CNN_DROME - dbPTM
CNN_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CNN_DROME
UniProt AC P54623
Protein Name Centrosomin
Gene Name cnn
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1320
Subcellular Localization Cytoplasm. Cytoplasm, cytoskeleton, microtubule organizing center, centrosome. Cytoplasm, cytoskeleton, flagellum basal body. Localized to the centrosomes through complete nuclear cycles in mitotic and meiotic cells. Redistributed into the cytoplasm
Protein Description Core component of the centrosome throughout spermatogenesis. May participate in mitotic spindle assembly and the mechanics of morphogenesis through an interaction with microtubules, either directly or indirectly. Is a target of several homeotic genes..
Protein Sequence MNSNRTSSSHNSRNLKILNASFDVPRPPGGGNSPLPSQGRSVRELEEQMSALRKENFNLKLRIYFLEEGQPGARADSSTESLSKQLIDAKIEIATLRKTVDVKMELLKDAARAISHHEELQRKADIDSQAIIDELQEQIHAYQMAESGGQPVENIAKTRKMLRLESEVQRLEEELVNIEARNVAARNELEFMLAERLESLTACEGKIQELAIKNSELVERLEKETASAESSNEAIDSLKVELEACRKENQDLVTSIRTLKHDMKRQVRSMKEAANTMDVQRQSILLLEATIKRKEKSCGSMQKNVLNYEALIAKLNAELETMRQQNVYFRELSENLQQKEVRQLDRGVAIVQPMRMTADAGRFVWQSGTIVAQEPLPLERQSAAATSNVSVSAVRLSSGPPPDQTYPVNGHDRAKYGLLQLFAAKLDWISAVPLALGHLALKIILLAMRLHSCLQNVHIPLRANRDLGAQLADKICELQEAQEKLKERERIHEQACRTIQKLMQKLSSQEKEIKKLNQENEQSANKENDCAKTVISPSSSGRSMSDNEASSQEMSTNLRVRYELKINEQEEKIKQLQTEVKKKTANLQNLVNKELWEKNREVERLTKLLANQQKTLPQISEESAGEADLQQSFTEAEYMRALERNKLLQRKVDVLFQRLADDQQNSAVIGQLRLELQQARTEVETADKWRLECVDVCSVLTNRLEELAGFLNSLLKHKDVLGVLAADRRNAMRKAVDRSLDLSKSLNMTLNITATSLADQSLAQLCNLSEILYTEGDASHKTFNSHEELHAATSMAPTVENLKAENKALKKELEKRRSSEGQRKERRSLPLPSQQFDNQSESEAWSEPDRKVSLARIGLDETSNSLAAPEQAISESESEGRTCATRQDRNRNSERIAQLEEQIAQKDERMLNVQCQMVELDNRYKQEQLRCLDITQQLEQLRAINEALTADLHAIGSHEEERMVELQRQLELKNQQIDQLKLAHSTLTADSQITEMELQALQQQMQEIEQLHADSVETLQSQLQKLKLDAVQQLEEHERLHREALERDWVALTTYQEQAQQLLELQRSLDYHQENEKELKQTLVENELATRALKKQLDESTLQASKAVMERTKAYNDKLQLEKRSEELRLQLEALKEEHQKLLQKRSNSSDVSQSGYTSEEVAVPMGPPSGQATTCKQAAAAVLGQRVNTSSPDLGIESDAGRISSVEVSNAQRAMLKTVEMKTEGSASPKAKSEESTSPDSKSNVATGAATVHDCAKVDLENAELRRKLIRTKRAFEDTYEKLRMANKAKAQVEKDIKNQILKTHNVLRNVRSNMENEL
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
7 (in isoform 3)Phosphorylation-26.9721082442
8 (in isoform 3)Phosphorylation-34.7021082442
9 (in isoform 3)Phosphorylation-26.8421082442
91 (in isoform 2)Phosphorylation-5.0530478224
536PhosphorylationDCAKTVISPSSSGRS
CHHCEECCCCCCCCC		17.8830478224
538PhosphorylationAKTVISPSSSGRSMS
HCEECCCCCCCCCCC		30.2825749252
543PhosphorylationSPSSSGRSMSDNEAS
CCCCCCCCCCCCCCC		26.6019429919
545PhosphorylationSSSGRSMSDNEASSQ
CCCCCCCCCCCCCCC		38.2319060867
739PhosphorylationMRKAVDRSLDLSKSL
HHHHHHHHCCHHHHH		23.0527626673
743PhosphorylationVDRSLDLSKSLNMTL
HHHHCCHHHHHCCEE		21.6225749252
782PhosphorylationEGDASHKTFNSHEEL
CCCCCCCCCCCHHHH		23.7119429919
785PhosphorylationASHKTFNSHEELHAA
CCCCCCCCHHHHHHH		28.2519429919
840PhosphorylationSQQFDNQSESEAWSE
HHHCCCCCHHHHCCC		49.7119429919
842PhosphorylationQFDNQSESEAWSEPD
HCCCCCHHHHCCCCC		37.5519429919
853PhosphorylationSEPDRKVSLARIGLD
CCCCHHHHHEHHCCC		21.2427626673
874PhosphorylationAAPEQAISESESEGR
CCHHHHHCCCHHCCC		37.7819429919
876PhosphorylationPEQAISESESEGRTC
HHHHHCCCHHCCCCC		39.3619429919
878PhosphorylationQAISESESEGRTCAT
HHHCCCHHCCCCCCC		55.4119429919
882PhosphorylationESESEGRTCATRQDR
CCHHCCCCCCCHHHH		19.8321082442
1191PhosphorylationLGQRVNTSSPDLGIE
HCCCCCCCCCCCCCC		34.3719429919
1192PhosphorylationGQRVNTSSPDLGIES
CCCCCCCCCCCCCCC		22.0119429919
1234PhosphorylationSASPKAKSEESTSPD
CCCCCCCCCCCCCCC		52.0022817900
1237PhosphorylationPKAKSEESTSPDSKS
CCCCCCCCCCCCCCC		30.0822817900
1238PhosphorylationKAKSEESTSPDSKSN
CCCCCCCCCCCCCCC		47.7822817900
1239PhosphorylationAKSEESTSPDSKSNV
CCCCCCCCCCCCCCC		35.6719060867
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 CNN_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CNN_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 CNN_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SINA_DROMEsinaphysical
14605208
BUN1_DROMEbunphysical
14605208
BUN2_DROMEbunphysical
14605208
CACT_DROMEcactphysical
14605208
ATPG_DROMEATPsyn-gammaphysical
14605208
MED4_DROMEMED4physical
14605208
MYB_DROMEMybphysical
14605208
TBB1_DROMEbetaTub56Dphysical
14605208
CCD22_DROMECG9951physical
14605208
EWG_DROMEewgphysical
22751930
GCP2_DROMEGrip84physical
22751930
TBG1_DROMEgammaTub23Cphysical
12939255
TBG1_DROMEgammaTub23Cphysical
22751930
LAM0_DROMELamphysical
22751930
CUP_DROMEcupphysical
22751930
GCP4_DROMEGrip75physical
22751930
EDC4_DROMEGe-1physical
22751930
QUAI_DROMEquaphysical
22751930
TBG2_DROMEgammaTub37Cphysical
12939255
TBG2_DROMEgammaTub37Cphysical
22751930
CNN_DROMEcnnphysical
26447129
CNN_DROMEcnnphysical
24656740
CNN_DROMEcnnphysical
27558293
EIF3C_DROMEeIF3-S8physical
22751930
OTE_DROMEOtephysical
22751930
TBB1_DROMEbetaTub56Dphysical
21694707
LBR_DROMELBRphysical
22751930
NUDEL_DROMEndlphysical
22751930
HSP27_DROMEHsp27physical
22751930
NHK1_DROMEballphysical
22751930
DDX3_DROMEbelphysical
22751930
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CNN_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-545; THR-782; SER-785;SER-874; SER-876; SER-878; SER-1191; SER-1234; SER-1237 AND SER-1239,AND MASS SPECTROMETRY.

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