dbPTM

ENAH_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	ENAH_HUMAN
UniProt AC	Q8N8S7
Protein Name	Protein enabled homolog
Gene Name	ENAH
Organism	Homo sapiens (Human).
Sequence Length	591
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton. Cell projection, lamellipodium. Cell projection, filopodium. Cell junction, synapse. Cell junction, focal adhesion. Targeted to the leading edge of lamellipodia and filopodia by MRL family members. Colocalizes at f
Protein Description	Ena/VASP proteins are actin-associated proteins involved in a range of processes dependent on cytoskeleton remodeling and cell polarity such as axon guidance and lamellipodial and filopodial dynamics in migrating cells. ENAH induces the formation of F-actin rich outgrowths in fibroblasts. Acts synergistically with BAIAP2-alpha and downstream of NTN1 to promote filipodia formation (By similarity)..
Protein Sequence	MSEQSICQARAAVMVYDDANKKWVPAGGSTGFSRVHIYHHTGNNTFRVVGRKIQDHQVVINCAIPKGLKYNQATQTFHQWRDARQVYGLNFGSKEDANVFASAMMHALEVLNSQETGPTLPRQNSQLPAQVQNGPSQEELEIQRRQLQEQQRQKELERERLERERMERERLERERLERERLERERLEQEQLERERQERERQERLERQERLERQERLERQERLDRERQERQERERLERLERERQERERQEQLEREQLEWERERRISSAAAPASVETPLNSVLGDSSASEPGLQAASQPAETPSQQGIVLGPLAPPPPPPLPPGPAQASVALPPPPGPPPPPPLPSTGPPPPPPPPPLPNQVPPPPPPPPAPPLPASGFFLASMSEDNRPLTGLAAAIAGAKLRKVSRMEDTSFPSGGNAIGVNSASSKTDTGRGNGPLPLGGSGLMEEMSALLARRRRIAEKGSTIETEQKEDKGEDSEPVTSKASSTSTPEPTRKPWERTNTMNGSKSPVISRRDSPRKNQIVFDNRSYDSLHRPKSTPLSQPSANGVQTEGLDYDRLKQDILDEMRKELTKLKEELIDAIRQELSKSNTA

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSEQSICQA ------CCHHHHHHH	44.32	24043423
2	Acetylation	------MSEQSICQA ------CCHHHHHHH	44.32	19413330
5	Phosphorylation	---MSEQSICQARAA ---CCHHHHHHHHEE	22.68	24043423
14	Sulfoxidation	CQARAAVMVYDDANK HHHHEEEEEEECCCC	1.66	30846556
16	Phosphorylation	ARAAVMVYDDANKKW HHEEEEEEECCCCCE	7.04	-
21	Acetylation	MVYDDANKKWVPAGG EEEECCCCCEEECCC	50.13	26051181
66	Acetylation	VINCAIPKGLKYNQA EEEEECCCCCCCCCC	71.42	26051181
69	Ubiquitination	CAIPKGLKYNQATQT EECCCCCCCCCCCCC	51.31	21890473
69	Acetylation	CAIPKGLKYNQATQT EECCCCCCCCCCCCC	51.31	26051181
69	Ubiquitination	CAIPKGLKYNQATQT EECCCCCCCCCCCCC	51.31	21890473
69 (in isoform 1)	Ubiquitination	-	51.31	21890473
69	Malonylation	CAIPKGLKYNQATQT EECCCCCCCCCCCCC	51.31	26320211
69 (in isoform 2)	Ubiquitination	-	51.31	21890473
116	Phosphorylation	EVLNSQETGPTLPRQ HHHHCCCCCCCCCCC	40.60	-
119	Phosphorylation	NSQETGPTLPRQNSQ HCCCCCCCCCCCCCC	51.22	-
125 (in isoform 2)	Phosphorylation	-	25.42	18669648
125	Phosphorylation	PTLPRQNSQLPAQVQ CCCCCCCCCCCCHHC	25.42	25159151
136	Phosphorylation	AQVQNGPSQEELEIQ CHHCCCCCHHHHHHH	52.18	23403867
265	Phosphorylation	WERERRISSAAAPAS HHHHHHHCCCCCCCC	16.47	20736484
266	Phosphorylation	ERERRISSAAAPASV HHHHHHCCCCCCCCC	21.40	20736484
284	Phosphorylation	LNSVLGDSSASEPGL HHHHHCCCCCCCCCC	26.46	20736484
405	Phosphorylation	GAKLRKVSRMEDTSF HHHHHHHHCCCCCCC	29.01	23927012
410	Phosphorylation	KVSRMEDTSFPSGGN HHHCCCCCCCCCCCC	20.97	23927012
411	Phosphorylation	VSRMEDTSFPSGGNA HHCCCCCCCCCCCCC	47.70	23927012
414	Phosphorylation	MEDTSFPSGGNAIGV CCCCCCCCCCCCEEC	58.27	30576142
423	Phosphorylation	GNAIGVNSASSKTDT CCCEECCCCCCCCCC	27.41	21406692
425	Phosphorylation	AIGVNSASSKTDTGR CEECCCCCCCCCCCC	31.99	21406692
426	Phosphorylation	IGVNSASSKTDTGRG EECCCCCCCCCCCCC	39.01	21406692
428	Phosphorylation	VNSASSKTDTGRGNG CCCCCCCCCCCCCCC	40.52	28111955
430	Phosphorylation	SASSKTDTGRGNGPL CCCCCCCCCCCCCCC	33.73	28111955
442	Phosphorylation	GPLPLGGSGLMEEMS CCCCCCCCHHHHHHH	27.27	27251275
449	Phosphorylation	SGLMEEMSALLARRR CHHHHHHHHHHHHHH	21.03	28111955
461	Acetylation	RRRRIAEKGSTIETE HHHHHHHHCCCCCHH	49.49	23954790
461	Ubiquitination	RRRRIAEKGSTIETE HHHHHHHHCCCCCHH	49.49	-
463 (in isoform 3)	Phosphorylation	-	36.96	28450419
463	O-linked_Glycosylation	RRIAEKGSTIETEQK HHHHHHCCCCCHHCC	36.96	30059200
463	Phosphorylation	RRIAEKGSTIETEQK HHHHHHCCCCCHHCC	36.96	22617229
464	Phosphorylation	RIAEKGSTIETEQKE HHHHHCCCCCHHCCC	31.34	23911959
464	O-linked_Glycosylation	RIAEKGSTIETEQKE HHHHHCCCCCHHCCC	31.34	30059200
465 (in isoform 3)	Phosphorylation	-	7.07	23927012
467	Phosphorylation	EKGSTIETEQKEDKG HHCCCCCHHCCCCCC	39.61	23403867
467	O-linked_Glycosylation	EKGSTIETEQKEDKG HHCCCCCHHCCCCCC	39.61	30059200
469 (in isoform 3)	Phosphorylation	-	62.95	25159151
470	Acetylation	STIETEQKEDKGEDS CCCCHHCCCCCCCCC	62.74	26051181
471 (in isoform 3)	Phosphorylation	-	65.73	28731282
473	Acetylation	ETEQKEDKGEDSEPV CHHCCCCCCCCCCCC	66.35	26051181
475 (in isoform 3)	Phosphorylation	-	65.19	23927012
477	O-linked_Glycosylation	KEDKGEDSEPVTSKA CCCCCCCCCCCCCCC	39.23	30059200
477	Phosphorylation	KEDKGEDSEPVTSKA CCCCCCCCCCCCCCC	39.23	25159151
479 (in isoform 3)	Phosphorylation	-	38.34	22496350
480 (in isoform 3)	Phosphorylation	-	9.18	18669648
481	Phosphorylation	GEDSEPVTSKASSTS CCCCCCCCCCCCCCC	34.91	23403867
481	O-linked_Glycosylation	GEDSEPVTSKASSTS CCCCCCCCCCCCCCC	34.91	30059200
482	Phosphorylation	EDSEPVTSKASSTST CCCCCCCCCCCCCCC	26.85	23403867
482	O-linked_Glycosylation	EDSEPVTSKASSTST CCCCCCCCCCCCCCC	26.85	30059200
483	Ubiquitination	DSEPVTSKASSTSTP CCCCCCCCCCCCCCC	42.81	-
485	Phosphorylation	EPVTSKASSTSTPEP CCCCCCCCCCCCCCC	37.57	23927012
486	Phosphorylation	PVTSKASSTSTPEPT CCCCCCCCCCCCCCC	31.10	30266825
487	Phosphorylation	VTSKASSTSTPEPTR CCCCCCCCCCCCCCC	33.84	30266825
488	Phosphorylation	TSKASSTSTPEPTRK CCCCCCCCCCCCCCC	43.86	30266825
489	Phosphorylation	SKASSTSTPEPTRKP CCCCCCCCCCCCCCC	31.59	29255136
493	Phosphorylation	STSTPEPTRKPWERT CCCCCCCCCCCCCCC	50.06	23927012
500	Phosphorylation	TRKPWERTNTMNGSK CCCCCCCCCCCCCCC	24.43	23927012
500 (in isoform 2)	Phosphorylation	-	24.43	28450419
502	Phosphorylation	KPWERTNTMNGSKSP CCCCCCCCCCCCCCC	16.05	23927012
502 (in isoform 2)	Phosphorylation	-	16.05	23927012
506 (in isoform 2)	Phosphorylation	-	25.59	25159151
506	Phosphorylation	RTNTMNGSKSPVISR CCCCCCCCCCCCCCC	25.59	30278072
508 (in isoform 2)	Phosphorylation	-	26.54	28731282
508	Phosphorylation	NTMNGSKSPVISRRD CCCCCCCCCCCCCCC	26.54	30278072
512 (in isoform 2)	Phosphorylation	-	22.84	23927012
512	Phosphorylation	GSKSPVISRRDSPRK CCCCCCCCCCCCCCC	22.84	23927012
516	Phosphorylation	PVISRRDSPRKNQIV CCCCCCCCCCCCEEE	25.45	24732914
516 (in isoform 2)	Phosphorylation	-	25.45	22496350
517 (in isoform 2)	Phosphorylation	-	56.40	18669648
527	Methylation	NQIVFDNRSYDSLHR CEEEECCCCCCCCCC	38.14	115483147
528	Phosphorylation	QIVFDNRSYDSLHRP EEEECCCCCCCCCCC	39.28	23312004
529	Phosphorylation	IVFDNRSYDSLHRPK EEECCCCCCCCCCCC	13.30	30183078
531	Phosphorylation	FDNRSYDSLHRPKST ECCCCCCCCCCCCCC	20.17	25159151
536	Ubiquitination	YDSLHRPKSTPLSQP CCCCCCCCCCCCCCC	67.90	-
537	Phosphorylation	DSLHRPKSTPLSQPS CCCCCCCCCCCCCCC	37.63	30266825
538	Phosphorylation	SLHRPKSTPLSQPSA CCCCCCCCCCCCCCC	34.08	30266825
541	Phosphorylation	RPKSTPLSQPSANGV CCCCCCCCCCCCCCC	41.05	30278072
544	Phosphorylation	STPLSQPSANGVQTE CCCCCCCCCCCCCCC	27.08	26657352
550	Phosphorylation	PSANGVQTEGLDYDR CCCCCCCCCCCCHHH	29.61	23403867
553 (in isoform 2)	Ubiquitination	-	4.48	21890473
559	Ubiquitination	GLDYDRLKQDILDEM CCCHHHHHHHHHHHH	46.98	-
559	2-Hydroxyisobutyrylation	GLDYDRLKQDILDEM CCCHHHHHHHHHHHH	46.98	-
574 (in isoform 1)	Ubiquitination	-	51.18	21890473
574	Ubiquitination	RKELTKLKEELIDAI HHHHHHHHHHHHHHH	51.18	21890473
574	Acetylation	RKELTKLKEELIDAI HHHHHHHHHHHHHHH	51.18	26051181
574	2-Hydroxyisobutyrylation	RKELTKLKEELIDAI HHHHHHHHHHHHHHH	51.18	-
574	Ubiquitination	RKELTKLKEELIDAI HHHHHHHHHHHHHHH	51.18	21890473

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
265	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
265	S	Phosphorylation		-
NTN1-induced PKA phosphorylation on Ser-265 directly parallels the formation of filopodial protrusions.

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 ENAH_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ABI1_HUMAN	ABI1	physical	12672821
ZYX_HUMAN	ZYX	physical	12672821
ZYX_HUMAN	ZYX	physical	10801818
MK01_HUMAN	MAPK1	physical	21988832
SEPT7_HUMAN	SEPT7	physical	22863883
CSN4_HUMAN	COPS4	physical	22863883
EVL_HUMAN	EVL	physical	26344197
RAC1_HUMAN	RAC1	physical	19277120

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 ENAH_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"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-125; SER-506 ANDSER-508, AND MASS SPECTROMETRY.	18669648 [Abstract]
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage."; Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.; Science 316:1160-1166(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125, AND MASSSPECTROMETRY.	17525332 [Abstract]
"Global proteomic profiling of phosphopeptides using electron transferdissociation tandem mass spectrometry."; Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.; Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-125; SER-405; THR-410;THR-502 AND SER-508, AND MASS SPECTROMETRY.	17287340 [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-508, AND MASSSPECTROMETRY.	17081983 [Abstract]
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization."; Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.; Nat. Biotechnol. 24:1285-1292(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-489, AND MASSSPECTROMETRY.	16964243 [Abstract]

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