dbPTM

EH1L1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	EH1L1_HUMAN
UniProt AC	Q8N3D4
Protein Name	EH domain-binding protein 1-like protein 1
Gene Name	EHBP1L1
Organism	Homo sapiens (Human).
Sequence Length	1523
Subcellular Localization	Endosome .
Protein Description	May act as Rab effector protein and play a role in vesicle trafficking..
Protein Sequence	MTSVWKRLQRVGKRAAKFQFVACYHELVLECTKKWQPDKLVVVWTRRNRRICSKAHSWQPGIQNPYRGTVVWMVPENVDISVTLYRDPHVDQYEAKEWTFIIENESKGQRKVLATAEVDLARHAGPVPVQVPVRLRLKPKSVKVVQAELSLTLSGVLLREGRATDDDMQSLASLMSVKPSDVGNLDDFAESDEDEAHGPGAPEARARVPQPDPSRELKTLCEEEEEGQGRPQQAVASPSNAEDTSPAPVSAPAPPARTSRGQGSERANEAGGQVGPEAPRPPETSPEMRSSRQPAQDTAPTPAPRLRKGSDALRPPVPQGEDEVPKASGAPPAGLGSARETQAQACPQEGTEAHGARLGPSIEDKGSGDPFGRQRLKAEEMDTEDRPEASGVDTEPRSGGREANTKRSGVRAGEAEESSAVCQVDAEQRSKVRHVDTKGPEATGVMPEARCRGTPEAPPRGSQGRLGVRTRDEAPSGLSLPPAEPAGHSGQLGDLEGARAAAGQEREGAEVRGGAPGIEGTGLEQGPSVGAISTRPQVSSWQGALLSTAQGAISRGLGGWEAEAGGSGDLETETEVVGLEVLGTQEKEVEGSGFPETRTLEIEILGALEKEAARSRVLESEVAGTAQCEGLETQETEVGVIETPGTETEVLGTQKTEAGGSGVLQTRTTIAETEVLVTQEISGDLGPLKIEDTIQSEMLGTQETEVEASRVPESEAEGTEAKILGTQEITARDSGVREIEAEIAESDILVAQEIEVGLLGVLGIETGAAEGAILGTQEIASRDSGVPGLEADTTGIQVKEVGGSEVPEIATGTAETEILGTQEIASRSSGVPGLESEVAGAQETEVGGSGISGPEAGMAEARVLMTRKTEIIVPEAEKEEAQTSGVQEAETRVGSALKYEALRAPVTQPRVLGSQEAKAEISGVQGSETQVLRVQEAEAGVWGMSEGKSGAWGAQEAEMKVLESPENKSGTFKAQEAEAGVLGNEKGKEAEGSLTEASLPEAQVASGAGAGAPRASSPEKAEEDRRLPGSQAPPALVSSSQSLLEWCQEVTTGYRGVRITNFTTSWRNGLAFCAILHRFYPDKIDYASLDPLNIKQNNKQAFDGFAALGVSRLLEPADMVLLSVPDKLIVMTYLCQIRAFCTGQELQLVQLEGGGGAGTYRVGSAQPSPPDDLDAGGLAQRLRGHGAEGPQEPKEAADRADGAAPGVASRNAVAGRASKDGGAEAPRESRPAEVPAEGLVNGAGAPGGGGVRLRRPSVNGEPGSVPPPRAHGSFSHVRDADLLKKRRSRLRNSSSFSMDDPDAGAMGAAAAEGQAPDPSPAPGPPTAADSQQPPGGSSPSEEPPPSPGEEAGLQRFQDTSQYVCAELQALEQEQRQIDGRAAEVEMQLRSLMESGANKLQEEVLIQEWFTLVNKKNALIRRQDQLQLLMEEQDLERRFELLSRELRAMLAIEDWQKTSAQQHREQLLLEELVSLVNQRDELVRDLDHKERIALEEDERLERGLEQRRRKLSRQLSRRERCVLS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
66	Phosphorylation	QPGIQNPYRGTVVWM CCCCCCCCCCEEEEE	29.26	-
85	Phosphorylation	VDISVTLYRDPHVDQ CEEEEEEEECCCCHH	12.01	-
134	Methylation	VPVQVPVRLRLKPKS CCCEEEEEEEECCCC	14.18	-
164	Phosphorylation	LLREGRATDDDMQSL HHHCCCCCHHHHHHH	38.30	29632367
170	Phosphorylation	ATDDDMQSLASLMSV CCHHHHHHHHHHHCC	21.18	25159151
173	Phosphorylation	DDMQSLASLMSVKPS HHHHHHHHHHCCCHH	29.87	21955146
176	Phosphorylation	QSLASLMSVKPSDVG HHHHHHHCCCHHHCC	32.08	21955146
180	Phosphorylation	SLMSVKPSDVGNLDD HHHCCCHHHCCCHHH	38.93	21955146
191	Phosphorylation	NLDDFAESDEDEAHG CHHHHHHCCCCHHCC	42.76	29255136
214	Phosphorylation	RVPQPDPSRELKTLC CCCCCCCCHHHHHHH	45.85	28555341
237	Phosphorylation	RPQQAVASPSNAEDT CCCCCCCCCCCCCCC	23.43	25159151
239	Phosphorylation	QQAVASPSNAEDTSP CCCCCCCCCCCCCCC	46.29	25627689
244	Phosphorylation	SPSNAEDTSPAPVSA CCCCCCCCCCCCCCC	28.28	25627689
245	Phosphorylation	PSNAEDTSPAPVSAP CCCCCCCCCCCCCCC	31.24	29496963
258	Phosphorylation	APAPPARTSRGQGSE CCCCCCCCCCCCCCH	25.53	23898821
264	Phosphorylation	RTSRGQGSERANEAG CCCCCCCCHHCHHCC	18.93	23917254
284	Phosphorylation	EAPRPPETSPEMRSS CCCCCCCCCHHHHHC	56.19	29255136
285	Phosphorylation	APRPPETSPEMRSSR CCCCCCCCHHHHHCC	19.73	29255136
301	Phosphorylation	PAQDTAPTPAPRLRK CCCCCCCCCCCCCCC	29.62	25159151
310	Phosphorylation	APRLRKGSDALRPPV CCCCCCCCCCCCCCC	23.81	29255136
328	Phosphorylation	EDEVPKASGAPPAGL CCCCCCCCCCCCCCC	41.43	23312004
337	Phosphorylation	APPAGLGSARETQAQ CCCCCCCCHHHHHHH	29.24	23312004
356	Ubiquitination	EGTEAHGARLGPSIE CCCHHCCCCCCCCCC	8.15	24816145
361	Phosphorylation	HGARLGPSIEDKGSG CCCCCCCCCCCCCCC	36.49	20068231
367	Phosphorylation	PSIEDKGSGDPFGRQ CCCCCCCCCCCCHHH	45.85	30624053
377	Ubiquitination	PFGRQRLKAEEMDTE CCHHHHHCHHHCCCC	56.81	24816145
383	Phosphorylation	LKAEEMDTEDRPEAS HCHHHCCCCCCCHHC	38.18	-
389	Ubiquitination	DTEDRPEASGVDTEP CCCCCCHHCCCCCCC	17.80	24816145
390	Phosphorylation	TEDRPEASGVDTEPR CCCCCHHCCCCCCCC	37.37	-
430	Phosphorylation	QVDAEQRSKVRHVDT ECCHHHHHCCEECCC	34.89	23186163
443	Phosphorylation	DTKGPEATGVMPEAR CCCCCCCCCCCCCCC	28.75	-
454	Phosphorylation	PEARCRGTPEAPPRG CCCCCCCCCCCCCCC	9.90	22617229
462	Phosphorylation	PEAPPRGSQGRLGVR CCCCCCCCCCCCCCC	30.64	21712546
489	Phosphorylation	PAEPAGHSGQLGDLE CCCCCCCCCCCCCHH	27.58	28348404
528	Phosphorylation	TGLEQGPSVGAISTR CCCCCCCCCCEEECC	39.75	28348404
533	Phosphorylation	GPSVGAISTRPQVSS CCCCCEEECCCCCCC	20.17	28348404
534	Phosphorylation	PSVGAISTRPQVSSW CCCCEEECCCCCCCH	40.01	28348404
539	Phosphorylation	ISTRPQVSSWQGALL EECCCCCCCHHHHHH	22.17	28348404
540	Phosphorylation	STRPQVSSWQGALLS ECCCCCCCHHHHHHH	25.27	28348404
547	Phosphorylation	SWQGALLSTAQGAIS CHHHHHHHHHHHHHH	23.65	28348404
597	Phosphorylation	EGSGFPETRTLEIEI CCCCCCCCCEEEEEE	29.23	-
599	Phosphorylation	SGFPETRTLEIEILG CCCCCCCEEEEEEHH	35.84	-
615	Phosphorylation	LEKEAARSRVLESEV HHHHHHHHHHHHHHH	23.24	22210691
656	Phosphorylation	EVLGTQKTEAGGSGV EEECEEECCCCCCCE	22.65	26437602
661	Phosphorylation	QKTEAGGSGVLQTRT EECCCCCCCEECCCC	25.47	26437602
668	Phosphorylation	SGVLQTRTTIAETEV CCEECCCCEEEEEEE	26.41	28985074
673	Phosphorylation	TRTTIAETEVLVTQE CCCEEEEEEEEEEEE	23.52	28985074
726	Phosphorylation	TEAKILGTQEITARD CEEEECCEEEEEECC	21.42	28176443
730	Phosphorylation	ILGTQEITARDSGVR ECCEEEEEECCCCCC	18.19	28176443
734	Phosphorylation	QEITARDSGVREIEA EEEEECCCCCCEEEE	33.37	30266825
784	Phosphorylation	QEIASRDSGVPGLEA HHHHHCCCCCCCCCC	40.35	23663014
794	Phosphorylation	PGLEADTTGIQVKEV CCCCCCCCCEEEEEE	32.60	28555341
828	Phosphorylation	TQEIASRSSGVPGLE CHHHHHCCCCCCCHH	29.02	23532336
829	Phosphorylation	QEIASRSSGVPGLES HHHHHCCCCCCCHHH	42.57	22210691
836	Phosphorylation	SGVPGLESEVAGAQE CCCCCHHHHCCCCEE	42.27	27251275
849	Phosphorylation	QETEVGGSGISGPEA EEEECCCCCCCCHHH	27.33	22210691
852	Phosphorylation	EVGGSGISGPEAGMA ECCCCCCCCHHHCHH	52.39	22210691
866	Phosphorylation	AEARVLMTRKTEIIV HHHEEHHCCCCEEEC	25.50	-
869	Phosphorylation	RVLMTRKTEIIVPEA EEHHCCCCEEECCHH	29.17	-
883	Phosphorylation	AEKEEAQTSGVQEAE HHHHHHHHCCCHHHH	34.20	-
884	O-linked_Glycosylation	EKEEAQTSGVQEAET HHHHHHHCCCHHHHH	25.53	30379171
884	Phosphorylation	EKEEAQTSGVQEAET HHHHHHHCCCHHHHH	25.53	-
895	Phosphorylation	EAETRVGSALKYEAL HHHHHHHHHHHHHHH	27.80	-
899	Phosphorylation	RVGSALKYEALRAPV HHHHHHHHHHHCCCC	13.79	28796482
914	Phosphorylation	TQPRVLGSQEAKAEI CCCCCCCCHHHHHHH	22.23	29214152
922	Phosphorylation	QEAKAEISGVQGSET HHHHHHHCCCCCCCE	25.15	27732954
927	Ubiquitination	EISGVQGSETQVLRV HHCCCCCCCEEEEEE	22.00	22817900
927	Phosphorylation	EISGVQGSETQVLRV HHCCCCCCCEEEEEE	22.00	27732954
929	Phosphorylation	SGVQGSETQVLRVQE CCCCCCCEEEEEEEE	26.19	27732954
948	Ubiquitination	VWGMSEGKSGAWGAQ CCCCCCCCCCCCCHH	41.48	22817900
960	Ubiquitination	GAQEAEMKVLESPEN CHHHHEEEEECCCCC	34.86	22817900
964	Phosphorylation	AEMKVLESPENKSGT HEEEEECCCCCCCCC	33.09	30266825
969	Phosphorylation	LESPENKSGTFKAQE ECCCCCCCCCCCHHH	55.43	26055452
971	Phosphorylation	SPENKSGTFKAQEAE CCCCCCCCCCHHHHH	29.11	28348404
993	Phosphorylation	KGKEAEGSLTEASLP CCCCCCCCCCCCCCC	24.51	30266825
995	Phosphorylation	KEAEGSLTEASLPEA CCCCCCCCCCCCCHH	31.07	26657352
998	Phosphorylation	EGSLTEASLPEAQVA CCCCCCCCCCHHHHH	37.92	21815630
1006	Phosphorylation	LPEAQVASGAGAGAP CCHHHHHCCCCCCCC	30.25	29514088
1016	Phosphorylation	GAGAPRASSPEKAEE CCCCCCCCCHHHHHH	47.94	28176443
1017	Phosphorylation	AGAPRASSPEKAEED CCCCCCCCHHHHHHH	35.77	23401153
1099	Ubiquitination	LNIKQNNKQAFDGFA CCCCCCCCHHHHHHH	51.02	33845483
1123	Phosphorylation	PADMVLLSVPDKLIV CCCEEEECCCCHHHH	27.69	28348404
1164	Phosphorylation	AGTYRVGSAQPSPPD CCEEECCCCCCCCCC	22.37	30266825
1168	Phosphorylation	RVGSAQPSPPDDLDA ECCCCCCCCCCCCCC	36.66	30266825
1218	Phosphorylation	NAVAGRASKDGGAEA CCCCCCCCCCCCCCC	29.89	26657352
1219	Methylation	AVAGRASKDGGAEAP CCCCCCCCCCCCCCC	60.45	-
1257	Phosphorylation	GVRLRRPSVNGEPGS CEEECCCCCCCCCCC	26.80	29255136
1264	Phosphorylation	SVNGEPGSVPPPRAH CCCCCCCCCCCCCCC	42.01	23927012
1273	Phosphorylation	PPPRAHGSFSHVRDA CCCCCCCCCCCCCCH	17.44	23401153
1275	Phosphorylation	PRAHGSFSHVRDADL CCCCCCCCCCCCHHH	23.83	20068231
1346	Phosphorylation	PSEEPPPSPGEEAGL CCCCCCCCCCHHHHH	51.84	24275569
1359	Phosphorylation	GLQRFQDTSQYVCAE HHHHHHHHHHHHHHH	13.62	-
1362	Phosphorylation	RFQDTSQYVCAELQA HHHHHHHHHHHHHHH	9.39	27642862
1442	Phosphorylation	ERRFELLSRELRAML HHHHHHHHHHHHHHH	36.01	24719451
1473	Phosphorylation	LLLEELVSLVNQRDE HHHHHHHHHHHHHHH	38.94	30301811
1511	Phosphorylation	EQRRRKLSRQLSRRE HHHHHHHHHHHHHHH	22.48	22817900
1511	O-linked_Glycosylation	EQRRRKLSRQLSRRE HHHHHHHHHHHHHHH	22.48	30379171
1515	Phosphorylation	RKLSRQLSRRERCVL HHHHHHHHHHHHHCC	22.43	22817900

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 EH1L1_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of EH1L1_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
301	Phosphorylation	307 (6)	R ⇒ Q	rs3741380	Coronary artery disease	29212778
310	Phosphorylation	307 (3)	R ⇒ Q	rs3741380	Coronary artery disease	29212778

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ANR40_HUMAN	ANKRD40	physical	22863883
RPB1_HUMAN	POLR2A	physical	22863883
PP4R1_HUMAN	PPP4R1	physical	22863883
TFG_HUMAN	TFG	physical	22863883
BIN1_HUMAN	BIN1	physical	26833786
RAB8A_HUMAN	RAB8A	physical	26833786
RAB8B_HUMAN	RAB8B	physical	26833786

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 EH1L1_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-310, AND MASSSPECTROMETRY.	19690332 [Abstract]
"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-170; SER-173; SER-191;SER-285; SER-310; SER-964 AND SER-1168, AND MASS SPECTROMETRY.	18669648 [Abstract]
"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-285, AND MASSSPECTROMETRY.	18220336 [Abstract]
"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-310 AND SER-1257, ANDMASS SPECTROMETRY.	17081983 [Abstract]