EHD2_HUMAN - dbPTM
EHD2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHD2_HUMAN
UniProt AC Q9NZN4
Protein Name EH domain-containing protein 2 {ECO:0000305}
Gene Name EHD2 {ECO:0000312|HGNC:HGNC:3243}
Organism Homo sapiens (Human).
Sequence Length 543
Subcellular Localization Cell membrane
Peripheral membrane protein
Cytoplasmic side . Membrane, caveola
Peripheral membrane protein
Cytoplasmic side . Endosome membrane
Peripheral membrane protein
Cytoplasmic side . Cytoplasm, cytosol . Colocalizes with GLUT4 in
Protein Description ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis (By similarity). Plays a role in membrane trafficking between the plasma membrane and endosomes. [PubMed: 17233914 Important for the internalization of GLUT4. Required for fusion of myoblasts to skeletal muscle myotubes. Required for normal translocation of FER1L5 to the plasma membrane (By similarity Regulates the equilibrium between cell surface-associated and cell surface-dissociated caveolae by constraining caveolae at the cell membrane]
Protein Sequence MFSWLKRGGARGQQPEAIRTVTSALKELYRTKLLPLEEHYRFGAFHSPALEDADFDGKPMVLVAGQYSTGKTSFIQYLLEQEVPGSRVGPEPTTDCFVAVMHGDTEGTVPGNALVVDPDKPFRKLNPFGNTFLNRFMCAQLPNQVLESISIIDTPGILSGAKQRVSRGYDFPAVLRWFAERVDLIILLFDAHKLEISDEFSEAIGALRGHEDKIRVVLNKADMVETQQLMRVYGALMWALGKVVGTPEVLRVYIGSFWSQPLLVPDNRRLFELEEQDLFRDIQGLPRHAALRKLNDLVKRARLVRVHAYIISYLKKEMPSVFGKENKKKQLILKLPVIFAKIQLEHHISPGDFPDCQKMQELLMAHDFTKFHSLKPKLLEALDEMLTHDIAKLMPLLRQEELESTEVGVQGGAFEGTHMGPFVERGPDEAMEDGEEGSDDEAEWVVTKDKSKYDEIFYNLAPADGKLSGSKAKTWMVGTKLPNSVLGRIWKLSDVDRDGMLDDEEFALASHLIEAKLEGHGLPANLPRRLVPPSKRRHKGSAE
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
3Phosphorylation-----MFSWLKRGGA
-----CCCCCCCCCC		30.1528857561
6Methylation--MFSWLKRGGARGQ
--CCCCCCCCCCCCC		42.62-
20PhosphorylationQQPEAIRTVTSALKE
CCHHHHHHHHHHHHH		23.2526437602
22PhosphorylationPEAIRTVTSALKELY
HHHHHHHHHHHHHHH		13.99-
23PhosphorylationEAIRTVTSALKELYR
HHHHHHHHHHHHHHH		27.5426437602
26AcetylationRTVTSALKELYRTKL
HHHHHHHHHHHHCCC		45.4427452117
26UbiquitinationRTVTSALKELYRTKL
HHHHHHHHHHHHCCC		45.44-
32UbiquitinationLKELYRTKLLPLEEH
HHHHHHCCCCCHHHH		38.74-
322-HydroxyisobutyrylationLKELYRTKLLPLEEH
HHHHHHCCCCCHHHH		38.74-
40PhosphorylationLLPLEEHYRFGAFHS
CCCHHHHHCCCCCCC		15.77-
60SulfoxidationADFDGKPMVLVAGQY
CCCCCCEEEEEEEEE		4.0830846556
93PhosphorylationSRVGPEPTTDCFVAV
CCCCCCCCCCCEEEE		33.3429978859
94PhosphorylationRVGPEPTTDCFVAVM
CCCCCCCCCCEEEEE		41.3029978859
105PhosphorylationVAVMHGDTEGTVPGN
EEEEECCCCCCCCCC		40.6929978859
108PhosphorylationMHGDTEGTVPGNALV
EECCCCCCCCCCEEE		19.8029978859
124MalonylationDPDKPFRKLNPFGNT
CCCCCCHHCCCCCCH		53.6632601280
124UbiquitinationDPDKPFRKLNPFGNT
CCCCCCHHCCCCCCH		53.66-
131PhosphorylationKLNPFGNTFLNRFMC
HCCCCCCHHHHHHHH		29.8528857561
180MethylationAVLRWFAERVDLIIL
HHHHHHHHHCCEEEE		43.70-
188MethylationRVDLIILLFDAHKLE
HCCEEEEEECHHHCC		2.29-
191MethylationLIILLFDAHKLEISD
EEEEEECHHHCCCCH		8.38-
2132-HydroxyisobutyrylationALRGHEDKIRVVLNK
HHCCCHHHHEEEEEH		29.45-
256PhosphorylationVLRVYIGSFWSQPLL
HHHHEECCCCCCCEE		17.6227251275
259PhosphorylationVYIGSFWSQPLLVPD
HEECCCCCCCEECCC		21.6527251275
309PhosphorylationRLVRVHAYIISYLKK
HHHHHHHHHHHHHHH		5.5023312004
312PhosphorylationRVHAYIISYLKKEMP
HHHHHHHHHHHHHCC		18.1728442448
313PhosphorylationVHAYIISYLKKEMPS
HHHHHHHHHHHHCCC		16.48-
316UbiquitinationYIISYLKKEMPSVFG
HHHHHHHHHCCCCCC		57.56-
316MethylationYIISYLKKEMPSVFG
HHHHHHHHHCCCCCC		57.56-
324MalonylationEMPSVFGKENKKKQL
HCCCCCCCCCCCCEE		46.8032601280
324MethylationEMPSVFGKENKKKQL
HCCCCCCCCCCCCEE		46.8023644510
324AcetylationEMPSVFGKENKKKQL
HCCCCCCCCCCCCEE		46.8019608861
327MethylationSVFGKENKKKQLILK
CCCCCCCCCCEEEEH		63.5423644510
328AcetylationVFGKENKKKQLILKL
CCCCCCCCCEEEEHH		58.287666465
358UbiquitinationGDFPDCQKMQELLMA
CCCCCHHHHHHHHHH		49.21-
373PhosphorylationHDFTKFHSLKPKLLE
CCHHHHHCCCHHHHH		41.0223403867
375UbiquitinationFTKFHSLKPKLLEAL
HHHHHCCCHHHHHHH		43.02-
385SulfoxidationLLEALDEMLTHDIAK
HHHHHHHHHHHHHHH		5.3730846556
419SulfoxidationGAFEGTHMGPFVERG
CCCCCCCCCCCCCCC		7.9730846556
438PhosphorylationMEDGEEGSDDEAEWV
CCCCCCCCCCCCEEE		45.2122167270
447PhosphorylationDEAEWVVTKDKSKYD
CCCEEEEECCHHHCC		24.7323403867
451PhosphorylationWVVTKDKSKYDEIFY
EEEECCHHHCCCHHH		46.7324702127
452UbiquitinationVVTKDKSKYDEIFYN
EEECCHHHCCCHHHC		63.56-
453PhosphorylationVTKDKSKYDEIFYNL
EECCHHHCCCHHHCC		26.3721945579
458PhosphorylationSKYDEIFYNLAPADG
HHCCCHHHCCCCCCC		18.2221945579
468PhosphorylationAPADGKLSGSKAKTW
CCCCCCCCCCCCCCE		44.5022167270
470PhosphorylationADGKLSGSKAKTWMV
CCCCCCCCCCCCEEC		26.5122167270
473UbiquitinationKLSGSKAKTWMVGTK
CCCCCCCCCEECCCC		46.59-
474PhosphorylationLSGSKAKTWMVGTKL
CCCCCCCCEECCCCC		24.5328857561
484PhosphorylationVGTKLPNSVLGRIWK
CCCCCCCCHHHHHHH		19.4425106551
493PhosphorylationLGRIWKLSDVDRDGM
HHHHHHHHCCCCCCC		31.6828857561
500SulfoxidationSDVDRDGMLDDEEFA
HCCCCCCCCCHHHHH		4.3130846556
516UbiquitinationASHLIEAKLEGHGLP
HHHHHHHHHCCCCCC		33.99-
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 EHD2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EHD2_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 EHD2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GTR4_HUMANSLC2A4physical
15182197
EPN1_HUMANEPN1physical
21115825
EPN3_HUMANEPN3physical
21115825
RBNS5_HUMANRBSNphysical
15020713
PICK1_HUMANPICK1physical
21988832
TAGL2_HUMANTAGLN2physical
21988832
TBC23_HUMANTBC1D23physical
21988832
SPA24_HUMANSPATA24physical
21988832
TCPG_HUMANCCT3physical
26344197
TCPD_HUMANCCT4physical
26344197
TCPZ_HUMANCCT6Aphysical
26344197
TCPH_HUMANCCT7physical
26344197
TCPQ_HUMANCCT8physical
26344197
CLH1_HUMANCLTCphysical
26344197
2AAA_HUMANPPP2R1Aphysical
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 EHD2_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Large-scale phosphoproteome analysis of human liver tissue byenrichment and fractionation of phosphopeptides with strong anionexchange chromatography.";
Han G., Ye M., Zhou H., Jiang X., Feng S., Jiang X., Tian R., Wan D.,Zou H., Gu J.;
Proteomics 8:1346-1361(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
"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-438 AND SER-468, ANDMASS SPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-438, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-458, AND MASSSPECTROMETRY.

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