dbPTM

MYO3A_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	MYO3A_HUMAN
UniProt AC	Q8NEV4
Protein Name	Myosin-IIIa
Gene Name	MYO3A
Organism	Homo sapiens (Human).
Sequence Length	1616
Subcellular Localization	Cytoplasm, cytoskeleton. Cytoplasm . Cell projection, filopodium tip . Cell projection, stereocilium . Increased localization at the filodium tip seen in the presence of MORN4.
Protein Description	Probable actin-based motor with a protein kinase activity. Probably plays a role in vision and hearing. [PubMed: 12032315 Required for normal cochlear hair bundle development and hearing. Plays an important role in the early steps of cochlear hair bundle morphogenesis. Influences the number and lengths of stereocilia to be produced and limits the growth of microvilli within the forming auditory hair bundles thereby contributing to the architecture of the hair bundle, including its staircase pattern. Involved in the elongation of actin in stereocilia tips by transporting the actin regulatory factor ESPN to the plus ends of actin filaments (By similarity]
Protein Sequence	MFPLIGKTIIFDNFPDPSDTWEITETIGKGTYGKVFKVLNKKNGQKAAVKILDPIHDIDEEIEAEYNILKALSDHPNVVRFYGIYFKKDKVNGDKLWLVLELCSGGSVTDLVKGFLKRGERMSEPLIAYILHEALMGLQHLHNNKTIHRDVKGNNILLTTEGGVKLVDFGVSAQLTSTRHRRNTSVGTPFWMAPEVIACEQQLDTTYDARCDTWSLGITAIELGDGDPPLADLHPMRALFKIPRNPPPKLRQPELWSAEFNDFISKCLTKDYEKRPTVSELLQHKFITQIEGKDVMLQKQLTEFIGIHQCMGGTEKARRERIHTKKGNFNRPLISNLKDVDDLATLEILDENTVSEQLEKCYSRDQIYVYVGDILIALNPFQSLGLYSTKHSKLYIGSKRTASPPHIFAMADLGYQSMITYNSDQCIVISGESGAGKTENAHLLVQQLTVLGKANNRTLQEKILQVNNLVEAFGNACTIINDNSSRFGKYLEMKFTSSGAVVGAQISEYLLEKSRVIHQAIGEKNFHIFYYIYAGLAEKKKLAHYKLPENKPPRYLQNDHLRTVQDIMNNSFYKSQYELIEQCFKVIGFTMEQLGSIYSILAAILNVGNIEFSSVATEHQIDKSHISNHTALENCASLLCIRADELQEALTSHCVVTRGETIIRPNTVEKATDVRDAMAKTLYGRLFSWIVNCINSLLKHDSSPSGNGDELSIGILDIFGFENFKKNSFEQLCINIANEQIQYYYNQHVFAWEQNEYLNEDVDARVIEYEDNWPLLDMFLQKPMGLLSLLDEESRFPKATDQTLVEKFEGNLKSQYFWRPKRMELSFGIHHYAGKVLYNASGFLAKNRDTLPTDIVLLLRSSDNSVIRQLVNHPLTKTGNLPHSKTKNVINYQMRTSEKLINLAKGDTGEATRHARETTNMKTQTVASYFRYSLMDLLSKMVVGQPHFVRCIKPNSERQARKYDKEKVLLQLRYTGILETARIRRLGFSHRILFANFIKRYYLLCYKSSEEPRMSPDTCATILEKAGLDNWALGKTKVFLKYYHVEQLNLMRKEAIDKLILIQACVRAFLCSRRYQKIQEKRKESAIIIQSAARGHLVRKQRKEIVDMKNTAVTTIQTSDQEFDYKKNFENTRESFVKKQAENAISANERFISAPNNKGSVSVVKTSTFKPEEETTNAVESNNRVYQTPKKMNNVYEEEVKQEFYLVGPEVSPKQKSVKDLEENSNLRKVEKEEAMIQSYYQRYTEERNCEESKAAYLERKAISERPSYPVPWLAENETSFKKTLEPTLSQRSIYQNANSMEKEKKTSVVTQRAPICSQEEGRGRLRHETVKERQVEPVTQAQEEEDKAAVFIQSKYRGYKRRQQLRKDKMSSFKHQRIVTTPTEVARNTHNLYSYPTKHEEINNIKKKDNKDSKATSEREACGLAIFSKQISKLSEEYFILQKKLNEMILSQQLKSLYLGVSHHKPINRRVSSQQCLSGVCKGEEPKILRPPRRPRKPKTLNNPEDSTYYYLLHKSIQEEKRRPRKDSQGKLLDLEDFYYKEFLPSRSGPKEHSPSLRERRPQQELQNQCIKANERCWAAESPEKEEEREPAANPYDFRRLLRKTSQRRRLVQQS

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
73	Phosphorylation	YNILKALSDHPNVVR HHHHHHHCCCCCEEE	38.44	-
82	Phosphorylation	HPNVVRFYGIYFKKD CCCEEEEEEEEEECC	7.64	-
85	Phosphorylation	VVRFYGIYFKKDKVN EEEEEEEEEECCCCC	12.65	-
177	Phosphorylation	GVSAQLTSTRHRRNT CCEEEECCCCCCCCC	31.84	-
178	Phosphorylation	VSAQLTSTRHRRNTS CEEEECCCCCCCCCC	25.84	-
184	Phosphorylation	STRHRRNTSVGTPFW CCCCCCCCCCCCCCC	23.99	-
188	Phosphorylation	RRNTSVGTPFWMAPE CCCCCCCCCCCCCHH	17.10	-
288	Phosphorylation	LLQHKFITQIEGKDV HHHHHHHHHCCCCCH	26.99	22468782
302	Phosphorylation	VMLQKQLTEFIGIHQ HHHHHHHHHHHCHHH	26.76	-
335	Phosphorylation	NFNRPLISNLKDVDD CCCCCCHHCCCCHHH	43.74	25690035
399	Ubiquitination	SKLYIGSKRTASPPH CEEECCCCCCCCCCE	48.86	-
484	Phosphorylation	CTIINDNSSRFGKYL CEEECCCCCCCCCEE	26.25	29514088
485	Phosphorylation	TIINDNSSRFGKYLE EEECCCCCCCCCEEE	37.57	29514088
509	Phosphorylation	VGAQISEYLLEKSRV CHHHHHHHHHHHCCH	15.14	22817900
513	Ubiquitination	ISEYLLEKSRVIHQA HHHHHHHHCCHHHHH	43.46	29901268
688	Phosphorylation	TLYGRLFSWIVNCIN HHHHHHHHHHHHHHH	22.08	-
696	Phosphorylation	WIVNCINSLLKHDSS HHHHHHHHHHCCCCC	18.37	24719451
838	Phosphorylation	HYAGKVLYNASGFLA CCCCCHHCCCCCHHH	16.21	27642862
841	Phosphorylation	GKVLYNASGFLAKNR CCHHCCCCCHHHCCC	26.83	29978859
853	Phosphorylation	KNRDTLPTDIVLLLR CCCCCCCCCEEEEEE	41.28	-
865	Phosphorylation	LLRSSDNSVIRQLVN EEECCCCHHHHHHHC	24.74	23025827
908	Phosphorylation	INLAKGDTGEATRHA HHHHCCCHHHHHHHH	45.66	-
919	Phosphorylation	TRHARETTNMKTQTV HHHHHHHCCCCHHHH	28.67	-
1125	Phosphorylation	TSDQEFDYKKNFENT CCCCCCCHHHHCCCH	29.23	19702290
1167	Phosphorylation	SVSVVKTSTFKPEEE CEEEEECCCCCCHHH	26.57	-
1279	Phosphorylation	PWLAENETSFKKTLE CCCCCCCCCCCHHCC	51.55	-
1280	Phosphorylation	WLAENETSFKKTLEP CCCCCCCCCCHHCCC	28.96	-
1306	Acetylation	NSMEKEKKTSVVTQR HHHHHHHCCCEEEEC	47.31	30590621
1355	Phosphorylation	KAAVFIQSKYRGYKR HHHHHHHHHHHCHHH	27.17	22817900
1394	Phosphorylation	ARNTHNLYSYPTKHE HHCCCCCCCCCCCHH	16.10	-
1396	Phosphorylation	NTHNLYSYPTKHEEI CCCCCCCCCCCHHHH	11.02	-
1429	Phosphorylation	ACGLAIFSKQISKLS HHHHHHHHHHHHHHC	19.96	24719451
1452	Phosphorylation	KLNEMILSQQLKSLY HHHHHHHHHHHHHHH	12.64	30108239
1459	Phosphorylation	SQQLKSLYLGVSHHK HHHHHHHHHCCCCCC	14.43	22817900
1547	Phosphorylation	YYKEFLPSRSGPKEH HHHHHCCCCCCCCCC	41.02	22210691
1555	Phosphorylation	RSGPKEHSPSLRERR CCCCCCCCCCHHHHC	19.78	24719451
1557	Phosphorylation	GPKEHSPSLRERRPQ CCCCCCCCHHHHCCH	42.97	20068231

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
178	T	Phosphorylation	Kinase	MYO3A	Q8NEV4	PSP
184	T	Phosphorylation	Kinase	MYO3A	Q8NEV4	PSP
188	T	Phosphorylation	Kinase	MYO3A	Q8NEV4	PSP
908	T	Phosphorylation	Kinase	MYO3A	Q8NEV4	PSP
919	T	Phosphorylation	Kinase	MYO3A	Q8NEV4	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of MYO3A_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 MYO3A_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference	Domain-Domain Interactions
Oops, there are no PPI records of MYO3A_HUMAN !!

Drug and Disease Associations

Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607101	Deafness, autosomal recessive, 30 (DFNB30)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.

Regulatory Network of MYO3A_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Large-scale characterization of HeLa cell nuclear phosphoproteins."; Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1355, AND MASSSPECTROMETRY.	15302935 [Abstract]