ANLN_DROME - dbPTM
ANLN_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID ANLN_DROME
UniProt AC Q9V4P1
Protein Name Anillin
Gene Name scra
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 1239
Subcellular Localization Nucleus. Cytoplasm, cytoskeleton. Cytoplasm, cell cortex. Mainly found in the nucleus during interphase. Colocalizes with cortical F-actin upon nuclear envelope breakdown in mitosis and subsequently concentrates in the area of the prospective contrac
Protein Description Required for cytokinesis. Essential for the structural integrity of the cleavage furrow and for completion of cleavage furrow ingression and proper formation of the midbody. Required during cellularization of syncytial embryos for the proper formation and function of the furrow canals, the stable inward folds of the plasma membrane which separate the peripheral nuclei. Also required for the formation of the pole cells, the progenitors of the adult germline which are formed by cytokinesis of the cytoplasmic buds at the posterior pole of the syncytial embryo. Essential for embryonic viability..
Protein Sequence MDPFTQHMLEKAEQRSRALGISNASKFPLVECSVPSSSATSASGGDAGVLAPRSRSPGGQSAASGGGKVVTLGKATLEASPAKPLRHYTAVNKENLDMGIEINITTDKPIGVQVEIQEQEVTDDEEQAEGGALNPLLEAEPVNQPLARLRDTSRSRLQRMGALYSNTDDLSSPIHRTEGQFHVTTGEEEDCGNRSSRQPKQRLGKLAALADTINQWEDDTSHHEVHRLLEAPPPKPHLSSRRAEKGPAPLPPKKDEVDEASRTKQLKWDPKVLSSLEAQGFQRRESSTIKHTYDYAKQEEAAPASKVEDAVLTAKPPVPQKSTTVSQVAKNFASSAPAPKPAPAPAVSVKSGLVSGRAALFENKGTGGQSQGLRNQKDPCELSLKERMKLFETGNNKAMLPMAPIGSAPSITQIRAEEVKQHLAAMHPVTAAAATTVVAATKPKQENKLRDKVAALVANAQSSAETRIKDIDRQRQEDMQIISNRFNKQKELFDNQPSDSSVAAQARPPAPAPSRVVRPMPPPPPPPIAALSPGLASSKRRSPGDAPTTDEDSKRARKSHSDRLYPALSDLDSSGDNCCAAETASATDDSHQQDEEETESCMDESDDQSQTEDSSAGMCNGSLGREIMSAVQRNEVEMQQQQTGKKTVRYADQDMYYDDSSLNSSQVSAGIDDYLDEALVEDYGSTQDDQSDSGDEQNASRLSLGSKGTTASNSFSFRKNPASICTPIEEHHEMEMDLQTPLLSGAQPVKSELSVNQDNDNLVTLVHTVSFYRRQQSANSSNSTPVRKICREQQVMRSALAGDCHAKHRLEYDSPQQSDYVAAATDIADQTDEDDEEMQNAREVNDASQAQDKIKKLLSEVCKQQQVIGQASQALNLCAATVEFSGSTESVEGERYLLLATHRRQACLDEVQRLRVENSIRPVGAPKEKGLLTVKDITIPLRQEYVRKMASNNINGHHLVCLLKYNEHVLATKTVPTMPGLLSVKFPDVLQLNNVYADFRITLEIYGMLAQRDQLPHELKYHINLNKKGGIKTPKKKGGENRLVMPPVQSPAGPHVVRTPQLVQYGFAIFSLREIQRTTWTLTQVLGVSPLEGVVHMKVNCELSVSVEYKGFLTMFEDISGFGAWHRRWCYLNGSVINYWKYPDDEKRKTPMGSIDLNSCTSQKVTTAPRDICARLNTMLLECERPALETDQESLIIVPNGRTTTVRHLLSADTKEEREEWCAYLNKALTLLRAWGTTH
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
54PhosphorylationAGVLAPRSRSPGGQS
CEEECCCCCCCCCCC		35.7319429919
56PhosphorylationVLAPRSRSPGGQSAA
EECCCCCCCCCCCCC		29.1919429919
61PhosphorylationSRSPGGQSAASGGGK
CCCCCCCCCCCCCCC		29.1319429919
64PhosphorylationPGGQSAASGGGKVVT
CCCCCCCCCCCCEEE		37.3719429919
71PhosphorylationSGGGKVVTLGKATLE
CCCCCEEEECEEEEE		32.5522817900
76PhosphorylationVVTLGKATLEASPAK
EEEECEEEEECCCCC		28.7221082442
80PhosphorylationGKATLEASPAKPLRH
CEEEEECCCCCCCCE		18.9319429919
83AcetylationTLEASPAKPLRHYTA
EEECCCCCCCCEEEE		48.22-
89PhosphorylationAKPLRHYTAVNKENL
CCCCCEEEECCHHHC		20.2922817900
164PhosphorylationLQRMGALYSNTDDLS
HHHHHHCCCCCCCCC		10.1918281928
165PhosphorylationQRMGALYSNTDDLSS
HHHHHCCCCCCCCCC		33.8219429919
167PhosphorylationMGALYSNTDDLSSPI
HHHCCCCCCCCCCCC		25.5819429919
171PhosphorylationYSNTDDLSSPIHRTE
CCCCCCCCCCCCCCC		40.8519429919
172PhosphorylationSNTDDLSSPIHRTEG
CCCCCCCCCCCCCCC		34.8619429919
261PhosphorylationKDEVDEASRTKQLKW
CCCCCHHHHHHHCCC		38.1322817900
366PhosphorylationALFENKGTGGQSQGL
EHHCCCCCCCCCCCC		39.4822817900
410PhosphorylationAPIGSAPSITQIRAE
CCCCCCCCCHHCCHH		37.6721082442
532PhosphorylationPPPIAALSPGLASSK
CCCCCCCCCCCCCCC		16.5223607784
537PhosphorylationALSPGLASSKRRSPG
CCCCCCCCCCCCCCC		41.2423607784
710PhosphorylationSLGSKGTTASNSFSF
ECCCCCCCCCCCCCC		36.4429892262
712PhosphorylationGSKGTTASNSFSFRK
CCCCCCCCCCCCCCC		30.8019060867
714PhosphorylationKGTTASNSFSFRKNP
CCCCCCCCCCCCCCC		21.5525749252
740PhosphorylationEMEMDLQTPLLSGAQ
CCCCCCCCCCCCCCC		24.1722817900
744PhosphorylationDLQTPLLSGAQPVKS
CCCCCCCCCCCCCCC		39.5018327897
751PhosphorylationSGAQPVKSELSVNQD
CCCCCCCCEEECCCC		43.9619429919
754PhosphorylationQPVKSELSVNQDNDN
CCCCCEEECCCCCCC		18.2519429919
770PhosphorylationVTLVHTVSFYRRQQS
EEEEEHHHHHHHHHH		20.0921082442
772PhosphorylationLVHTVSFYRRQQSAN
EEEHHHHHHHHHHCC		9.4421082442
777PhosphorylationSFYRRQQSANSSNST
HHHHHHHHCCCCCCC		22.5322817900
780PhosphorylationRRQQSANSSNSTPVR
HHHHHCCCCCCCCHH		30.5221082442
784PhosphorylationSANSSNSTPVRKICR
HCCCCCCCCHHHHHH		30.0121082442
798PhosphorylationREQQVMRSALAGDCH
HHHHHHHHHHHCCCH		15.0022817900
831PhosphorylationATDIADQTDEDDEEM
HHCCCCCCCCCHHHH		41.7319429919
1033PhosphorylationNKKGGIKTPKKKGGE
CCCCCCCCCCCCCCC		38.1222817900
1050PhosphorylationLVMPPVQSPAGPHVV
CCCCCCCCCCCCCCC		19.5621082442
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 ANLN_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of ANLN_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 ANLN_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
BOREA_DROMEborrphysical
14605208
SCLLA_DROMEscylphysical
14605208
CADE_DROMEshggenetic
20237160
ACT1_DROMEAct5Cphysical
18349071
SQH_DROMEsqhphysical
18349071
MY31D_DROMEMyo31DFphysical
18349071
ARPC2_DROMEArpc2physical
18349071
ACT2_DROMEAct42Aphysical
18349071
PNUT_DROMEpnutphysical
18349071
ACT3_DROMEAct57Bphysical
18349071
MYSN_DROMEzipphysical
18349071
MY61F_DROMEMyo61Fphysical
18349071
SPTCA_DROMEalpha-Specphysical
18349071
ACT4_DROMEAct79Bphysical
18349071
ACT6_DROMEAct88Fphysical
18349071
SEPT2_DROMESep2physical
18349071
ACT5_DROMEAct87Ephysical
18349071
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of ANLN_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-712; THR-740; SER-744;SER-754 AND THR-831, AND MASS SPECTROMETRY.

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