RRP12_DROME - dbPTM
RRP12_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID RRP12_DROME
UniProt AC Q9VYA7
Protein Name RRP12-like protein
Gene Name CG2691
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1384
Subcellular Localization Nucleus.
Protein Description
Protein Sequence MGKFRSKLKRNGKGKTWSRGESATSNPTQMKHRMKAKSRFFQPNLSLAAATTTGLTMEAVHKHEQSQAFNAETTTVNDVAGSLRSFKLDDDDDGMSGSGTAPTGTAPTGTIKTFQTFASNYSGCSNTCFQKLVTSFRSSSALHKEMLAILSALTEIIRENGGGESSTEYFLLLMEQIEAATEERDIVAGVTLLAMGINSVPAPVLKKRFAQTADTMQRLLQRFMESTNQSVIRHVIGCLSVILRAQDYAAWSYSSTFQYFDAILAFSIHSQPKIRKAAQHAIALIIHGSCFMLPAIKSDDNEMDEAVEQPKVKHHPASSRVAKFCLAQFKPEVLANAQTTVLHTLELLKDTLYGFKTEDIRSVCEHLLSIMTAANVLVRTNCFQTLYSLFLKKSPNLNASLCAKLLAAIHEYRPDKSDIRQTIAWVTVLKEGHLHLATMQLDLCMQALPRLIDVCTTDLWLSDQKELVAGVSNCIKELLQDCVSRACATAEDAQCNRQSVSRIIASLHKMLNAPFGEISRFVILIFSFVFEACGKLFGSELTPPLMTICKRYDTQSAHRLQIEHTVISAIKALGPELVLTAIPLADGKGVMQLERSWLLPLLREGANGASLQFFKEKIVALAMDCQLKWKEFAEAKNNSSSHIYELLCCQLWGLFPGFCRQPRDPEYLRYLAPTLGAAVEKNPEFRPPIYDGLMELLGDNQSAECHQAIGQYAKNFLPRLFNIYTQKPNGTYEADQRKRVLEVIRLYISRAPADVQLELFENAQEQLAASALASFEYDAFFDINAAIVRVQTCKGIKAYFDKYMAPILRNDKSKLVAKDEQKLKKQQRKTYELLRELMTSELPSCQKFTRKNSIVLQQILLDSFNTSCNVCQASRLHCLKSLIDCHSNLAYNDQLVMKAIPEAVLNYKEFSNYKEQVAEQLIKSITQLYHDAGKINDFVDILTAGFAGDEMLVTNTILAFRAVLQQQGEHLTVATLEFVLQQVSVFLVQKSRKQAEAAIAFLITFIKVMPIPLVANHLEAIMRSLSAMTKDTKRYCRIQIGYLLKKLCIRFSPGELAGFVPGDDDVIHRRLKMIRKRTRRDLRKKQNLEAQEDSSDDELVSGLQEKSYTIDDMLADSDSDLPEDMDAKDEAGAAAAASKRSKNAKQQKSTYIREDPDEIVDLADLKSIGNVLTSGSAQTATPAQSQKTKAQLPNGGFKTADDGRLIISDKALRGQGGNDQSDDDSDSDASMAYGTVAKQPKVKRGMEDDSSDEDKLQQKLVPKRVRKGDDAMSMKSGKTTASSRYTAGGKGIHRQLTAGNSDAMSVKSGKSTSRPAGSEYGSKKAKGDMKKSGKLDPYAYIPLTRNNLNKRKRSMNSRKFKSVLRGAGAENGGAGGGRVSKKYK
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
82PhosphorylationTVNDVAGSLRSFKLD
CHHHHCHHHHCEECC		15.7519429919
85PhosphorylationDVAGSLRSFKLDDDD
HHCHHHHCEECCCCC		31.8419429919
96PhosphorylationDDDDDGMSGSGTAPT
CCCCCCCCCCCCCCC		35.0219429919
98PhosphorylationDDDGMSGSGTAPTGT
CCCCCCCCCCCCCCC		26.1819429919
100PhosphorylationDGMSGSGTAPTGTAP
CCCCCCCCCCCCCCC		31.0319429919
103PhosphorylationSGSGTAPTGTAPTGT
CCCCCCCCCCCCCCC		44.7119429919
499PhosphorylationDAQCNRQSVSRIIAS
HHHCCHHHHHHHHHH		20.8722817900
501PhosphorylationQCNRQSVSRIIASLH
HCCHHHHHHHHHHHH		24.0222817900
506PhosphorylationSVSRIIASLHKMLNA
HHHHHHHHHHHHHCC		22.1622817900
847AcetylationSELPSCQKFTRKNSI
CCCCHHHHHHCCCCH		53.6921791702
1094PhosphorylationNLEAQEDSSDDELVS
CCHHCCCCCHHHHHH		34.6119429919
1095PhosphorylationLEAQEDSSDDELVSG
CHHCCCCCHHHHHHH		62.4919429919
1101PhosphorylationSSDDELVSGLQEKSY
CCHHHHHHHHHHCCC		46.5422668510
1107PhosphorylationVSGLQEKSYTIDDML
HHHHHHCCCCHHHHH		27.1023607784
1108PhosphorylationSGLQEKSYTIDDMLA
HHHHHCCCCHHHHHC		20.8423607784
1109PhosphorylationGLQEKSYTIDDMLAD
HHHHCCCCHHHHHCC		25.6422668510
1117PhosphorylationIDDMLADSDSDLPED
HHHHHCCCCCCCCCC		33.1519429919
1119PhosphorylationDMLADSDSDLPEDMD
HHHCCCCCCCCCCCC		45.0219429919
1221PhosphorylationGQGGNDQSDDDSDSD
CCCCCCCCCCCCCCC		45.9619429919
1225PhosphorylationNDQSDDDSDSDASMA
CCCCCCCCCCCCHHH		46.1119429919
1227PhosphorylationQSDDDSDSDASMAYG
CCCCCCCCCCHHHHH		38.7419429919
1230PhosphorylationDDSDSDASMAYGTVA
CCCCCCCHHHHHHHC		14.6719429919
1233PhosphorylationDSDASMAYGTVAKQP
CCCCHHHHHHHCCCC		12.5119429919
1235PhosphorylationDASMAYGTVAKQPKV
CCHHHHHHHCCCCCC		12.4819429919
1250PhosphorylationKRGMEDDSSDEDKLQ
CCCCCCCCCCHHHHH		52.6019429919
1251PhosphorylationRGMEDDSSDEDKLQQ
CCCCCCCCCHHHHHH		52.6019429919
1273PhosphorylationRKGDDAMSMKSGKTT
CCCCCCCCCCCCCCC		25.4427626673
1276PhosphorylationDDAMSMKSGKTTASS
CCCCCCCCCCCCCCC		36.5627626673
1290AcetylationSRYTAGGKGIHRQLT
CCCCCCCCCHHHHCC		54.4921791702
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 RRP12_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of RRP12_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 RRP12_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 RRP12_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-82; SER-85; SER-96;SER-1094; SER-1095; SER-1117; SER-1119; SER-1221; SER-1225; SER-1227;SER-1230; SER-1250 AND SER-1251, 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-82, AND MASSSPECTROMETRY.

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