CWC22_DROME - dbPTM
CWC22_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CWC22_DROME
UniProt AC Q9VJ87
Protein Name Pre-mRNA-splicing factor CWC22 homolog
Gene Name ncm
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1330
Subcellular Localization Nucleus speckle .
Protein Description Required for pre-mRNA splicing and for exon-junction complex (EJC) assembly. Hinders eIF4AIII from non-specifically binding RNA and escorts it to the splicing machinery to promote EJC assembly on mature mRNAs..
Protein Sequence MGESDAESDSSSNSSSSDTSSGSDSDARSESSSSESSGREEEEAKQEESAKDAKKTDDTDRGEKRAKERDAGQDEQPTEQKKTPAAEPRSERQHISHSAGVEKQQEEAVAAAEAESEKLNEAKKVETPVQRKEEAEASSVTKELNSPKAQEENAARELEERRKDEEQPVTTNGSSKESPVEAAAETVKPPTADHIEEGEITDKDEDDLPTKEEKKAVASKSPPKETQRKQSRSPDGKRRRPRSSSRSPSPSSRRRRRSRSKGSRTRSRSKSPIRRRSNSLERRRVERQRRHEERDKRDEERAKEREKRHQKGEPTSSRRRDDSREKKRSPERKRDRSSSTPKSKSSKTPRHTETTETNADNETVTEPAAKITERQRKTVDVLTSRTGGAYIPPAKLRMMQSQITDKSSAAYQRIAWEALKKSIHGYINKVNVTNIAIITRELLRENIVRGRGLLSRSIIQAQAASPTFTHVYAALVSIINSKFPNIGELLLKRLVIQFRRAFRRNDKMVCMSATRFIGHLVNQRVAHEILALEILTLLVETPTDDSVEVAIAFLKECGMKLTEVSSKGIGAIFEMLRNILHEGKLDKRVQYMIEVLFQIRKDGFKDHQAVVPELELVEEDDQFTHLMMLDEATETEDILNVFKFDDNYAENEDKYKGLSREILGSDDGSSSGSGSGSDSDSDSDGESGSDAEKKAEAGDIIDSTETNLIALRRTIYLTINSSLDYEECAHKLMKMQLKPGQEIELCHMFLDCCAEQRTYEKFYGLLAQRFCNINKIYIPPFEEIFKDTYQTTHRLDTNRLRNVSKFFAHLLFTDAISWDVLECIQLNEDDTTSSSRIFIKILFQELAEYMGLGKLNAKLKDDVLVESIAGLFPKDNPRNTRFSINFFTSIGLGGLTDDLRRFLKNAPKSVPAINAEILANAGGNPFRDGSAPAGNTKVAPSSSSSSSSSSDTDSEDSSEEDSSSDSSSESSSSDSSSEPKKKRKRKDKDKKKSKKATKEKSKKTKNKKKKKKAEKEQEKEKEKQRKSKKEKEKDKKRKKEEKKAAKKKSKHRRKSQESSDSSGSEDSDKSTSESSDSSNSSSDESDAEPQAKIKRQEHVEKNKFRGRTQDSDEFNLEGPGSKNRFQPNGNGQRRRDNSTGRERNRENSSYDRERNRGNSSYDRERKRGNSSYDRERNRESSYDKERKNRNAVAHDRQRKRDRSRSYERPTIRENSAPREKRMESSRSEKDSRRGDRSSRNERSDRGERSDRGERSDRGERSDRGERSDRGERSDRGERSDREKERSRAKERERDRDRDLKGQRERKRERDDGSRDRSRRERSSRRSKGRS
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
90PhosphorylationTPAAEPRSERQHISH
CCCCCCHHHHHHHHH		48.0922817900
127PhosphorylationNEAKKVETPVQRKEE
HHHHCCCCCCCHHHH		31.5722817900
146PhosphorylationSVTKELNSPKAQEEN
HHHHHHCCHHHHHHH		40.1625749252
178PhosphorylationTNGSSKESPVEAAAE
CCCCCCCCHHHHHHH		37.6722668510
191PhosphorylationAETVKPPTADHIEEG
HHHCCCCCCCCCCCC		53.9318327897
201PhosphorylationHIEEGEITDKDEDDL
CCCCCCCCCCCCCCC		32.4719429919
219PhosphorylationEEKKAVASKSPPKET
HHHHHHHCCCCCHHH		27.3722817900
221PhosphorylationKKAVASKSPPKETQR
HHHHHCCCCCHHHHC		43.8919429919
267PhosphorylationSKGSRTRSRSKSPIR
CCCCCCCCCCCCCCH		40.0519429919
269PhosphorylationGSRTRSRSKSPIRRR
CCCCCCCCCCCCHHH		38.4419429919
271PhosphorylationRTRSRSKSPIRRRSN
CCCCCCCCCCHHHCH		27.1419429919
277PhosphorylationKSPIRRRSNSLERRR
CCCCHHHCHHHHHHH		29.0322817900
279PhosphorylationPIRRRSNSLERRRVE
CCHHHCHHHHHHHHH		32.6222817900
654AcetylationNYAENEDKYKGLSRE
CCCCCHHHHCCCCHH		42.5621791702
930PhosphorylationGNPFRDGSAPAGNTK
CCCCCCCCCCCCCCE		35.0527626673
1108PhosphorylationKNKFRGRTQDSDEFN
HCCCCCCCCCCCCCC		39.2819429919
1111PhosphorylationFRGRTQDSDEFNLEG
CCCCCCCCCCCCCCC		29.2621082442
1121PhosphorylationFNLEGPGSKNRFQPN
CCCCCCCCCCCCCCC		29.8617372656
1148PhosphorylationRERNRENSSYDRERN
CHHHCCCCHHHHHHC		26.0619429919
1149PhosphorylationERNRENSSYDRERNR
HHHCCCCHHHHHHCC		42.5119429919
1150PhosphorylationRNRENSSYDRERNRG
HHCCCCHHHHHHCCC		20.8822817900
1159PhosphorylationRERNRGNSSYDRERK
HHHCCCCCHHHHHHH		32.8519429919
1160PhosphorylationERNRGNSSYDRERKR
HHCCCCCHHHHHHHC		34.7419429919
1161PhosphorylationRNRGNSSYDRERKRG
HCCCCCHHHHHHHCC		20.8819429919
1170PhosphorylationRERKRGNSSYDRERN
HHHHCCCCHHHHHHH		32.8519429919
1171PhosphorylationERKRGNSSYDRERNR
HHHCCCCHHHHHHHH		34.7419429919
1172PhosphorylationRKRGNSSYDRERNRE
HHCCCCHHHHHHHHH		20.8819429919
1180PhosphorylationDRERNRESSYDKERK
HHHHHHHCHHHHHHH		30.8425749252
1181PhosphorylationRERNRESSYDKERKN
HHHHHHCHHHHHHHH		32.3725749252
1182PhosphorylationERNRESSYDKERKNR
HHHHHCHHHHHHHHH		40.0718327897
1203PhosphorylationRQRKRDRSRSYERPT
HHHHHHHHHCCCCCC		29.8419429919
1205PhosphorylationRKRDRSRSYERPTIR
HHHHHHHCCCCCCCC		32.3719429919
1206PhosphorylationKRDRSRSYERPTIRE
HHHHHHCCCCCCCCC		18.1719429919
1210PhosphorylationSRSYERPTIRENSAP
HHCCCCCCCCCCCCC		38.6019429919
1215PhosphorylationRPTIRENSAPREKRM
CCCCCCCCCCHHHHH		34.5925749252
1224PhosphorylationPREKRMESSRSEKDS
CHHHHHHHHHHHHHH		23.0019429919
1225PhosphorylationREKRMESSRSEKDSR
HHHHHHHHHHHHHHC		26.9019429919
1227PhosphorylationKRMESSRSEKDSRRG
HHHHHHHHHHHHCCC		51.4519429919
1249PhosphorylationRSDRGERSDRGERSD
CCCCCCCCCCCCCCC		27.6222817900
1313PhosphorylationKRERDDGSRDRSRRE
HHHCCCCCCHHHHHH		37.6922817900
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 CWC22_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CWC22_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 CWC22_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CWC22_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 THR-191; THR-201; SER-219;SER-221; THR-1108; SER-1111; SER-1180; SER-1181 AND TYR-1182, AND MASSSPECTROMETRY.
"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-1121, AND MASSSPECTROMETRY.

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