCCCCCCC		26.3121082442
925PhosphorylationEDSPIPHSDSVAELR
CCCCCCCCCCHHHHH		26.6519060867
927PhosphorylationSPIPHSDSVAELREA
CCCCCCCCHHHHHHH		26.6622817900
936PhosphorylationAELREAVTASEGEDD
HHHHHHHHHCCCCCC		31.3619429919
938PhosphorylationLREAVTASEGEDDVH
HHHHHHHCCCCCCCC		36.4521082442
975PhosphorylationQEKDIVQSEENATTE
HHCCCCCCCHHHHHH		35.6619429919
989PhosphorylationEALDRSVTDEDDLVP
HHHHHCCCCCCCCCC		34.6129892262
998PhosphorylationEDDLVPPTQVSTEQM
CCCCCCCCCCCCCCE		35.2229892262
1001PhosphorylationLVPPTQVSTEQMEID
CCCCCCCCCCCEECC		19.1929892262
1002PhosphorylationVPPTQVSTEQMEIDE
CCCCCCCCCCEECCH		31.2329892262
1022PhosphorylationAAENNEDTRTADEKE
HHHCCCCCCCHHHHH		24.6019429919
1024PhosphorylationENNEDTRTADEKEAV
HCCCCCCCHHHHHHH		40.3219429919
1060PhosphorylationKAGDEATSGEAASVD
CCCCCCCCCCCCCHH		41.5021082442
1065PhosphorylationATSGEAASVDKVKSL
CCCCCCCCHHHHHHH		37.5922668510
1071PhosphorylationASVDKVKSLISEWGD
CCHHHHHHHHHHHCC		33.6422817900
1074PhosphorylationDKVKSLISEWGDDDE
HHHHHHHHHHCCCCC		32.3722817900
Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)
Modified Location Modified Residue Modification Type of Upstream Proteins Gene Name of Upstream Proteins UniProt AC of Upstream Proteins Sources

Oops, there are no upstream regulatory protein records of CP190_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CP190_DROME !!
Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Modified Location Modification Variant Position
(Distance <= 10) 		Residue Change SAP Related Disease Reference

Oops, there are no SNP-PTM records of CP190_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SQH_DROMEsqhgenetic
16051175
FSH_DROMEfs(1)hphysical
23945939
TBG1_DROMEgammaTub23Cphysical
8491775
PIWI_DROMEpiwiphysical
21852534
TBG2_DROMEgammaTub37Cphysical
8491775
CNN_DROMEcnnphysical
21694707
MSH6_DROMEMsh6physical
23917615
AGO2_DROMEAGO2physical
21852534
BRM_DROMEbrmphysical
23917615
DDX17_DROMERm62physical
16862159
DDX17_DROMERm62physical
21852534
EMS_DROMEemsphysical
23917615
SUHW_DROMEsu(Hw)physical
24502977
SUHW_DROMEsu(Hw)physical
25242320
SUHW_DROMEsu(Hw)physical
25342723
SUHW_DROMEsu(Hw)physical
23917615
SUHW_DROMEsu(Hw)physical
15574329
SUHW_DROMEsu(Hw)physical
16862159
SUHW_DROMEsu(Hw)physical
18082602
SUHW_DROMEsu(Hw)physical
21852534
CP190_DROMECp190physical
23917615
NU301_DROMEE(bx)physical
27046080
MMD4_DROMEmod(mdg4)physical
24502977
MMD4_DROMEmod(mdg4)physical
25342723
MMD4_DROMEmod(mdg4)physical
15574329
MMD4_DROMEmod(mdg4)physical
16862159
MMD4_DROMEmod(mdg4)physical
18082602
MMD4_DROMEmod(mdg4)physical
23358822
MMD4_DROMEmod(mdg4)physical
21852534
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CP190_DROME

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome analysis of Drosophila melanogaster embryos.";
Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P.;
J. Proteome Res. 7:1675-1682(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-197; THR-229; SER-233;SER-298; THR-603; SER-610; SER-708; SER-723; THR-727; SER-745;SER-748; SER-757; SER-760; THR-817; SER-920; SER-927; THR-936;SER-938; SER-1071 AND SER-1074, AND MASS SPECTROMETRY.
"An integrated chemical, mass spectrometric and computational strategyfor (quantitative) phosphoproteomics: application to Drosophilamelanogaster Kc167 cells.";
Bodenmiller B., Mueller L.N., Pedrioli P.G.A., Pflieger D.,Juenger M.A., Eng J.K., Aebersold R., Tao W.A.;
Mol. Biosyst. 3:275-286(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-211; SER-319; SER-920AND SER-925, AND MASS SPECTROMETRY.

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