dbPTM

MYO1E_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MYO1E_HUMAN
UniProt AC	Q12965
Protein Name	Unconventional myosin-Ie
Gene Name	MYO1E
Organism	Homo sapiens (Human).
Sequence Length	1108
Subcellular Localization	Cytoplasm. Cytoplasm, cytoskeleton. Cytoplasmic vesicle. Cytoplasmic vesicle, clathrin-coated vesicle. Cell junction. Colocalizes with F-actin (By similarity). In cultured podocytes, it localizes close to and is associated with the cytoplasmic membra
Protein Description	Myosins are actin-based motor molecules with ATPase activity. Unconventional myosins serve in intracellular movements. Their highly divergent tails bind to membranous compartments, which are then moved relative to actin filaments. Binds to membranes containing anionic phospholipids via its tail domain. Required for normal morphology of the glomerular basement membrane, normal development of foot processes by kidney podocytes and normal kidney function. In dendritic cells, may control the movement of class II-containing cytoplasmic vesicles along the actin cytoskeleton by connecting them with the actin network via ARL14EP and ARL14..
Protein Sequence	MGSKGVYQYHWQSHNVKHSGVDDMVLLSKITENSIVENLKKRYMDDYIFTYIGSVLISVNPFKQMPYFGEKEIEMYQGAAQYENPPHIYALADNMYRNMIIDRENQCVIISGESGAGKTVAAKYIMSYISRVSGGGTKVQHVKDIILQSNPLLEAFGNAKTVRNNNSSRFGKYFEIQFSPGGEPDGGKISNFLLEKSRVVMRNPGERSFHIFYQLIEGASAEQKHSLGITSMDYYYYLSLSGSYKVDDIDDRREFQETLHAMNVIGIFAEEQTLVLQIVAGILHLGNISFKEVGNYAAVESEEFLAFPAYLLGINQDRLKEKLTSRQMDSKWGGKSESIHVTLNVEQACYTRDALAKALHARVFDFLVDSINKAMEKDHEEYNIGVLDIYGFEIFQKNGFEQFCINFVNEKLQQIFIELTLKAEQEEYVQEGIRWTPIEYFNNKIVCDLIENKVNPPGIMSILDDVCATMHAVGEGADQTLLQKLQMQIGSHEHFNSWNQGFIIHHYAGKVSYDMDGFCERNRDVLFMDLIELMQSSELPFIKSLFPENLQADKKGRPTTAGSKIKKQANDLVSTLMKCTPHYIRCIKPNETKKPRDWEESRVKHQVEYLGLKENIRVRRAGYAYRRIFQKFLQRYAILTKATWPSWQGEEKQGVLHLLQSVNMDSDQFQLGRSKVFIKAPESLFLLEEMRERKYDGYARVIQKSWRKFVARKKYVQMREEASDLLLNKKERRRNSINRNFIGDYIGMEEHPELQQFVGKREKIDFADTVTKYDRRFKGVKRDLLLTPKCLYLIGREKVKQGPDKGLVKEVLKRKIEIERILSVSLSTMQDDIFILHEQEYDSLLESVFKTEFLSLLAKRYEEKTQKQLPLKFSNTLELKLKKENWGPWSAGGSRQVQFHQGFGDLAVLKPSNKVLQVSIGPGLPKNSRPTRRNTTQNTGYSSGTQNANYPVRAAPPPPGYHQNGVIRNQYVPYPHAPGSQRSNQKSLYTSMARPPLPRQQSTSSDRVSQTPESLDFLKVPDQGAAGVRRQTTSRPPPAGGRPKPQPKPKPQVPQCKALYAYDAQDTDELSFNANDIIDIIKEDPSGWWTGRLRGKQGLFPNNYVTKI

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
7	Phosphorylation	-MGSKGVYQYHWQSH -CCCCCCEEEECCCC	16.42	21945579
9	Phosphorylation	GSKGVYQYHWQSHNV CCCCCEEEECCCCCC	6.32	21945579
13	Phosphorylation	VYQYHWQSHNVKHSG CEEEECCCCCCCCCC	16.31	21945579
17	Ubiquitination	HWQSHNVKHSGVDDM ECCCCCCCCCCCCHH	37.05	-
29	Ubiquitination	DDMVLLSKITENSIV CHHHHHHHCCCCCHH	54.33	-
40	Ubiquitination	NSIVENLKKRYMDDY CCHHHHHHHHHCCHH	46.95	-
47	Phosphorylation	KKRYMDDYIFTYIGS HHHHCCHHHHHHCCC	8.15	-
51	Phosphorylation	MDDYIFTYIGSVLIS CCHHHHHHCCCEEEE	7.79	-
67	Phosphorylation	NPFKQMPYFGEKEIE CCCCCCCCCCHHHHE	20.90	-
103	Dimethylation	YRNMIIDRENQCVII HHCCEECCCCCEEEE	34.06	-
103	Methylation	YRNMIIDRENQCVII HHCCEECCCCCEEEE	34.06	30762633
111	Phosphorylation	ENQCVIISGESGAGK CCCEEEEECCCCCCH	25.94	-
118	Ubiquitination	SGESGAGKTVAAKYI ECCCCCCHHHHHHHH	39.01	-
119	Phosphorylation	GESGAGKTVAAKYIM CCCCCCHHHHHHHHH	17.92	29083192
124	Phosphorylation	GKTVAAKYIMSYISR CHHHHHHHHHHHHHH	9.34	29083192
127	O-linked_Glycosylation	VAAKYIMSYISRVSG HHHHHHHHHHHHHCC	15.12	OGP
127	Phosphorylation	VAAKYIMSYISRVSG HHHHHHHHHHHHHCC	15.12	29083192
128	Phosphorylation	AAKYIMSYISRVSGG HHHHHHHHHHHHCCC	5.87	29083192
130	Phosphorylation	KYIMSYISRVSGGGT HHHHHHHHHHCCCCC	20.56	29083192
133	Phosphorylation	MSYISRVSGGGTKVQ HHHHHHHCCCCCEEE	30.52	20068231
137	Phosphorylation	SRVSGGGTKVQHVKD HHHCCCCCEEEEHHH	31.17	20068231
138	2-Hydroxyisobutyrylation	RVSGGGTKVQHVKDI HHCCCCCEEEEHHHH	43.08	-
138	Ubiquitination	RVSGGGTKVQHVKDI HHCCCCCEEEEHHHH	43.08	-
143	Ubiquitination	GTKVQHVKDIILQSN CCEEEEHHHHHHHCC	40.88	-
160	Ubiquitination	LEAFGNAKTVRNNNS HHHHCCCEEECCCCC	52.10	21890473
188	Ubiquitination	GGEPDGGKISNFLLE CCCCCCCCCCCHHHE	48.79	-
196	Ubiquitination	ISNFLLEKSRVVMRN CCCHHHEECEEEEEC	43.46	-
197	Phosphorylation	SNFLLEKSRVVMRNP CCHHHEECEEEEECC	22.41	20058876
289	Phosphorylation	ILHLGNISFKEVGNY HHHHCCCCHHHCCCE	33.98	24719451
320	Ubiquitination	GINQDRLKEKLTSRQ CCCHHHHHHHHHHCC	54.41	-
322	Ubiquitination	NQDRLKEKLTSRQMD CHHHHHHHHHHCCCC	56.32	-
331	Ubiquitination	TSRQMDSKWGGKSES HHCCCCCCCCCCCCE	45.66	-
357	2-Hydroxyisobutyrylation	YTRDALAKALHARVF CCHHHHHHHHHHHHH	52.94	-
370	Phosphorylation	VFDFLVDSINKAMEK HHHHHHHHHHHHHHH	22.15	21712546
440	Phosphorylation	IRWTPIEYFNNKIVC CCCCCHHHCCCEEHH	16.60	28152594
444	Ubiquitination	PIEYFNNKIVCDLIE CHHHCCCEEHHHHHC	37.31	-
453	Ubiquitination	VCDLIENKVNPPGIM HHHHHCCCCCCCCHH	30.51	-
513	Phosphorylation	HYAGKVSYDMDGFCE EECCCCEECCCCHHH	20.48	27642862
554	Ubiquitination	PENLQADKKGRPTTA CCCCCCCCCCCCCCC	61.21	-
555	Ubiquitination	ENLQADKKGRPTTAG CCCCCCCCCCCCCCH	61.78	-
560	Phosphorylation	DKKGRPTTAGSKIKK CCCCCCCCCHHHHHH	31.53	22817900
564	Ubiquitination	RPTTAGSKIKKQAND CCCCCHHHHHHHHHH	58.59	-
575	Phosphorylation	QANDLVSTLMKCTPH HHHHHHHHHHHHCHH	24.32	20068231
604	Ubiquitination	DWEESRVKHQVEYLG CHHHHHHHHHHHHCC	27.49	-
609	Phosphorylation	RVKHQVEYLGLKENI HHHHHHHHCCCHHCH	13.76	25627689
613	Acetylation	QVEYLGLKENIRVRR HHHHCCCHHCHHHHH	47.09	42359013
613	Ubiquitination	QVEYLGLKENIRVRR HHHHCCCHHCHHHHH	47.09	21906983
623	Phosphorylation	IRVRRAGYAYRRIFQ HHHHHHHHHHHHHHH	10.24	-
625	Phosphorylation	VRRAGYAYRRIFQKF HHHHHHHHHHHHHHH	7.61	-
631	Acetylation	AYRRIFQKFLQRYAI HHHHHHHHHHHHHHH	36.97	25825284
631	Ubiquitination	AYRRIFQKFLQRYAI HHHHHHHHHHHHHHH	36.97	-
641	Ubiquitination	QRYAILTKATWPSWQ HHHHHHHHCCCCCCC	40.13	-
694	Ubiquitination	LEEMRERKYDGYARV HHHHHHCCCCCHHHH	42.83	-
698	Phosphorylation	RERKYDGYARVIQKS HHCCCCCHHHHHHHH	6.58	-
704	Ubiquitination	GYARVIQKSWRKFVA CHHHHHHHHHHHHHH	40.64	-
715	Phosphorylation	KFVARKKYVQMREEA HHHHHHHHHHHHHHH	10.03	22817900
729	2-Hydroxyisobutyrylation	ASDLLLNKKERRRNS HHHHHCCHHHHHHHH	56.85	-
729	Ubiquitination	ASDLLLNKKERRRNS HHHHHCCHHHHHHHH	56.85	-
736	Phosphorylation	KKERRRNSINRNFIG HHHHHHHHCCHHHHH	21.30	25159151
745	Phosphorylation	NRNFIGDYIGMEEHP CHHHHHHHCCCCCCH	8.31	22199227
760	Ubiquitination	ELQQFVGKREKIDFA HHHHHHCCHHHCCHH	52.67	-
763	2-Hydroxyisobutyrylation	QFVGKREKIDFADTV HHHCCHHHCCHHHHC	52.16	-
763	Ubiquitination	QFVGKREKIDFADTV HHHCCHHHCCHHHHC	52.16	-
772	Ubiquitination	DFADTVTKYDRRFKG CHHHHCHHHHHHCCC	40.60	-
805	Ubiquitination	KVKQGPDKGLVKEVL HHHCCCCCCHHHHHH	58.22	-
809	Ubiquitination	GPDKGLVKEVLKRKI CCCCCHHHHHHHHHH	47.34	-
859	2-Hydroxyisobutyrylation	EFLSLLAKRYEEKTQ HHHHHHHHHHHHHHC	56.32	-
859	Ubiquitination	EFLSLLAKRYEEKTQ HHHHHHHHHHHHHHC	56.32	-
872	Ubiquitination	TQKQLPLKFSNTLEL HCCCCCCCCCCCEEE	44.82	-
874	Phosphorylation	KQLPLKFSNTLELKL CCCCCCCCCCEEEEE	27.58	23186163
876	Phosphorylation	LPLKFSNTLELKLKK CCCCCCCCEEEEEEC	22.02	25159151
880	Ubiquitination	FSNTLELKLKKENWG CCCCEEEEEECCCCC	49.21	-
883	Ubiquitination	TLELKLKKENWGPWS CEEEEEECCCCCCCC	67.71	-
890	Phosphorylation	KENWGPWSAGGSRQV CCCCCCCCCCCCEEE	21.85	25159151
894	Phosphorylation	GPWSAGGSRQVQFHQ CCCCCCCCEEEEEEC	20.72	28857561
910	Ubiquitination	FGDLAVLKPSNKVLQ CCCEEEECCCCCEEE	39.54	-
914	Ubiquitination	AVLKPSNKVLQVSIG EEECCCCCEEEEEEC	48.97	-
919	Phosphorylation	SNKVLQVSIGPGLPK CCCEEEEEECCCCCC	14.63	21406692
928	Phosphorylation	GPGLPKNSRPTRRNT CCCCCCCCCCCCCCC	45.85	21406692
935	Phosphorylation	SRPTRRNTTQNTGYS CCCCCCCCCCCCCCC	28.13	21945579
936	Phosphorylation	RPTRRNTTQNTGYSS CCCCCCCCCCCCCCC	24.30	21945579
939	Phosphorylation	RRNTTQNTGYSSGTQ CCCCCCCCCCCCCCC	27.90	21945579
941	Phosphorylation	NTTQNTGYSSGTQNA CCCCCCCCCCCCCCC	9.53	21945579
942	Phosphorylation	TTQNTGYSSGTQNAN CCCCCCCCCCCCCCC	24.52	21945579
943	Phosphorylation	TQNTGYSSGTQNANY CCCCCCCCCCCCCCC	37.06	21945579
945	Phosphorylation	NTGYSSGTQNANYPV CCCCCCCCCCCCCCC	22.16	21945579
950	Phosphorylation	SGTQNANYPVRAAPP CCCCCCCCCCCCCCC	10.74	21945579
961	Phosphorylation	AAPPPPGYHQNGVIR CCCCCCCCCCCCCCC	13.15	23917254
971	Phosphorylation	NGVIRNQYVPYPHAP CCCCCCCCCCCCCCC	13.62	21945579
974	Phosphorylation	IRNQYVPYPHAPGSQ CCCCCCCCCCCCCCC	9.52	21945579
980	Phosphorylation	PYPHAPGSQRSNQKS CCCCCCCCCCCCCCC	22.74	21945579
983	Phosphorylation	HAPGSQRSNQKSLYT CCCCCCCCCCCCHHH	35.66	27642862
987	Phosphorylation	SQRSNQKSLYTSMAR CCCCCCCCHHHHCCC	19.49	21945579
989	Phosphorylation	RSNQKSLYTSMARPP CCCCCCHHHHCCCCC	12.12	21945579
990	Phosphorylation	SNQKSLYTSMARPPL CCCCCHHHHCCCCCC	19.81	21945579
991	Phosphorylation	NQKSLYTSMARPPLP CCCCHHHHCCCCCCC	9.26	21945579
1002	Phosphorylation	PPLPRQQSTSSDRVS CCCCCCCCCCCCCCC	23.17	20201521
1003	Phosphorylation	PLPRQQSTSSDRVSQ CCCCCCCCCCCCCCC	28.10	28355574
1004	Phosphorylation	LPRQQSTSSDRVSQT CCCCCCCCCCCCCCC	35.17	25463755
1005	Phosphorylation	PRQQSTSSDRVSQTP CCCCCCCCCCCCCCH	29.53	25463755
1009	Phosphorylation	STSSDRVSQTPESLD CCCCCCCCCCHHHCC	29.27	25159151
1011	Phosphorylation	SSDRVSQTPESLDFL CCCCCCCCHHHCCCC	22.86	25159151
1014	Phosphorylation	RVSQTPESLDFLKVP CCCCCHHHCCCCCCC	34.15	23663014
1019	Ubiquitination	PESLDFLKVPDQGAA HHHCCCCCCCCCCCC	52.28	-
1090	Phosphorylation	EDPSGWWTGRLRGKQ HCCCCCCCCCCCCCC	13.10	20068231
1104	Phosphorylation	QGLFPNNYVTKI--- CCCCCCCCEECC---	19.01	27642862

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 MYO1E_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MYO1E_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 MYO1E_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
ASNS_HUMAN	ASNS	physical	22863883
PUR9_HUMAN	ATIC	physical	22863883
CPNS1_HUMAN	CAPNS1	physical	22863883
ISOC1_HUMAN	ISOC1	physical	22863883
MCTS1_HUMAN	MCTS1	physical	22863883
LIS1_HUMAN	PAFAH1B1	physical	22863883
PDIA4_HUMAN	PDIA4	physical	22863883
PLPHP_HUMAN	PROSC	physical	22863883
RUXF_HUMAN	SNRPF	physical	22863883
TBCB_HUMAN	TBCB	physical	22863883
1433F_HUMAN	YWHAH	physical	22863883
ARPC4_HUMAN	ARPC4	physical	26344197
CAND1_HUMAN	CAND1	physical	26344197
MYH9_HUMAN	MYH9	physical	26344197
MYO5A_HUMAN	MYO5A	physical	26344197
IPYR_HUMAN	PPA1	physical	26344197

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614131	Focal segmental glomerulosclerosis 6 (FSGS6)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MYO1E_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-980, AND MASSSPECTROMETRY.	18669648 [Abstract]