EHD1_HUMAN - dbPTM
EHD1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHD1_HUMAN
UniProt AC Q9H4M9
Protein Name EH domain-containing protein 1 {ECO:0000305}
Gene Name EHD1 {ECO:0000312|HGNC:HGNC:3242}
Organism Homo sapiens (Human).
Sequence Length 534
Subcellular Localization Recycling endosome membrane
Peripheral membrane protein
Cytoplasmic side . Early endosome membrane
Peripheral membrane protein
Cytoplasmic side . Cell membrane
Peripheral membrane protein
Cytoplasmic side . Cell projection, cilium membrane
P
Protein Description ATP- and membrane-binding protein that controls membrane reorganization/tubulation upon ATP hydrolysis. In vitro causes vesiculation of endocytic membranes. [PubMed: 24019528 Acts in early endocytic membrane fusion and membrane trafficking of recycling endosomes]
Protein Sequence MFSWVSKDARRKKEPELFQTVAEGLRQLYAQKLLPLEEHYRFHEFHSPALEDADFDNKPMVLLVGQYSTGKTTFIRHLIEQDFPGMRIGPEPTTDSFIAVMHGPTEGVVPGNALVVDPRRPFRKLNAFGNAFLNRFMCAQLPNPVLDSISIIDTPGILSGEKQRISRGYDFAAVLEWFAERVDRIILLFDAHKLDISDEFSEVIKALKNHEDKIRVVLNKADQIETQQLMRVYGALMWSLGKIINTPEVVRVYIGSFWSHPLLIPDNRKLFEAEEQDLFKDIQSLPRNAALRKLNDLIKRARLAKVHAYIISSLKKEMPNVFGKESKKKELVNNLGEIYQKIEREHQISPGDFPSLRKMQELLQTQDFSKFQALKPKLLDTVDDMLANDIARLMVMVRQEESLMPSQVVKGGAFDGTMNGPFGHGYGEGAGEGIDDVEWVVGKDKPTYDEIFYTLSPVNGKITGANAKKEMVKSKLPNTVLGKIWKLADVDKDGLLDDEEFALANHLIKVKLEGHELPADLPPHLVPPSKRRHE
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-------MFSWVSKD
-------CCCCCCHH		5.6122814378
6Phosphorylation--MFSWVSKDARRKK
--CCCCCCHHHHHHC		20.6824719451
7Ubiquitination-MFSWVSKDARRKKE
-CCCCCCHHHHHHCC		45.87-
27UbiquitinationTVAEGLRQLYAQKLL
HHHHHHHHHHHHHHC		43.82-
29PhosphorylationAEGLRQLYAQKLLPL
HHHHHHHHHHHHCCH		9.9223403867
32UbiquitinationLRQLYAQKLLPLEEH
HHHHHHHHHCCHHHH		43.7621890473
40PhosphorylationLLPLEEHYRFHEFHS
HCCHHHHHCHHCCCC		20.46-
46UbiquitinationHYRFHEFHSPALEDA
HHCHHCCCCCCCCCC		29.86-
54PhosphorylationSPALEDADFDNKPMV
CCCCCCCCCCCCCEE		64.85-
69PhosphorylationLLVGQYSTGKTTFIR
EEEEEECCCCCHHHH		37.45-
124UbiquitinationDPRRPFRKLNAFGNA
CCCCCCHHCHHHHHH		46.61-
138UbiquitinationAFLNRFMCAQLPNPV
HHHHHHHHCCCCCCC		1.69-
150PhosphorylationNPVLDSISIIDTPGI
CCCCCEEEEECCCCC		19.9028348404
154PhosphorylationDSISIIDTPGILSGE
CEEEEECCCCCCCCC		17.0128348404
159PhosphorylationIDTPGILSGEKQRIS
ECCCCCCCCCHHHHC		42.8828348404
162UbiquitinationPGILSGEKQRISRGY
CCCCCCCHHHHCCCC		48.69-
176UbiquitinationYDFAAVLEWFAERVD
CCHHHHHHHHHHHCC		33.67-
208SumoylationSEVIKALKNHEDKIR
HHHHHHHHCCHHHHH		62.20-
219UbiquitinationDKIRVVLNKADQIET
HHHHHEEEHHHHHHH		26.34-
220UbiquitinationKIRVVLNKADQIETQ
HHHHEEEHHHHHHHH		49.5321890473
222SumoylationRVVLNKADQIETQQL
HHEEEHHHHHHHHHH		52.15-
226PhosphorylationNKADQIETQQLMRVY
EHHHHHHHHHHHHHH		24.2020860994
230SulfoxidationQIETQQLMRVYGALM
HHHHHHHHHHHHHHH		2.0621406390
233PhosphorylationTQQLMRVYGALMWSL
HHHHHHHHHHHHHHH		6.0620068231
234UbiquitinationQQLMRVYGALMWSLG
HHHHHHHHHHHHHHH		14.91-
239PhosphorylationVYGALMWSLGKIINT
HHHHHHHHHHHHHCC		17.1820068231
240PhosphorylationYGALMWSLGKIINTP
HHHHHHHHHHHHCCH		4.84-
246PhosphorylationSLGKIINTPEVVRVY
HHHHHHCCHHHEEEE		15.4920068231
260PhosphorylationYIGSFWSHPLLIPDN
EECCCCCCCEECCCC		13.9720068231
280UbiquitinationAEEQDLFKDIQSLPR
HHHHHHHHHHHHCCH		62.3121890473
284PhosphorylationDLFKDIQSLPRNAAL
HHHHHHHHCCHHHHH		40.4530266825
294UbiquitinationRNAALRKLNDLIKRA
HHHHHHHHHHHHHHH		4.95-
298PhosphorylationLRKLNDLIKRARLAK
HHHHHHHHHHHHHHH		2.94-
307UbiquitinationRARLAKVHAYIISSL
HHHHHHHHHHHHHHH		16.47-
312PhosphorylationKVHAYIISSLKKEMP
HHHHHHHHHHHHHCC		21.7624719451
313UbiquitinationVHAYIISSLKKEMPN
HHHHHHHHHHHHCCC		33.52-
315AcetylationAYIISSLKKEMPNVF
HHHHHHHHHHCCCCC		48.9425953088
324AcetylationEMPNVFGKESKKKEL
HCCCCCCCHHHHHHH		47.5623236377
326PhosphorylationPNVFGKESKKKELVN
CCCCCCHHHHHHHHH		53.9428857561
327AcetylationNVFGKESKKKELVNN
CCCCCHHHHHHHHHH		69.8024886937
328UbiquitinationVFGKESKKKELVNNL
CCCCHHHHHHHHHHH		61.84-
329UbiquitinationFGKESKKKELVNNLG
CCCHHHHHHHHHHHH		61.08-
330UbiquitinationGKESKKKELVNNLGE
CCHHHHHHHHHHHHH		67.82-
338UbiquitinationLVNNLGEIYQKIERE
HHHHHHHHHHHHHHH		4.13-
339PhosphorylationVNNLGEIYQKIEREH
HHHHHHHHHHHHHHH		10.23-
341AcetylationNLGEIYQKIEREHQI
HHHHHHHHHHHHHCC		29.5725953088
341UbiquitinationNLGEIYQKIEREHQI
HHHHHHHHHHHHHCC		29.57-
349PhosphorylationIEREHQISPGDFPSL
HHHHHCCCCCCCHHH		19.0923403867
353PhosphorylationHQISPGDFPSLRKMQ
HCCCCCCCHHHHHHH		5.69-
355UbiquitinationISPGDFPSLRKMQEL
CCCCCCHHHHHHHHH		40.58-
355PhosphorylationISPGDFPSLRKMQEL
CCCCCCHHHHHHHHH		40.5829255136
363PhosphorylationLRKMQELLQTQDFSK
HHHHHHHHHCCCHHH		5.22-
369PhosphorylationLLQTQDFSKFQALKP
HHHCCCHHHHHHHCH		40.63-
372UbiquitinationTQDFSKFQALKPKLL
CCCHHHHHHHCHHHH		49.90-
375AcetylationFSKFQALKPKLLDTV
HHHHHHHCHHHHHCH		43.0225953088
375MalonylationFSKFQALKPKLLDTV
HHHHHHHCHHHHHCH		43.0226320211
384UbiquitinationKLLDTVDDMLANDIA
HHHHCHHHHHHHHHH		29.65-
385SulfoxidationLLDTVDDMLANDIAR
HHHCHHHHHHHHHHH		3.0930846556
389UbiquitinationVDDMLANDIARLMVM
HHHHHHHHHHHHHHH		30.25-
404SulfoxidationVRQEESLMPSQVVKG
HHCCCCCCCHHEECC		4.1221406390
417PhosphorylationKGGAFDGTMNGPFGH
CCCCCCCCCCCCCCC		14.8727307780
426PhosphorylationNGPFGHGYGEGAGEG
CCCCCCCCCCCCCCC		13.3127307780
447PhosphorylationVVGKDKPTYDEIFYT
EECCCCCCCCEEEEE		49.7121945579
448PhosphorylationVGKDKPTYDEIFYTL
ECCCCCCCCEEEEEC		21.8021945579
453PhosphorylationPTYDEIFYTLSPVNG
CCCCEEEEECCCCCC		16.6621945579
454PhosphorylationTYDEIFYTLSPVNGK
CCCEEEEECCCCCCE		15.2621945579
456PhosphorylationDEIFYTLSPVNGKIT
CEEEEECCCCCCEEC		20.9925159151
463PhosphorylationSPVNGKITGANAKKE
CCCCCEECCCHHHHH		33.4526074081
467PhosphorylationGKITGANAKKEMVKS
CEECCCHHHHHHHHC		24.6215592455
468PhosphorylationKITGANAKKEMVKSK
EECCCHHHHHHHHCC		49.4218691976
470PhosphorylationTGANAKKEMVKSKLP
CCCHHHHHHHHCCCC		48.8018691976
474PhosphorylationAKKEMVKSKLPNTVL
HHHHHHHCCCCCCHH		28.1928060719
475UbiquitinationKKEMVKSKLPNTVLG
HHHHHHCCCCCCHHH		63.35-
479PhosphorylationVKSKLPNTVLGKIWK
HHCCCCCCHHHHHHH		18.3721815630
483AcetylationLPNTVLGKIWKLADV
CCCCHHHHHHHHHCC		41.0325953088
483MalonylationLPNTVLGKIWKLADV
CCCCHHHHHHHHHCC		41.0326320211
486AcetylationTVLGKIWKLADVDKD
CHHHHHHHHHCCCCC		36.9526051181
489UbiquitinationGKIWKLADVDKDGLL
HHHHHHHCCCCCCCC		60.63-
493PhosphorylationKLADVDKDGLLDDEE
HHHCCCCCCCCCHHH		48.81-
506UbiquitinationEEFALANHLIKVKLE
HHHHHHHCEEEEEEC		24.27-
523UbiquitinationELPADLPPHLVPPSK
CCCCCCCCCCCCCCC		40.52-
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 EHD1_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EHD1_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 EHD1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
AP2A1_HUMANAP2A1physical
11423532
CLH1_HUMANCLTCphysical
11423532
IGF1R_HUMANIGF1Rphysical
11423532
SNP29_HUMANSNAP29physical
11423532
EHD1_HUMANEHD1physical
12121420
EHD3_MOUSEEhd3physical
12121420
EHD3_HUMANEHD3physical
12121420
EPN1_HUMANEPN1physical
21115825
EPN3_HUMANEPN3physical
21115825
ANFY1_HUMANANKFY1physical
22284051
MICA1_HUMANMICAL1physical
20106972
RBNS5_HUMANRBSNphysical
15020713
EHD4_HUMANEHD4physical
22939629
RBNS5_HUMANRBSNphysical
20329706
RFIP2_HUMANRAB11FIP2physical
20329706
API5_HUMANAPI5physical
22863883
ARI2_HUMANARIH2physical
22863883
ATE1_HUMANATE1physical
22863883
PYRG2_HUMANCTPS2physical
22863883
EHD4_HUMANEHD4physical
22863883
TF3C4_HUMANGTF3C4physical
22863883
KTN1_HUMANKTN1physical
22863883
LIMD1_HUMANLIMD1physical
22863883
NOL3_HUMANNOL3physical
22863883
NUBP1_HUMANNUBP1physical
22863883
PDE12_HUMANPDE12physical
22863883
PGTB1_HUMANPGGT1Bphysical
22863883
PRKDC_HUMANPRKDCphysical
22863883
STK39_HUMANSTK39physical
22863883
UBA6_HUMANUBA6physical
22863883
SYWC_HUMANWARSphysical
22863883
XPP1_HUMANXPNPEP1physical
22863883
RFIP2_HUMANRAB11FIP2physical
16251358
RBNS5_HUMANRBSNphysical
16251358
EHD1_HUMANEHD1physical
16251358
EHD3_HUMANEHD3physical
16251358
NNRE_HUMANAPOA1BPphysical
26344197
CLH1_HUMANCLTCphysical
26344197
FADD_HUMANFADDphysical
26344197
FA98B_HUMANFAM98Bphysical
26344197
OPA1_HUMANOPA1physical
26344197
PRKRA_HUMANPRKRAphysical
26344197
STXB1_HUMANSTXBP1physical
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 EHD1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, 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-456, AND MASSSPECTROMETRY.
"Kinase-selective enrichment enables quantitative phosphoproteomics ofthe kinome across the cell cycle.";
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,Greff Z., Keri G., Stemmann O., Mann M.;
Mol. Cell 31:438-448(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-456, AND MASSSPECTROMETRY.
"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-456, AND MASSSPECTROMETRY.

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