EHD4_HUMAN - dbPTM
EHD4_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHD4_HUMAN
UniProt AC Q9H223
Protein Name EH domain-containing protein 4 {ECO:0000305}
Gene Name EHD4 {ECO:0000312|HGNC:HGNC:3245}
Organism Homo sapiens (Human).
Sequence Length 541
Subcellular Localization Early endosome membrane
Peripheral membrane protein
Cytoplasmic side . Recycling endosome membrane
Peripheral membrane protein
Cytoplasmic side . Cell membrane
Peripheral membrane protein
Cytoplasmic side .
Protein Description ATP- and membrane-binding protein that probably controls membrane reorganization/tubulation upon ATP hydrolysis. Plays a role in early endosomal transport..
Protein Sequence MFSWMGRQAGGRERAGGADAVQTVTGGLRSLYLRKVLPLEEAYRFHEFHSPALEDADFENKPMILLVGQYSTGKTTFIRYLLEQDFPGMRIGPEPTTDSFIAVMYGETEGSTPGNALVVDPKKPFRKLSRFGNAFLNRFMCSQLPNQVLKSISVIDSPGILSGEKQRISRGYDFCQVLQWFAERVDRIILLFDAHKLDISDEFSEAIKAFRGQDDKIRVVLNKADQVDTQQLMRVYGALMWSLGKVINTPEVLRVYIGSFWAQPLQNTDNRRLFEAEAQDLFRDIQSLPQKAAVRKLNDLIKRARLAKVHAYIISYLKKEMPSVFGKENKKRELISRLPEIYIQLQREYQISAGDFPEVKAMQEQLENYDFTKFHSLKPKLIEAVDNMLSNKISPLMNLISQEETSTPTQLVQGGAFDGTTEGPFNQGYGEGAKEGADEEEWVVAKDKPVYDELFYTLSPINGKISGVNAKKEMVTSKLPNSVLGKIWKLADCDCDGMLDEEEFALAKHLIKIKLDGYELPSSLPPHLVPPSHRKSLPKAD
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
1Acetylation-------MFSWMGRQ
-------CCCCCCCC		5.61-
25PhosphorylationADAVQTVTGGLRSLY
CCHHHHHHCHHHHHH		28.9928857561
35MalonylationLRSLYLRKVLPLEEA
HHHHHHHCCCCHHHH		45.5926320211
35UbiquitinationLRSLYLRKVLPLEEA
HHHHHHHCCCCHHHH		45.5921890473
70PhosphorylationMILLVGQYSTGKTTF
EEEEEEECCCCHHHH		11.4124719451
72PhosphorylationLLVGQYSTGKTTFIR
EEEEECCCCHHHHHH		37.4524719451
129PhosphorylationKKPFRKLSRFGNAFL
CCCCHHHHHHHHHHH		28.7127067055
140SulfoxidationNAFLNRFMCSQLPNQ
HHHHHHHHHHCCCHH		1.6228465586
157PhosphorylationKSISVIDSPGILSGE
HHCEEECCCCCCCCC		17.5725159151
162PhosphorylationIDSPGILSGEKQRIS
ECCCCCCCCCHHHHH		42.8827050516
165UbiquitinationPGILSGEKQRISRGY
CCCCCCCHHHHHCCC		48.6921890473
208UbiquitinationDEFSEAIKAFRGQDD
HHHHHHHHHHCCCCC		48.82-
223UbiquitinationKIRVVLNKADQVDTQ
EEEEEEECHHCCCHH		49.5321890473
233SulfoxidationQVDTQQLMRVYGALM
CCCHHHHHHHHHHHH		2.0621406390
249PhosphorylationSLGKVINTPEVLRVY
HHHHHCCCHHHHHHE		15.09-
291UbiquitinationDIQSLPQKAAVRKLN
HHHHCCHHHHHHHHH		36.0521890473
296UbiquitinationPQKAAVRKLNDLIKR
CHHHHHHHHHHHHHH		45.07-
302UbiquitinationRKLNDLIKRARLAKV
HHHHHHHHHHHHHHH		47.50-
312PhosphorylationRLAKVHAYIISYLKK
HHHHHHHHHHHHHHH		5.5023312004
315PhosphorylationKVHAYIISYLKKEMP
HHHHHHHHHHHHHCC		18.1728442448
316PhosphorylationVHAYIISYLKKEMPS
HHHHHHHHHHHHCCC		16.48-
319UbiquitinationYIISYLKKEMPSVFG
HHHHHHHHHCCCCCC		57.56-
319MethylationYIISYLKKEMPSVFG
HHHHHHHHHCCCCCC		57.5623644510
327MethylationEMPSVFGKENKKREL
HCCCCCCCHHHHHHH		46.80-
327AcetylationEMPSVFGKENKKREL
HCCCCCCCHHHHHHH		46.8025953088
330MethylationSVFGKENKKRELISR
CCCCCHHHHHHHHHC		55.06-
331AcetylationVFGKENKKRELISRL
CCCCHHHHHHHHHCC		63.797666409
336PhosphorylationNKKRELISRLPEIYI
HHHHHHHHCCHHHHH		40.1524719451
342PhosphorylationISRLPEIYIQLQREY
HHCCHHHHHHHHHHH		4.8727642862
349PhosphorylationYIQLQREYQISAGDF
HHHHHHHHCCCCCCC		17.2123898821
352PhosphorylationLQREYQISAGDFPEV
HHHHHCCCCCCCHHH		15.6323898821
369PhosphorylationMQEQLENYDFTKFHS
HHHHHHCCCCHHHHC		11.7627642862
372PhosphorylationQLENYDFTKFHSLKP
HHHCCCCHHHHCCCH		29.8724719451
373UbiquitinationLENYDFTKFHSLKPK
HHCCCCHHHHCCCHH		40.86-
376PhosphorylationYDFTKFHSLKPKLIE
CCCHHHHCCCHHHHH		41.0223403867
378UbiquitinationFTKFHSLKPKLIEAV
CHHHHCCCHHHHHHH		43.02-
378AcetylationFTKFHSLKPKLIEAV
CHHHHCCCHHHHHHH		43.0225953088
394PhosphorylationNMLSNKISPLMNLIS
HHHHCCHHHHHHHHC		17.3729496963
401PhosphorylationSPLMNLISQEETSTP
HHHHHHHCCCCCCCC		34.4028857561
405PhosphorylationNLISQEETSTPTQLV
HHHCCCCCCCCCEEE		36.8328857561
406PhosphorylationLISQEETSTPTQLVQ
HHCCCCCCCCCEEEC		35.3528857561
407PhosphorylationISQEETSTPTQLVQG
HCCCCCCCCCEEECC		37.4626657352
409PhosphorylationQEETSTPTQLVQGGA
CCCCCCCCEEECCCC		34.3227251275
420PhosphorylationQGGAFDGTTEGPFNQ
CCCCCCCCCCCCCCC		24.4228348404
421PhosphorylationGGAFDGTTEGPFNQG
CCCCCCCCCCCCCCC		44.4628348404
451PhosphorylationVAKDKPVYDELFYTL
EECCCCCCEECEEEC		16.5421082442
456PhosphorylationPVYDELFYTLSPING
CCCEECEEECCCCCC		21.2822167270
457PhosphorylationVYDELFYTLSPINGK
CCEECEEECCCCCCE		17.2722167270
459PhosphorylationDELFYTLSPINGKIS
EECEEECCCCCCEEC		18.8822167270
466PhosphorylationSPINGKISGVNAKKE
CCCCCEECCCCCCHH		39.9326074081
478UbiquitinationKKEMVTSKLPNSVLG
CHHHHHCCCCCCHHH		59.61-
482PhosphorylationVTSKLPNSVLGKIWK
HHCCCCCCHHHHHHH		19.4425159151
486AcetylationLPNSVLGKIWKLADC
CCCCHHHHHHHHHCC		41.0325953088
508UbiquitinationEEEFALAKHLIKIKL
HHHHHHHHHHHEEEE		39.53-
518PhosphorylationIKIKLDGYELPSSLP
HEEEECCCCCCCCCC		17.6028796482
532PhosphorylationPPHLVPPSHRKSLPK
CCCCCCHHHHCCCCC		29.83-
536PhosphorylationVPPSHRKSLPKAD--
CCHHHHCCCCCCC--		50.2729496963
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 EHD4_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EHD4_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 EHD4_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RGRF1_HUMANRASGRF1physical
21988832
PUR8_HUMANADSLphysical
22863883
SZRD1_HUMANSZRD1physical
22863883
PYRG2_HUMANCTPS2physical
22863883
LRSM1_HUMANLRSAM1physical
22863883
MTMR2_HUMANMTMR2physical
22863883
5NTC_HUMANNT5C2physical
22863883
SAE2_HUMANUBA2physical
22863883
OST48_HUMANDDOSTphysical
26344197
QCR2_HUMANUQCRC2physical
26344197
SYWC_HUMANWARSphysical
26344197
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 EHD4_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-327, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-459 AND SER-482, ANDMASS SPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-451 AND TYR-456, ANDMASS SPECTROMETRY.

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