DIEXF_HUMAN - dbPTM
DIEXF_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DIEXF_HUMAN
UniProt AC Q68CQ4
Protein Name Digestive organ expansion factor homolog
Gene Name DIEXF
Organism Homo sapiens (Human).
Sequence Length 756
Subcellular Localization Nucleus. Nucleus, nucleolus .
Protein Description Regulates the p53 pathway to control the expansion growth of digestive organs..
Protein Sequence MGKRGSRSQSQLLNTLTKKQKKHLRDFGEEHPFYDRVSRKEAKPQICQLSESSDSSDSESDSESEPQQVSGYHRLLATLKNVSEEEEEDEEEEEEEDSIVDDAEMNDEDGGSDVSVEEEMAAESTESPENVALSADPEGKEDGEEPPGTSQTSPEEFTDAKHESLFSLETNFLEEESGDNSSLKASQDPFLQHVNKELKEKAIQAVATNPKTTHELKWPILGQLFFSSKFQKLETFKPPKDIDLKSLHLQKPLESTWTKTNSQFLSGPQKSSSPFTPLQKELFLIMNSYRDLFYPERTALKNGEEIRHVYCLHVINHILKANAQVLGNNSRRRSQKFGVGDDDDFRDQGLTRPKVLIVVPFREAALRVVQLFISLLEGDSKKKIIVSNKKRFQGEYGSDPEERPPNLKRPEDYEAVFVGNIDDHFRIGVAILQRSIRLYAPFYSSDILIASPLGLRTIIGGEGEKKRDFDFLSSIELLIIDQADIYLMQNWEHVLHLMNHMNLLPLDSHGVDFSRVRMWSLNNWSKYYRQTLLFGALQDAQINSVFNKYCVNMQGQVAVRNVPMTGSISHVLVQLPHVFQRMEAENLASVIDARFNFFVNKILPQYRDAVMSHTLIYIPSYFDFVRLRNYFKKEELNFTHICEYTQKSGVSRARHFFLQGEKQFLLFTERFHFYKRYTIKGIRNLIFYELPTYPHFYSEICNMLRATNRGEEATWTCTVLYSKYDAQRLAAVVGVERAAQMLQSNKNVHLFITGEK
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
8PhosphorylationMGKRGSRSQSQLLNT
CCCCCCHHHHHHHHH		35.5625159151
10PhosphorylationKRGSRSQSQLLNTLT
CCCCHHHHHHHHHHC		24.8425159151
15PhosphorylationSQSQLLNTLTKKQKK
HHHHHHHHHCHHHHH		35.4625159151
17PhosphorylationSQLLNTLTKKQKKHL
HHHHHHHCHHHHHHH		33.8729396449
18AcetylationQLLNTLTKKQKKHLR
HHHHHHCHHHHHHHH		57.2125953088
25MethylationKKQKKHLRDFGEEHP
HHHHHHHHHHCCCCC		36.61-
34PhosphorylationFGEEHPFYDRVSRKE
HCCCCCCHHHCCHHH		13.8028796482
36MethylationEEHPFYDRVSRKEAK
CCCCCHHHCCHHHCC		19.55-
38PhosphorylationHPFYDRVSRKEAKPQ
CCCHHHCCHHHCCCC		38.2323186163
149PhosphorylationDGEEPPGTSQTSPEE
CCCCCCCCCCCCHHH		24.3620873877
150PhosphorylationGEEPPGTSQTSPEEF
CCCCCCCCCCCHHHH		37.0626657352
152PhosphorylationEPPGTSQTSPEEFTD
CCCCCCCCCHHHHCC		46.1225262027
153PhosphorylationPPGTSQTSPEEFTDA
CCCCCCCCHHHHCCC		23.7625159151
158PhosphorylationQTSPEEFTDAKHESL
CCCHHHHCCCCHHHH		38.0226074081
180UbiquitinationLEEESGDNSSLKASQ
CCCCCCCCCCCCHHC		36.7024816145
186PhosphorylationDNSSLKASQDPFLQH
CCCCCCHHCCHHHHH		33.2625849741
201UbiquitinationVNKELKEKAIQAVAT
HCHHHHHHHHHHHHC		49.5633845483
227PhosphorylationILGQLFFSSKFQKLE
HHHHHHHCCCCCCCC		25.8624719451
228PhosphorylationLGQLFFSSKFQKLET
HHHHHHCCCCCCCCC		32.1226074081
237UbiquitinationFQKLETFKPPKDIDL
CCCCCCCCCCCCCCH		68.7629967540
246PhosphorylationPKDIDLKSLHLQKPL
CCCCCHHHCCCCCCC		28.4620873877
251UbiquitinationLKSLHLQKPLESTWT
HHHCCCCCCCHHCCC		58.9129967540
251AcetylationLKSLHLQKPLESTWT
HHHCCCCCCCHHCCC		58.9126051181
259UbiquitinationPLESTWTKTNSQFLS
CCHHCCCCCCCCCCC		36.9529967540
260PhosphorylationLESTWTKTNSQFLSG
CHHCCCCCCCCCCCC		32.5021406692
262PhosphorylationSTWTKTNSQFLSGPQ
HCCCCCCCCCCCCCC		27.7821406692
266PhosphorylationKTNSQFLSGPQKSSS
CCCCCCCCCCCCCCC		50.1121406692
270UbiquitinationQFLSGPQKSSSPFTP
CCCCCCCCCCCCCCH		56.2822817900
273PhosphorylationSGPQKSSSPFTPLQK
CCCCCCCCCCCHHHH		30.9925159151
276PhosphorylationQKSSSPFTPLQKELF
CCCCCCCCHHHHHHH		26.86-
288PhosphorylationELFLIMNSYRDLFYP
HHHHHHHHHHHHHCC		12.2629759185
289PhosphorylationLFLIMNSYRDLFYPE
HHHHHHHHHHHHCCH		11.8029759185
334PhosphorylationGNNSRRRSQKFGVGD
CCCCCCCHHCCCCCC		35.5929214152
336UbiquitinationNSRRRSQKFGVGDDD
CCCCCHHCCCCCCCC		45.3829967540
336AcetylationNSRRRSQKFGVGDDD
CCCCCHHCCCCCCCC		45.3826051181
398PhosphorylationRFQGEYGSDPEERPP
CCCCCCCCCCCCCCC		49.4420873877
413PhosphorylationNLKRPEDYEAVFVGN
CCCCCCCCEEEEECC		12.2527642862
451PhosphorylationSSDILIASPLGLRTI
CCCEEEECCCCCCEE		17.42-
465UbiquitinationIIGGEGEKKRDFDFL
ECCCCCCCCCCCCCH		65.0624816145
520PhosphorylationFSRVRMWSLNNWSKY
HHHEEEHHCCCHHHH		16.3327794612
525PhosphorylationMWSLNNWSKYYRQTL
EHHCCCHHHHHHHHH		16.9527794612
526AcetylationWSLNNWSKYYRQTLL
HHCCCHHHHHHHHHH		37.6126051181
569PhosphorylationVPMTGSISHVLVQLP
CCCCCCEEEHHHHCH		14.8322210691
621PhosphorylationTLIYIPSYFDFVRLR
EEEECCCCHHHHHHH		11.2118083107
630PhosphorylationDFVRLRNYFKKEELN
HHHHHHHHCCHHHCC		15.4418083107
688PhosphorylationGIRNLIFYELPTYPH
CHHHHEEEECCCCHH		15.01-
746AcetylationAQMLQSNKNVHLFIT
HHHHHHCCCEEEEEE		66.6426051181
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 DIEXF_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DIEXF_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 DIEXF_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
RUFY1_HUMANRUFY1physical
25416956
CEP70_HUMANCEP70physical
25416956
MIPO1_HUMANMIPOL1physical
25416956
MY18A_HUMANMYO18Aphysical
26344197
DIEXF_HUMANDIEXFphysical
26472760
AP2A1_HUMANAP2A1physical
26472760
PSME3_HUMANPSME3physical
26472760
AP2B1_HUMANAP2B1physical
26472760
MPP10_HUMANMPHOSPH10physical
26472760
AP2A2_HUMANAP2A2physical
26472760
AP2S1_HUMANAP2S1physical
26472760
IMP3_HUMANIMP3physical
26472760
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 DIEXF_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-153, AND MASSSPECTROMETRY.

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