CRB_DROME - dbPTM
CRB_DROME - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CRB_DROME
UniProt AC P10040
Protein Name Protein crumbs
Gene Name crb
Organism Drosophila melanogaster (Fruit fly).
Sequence Length 2146
Subcellular Localization Apical cell membrane
Single-pass type I membrane protein . Cytoplasm, cytoskeleton, spindle . Specifically localized to the apical membrane (PubMed:11076972, PubMed:2344615). Expressed in a mesh punctate pattern that overlaps with metaphase spindle
Protein Description Plays a central role in cell polarity establishment. [PubMed: 2344615]
Protein Sequence MAKIANASLSQQQKQRQAETATTTTTTVAASVETATTTARSRDRTKSAAQITSHLLKRAISVYSSPQWIPLFILIYLATDVASVAVPTKEAYFNGSTYLRLTTPMPIWDHSAISFRSCRGGEILAQQYNKNSIVISVLNDFLQISLAGPAVHGPNNRLDVKLPYQLLDNRWHTLQFKYEYGNLYLHVDRAASIFANSTYNSQFLTNQDIGYKDAILILGNSFSGCLLDGPGLQFVNNSTVQNVVFGHCPLTPGPCSDHDLFTRLPDNFCLNDPCMGHGTCSSSPEGYECRCTARYSGKNCQKDNGSPCAKNPCENGGSCLENSRGDYQCFCDPNHSGQHCETEVNIHPLCQTNPCLNNGACVVIGGSGALTCECPKGYAGARCEVDTDECASQPCQNNGSCIDRINGFSCDCSGTGYTGAFCQTNVDECDKNPCLNGGRCFDTYGWYTCQCLDGWGGEICDRPMTCQTQQCLNGGTCLDKPIGFQCLCPPEYTGELCQIAPSCAQQCPIDSECVGGKCVCKPGSSGYNCQTSTGDGASALALTPINCNATNGKCLNGGTCSMNGTHCYCAVGYSGDRCEKAENCSPLNCQEPMVCVQNQCLCPENKVCNQCATQPCQNGGECVDLPNGDYECKCTRGWTGRTCGNDVDECTLHPKICGNGICKNEKGSYKCYCTPGFTGVHCDSDVDECLSFPCLNGATCHNKINAYECVCQPGYEGENCEVDIDECGSNPCSNGSTCIDRINNFTCNCIPGMTGRICDIDIDDCVGDPCLNGGQCIDQLGGFRCDCSGTGYEGENCELNIDECLSNPCTNGAKCLDRVKDYFCDCHNGYKGKNCEQDINECESNPCQYNGNCLERSNITLYQMSRITDLPKVFSQPFSFENASGYECVCVPGIIGKNCEININECDSNPCSKHGNCNDGIGTYTCECEPGFEGTHCEINIDECDRYNPCQRGTCYDQIDDYDCDCDANYGGKNCSVLLKGCDQNPCLNGGACLPYLINEVTHLYNCTCENGFQGDKCEKTTTLSMVATSLISVTTEREEGYDINLQFRTTLPNGVLAFGTTGEKNEPVSYILELINGRLNLHSSLLNKWEGVFIGSKLNDSNWHKVFVAINTSHLVLSANDEQAIFPVGSYETANNSQPSFPRTYLGGTIPNLKSYLRHLTHQPSAFVGCMQDIMVNGKWIFPDEQDANISYTKLENVQSGCPRTEQCKPNPCHSNGECTDLWHTFACHCPRPFFGHTCQHNMTAATFGHENTTHSAVIVETTDVARRAIRSILDISMFIRTREPTGQVFYLGTDPRKAPTKNIGDSYVAAKLHGGELLVKMQFSGTPEAYTVGGQKLDNGYNHLIEVVRNQTLVQVKLNGTEYFRKTLSTTGLLDAQVLYLGGPAPTRESLLGATTEPGIIPVPGAGIPIEDTTVPKEADDSRDYFKGIIQDVKVSNGSLNLIVEMYSLNVTDVQVNAKPLGAVTIDRASVLPGEVSDDLCRKNPCLHNAECRNTWNDYTCKCPNGYKGKNCQEIEFCQHVTCPGQSLCQNLDDGYECVTNTTFTGQERSPLAFFYFQEQQSDDIVSEASPKQTLKPVIDIAFRTRAGGTLLYIDNVDGFFEIGVNGGRVTITWKLSALHFGESARFEKENTDGEWSRIYLRAHNSKLEGGWKGWESMVDPTPAFSTDIDQAAFQSLIATSTQVYLGGMPESRQARGSTLSAQQGSQFKGCVGEARVGDLLLPYFSMAELYSRTNVSVQQKAQFRLNATRPEEGCILCFQSDCKNDGFCQSPSDEYACTCQPGFEGDDCGTDIDECLNTECLNNGTCINQVAAFFCQCQPGFEGQHCEQNIDECADQPCHNGGNCTDLIASYVCDCPEDYMGPQCDVLKQMTCENEPCRNGSTCQNGFNASTGNNFTCTCVPGFEGPLCDIPFCEITPCDNGGLCLTTGAVPMCKCSLGYTGRLCEQDINECESNPCQNGGQCKDLVGRYECDCQGTGFEGIRCENDIDECNMEGDYCGGLGRCFNKPGSFQCICQKPYCGAYCNFTDPCNATDLCSNGGRCVESCGAKPDYYCECPEGFAGKNCTAPITAKEDGPSTTDIAIIVIPVVVVLLLIAGALLGTFLVMARNKRATRGTYSPSAQEYCNPRLEMDNVLKPPPEERLI
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
94N-linked_GlycosylationPTKEAYFNGSTYLRL
CCCCEECCCCEEEEE		30.72-
196N-linked_GlycosylationRAASIFANSTYNSQF
EHHHHHCCCCCCCCC		24.92-
236N-linked_GlycosylationGPGLQFVNNSTVQNV
CCCCEEECCCCCCEE		37.71-
237N-linked_GlycosylationPGLQFVNNSTVQNVV
CCCEEECCCCCCEEE		33.48-
334N-linked_GlycosylationYQCFCDPNHSGQHCE
EEEEECCCCCCCCEE		28.80-
398N-linked_GlycosylationASQPCQNNGSCIDRI
HCCCCCCCCCCCCEE		20.20-
548N-linked_GlycosylationALTPINCNATNGKCL
EEEEECCCCCCCCCC		45.36-
563N-linked_GlycosylationNGGTCSMNGTHCYCA
CCCEECCCCCEEEEE		35.60-
734N-linked_GlycosylationCGSNPCSNGSTCIDR
CCCCCCCCCCCHHHH		55.97-
744N-linked_GlycosylationTCIDRINNFTCNCIP
CHHHHHHCEECCCCC		31.09-
858N-linked_GlycosylationGNCLERSNITLYQMS
CCCCCCCCCEEEEEC		37.17-
882N-linked_GlycosylationSQPFSFENASGYECV
CCCCCCCCCCCCEEE		37.08-
974N-linked_GlycosylationDANYGGKNCSVLLKG
CCCCCCCCEEEEEEC		26.94-
1006N-linked_GlycosylationNEVTHLYNCTCENGF
HHHHHHHCCCCCCCC		22.45-
1100N-linked_GlycosylationVFIGSKLNDSNWHKV
EEEECCCCCCCCEEE		55.1717893096
1112N-linked_GlycosylationHKVFVAINTSHLVLS
EEEEEEEECCEEEEE		26.28-
1136N-linked_GlycosylationVGSYETANNSQPSFP
CCCCCCCCCCCCCCC		56.98-
1190N-linked_GlycosylationFPDEQDANISYTKLE
CCCCCCCCCCEEEEE		31.84-
1243N-linked_GlycosylationFGHTCQHNMTAATFG
CCCCCCCCCCCHHCC		12.01-
1253N-linked_GlycosylationAATFGHENTTHSAVI
CHHCCCCCCCCEEEE		44.60-
1352N-linked_GlycosylationHLIEVVRNQTLVQVK
HHHEECCCCEEEEEE		27.81-
1361N-linked_GlycosylationTLVQVKLNGTEYFRK
EEEEEEECCCHHHHH		50.01-
1439N-linked_GlycosylationIQDVKVSNGSLNLIV
EEEEEECCCCEEEEE		47.24-
1452N-linked_GlycosylationIVEMYSLNVTDVQVN
EEEEEEECCCEEEEC		28.80-
1543N-linked_GlycosylationDGYECVTNTTFTGQE
CCCEEEECCEECCCC		19.41-
1737N-linked_GlycosylationAELYSRTNVSVQQKA
HHHHHCCCCCHHHHH		23.98-
1749N-linked_GlycosylationQKAQFRLNATRPEEG
HHHEEECCCCCCCCC		34.70-
1806N-linked_GlycosylationLNTECLNNGTCINQV
CCCHHHCCCCCHHHH		33.91-
1846N-linked_GlycosylationQPCHNGGNCTDLIAS
CCCCCCCCHHHHHHH		27.24-
1882N-linked_GlycosylationCENEPCRNGSTCQNG
CCCCCCCCCCCCCCC		56.32-
1891N-linked_GlycosylationSTCQNGFNASTGNNF
CCCCCCCCCCCCCCE		34.09-
1897N-linked_GlycosylationFNASTGNNFTCTCVP
CCCCCCCCEEEEECC		34.64-
2027N-linked_GlycosylationPYCGAYCNFTDPCNA
CCCCCCCCCCCCCCH		30.12-
2033N-linked_GlycosylationCNFTDPCNATDLCSN
CCCCCCCCHHHCCCC		51.79-
2066N-linked_GlycosylationPEGFAGKNCTAPITA
CCCCCCCCCCCCEEE		27.70-
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 CRB_DROME !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CRB_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 CRB_DROME !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MOEH_DROMEMoegenetic
26544546
DLG1_DROMEdlg1genetic
12510193
SPTCB_DROMEbeta-Specgenetic
19672952
L2GL_DROMEl(2)glgenetic
12510193
EXPA_DROMEexgenetic
26954546
MAM_DROMEmamgenetic
20110329
RHO1_DROMERho1genetic
26544546
CADE_DROMEshggenetic
26544546
RAC1_DROMERac1genetic
11973353
SPTCA_DROMEalpha-Specgenetic
19672952
ARP3_DROMEArp3genetic
26544546
U195A_DROMECG7949genetic
25065591
PATJ_DROMEPatjgenetic
23136386
PP1B_DROMEflwgenetic
26544546
LAP4_DROMEscribgenetic
12510193
LAP4_DROMEscribgenetic
12510194
APKC_DROMEaPKCgenetic
15302858
U195B_DROMECG30152genetic
25065591
U195B_DROMECG30152physical
25065591
EBI_DROMEebiphysical
27702784
EXPA_DROMEexphysical
20498073
U195A_DROMECG7949physical
25065591
PATJ_DROMEPatjphysical
10102271
PATJ_DROMEPatjphysical
10662667
PATJ_DROMEPatjphysical
15302858
PATJ_DROMEPatjphysical
25847234
APKC_DROMEaPKCphysical
15302858
APKC_DROMEaPKCphysical
16697075
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CRB_DROME

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Related Literatures of Post-Translational Modification
N-linked Glycosylation
ReferencePubMed
"Identification of N-glycosylated proteins from the central nervoussystem of Drosophila melanogaster.";
Koles K., Lim J.-M., Aoki K., Porterfield M., Tiemeyer M., Wells L.,Panin V.;
Glycobiology 17:1388-1403(2007).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-1100, AND MASSSPECTROMETRY.

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