CUP_DROME - dbPTM
CUP_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CUP_DROME
UniProt AC Q9VMA3
Protein Name Protein cup
Gene Name cup
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1117
Subcellular Localization Cytoplasm . Nucleus . Retained in the cytoplasm by interaction with eIF4E1. Located throughout the cytoplasm of all germline cells and is excluded from the nucleus of nurse cells, oocytes and follicular cells (PubMed:15465908). During oogenesis, accu
Protein Description Adapter protein that plays a central role in localization of transcripts in the oocyte and in young embryos. [PubMed: 9118812 Maintains RNA targets in a repressed state by promoting their deadenylation and protects deadenylated mRNAs from further degradation]
Protein Sequence MQMAEAEQENGAGALKIATNAGATDRPAHQQLPLPVEDQQDEVLTPAEKGKFEYPPPPPPPTPVQAPLATKATALNASQEHDDDEANSEKWEDPCAPPPPPPLPTSAFLATGLGYLKLPAFKLKDALEKAITKLEANKRTLKASPESSRSIKNKNVVALEMLPRRSNPETIGDGSMLASTSTAVMLQTKKPAVIVEMERRCKIINLLAKQNQILESISGEAIPMHGPSKHLHEDEGLTLQVLSARASTPYTQPSSMLSCTAVSCDLEHDSPRKQVASKEAVPEQQSSQVQQKRPPSTGIHKPGSLRAPKAVRPTTAPVVSSKPVKSYTRSRLMDIRNGMFNALMHRSKESFVMPRIATCDDIELEGRLRRMNIWRTSDGTRFRTRSTTANLNMNNNNNNECMPAFFKNKNKPNLISDESIIQSQPPQPQTEFQDPAIVNQRRIGSGRLNHSKWGYNDEDYHSYHNGKSQHMEEVNSKNSKNMTVLQFFDNGEISSQPQRRPNTPVMGMSINRSENDTLHSNESSEDLSRANENYVKRVMSGFLVVSKPKSRDVEDRHHRRYRNQNEEPEWFSCGPTSRLDTIELCGFDEDEEKMLKEGNKNHGLGETERETSKQKMDHKYKWTHAEPMGRSKYMPKHDTNNNHNVENMNNVMATEHQQQKEEKRPGSGRSFQFDKFNQSQQNYESSSYVNHQQPPQTQPQQMQQQSNTNTNNSKFMSFFANEGNSSSSSLNEFFKQAINQGHGNNPEQPKSLGHIGQMPSVDQLEAKWRRNSLNNVGETANKQTDNFQKLIGSLSSAKPQSQAVGYDAISNFIMQQQQYQQQQQKQHLIIQQQQQHTAFLASLQLKAILGRADTQLLLLRLTKGEISKHGLLVQLANPRLTDMDREAITAVLQFTNTQQQQQQHKQQLDMLSSTVIASQLQNLHNLAIVQQTLAARQQPQHNPQTQAPHQLSQEDLQAHANVIMRNAVMKRKIEEQTSKLINGGAKHQAQQQYLNRGQQRQARPDANSNALLHALISGGGNNHASGYPMNGQPQKHHSNLRFGDNQNFQSFESNQPHFATQYKQQYQQSQQQHPHQQPQQLNSLHQNNAGAVNSFNKAQMQAQSAISMLPNSGDEFH
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
45PhosphorylationDQQDEVLTPAEKGKF
CCCCCCCCHHHCCCC		26.1528490779
62PhosphorylationPPPPPPPTPVQAPLA
CCCCCCCCCCCCCCC		41.6928490779
70PhosphorylationPVQAPLATKATALNA
CCCCCCCCHHHHHCC		28.9728490779
78PhosphorylationKATALNASQEHDDDE
HHHHHCCHHHCCCCH		34.7222817900
140PhosphorylationKLEANKRTLKASPES
HHHHCHHHHCCCHHH		33.9327626673
144PhosphorylationNKRTLKASPESSRSI
CHHHHCCCHHHHHHH		27.8422817900
147PhosphorylationTLKASPESSRSIKNK
HHCCCHHHHHHHCCC		34.1425749252
175PhosphorylationPETIGDGSMLASTST
CCCCCCCCCCCCCCC		18.5021082442
255PhosphorylationTPYTQPSSMLSCTAV
CCCCCCCHHHCCEEE		30.3518327897
263PhosphorylationMLSCTAVSCDLEHDS
HHCCEEEECCCCCCC		10.2322817900
270PhosphorylationSCDLEHDSPRKQVAS
ECCCCCCCCCHHHCC		28.6322817900
278PhosphorylationPRKQVASKEAVPEQQ
CCHHHCCCCCCCHHH		39.7018327897
285PhosphorylationKEAVPEQQSSQVQQK
CCCCCHHHCHHHHHH		43.3118327897
347PhosphorylationFNALMHRSKESFVMP
HHHHHHHCHHCCCCC		26.5422817900
350PhosphorylationLMHRSKESFVMPRIA
HHHHCHHCCCCCCEE		27.2018327897
362PhosphorylationRIATCDDIELEGRLR
CEEECCCCEEECCHH		4.0918327897
365PhosphorylationTCDDIELEGRLRRMN
ECCCCEEECCHHHCC		29.4918327897
419PhosphorylationPNLISDESIIQSQPP
CCCCCCHHHHCCCCC		29.9530478224
494PhosphorylationFFDNGEISSQPQRRP
EEECCCCCCCCCCCC		20.7218327897
503PhosphorylationQPQRRPNTPVMGMSI
CCCCCCCCCCCCEEE		21.6825749252
509PhosphorylationNTPVMGMSINRSEND
CCCCCCEEECCCCCC		15.8122817900
513PhosphorylationMGMSINRSENDTLHS
CCEEECCCCCCCCCC		35.9422817900
517PhosphorylationINRSENDTLHSNESS
ECCCCCCCCCCCCCH		37.6422817900
518PhosphorylationNRSENDTLHSNESSE
CCCCCCCCCCCCCHH		4.6818327897
520PhosphorylationSENDTLHSNESSEDL
CCCCCCCCCCCHHHH		45.4622817900
523PhosphorylationDTLHSNESSEDLSRA
CCCCCCCCHHHHHHH		43.1928490779
524PhosphorylationTLHSNESSEDLSRAN
CCCCCCCHHHHHHHH		29.0214685270
528PhosphorylationNESSEDLSRANENYV
CCCHHHHHHHHHHHH		41.4918327897
535PhosphorylationSRANENYVKRVMSGF
HHHHHHHHHHHHCCE		4.8718327897
538PhosphorylationNENYVKRVMSGFLVV
HHHHHHHHHCCEEEE		2.7218327897
539PhosphorylationENYVKRVMSGFLVVS
HHHHHHHHCCEEEEE		3.6318327897
540PhosphorylationNYVKRVMSGFLVVSK
HHHHHHHCCEEEEEC		24.4421082442
697PhosphorylationNHQQPPQTQPQQMQQ
CCCCCCCCCHHHHHH		48.2530478224
751PhosphorylationNNPEQPKSLGHIGQM
CCCCCCCCCCCCCCC		46.3921082442
772PhosphorylationEAKWRRNSLNNVGET
HHHHHHHCCCHHHHH		30.5728490779
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 CUP_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CUP_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 CUP_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
DDX6_DROMEme31Bphysical
14605208
GUS_DROMEgusphysical
14605208
HSP7D_DROMEHsc70-4physical
14605208
RL3_DROMERpL3physical
14605208
RL22_DROMERpL22physical
14605208
PDK_DROMEPdkphysical
14605208
CHI10_DROMECht3physical
14605208
IF4E_DROMEeIF-4Ephysical
14685270
NANOS_DROMEnosphysical
11060247
OTU_DROMEotugenetic
9118812
HSP83_DROMEHsp83genetic
19101615
SH3G3_DROMEEndoAgenetic
26102195
IF4E_DROMEeIF-4Egenetic
15465908
DDX6_DROMEme31Bphysical
21937713
PABP_DROMEpAbpphysical
18082158
NANOS_DROMEnosphysical
21081899
IF4E_DROMEeIF-4Ephysical
14723848
IF4E_DROMEeIF-4Ephysical
21937713
IF4E_DROMEeIF-4Ephysical
25179781
IF4E_DROMEeIF-4Ephysical
14691132
IF4E_DROMEeIF-4Ephysical
15465908
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CUP_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-263; SER-270; SER-347;SER-350; THR-503; SER-509; SER-513; SER-520; SER-523 AND SER-524, ANDMASS SPECTROMETRY.

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