DIXC1_HUMAN - dbPTM
DIXC1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DIXC1_HUMAN
UniProt AC Q155Q3
Protein Name Dixin
Gene Name DIXDC1
Organism Homo sapiens (Human).
Sequence Length 683
Subcellular Localization Cytoplasm, cytosol . Colocalizes with gamma-tubulin at the centrosome, both during interphase and mitosis.
Isoform 1: Cell junction, focal adhesion. Associated with actin stress fiber at the filament ends.
Isoform 2: Cytoplasm.
Protein Description Positive effector of the Wnt signaling pathway; activates WNT3A signaling via DVL2. Regulates JNK activation by AXIN1 and DVL2..
Protein Sequence MLACLTRGNLLDVLQEGFNEQQLQAYVAWVNAQLKKRPAVKPVQDLRQDLRDGVILAYLIEIVAGEKLSGVQLSPGNQQEMKNNVEKVLQFVASKKIRMHQTSAKDIVDGNLKSIMRLVLALAAHFKPGSSRTVNQGRDSRAPLQSHRPHCATAVAQGAAAALADVCHDMSRSGRDVFRYRQRNSSMDEEIENPYWSVRALVQQYEGQQRSPSESSCSSLTSPSPIHSAKSESIITQSEEKADFVIIPAEGIENRTEGTDSPLSRDWRPGSPGTYLETSWEEQLLEQQEYLEKEMEEAKKMISGLQALLLNGSLPEDEQERPLALCEPGVNPEEQLIIIQSRLDQSMEENQDLKKELLKCKQEARNLQGIKDALQQRLTQQDTSVLQLKQELLRANMDKDELHNQNVDLQRKLDERNRLLGEYKKELGQKDRLLQQHQAKLEEALRKLSDVSYHQVDLERELEHKDVLLAHCMKREADEATNYNSHNSQSNGFLLPTAGKGATSVSNRGTSDLQLVRDALRSLRNSFSGHDPQHHTIDSLEQGISSLMERLHVMETQKKQERKVRVKSPRTQVGSEYRESWPPNSKLPHSQSSPTVSSTCTKVLYFTDRSLTPFMVNIPKRLEEVTLKDFKAAIDREGNHRYHFKALDPEFGTVKEEIFHDDDAIPGWEGKIVAWVEEDHGEN
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
2 (in isoform 2)Myristoylation-4.6620213681
13 (in isoform 2)Phosphorylation-6.3227251275
13PhosphorylationTRGNLLDVLQEGFNE
CCCCHHHHHHHCCCH		6.3227251275
73PhosphorylationEKLSGVQLSPGNQQE
CCCCCCCCCCCCHHH		6.57-
74PhosphorylationKLSGVQLSPGNQQEM
CCCCCCCCCCCHHHH		17.4225159151
94PhosphorylationKVLQFVASKKIRMHQ
HHHHHHHHCCCCCCC		29.22-
130PhosphorylationAAHFKPGSSRTVNQG
HHHCCCCCCCCCCCC		25.7723898821
131PhosphorylationAHFKPGSSRTVNQGR
HHCCCCCCCCCCCCC		37.5723898821
178UbiquitinationSRSGRDVFRYRQRNS
CCCCHHHHHHHHHCC		7.1429967540
180PhosphorylationSGRDVFRYRQRNSSM
CCHHHHHHHHHCCCC		10.30-
184PhosphorylationVFRYRQRNSSMDEEI
HHHHHHHCCCCCHHC		30.05-
185PhosphorylationFRYRQRNSSMDEEIE
HHHHHHCCCCCHHCC		29.2721712546
186PhosphorylationRYRQRNSSMDEEIEN
HHHHHCCCCCHHCCC		33.5328348404
195PhosphorylationDEEIENPYWSVRALV
CHHCCCCHHHHHHHH		23.1529888752
197PhosphorylationEIENPYWSVRALVQQ
HCCCCHHHHHHHHHH		8.9029888752
204PhosphorylationSVRALVQQYEGQQRS
HHHHHHHHHCCCCCC		30.66-
205PhosphorylationVRALVQQYEGQQRSP
HHHHHHHHCCCCCCC		12.6328270605
211PhosphorylationQYEGQQRSPSESSCS
HHCCCCCCCCCCCCC		28.5623663014
213PhosphorylationEGQQRSPSESSCSSL
CCCCCCCCCCCCCCC		51.8923663014
221PhosphorylationESSCSSLTSPSPIHS
CCCCCCCCCCCCCCC		40.31-
222PhosphorylationSSCSSLTSPSPIHSA
CCCCCCCCCCCCCCC		28.7729978859
224PhosphorylationCSSLTSPSPIHSAKS
CCCCCCCCCCCCCCC		35.9329978859
228PhosphorylationTSPSPIHSAKSESII
CCCCCCCCCCCCCCC		37.8029978859
231PhosphorylationSPIHSAKSESIITQS
CCCCCCCCCCCCCCC		35.97-
236PhosphorylationAKSESIITQSEEKAD
CCCCCCCCCCHHHCC		25.1126471730
236UbiquitinationAKSESIITQSEEKAD
CCCCCCCCCCHHHCC		25.1129967540
238PhosphorylationSESIITQSEEKADFV
CCCCCCCCHHHCCEE		38.7925627689
259PhosphorylationIENRTEGTDSPLSRD
CCCCCCCCCCCCCCC		27.3728348404
261PhosphorylationNRTEGTDSPLSRDWR
CCCCCCCCCCCCCCC		27.8121815630
264PhosphorylationEGTDSPLSRDWRPGS
CCCCCCCCCCCCCCC		31.4228258704
271PhosphorylationSRDWRPGSPGTYLET
CCCCCCCCCCCCCCC		23.8828450419
274PhosphorylationWRPGSPGTYLETSWE
CCCCCCCCCCCCCHH		28.4628450419
275PhosphorylationRPGSPGTYLETSWEE
CCCCCCCCCCCCHHH		14.4127732954
278PhosphorylationSPGTYLETSWEEQLL
CCCCCCCCCHHHHHH		36.2227732954
279PhosphorylationPGTYLETSWEEQLLE
CCCCCCCCHHHHHHH		24.1027732954
346PhosphorylationIQSRLDQSMEENQDL
EHHHHHHHHHHCHHH		28.0325159151
371AcetylationARNLQGIKDALQQRL
HHHHHCHHHHHHHHH		43.717683661
381PhosphorylationLQQRLTQQDTSVLQL
HHHHHHHHCCHHHHH		51.1932142685
389UbiquitinationDTSVLQLKQELLRAN
CCHHHHHHHHHHHHC		28.8529967540
394MethylationQLKQELLRANMDKDE
HHHHHHHHHCCCHHH		36.22-
420UbiquitinationLDERNRLLGEYKKEL
HHHHHHHHHHHHHHH		4.4129967540
434UbiquitinationLGQKDRLLQQHQAKL
HCHHHHHHHHHHHHH		4.8629967540
447UbiquitinationKLEEALRKLSDVSYH
HHHHHHHHHHCCCHH		53.8729967540
449PhosphorylationEEALRKLSDVSYHQV
HHHHHHHHCCCHHHC		38.7122210691
452PhosphorylationLRKLSDVSYHQVDLE
HHHHHCCCHHHCCCH		23.1422210691
522PhosphorylationLVRDALRSLRNSFSG
HHHHHHHHHHHHCCC		32.3126670566
590PhosphorylationPNSKLPHSQSSPTVS
CCCCCCCCCCCCCCC		29.8028555341
592PhosphorylationSKLPHSQSSPTVSST
CCCCCCCCCCCCCCC		41.1026657352
593PhosphorylationKLPHSQSSPTVSSTC
CCCCCCCCCCCCCCC		19.5626657352
595PhosphorylationPHSQSSPTVSSTCTK
CCCCCCCCCCCCCCE		34.6627732954
598PhosphorylationQSSPTVSSTCTKVLY
CCCCCCCCCCCEEEE		24.1430576142
601PhosphorylationPTVSSTCTKVLYFTD
CCCCCCCCEEEEEEC		25.0330576142
610PhosphorylationVLYFTDRSLTPFMVN
EEEEECCCCCCCEEC		39.1330631047
612PhosphorylationYFTDRSLTPFMVNIP
EEECCCCCCCEECCC		18.7428555341
621DimethylationFMVNIPKRLEEVTLK
CEECCCHHHHHCCHH		41.81-
631UbiquitinationEVTLKDFKAAIDREG
HCCHHHHHHHHCCCC		47.2229967540
642PhosphorylationDREGNHRYHFKALDP
CCCCCCCEEEEEECC		12.2117053785
645UbiquitinationGNHRYHFKALDPEFG
CCCCEEEEEECCCCC		34.4329967540
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
381SPhosphorylationKinaseMARK1Q9P0L2
PSP
592SPhosphorylationKinaseMARK1Q9P0L2
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DIXC1_HUMAN !!
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 DIXC1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
ULK2_HUMANULK2physical
21988832
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DIXC1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Tyrosine phosphorylated Par3 regulates epithelial tight junctionassembly promoted by EGFR signaling.";
Wang Y., Du D., Fang L., Yang G., Zhang C., Zeng R., Ullrich A.,Lottspeich F., Chen Z.;
EMBO J. 25:5058-5070(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-642, AND MASSSPECTROMETRY.

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