DIAP3_HUMAN - dbPTM
DIAP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID DIAP3_HUMAN
UniProt AC Q9NSV4
Protein Name Protein diaphanous homolog 3
Gene Name DIAPH3
Organism Homo sapiens (Human).
Sequence Length 1193
Subcellular Localization Cytoplasm, cytosol . During mitosis, co-localizes with the actin-rich cleavage furrow and with the microtubule-rich central spindle during cytokinesis.
Protein Description Binds to GTP-bound form of Rho and to profilin. Acts in a Rho-dependent manner to recruit profilin to the membrane, where it promotes actin polymerization. It is required for cytokinesis, stress fiber formation, and transcriptional activation of the serum response factor. DFR proteins couple Rho and Src tyrosine kinase during signaling and the regulation of actin dynamics (By similarity)..
Protein Sequence MERHQPRLHHPAQGSAAGTPYPSSASLRGCRESKMPRRKGPQHPPPPSGPEEPGEKRPKFHLNIRTLTDDMLDKFASIRIPGSKKERPPLPNLKTAFASSDCSAAPLEMMENFPKPLSENELLELFEKMMEDMNLNEDKKAPLREKDFSIKKEMVMQYINTASKTGSLKRSRQISPQEFIHELKMGSADERLVTCLESLRVSLTSNPVSWVESFGHEGLGLLLDILEKLISGKIQEKVVKKNQHKVIQCLKALMNTQYGLERIMSEERSLSLLAKAVDPRHPNMMTDVVKLLSAVCIVGEESILEEVLEALTSAGEEKKIDRFFCIVEGLRHNSVQLQVACMQLINALVTSPDDLDFRLHIRNEFMRCGLKEILPNLKCIKNDGLDIQLKVFDEHKEEDLFELSHRLEDIRAELDEAYDVYNMVWSTVKETRAEGYFISILQHLLLIRNDYFIRQQYFKLIDECVSQIVLHRDGMDPDFTYRKRLDLDLTQFVDICIDQAKLEEFEEKASELYKKFEKEFTDHQETQAELQKKEAKINELQAELQAFKSQFGALPADCNIPLPPSKEGGTGHSALPPPPPLPSGGGVPPPPPPPPPPPLPGMRMPFSGPVPPPPPLGFLGGQNSPPLPILPFGLKPKKEFKPEISMRRLNWLKIRPHEMTENCFWIKVNENKYENVDLLCKLENTFCCQQKERREEEDIEEKKSIKKKIKELKFLDSKIAQNLSIFLSSFRVPYEEIRMMILEVDETRLAESMIQNLIKHLPDQEQLNSLSQFKSEYSNLCEPEQFVVVMSNVKRLRPRLSAILFKLQFEEQVNNIKPDIMAVSTACEEIKKSKSFSKLLELVLLMGNYMNAGSRNAQTFGFNLSSLCKLKDTKSADQKTTLLHFLVEICEEKYPDILNFVDDLEPLDKASKVSVETLEKNLRQMGRQLQQLEKELETFPPPEDLHDKFVTKMSRFVISAKEQYETLSKLHENMEKLYQSIIGYYAIDVKKVSVEDFLTDLNNFRTTFMQAIKENIKKREAEEKEKRVRIAKELAERERLERQQKKKRLLEMKTEGDETGVMDNLLEALQSGAAFRDRRKRTPMPKDVRQSLSPMSQRPVLKVCNHENQKVQLTEGSRSHYNINCNSTRTPVAKELNYNLDTHTSTGRIKAAEKKEACNVESNRKKETELLGSFSKNESVPEVEALLARLRAL
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
7Methylation-MERHQPRLHHPAQG
-CCCCCCCCCCCCCC		39.83-
15PhosphorylationLHHPAQGSAAGTPYP
CCCCCCCCCCCCCCC		11.6723927012
19PhosphorylationAQGSAAGTPYPSSAS
CCCCCCCCCCCCCHH		18.2123927012
21PhosphorylationGSAAGTPYPSSASLR
CCCCCCCCCCCHHHC		18.6523927012
23PhosphorylationAAGTPYPSSASLRGC
CCCCCCCCCHHHCCC		32.4723401153
24PhosphorylationAGTPYPSSASLRGCR
CCCCCCCCHHHCCCC		19.8523927012
26PhosphorylationTPYPSSASLRGCRES
CCCCCCHHHCCCCCC		22.1323927012
28MethylationYPSSASLRGCRESKM
CCCCHHHCCCCCCCC		39.40-
31MethylationSASLRGCRESKMPRR
CHHHCCCCCCCCCCC		54.79-
48PhosphorylationPQHPPPPSGPEEPGE
CCCCCCCCCCCCCCC		73.1528555341
66 (in isoform 5)Phosphorylation-30.1625056879
66PhosphorylationKFHLNIRTLTDDMLD
CCCEEEEECCHHHHH		30.1628555341
66 (in isoform 4)Phosphorylation-30.1625056879
68PhosphorylationHLNIRTLTDDMLDKF
CEEEEECCHHHHHHH		29.3723917254
77PhosphorylationDMLDKFASIRIPGSK
HHHHHHHCCCCCCCC		18.6125159151
94MethylationRPPLPNLKTAFASSD
CCCCCCCCHHHCCCC		44.43-
118PhosphorylationENFPKPLSENELLEL
HHCCCCCCHHHHHHH		47.0724719451
139UbiquitinationDMNLNEDKKAPLREK
HCCCCCCCCCCCCCC		44.6617370265
149PhosphorylationPLREKDFSIKKEMVM
CCCCCCCCCCHHHHH		43.56-
158PhosphorylationKKEMVMQYINTASKT
CHHHHHHHHHHHHCC		4.3229116813
161PhosphorylationMVMQYINTASKTGSL
HHHHHHHHHHCCCCC		23.8128450419
163PhosphorylationMQYINTASKTGSLKR
HHHHHHHHCCCCCHH		28.8128450419
165PhosphorylationYINTASKTGSLKRSR
HHHHHHCCCCCHHHC		29.5229116813
167PhosphorylationNTASKTGSLKRSRQI
HHHHCCCCCHHHCCC		35.6324719451
171PhosphorylationKTGSLKRSRQISPQE
CCCCCHHHCCCCHHH		27.2723312004
175PhosphorylationLKRSRQISPQEFIHE
CHHHCCCCHHHHHHH		16.5222199227
202PhosphorylationCLESLRVSLTSNPVS
HHHHHCEECCCCCCH		21.35-
361PhosphorylationDLDFRLHIRNEFMRC
HCCHHHHHCHHHHHC		6.3120068231
484PhosphorylationPDFTYRKRLDLDLTQ
CCCCCCCCCCCCHHH		25.1617322306
489PhosphorylationRKRLDLDLTQFVDIC
CCCCCCCHHHHHHHH		5.4320068231
570PhosphorylationPPSKEGGTGHSALPP
CCCCCCCCCCCCCCC		42.4520068231
607PhosphorylationPGMRMPFSGPVPPPP
CCCCCCCCCCCCCCC		36.0027174698
624PhosphorylationGFLGGQNSPPLPILP
CCCCCCCCCCCCCCC		21.7328450419
653MethylationMRRLNWLKIRPHEMT
HHHCCCCCCCCCCCC		28.43-
673PhosphorylationIKVNENKYENVDLLC
EEECCCCCCCCHHEH		25.0728674419
691AcetylationNTFCCQQKERREEED
CCCCCCHHHHHCHHH		27.5826051181
717PhosphorylationKELKFLDSKIAQNLS
HHHHHCCHHHHHHHH		28.27-
728PhosphorylationQNLSIFLSSFRVPYE
HHHHHHHHHCCCCHH		19.38-
729PhosphorylationNLSIFLSSFRVPYEE
HHHHHHHHCCCCHHH		21.15-
740OxidationPYEEIRMMILEVDET
CHHHHHHHHHCCCHH		1.9617322306
747PhosphorylationMILEVDETRLAESMI
HHHCCCHHHHHHHHH		26.9030576142
752PhosphorylationDETRLAESMIQNLIK
CHHHHHHHHHHHHHH		18.6420068231
828PhosphorylationMAVSTACEEIKKSKS
HHHHHHHHHHHCCCC		61.3619651622
830 (in isoform 1)Phosphorylation-2.9625849741
830PhosphorylationVSTACEEIKKSKSFS
HHHHHHHHHCCCCHH		2.9620068231
833PhosphorylationACEEIKKSKSFSKLL
HHHHHHCCCCHHHHH		28.6420068231
835PhosphorylationEEIKKSKSFSKLLEL
HHHHCCCCHHHHHHH		41.6724719451
837PhosphorylationIKKSKSFSKLLELVL
HHCCCCHHHHHHHHH		29.5020068231
849PhosphorylationLVLLMGNYMNAGSRN
HHHHHHHHCCCCCCC		5.9920068231
865PhosphorylationQTFGFNLSSLCKLKD
CCCCCCHHHHHCCCC		23.5121712546
866PhosphorylationTFGFNLSSLCKLKDT
CCCCCHHHHHCCCCC		40.7421712546
959PhosphorylationKMSRFVISAKEQYET
HHHHHHHCHHHHHHH		28.1728509920
968PhosphorylationKEQYETLSKLHENME
HHHHHHHHHHHHHHH		40.3628509920
980PhosphorylationNMEKLYQSIIGYYAI
HHHHHHHHHHHHHHC		11.5620860994
1091PhosphorylationMPKDVRQSLSPMSQR
CCHHHHHHCCCCCCC		21.9130266825
1093 (in isoform 7)Phosphorylation-24.6525849741
1093PhosphorylationKDVRQSLSPMSQRPV
HHHHHHCCCCCCCCC		24.6530266825
1096PhosphorylationRQSLSPMSQRPVLKV
HHHCCCCCCCCCEEE		26.8230266825
1117PhosphorylationKVQLTEGSRSHYNIN
EEEECCCCCCCCCCC		25.1128555341
1121PhosphorylationTEGSRSHYNINCNST
CCCCCCCCCCCCCCC		20.9828674419
1127PhosphorylationHYNINCNSTRTPVAK
CCCCCCCCCCCCHHH		22.8225159151
1128PhosphorylationYNINCNSTRTPVAKE
CCCCCCCCCCCHHHH		25.2725627689
1130PhosphorylationINCNSTRTPVAKELN
CCCCCCCCCHHHHHC		23.3925159151
1138PhosphorylationPVAKELNYNLDTHTS
CHHHHHCCCCCCCCC		29.7225159151
1142PhosphorylationELNYNLDTHTSTGRI
HHCCCCCCCCCCCCC		30.1621712546
1144PhosphorylationNYNLDTHTSTGRIKA
CCCCCCCCCCCCCCH		30.0325159151
1145PhosphorylationYNLDTHTSTGRIKAA
CCCCCCCCCCCCCHH		22.6625159151
1145O-linked_GlycosylationYNLDTHTSTGRIKAA
CCCCCCCCCCCCCHH		22.6630059200
1146PhosphorylationNLDTHTSTGRIKAAE
CCCCCCCCCCCCHHH		31.4728674419
1162PhosphorylationKEACNVESNRKKETE
HHHCCCCCCCCHHHH		37.3427732954
1173PhosphorylationKETELLGSFSKNESV
HHHHHHHHCCCCCCC		26.7320873877
1175PhosphorylationTELLGSFSKNESVPE
HHHHHHCCCCCCCHH		35.9520873877
1179PhosphorylationGSFSKNESVPEVEAL
HHCCCCCCCHHHHHH		52.9820873877
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
19TPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of DIAP3_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 DIAP3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SPN90_HUMANNCKIPSDphysical
11509578
CDC42_HUMANCDC42physical
15085137
RHOA_HUMANRHOAphysical
15085137
RAC1_HUMANRAC1physical
15085137
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609129Auditory neuropathy, autosomal dominant, 1 (AUNA1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of DIAP3_HUMAN

loading...

Related Literatures of Post-Translational Modification
Ubiquitylation
ReferencePubMed
"Tryptic digestion of ubiquitin standards reveals an improved strategyfor identifying ubiquitinated proteins by mass spectrometry.";
Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
Proteomics 7:868-874(2007).
Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-139, AND MASSSPECTROMETRY.

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory