EHBP1_HUMAN - dbPTM
EHBP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID EHBP1_HUMAN
UniProt AC Q8NDI1
Protein Name EH domain-binding protein 1
Gene Name EHBP1
Organism Homo sapiens (Human).
Sequence Length 1231
Subcellular Localization Cytoplasm . Membrane . Endosome . Mostly found in cytosol and plasma membrane.
Protein Description May play a role in actin reorganization. Links clathrin-mediated endocytosis to the actin cytoskeleton. May act as Rab effector protein and play a role in vesicle trafficking. [PubMed: 14676205]
Protein Sequence MASVWKRLQRVGKHASKFQFVASYQELMVECTKKWQPDKLVVVWTRRSRRKSSKAHSWQPGIKNPYRGVVVWPVPENIEITVTLFKDPHAEEFEDKEWTFVIENESPSGRRKALATSSINMKQYASPMPTQTDVKLKFKPLSKKVVSAALQFSLSCIFLREGKATDEDMQSLASLMSMKQADIGNLDDFEEDNEDDDENRVNQEEKAAKITEIVNQLNALSSLDEDQDDCIKQANMRSAKSASSSEELINKLNFLDEAEKDLATVNSNPFDDPDAAELNPFGDPDSEEPITETASPRKTEDSFYNNSYNPFKEVQTPQYLNPFDEPEAFVTIKDSPPQSTKRKNIRPVDMSKYLYADSSKTEEEELDESNPFYEPKSTPPPNNLVNPVQELETERRVKRKAPAPPVLSPKTGVLNENTVSAGKDLSTSPKPSPIPSPVLGRKPNASQSLLVWCKEVTKNYRGVKITNFTTSWRNGLSFCAILHHFRPDLIDYKSLNPQDIKENNKKAYDGFASIGISRLLEPSDMVLLAIPDKLTVMTYLYQIRAHFSGQELNVVQIEENSSKSTYKVGNYETDTNSSVDQEKFYAELSDLKREPELQQPISGAVDFLSQDDSVFVNDSGVGESESEHQTPDDHLSPSTASPYCRRTKSDTEPQKSQQSSGRTSGSDDPGICSNTDSTQAQVLLGKKRLLKAETLELSDLYVSDKKKDMSPPFICEETDEQKLQTLDIGSNLEKEKLENSRSLECRSDPESPIKKTSLSPTSKLGYSYSRDLDLAKKKHASLRQTESDPDADRTTLNHADHSSKIVQHRLLSRQEELKERARVLLEQARRDAALKAGNKHNTNTATPFCNRQLSDQQDEERRRQLRERARQLIAEARSGVKMSELPSYGEMAAEKLKERSKASGDENDNIEIDTNEEIPEGFVVGGGDELTNLENDLDTPEQNSKLVDLKLKKLLEVQPQVANSPSSAAQKAVTESSEQDMKSGTEDLRTERLQKTTERFRNPVVFSKDSTVRKTQLQSFSQYIENRPEMKRQRSIQEDTKKGNEEKAAITETQRKPSEDEVLNKGFKDTSQYVVGELAALENEQKQIDTRAALVEKRLRYLMDTGRNTEEEEAMMQEWFMLVNKKNALIRRMNQLSLLEKEHDLERRYELLNRELRAMLAIEDWQKTEAQKRREQLLLDELVALVNKRDALVRDLDAQEKQAEEEDEHLERTLEQNKGKMAKKEEKCVLQ
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
33AcetylationELMVECTKKWQPDKL
HHHHHHHHHCCCCCE
64.7719667021
34AcetylationLMVECTKKWQPDKLV
HHHHHHHHCCCCCEE
32.6719667031
106PhosphorylationTFVIENESPSGRRKA
EEEEECCCCCCCCCE
35.6328348404
124PhosphorylationSSINMKQYASPMPTQ
CCCCHHHHCCCCCCC
11.9722210691
126PhosphorylationINMKQYASPMPTQTD
CCHHHHCCCCCCCCC
19.4622210691
130PhosphorylationQYASPMPTQTDVKLK
HHCCCCCCCCCEEEE
37.5422210691
132PhosphorylationASPMPTQTDVKLKFK
CCCCCCCCCEEEEEC
45.2822210691
163UbiquitinationCIFLREGKATDEDMQ
HHHHCCCCCCHHHHH
43.2821906983
163 (in isoform 1)Ubiquitination-43.2821890473
163 (in isoform 2)Ubiquitination-43.2821890473
163 (in isoform 3)Ubiquitination-43.2821890473
165PhosphorylationFLREGKATDEDMQSL
HHCCCCCCHHHHHHH
43.3323927012
171PhosphorylationATDEDMQSLASLMSM
CCHHHHHHHHHHHHH
21.1829255136
171 (in isoform 2)Phosphorylation-21.1821406692
174PhosphorylationEDMQSLASLMSMKQA
HHHHHHHHHHHHHHH
29.8729255136
174 (in isoform 2)Phosphorylation-29.8721406692
177PhosphorylationQSLASLMSMKQADIG
HHHHHHHHHHHHCCC
28.2829255136
206UbiquitinationNRVNQEEKAAKITEI
CCCCHHHHHHHHHHH
53.55-
222PhosphorylationNQLNALSSLDEDQDD
HHHHHHHCCCCCHHH
40.46-
238PhosphorylationIKQANMRSAKSASSS
HHHHHHHHHCCCCCH
29.3124905233
241PhosphorylationANMRSAKSASSSEEL
HHHHHHCCCCCHHHH
32.8524905233
243PhosphorylationMRSAKSASSSEELIN
HHHHCCCCCHHHHHH
41.3024905233
244PhosphorylationRSAKSASSSEELINK
HHHCCCCCHHHHHHH
41.2924905233
245PhosphorylationSAKSASSSEELINKL
HHCCCCCHHHHHHHH
32.3725307156
264PhosphorylationEAEKDLATVNSNPFD
HHHHHHHCCCCCCCC
27.7626074081
267PhosphorylationKDLATVNSNPFDDPD
HHHHCCCCCCCCCCC
41.3626074081
286PhosphorylationNPFGDPDSEEPITET
CCCCCCCCCCCCCCC
49.6128450419
291PhosphorylationPDSEEPITETASPRK
CCCCCCCCCCCCCCC
37.6928450419
293PhosphorylationSEEPITETASPRKTE
CCCCCCCCCCCCCCC
24.6428450419
295PhosphorylationEPITETASPRKTEDS
CCCCCCCCCCCCCCC
32.4328387310
299PhosphorylationETASPRKTEDSFYNN
CCCCCCCCCCCCCCC
46.4328796482
302PhosphorylationSPRKTEDSFYNNSYN
CCCCCCCCCCCCCCC
24.3325159151
304PhosphorylationRKTEDSFYNNSYNPF
CCCCCCCCCCCCCCC
19.8628796482
307PhosphorylationEDSFYNNSYNPFKEV
CCCCCCCCCCCCCCC
23.7325159151
308PhosphorylationDSFYNNSYNPFKEVQ
CCCCCCCCCCCCCCC
29.0428796482
316PhosphorylationNPFKEVQTPQYLNPF
CCCCCCCCCCCCCCC
19.9630266825
319PhosphorylationKEVQTPQYLNPFDEP
CCCCCCCCCCCCCCC
15.0630266825
331PhosphorylationDEPEAFVTIKDSPPQ
CCCCCEEEECCCCCC
18.8230266825
335PhosphorylationAFVTIKDSPPQSTKR
CEEEECCCCCCCCCC
33.2125159151
339PhosphorylationIKDSPPQSTKRKNIR
ECCCCCCCCCCCCCC
41.4930266825
340PhosphorylationKDSPPQSTKRKNIRP
CCCCCCCCCCCCCCC
29.6230266825
351PhosphorylationNIRPVDMSKYLYADS
CCCCCCHHHHHCCCC
17.4328555341
353PhosphorylationRPVDMSKYLYADSSK
CCCCHHHHHCCCCCC
9.5328796482
355PhosphorylationVDMSKYLYADSSKTE
CCHHHHHCCCCCCCC
12.7926657352
358PhosphorylationSKYLYADSSKTEEEE
HHHHCCCCCCCCCHH
26.0926657352
359PhosphorylationKYLYADSSKTEEEEL
HHHCCCCCCCCCHHH
44.1121815630
361PhosphorylationLYADSSKTEEEELDE
HCCCCCCCCCHHHHC
51.0528348404
369PhosphorylationEEEELDESNPFYEPK
CCHHHHCCCCCCCCC
49.8521815630
373PhosphorylationLDESNPFYEPKSTPP
HHCCCCCCCCCCCCC
32.3626074081
377PhosphorylationNPFYEPKSTPPPNNL
CCCCCCCCCCCCCCC
57.7930266825
378PhosphorylationPFYEPKSTPPPNNLV
CCCCCCCCCCCCCCC
46.0430266825
391 (in isoform 2)Phosphorylation-5.7321406692
392 (in isoform 2)Phosphorylation-48.1221406692
393O-linked_GlycosylationNPVQELETERRVKRK
CHHHHHHHHHHHHHC
47.6330379171
393PhosphorylationNPVQELETERRVKRK
CHHHHHHHHHHHHHC
47.6323927012
397 (in isoform 2)Phosphorylation-9.8421406692
401 (in isoform 2)Phosphorylation-14.9821406692
408PhosphorylationAPAPPVLSPKTGVLN
CCCCCCCCCCCCCCC
25.2829255136
411PhosphorylationPPVLSPKTGVLNENT
CCCCCCCCCCCCCCC
35.5923927012
418PhosphorylationTGVLNENTVSAGKDL
CCCCCCCCCCCCCCC
15.0626434776
420PhosphorylationVLNENTVSAGKDLST
CCCCCCCCCCCCCCC
29.3025159151
426PhosphorylationVSAGKDLSTSPKPSP
CCCCCCCCCCCCCCC
36.6529255136
427PhosphorylationSAGKDLSTSPKPSPI
CCCCCCCCCCCCCCC
57.2429255136
428PhosphorylationAGKDLSTSPKPSPIP
CCCCCCCCCCCCCCC
27.7929255136
432PhosphorylationLSTSPKPSPIPSPVL
CCCCCCCCCCCCCCC
41.4029255136
436PhosphorylationPKPSPIPSPVLGRKP
CCCCCCCCCCCCCCC
28.4929255136
446PhosphorylationLGRKPNASQSLLVWC
CCCCCCCCCHHHHHH
27.2628122231
448PhosphorylationRKPNASQSLLVWCKE
CCCCCCCHHHHHHHH
22.6028122231
508PhosphorylationKENNKKAYDGFASIG
HHHCHHHHHHCHHHC
26.0224719451
571PhosphorylationSTYKVGNYETDTNSS
CEEEECCEECCCCCC
17.8027642862
573PhosphorylationYKVGNYETDTNSSVD
EEECCEECCCCCCCC
37.4527251275
575PhosphorylationVGNYETDTNSSVDQE
ECCEECCCCCCCCHH
44.4129978859
577PhosphorylationNYETDTNSSVDQEKF
CEECCCCCCCCHHHH
33.5529978859
578PhosphorylationYETDTNSSVDQEKFY
EECCCCCCCCHHHHH
31.6125159151
585PhosphorylationSVDQEKFYAELSDLK
CCCHHHHHHHHHHHC
15.3825884760
589PhosphorylationEKFYAELSDLKREPE
HHHHHHHHHHCCCHH
32.1929978859
592UbiquitinationYAELSDLKREPELQQ
HHHHHHHCCCHHHCC
60.76-
636PhosphorylationQTPDDHLSPSTASPY
CCCCCCCCCCCCCHH
17.24-
647PhosphorylationASPYCRRTKSDTEPQ
CCHHHCCCCCCCCCC
18.6226699800
649PhosphorylationPYCRRTKSDTEPQKS
HHHCCCCCCCCCCHH
49.5028985074
651PhosphorylationCRRTKSDTEPQKSQQ
HCCCCCCCCCCHHHH
57.5726699800
656PhosphorylationSDTEPQKSQQSSGRT
CCCCCCHHHHCCCCC
28.3623927012
659PhosphorylationEPQKSQQSSGRTSGS
CCCHHHHCCCCCCCC
27.4223927012
660PhosphorylationPQKSQQSSGRTSGSD
CCHHHHCCCCCCCCC
28.1423927012
663PhosphorylationSQQSSGRTSGSDDPG
HHHCCCCCCCCCCCC
40.7525159151
664PhosphorylationQQSSGRTSGSDDPGI
HHCCCCCCCCCCCCC
34.6323927012
666PhosphorylationSSGRTSGSDDPGICS
CCCCCCCCCCCCCCC
38.3125159151
673PhosphorylationSDDPGICSNTDSTQA
CCCCCCCCCCCCHHH
40.6230108239
675PhosphorylationDPGICSNTDSTQAQV
CCCCCCCCCCHHHHH
18.2930108239
677PhosphorylationGICSNTDSTQAQVLL
CCCCCCCCHHHHHHH
22.0023927012
678PhosphorylationICSNTDSTQAQVLLG
CCCCCCCHHHHHHHC
30.6323927012
694PhosphorylationKRLLKAETLELSDLY
HHHHCCEEEEHHHHC
30.3222617229
698PhosphorylationKAETLELSDLYVSDK
CCEEEEHHHHCCCCC
19.0522199227
701PhosphorylationTLELSDLYVSDKKKD
EEEHHHHCCCCCCCC
11.6929978859
703PhosphorylationELSDLYVSDKKKDMS
EHHHHCCCCCCCCCC
30.1029978859
710PhosphorylationSDKKKDMSPPFICEE
CCCCCCCCCCCCCCC
39.2825159151
718PhosphorylationPPFICEETDEQKLQT
CCCCCCCCCHHHCHH
23.65-
725PhosphorylationTDEQKLQTLDIGSNL
CCHHHCHHCCCCCCH
36.5129255136
728 (in isoform 2)Ubiquitination-7.9821890473
728 (in isoform 3)Ubiquitination-7.9821890473
730PhosphorylationLQTLDIGSNLEKEKL
CHHCCCCCCHHHHHH
38.2825850435
740PhosphorylationEKEKLENSRSLECRS
HHHHHHCCCCCCCCC
17.5523898821
742PhosphorylationEKLENSRSLECRSDP
HHHHCCCCCCCCCCC
28.4823403867
747PhosphorylationSRSLECRSDPESPIK
CCCCCCCCCCCCCCC
70.0025159151
751PhosphorylationECRSDPESPIKKTSL
CCCCCCCCCCCCCCC
37.0029255136
756PhosphorylationPESPIKKTSLSPTSK
CCCCCCCCCCCCCCC
29.8723403867
757PhosphorylationESPIKKTSLSPTSKL
CCCCCCCCCCCCCCC
35.4123403867
759PhosphorylationPIKKTSLSPTSKLGY
CCCCCCCCCCCCCCC
26.3725159151
761PhosphorylationKKTSLSPTSKLGYSY
CCCCCCCCCCCCCCC
34.8127794612
762PhosphorylationKTSLSPTSKLGYSYS
CCCCCCCCCCCCCCC
29.3023403867
763UbiquitinationTSLSPTSKLGYSYSR
CCCCCCCCCCCCCCC
48.7021890473
763 (in isoform 1)Ubiquitination-48.7021890473
766PhosphorylationSPTSKLGYSYSRDLD
CCCCCCCCCCCCCHH
18.1827642862
767PhosphorylationPTSKLGYSYSRDLDL
CCCCCCCCCCCCHHH
18.1625159151
768PhosphorylationTSKLGYSYSRDLDLA
CCCCCCCCCCCHHHH
10.1530576142
769PhosphorylationSKLGYSYSRDLDLAK
CCCCCCCCCCHHHHH
17.2427251275
781PhosphorylationLAKKKHASLRQTESD
HHHHHCHHHHCCCCC
24.6529514088
785PhosphorylationKHASLRQTESDPDAD
HCHHHHCCCCCCCCC
30.9029116813
787PhosphorylationASLRQTESDPDADRT
HHHHCCCCCCCCCCC
58.8125159151
794PhosphorylationSDPDADRTTLNHADH
CCCCCCCCCCCHHHH
35.8629514088
795PhosphorylationDPDADRTTLNHADHS
CCCCCCCCCCHHHHH
26.8529514088
802PhosphorylationTLNHADHSSKIVQHR
CCCHHHHHHHHHHHH
33.6023186163
803PhosphorylationLNHADHSSKIVQHRL
CCHHHHHHHHHHHHH
24.0023186163
812PhosphorylationIVQHRLLSRQEELKE
HHHHHHHHCHHHHHH
36.1924719451
846PhosphorylationKHNTNTATPFCNRQL
CCCCCCCCCCCCCCC
18.1728555341
854PhosphorylationPFCNRQLSDQQDEER
CCCCCCCCCCCHHHH
25.6528258704
883PhosphorylationARSGVKMSELPSYGE
HHHCCCHHHCCCHHH
30.2027251275
887PhosphorylationVKMSELPSYGEMAAE
CCHHHCCCHHHHHHH
59.3928555341
888PhosphorylationKMSELPSYGEMAAEK
CHHHCCCHHHHHHHH
18.3729978859
964PhosphorylationVQPQVANSPSSAAQK
HCCCCCCCCCHHHHH
19.2029255136
966PhosphorylationPQVANSPSSAAQKAV
CCCCCCCCHHHHHHH
32.2229255136
967PhosphorylationQVANSPSSAAQKAVT
CCCCCCCHHHHHHHH
30.8929255136
974PhosphorylationSAAQKAVTESSEQDM
HHHHHHHHHCHHHHH
34.70-
976PhosphorylationAQKAVTESSEQDMKS
HHHHHHHCHHHHHHH
29.79-
977PhosphorylationQKAVTESSEQDMKSG
HHHHHHCHHHHHHHC
32.80-
981SulfoxidationTESSEQDMKSGTEDL
HHCHHHHHHHCCHHH
3.5830846556
1000 (in isoform 2)Phosphorylation-7.8221406692
1005 (in isoform 2)Phosphorylation-4.7721406692
1010PhosphorylationPVVFSKDSTVRKTQL
CEECCCCCCCCHHHH
32.3228857561
1011PhosphorylationVVFSKDSTVRKTQLQ
EECCCCCCCCHHHHH
34.1728857561
1015PhosphorylationKDSTVRKTQLQSFSQ
CCCCCCHHHHHHHHH
24.7729978859
1016 (in isoform 2)Phosphorylation-40.3121406692
1019PhosphorylationVRKTQLQSFSQYIEN
CCHHHHHHHHHHHHC
35.1425159151
1021PhosphorylationKTQLQSFSQYIENRP
HHHHHHHHHHHHCCH
27.5923186163
1023PhosphorylationQLQSFSQYIENRPEM
HHHHHHHHHHCCHHH
14.7029978859
1023 (in isoform 2)Phosphorylation-14.7021406692
1035PhosphorylationPEMKRQRSIQEDTKK
HHHHHHHHHHHHHHH
21.9325159151
1040PhosphorylationQRSIQEDTKKGNEEK
HHHHHHHHHHCHHHH
33.6228176443
1051PhosphorylationNEEKAAITETQRKPS
HHHHHHCHHCCCCCC
28.4023927012
1053PhosphorylationEKAAITETQRKPSED
HHHHCHHCCCCCCHH
25.6423927012
1058PhosphorylationTETQRKPSEDEVLNK
HHCCCCCCHHHHHHC
61.7929255136
1070PhosphorylationLNKGFKDTSQYVVGE
HHCCCCCHHHHHHHH
20.51-
1073PhosphorylationGFKDTSQYVVGELAA
CCCCHHHHHHHHHHH
9.2527642862
1097UbiquitinationTRAALVEKRLRYLMD
HHHHHHHHHHHHHHH
49.61-
1101PhosphorylationLVEKRLRYLMDTGRN
HHHHHHHHHHHCCCC
15.80-
1137PhosphorylationIRRMNQLSLLEKEHD
HHHHHHHHHHHHHCC
22.5724719451
1188UbiquitinationELVALVNKRDALVRD
HHHHHHHHHHHHHHH
44.14-

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 EHBP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of EHBP1_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 EHBP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
EHD2_HUMANEHD2physical
14676205
ACAP2_HUMANACAP2physical
27173435

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
611868Prostate cancer, hereditary, 12 (HPC12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of EHBP1_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-171; SER-174; SER-432;SER-436 AND SER-1058, AND MASS SPECTROMETRY.
"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-426; THR-427; SER-428;SER-432; SER-436 AND SER-964, AND MASS SPECTROMETRY.
"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-171; SER-174; SER-177;SER-428; SER-432; SER-436; SER-710; SER-964 AND SER-1058, 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 SER-426; SER-428 ANDSER-436, AND MASS SPECTROMETRY.

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