USH_DROME - dbPTM
USH_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID USH_DROME
UniProt AC Q9VPQ6
Protein Name Zinc finger protein ush
Gene Name ush
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1191
Subcellular Localization Nucleus .
Protein Description Transcription regulator that modulates expression mediated by transcription factors of the GATA family such as pnr and srp. Represses transcription of proneural achaete-scute complex (AS-C), which is usually activated by pnr. Involved in cardiogenesis, blood, and eye development. During hematopoiesis, it is required to restrict the number of crystal cells, probably via its interaction with the isoform SrpNC of srp. Negatively regulates expression of sr. Probably acts by interacting with the GATA-type zinc finger of proteins such as pnr and srp, possibly antagonizing the interaction between the GATA-type zinc finger and some cofactor..
Protein Sequence MLSSNTRGDCSDTAEEMTVDSRDSKDLSAQDIGEQKQQQMEDQLEDQLNDSRDPQNNNNNIDDDADEDAEFEEPEKANPQQDQDLGETEMEQEHDLQQEDLQQELPANSPSTPPRSPSSPQLIPKLEQPATPPSEPEASPCPSPSPCPTPKYPKVRLNALLASDPALKPDAKELTLPDSRLLAPPPLVKPDTQAQPEVAEPLLKPARFMCLPCGIAFSSPSTLEAHQAYYCSHRIKDTDEAGSDKSGAGGSGATAGDAAGLTGGSTEPPAKMARTGKQYGCTQCSYSADKKVSLNRHMRMHQTSPAAPTLAGLPSLLQNGIAPPGVTPNPMEDSSSQQTDRYCSHCDIRFNNIKTYRAHKQHYCSSRRPEGQLTPKPDASPGAGSGPGSAGGSIGVSAQAATPGKLSPQARNKTPTPAMVAVAAAAAAAAASLQATPHSHPPFLALPTHPIIIVPCSLIRAASFIPGPLPTPNSGIVNPETTCFTVDNGTIKPLATALVGATLEPERPSAPSSAAEATEAKSSPPEPKRKEAGLTRESAPLDLSLRRSPITLNSLSLRQRQLRNALLDVEEVLLAGVGTGKENVETPRGGGSVTPEQIVCAPSLPSSPSMSPSPKRRAISPRSSGAGSASSMSPPGLNVAVPHLLDMRSMLPADFGLSESLLAKTNPELALKLAAAAAAAAVAGSSGAAAFPPASLPAQTSSGNPGSGGSAGGAQQPQIYVKKGVSKCMECNIVFCKYENYLAHKQHYCSARSQEGASEVDVKSAVSPSIAGAGGLGAGAAEAASSVETTPVAYQQLICAACGIKYTSLDNLRAHQNYYCPKGGAVAAPAATPTDPGQLGMPKEKCGKCKTLHEIGLPCPPPVANPLAAPTVNPQPATNSLNKCPVCGVVSPTAALAKKHMEMHGTVKAYRCSICQYKGNTLRGMRTHIRTHFDKKTSDVNEELYMTCIFEEDASALSQELVTPTGASTTTGHDSMDHPSQMFNCDYCNYVSTYKGNVLRHMKLMHPHVAINSPSISPDTRDQDVTSNPTTNQHSNSDVSNGEAPSFHIKSEPLDPPPTVNLVHENNNSPIATPHIKAEPIEVGADAAPGGLVPPMTSPLGNSSSVAAAAAAAAEVMKKYCSTCDISFNYVKTYLAHKQFYCKNKPIRPEASDSPSPNHLGGGVAVGLGIGGLVGGHGQQKNKENLQEAAI
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
11PhosphorylationSNTRGDCSDTAEEMT
CCCCCCCCCCHHHCC		42.6129892262
25AcetylationTVDSRDSKDLSAQDI
CCCCCCCCCCCHHHH		67.9621791702
28PhosphorylationSRDSKDLSAQDIGEQ
CCCCCCCCHHHHHHH		33.7429892262
109PhosphorylationQQELPANSPSTPPRS
HHHCCCCCCCCCCCC		23.4922817900
112PhosphorylationLPANSPSTPPRSPSS
CCCCCCCCCCCCCCC		40.4722817900
116PhosphorylationSPSTPPRSPSSPQLI
CCCCCCCCCCCCCCC		34.6029892262
118PhosphorylationSTPPRSPSSPQLIPK
CCCCCCCCCCCCCCC		56.7618327897
119PhosphorylationTPPRSPSSPQLIPKL
CCCCCCCCCCCCCCC		21.7622668510
131PhosphorylationPKLEQPATPPSEPEA
CCCCCCCCCCCCCCC		42.2719429919
134PhosphorylationEQPATPPSEPEASPC
CCCCCCCCCCCCCCC		67.9719429919
139PhosphorylationPPSEPEASPCPSPSP
CCCCCCCCCCCCCCC		25.9319429919
143PhosphorylationPEASPCPSPSPCPTP
CCCCCCCCCCCCCCC		44.7319429919
145PhosphorylationASPCPSPSPCPTPKY
CCCCCCCCCCCCCCC		43.3919429919
149PhosphorylationPSPSPCPTPKYPKVR
CCCCCCCCCCCCCHH		38.8519429919
168AcetylationLASDPALKPDAKELT
HHCCCCCCCCCCCCC		42.8521791702
303PhosphorylationRHMRMHQTSPAAPTL
HHHHHHCCCCCCCHH		23.2321082442
304PhosphorylationHMRMHQTSPAAPTLA
HHHHHCCCCCCCHHC		13.1321082442
354AcetylationDIRFNNIKTYRAHKQ
CEECCCCCCHHHHHH		41.4421791702
509PhosphorylationTLEPERPSAPSSAAE
CCCCCCCCCCCHHHH		60.0619429919
512PhosphorylationPERPSAPSSAAEATE
CCCCCCCCHHHHHHH		32.1219429919
513PhosphorylationERPSAPSSAAEATEA
CCCCCCCHHHHHHHH		30.3619429919
518PhosphorylationPSSAAEATEAKSSPP
CCHHHHHHHHHCCCC		28.1619429919
548PhosphorylationLDLSLRRSPITLNSL
CCHHHCCCCCCHHHH		17.7719429919
556PhosphorylationPITLNSLSLRQRQLR
CCCHHHHHHHHHHHH		22.7121082442
623PhosphorylationRRAISPRSSGAGSAS
CCCCCCCCCCCCCCC		36.1919429919
624PhosphorylationRAISPRSSGAGSASS
CCCCCCCCCCCCCCC		33.6619429919
628PhosphorylationPRSSGAGSASSMSPP
CCCCCCCCCCCCCCC		25.1719429919
630PhosphorylationSSGAGSASSMSPPGL
CCCCCCCCCCCCCCC		28.4219429919
631PhosphorylationSGAGSASSMSPPGLN
CCCCCCCCCCCCCCC		24.0119429919
633PhosphorylationAGSASSMSPPGLNVA
CCCCCCCCCCCCCCC		29.8619429919
764PhosphorylationASEVDVKSAVSPSIA
CCCCCHHHHCCCCCC		33.4821082442
1013PhosphorylationHPHVAINSPSISPDT
CCCEEECCCCCCCCC		17.5719429919
1015PhosphorylationHVAINSPSISPDTRD
CEEECCCCCCCCCCC		35.2019429919
1017PhosphorylationAINSPSISPDTRDQD
EECCCCCCCCCCCCC		22.5119429919
1020PhosphorylationSPSISPDTRDQDVTS
CCCCCCCCCCCCCCC		39.2619429919
1059PhosphorylationEPLDPPPTVNLVHEN
CCCCCCCCEEEEECC		28.0019429919
1069PhosphorylationLVHENNNSPIATPHI
EEECCCCCCCCCCCE		21.5819429919
1073PhosphorylationNNNSPIATPHIKAEP
CCCCCCCCCCEECEE		19.0019429919
1138AcetylationVKTYLAHKQFYCKNK
HHHHHHCCEEEECCC		36.1721791702
1152PhosphorylationKPIRPEASDSPSPNH
CCCCCCCCCCCCCCC		36.6423607784
1154PhosphorylationIRPEASDSPSPNHLG
CCCCCCCCCCCCCCC		25.4523607784
1156PhosphorylationPEASDSPSPNHLGGG
CCCCCCCCCCCCCCC		42.1423607784
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 USH_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of USH_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 USH_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SRP_DROMEsrpgenetic
8946251
SRP_DROMEsrpgenetic
14504400
SRP_DROMEsrpgenetic
17936744
FGFR1_DROMEhtlgenetic
10861002
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of USH_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-116; SER-118; SER-1013;SER-1015; SER-1017 AND SER-1156, AND MASS SPECTROMETRY.

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