MYL6_HUMAN - dbPTM
MYL6_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYL6_HUMAN
UniProt AC P60660
Protein Name Myosin light polypeptide 6
Gene Name MYL6
Organism Homo sapiens (Human).
Sequence Length 151
Subcellular Localization
Protein Description Regulatory light chain of myosin. Does not bind calcium..
Protein Sequence MCDFTEDQTAEFKEAFQLFDRTGDGKILYSQCGDVMRALGQNPTNAEVLKVLGNPKSDEMNVKVLDFEHFLPMLQTVAKNKDQGTYEDYVEGLRVFDKEGNGTVMGAEIRHVLVTLGEKMTEEEVEMLVAGHEDSNGCINYEAFVRHILSG
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
2Acetylation------MCDFTEDQT
------CCCCCCCCC		6.2319413330
13UbiquitinationEDQTAEFKEAFQLFD
CCCCHHHHHHHHHHH		39.3729967540
21MethylationEAFQLFDRTGDGKIL
HHHHHHHCCCCCCEE		33.02115484223
22PhosphorylationAFQLFDRTGDGKILY
HHHHHHCCCCCCEEE		41.2825159151
26 (in isoform 2)Ubiquitination-33.9921890473
26 (in isoform 1)Ubiquitination-33.9921890473
26AcetylationFDRTGDGKILYSQCG
HHCCCCCCEEEEEHH		33.9923954790
26UbiquitinationFDRTGDGKILYSQCG
HHCCCCCCEEEEEHH		33.9923000965
29PhosphorylationTGDGKILYSQCGDVM
CCCCCEEEEEHHHHH		10.5221945579
30PhosphorylationGDGKILYSQCGDVMR
CCCCEEEEEHHHHHH		18.6221945579
32GlutathionylationGKILYSQCGDVMRAL
CCEEEEEHHHHHHHC		4.0622555962
36SulfoxidationYSQCGDVMRALGQNP
EEEHHHHHHHCCCCC		2.1730846556
44PhosphorylationRALGQNPTNAEVLKV
HHCCCCCCCHHHHHH		55.3921712546
50AcetylationPTNAEVLKVLGNPKS
CCCHHHHHHHCCCCC		40.3622638923
50NeddylationPTNAEVLKVLGNPKS
CCCHHHHHHHCCCCC		40.3632015554
50 (in isoform 1)Ubiquitination-40.3621890473
50UbiquitinationPTNAEVLKVLGNPKS
CCCHHHHHHHCCCCC		40.3623000965
50 (in isoform 2)Ubiquitination-40.3621890473
56UbiquitinationLKVLGNPKSDEMNVK
HHHHCCCCCCCCCEE		74.6423000965
56 (in isoform 1)Ubiquitination-74.6421890473
56SumoylationLKVLGNPKSDEMNVK
HHHHCCCCCCCCCEE		74.64-
56MalonylationLKVLGNPKSDEMNVK
HHHHCCCCCCCCCEE		74.6426320211
56AcetylationLKVLGNPKSDEMNVK
HHHHCCCCCCCCCEE		74.6423236377
56SumoylationLKVLGNPKSDEMNVK
HHHHCCCCCCCCCEE		74.64-
56 (in isoform 2)Ubiquitination-74.6421890473
57PhosphorylationKVLGNPKSDEMNVKV
HHHCCCCCCCCCEEE		39.8123401153
60SulfoxidationGNPKSDEMNVKVLDF
CCCCCCCCCEEEECH		9.3130846556
63UbiquitinationKSDEMNVKVLDFEHF
CCCCCCEEEECHHHH		31.88639865
63 (in isoform 2)Ubiquitination-31.8821890473
63 (in isoform 1)Ubiquitination-31.8821890473
73SulfoxidationDFEHFLPMLQTVAKN
CHHHHHHHHHHHHHC		4.7530846556
79 (in isoform 2)Ubiquitination-61.2621890473
79AcetylationPMLQTVAKNKDQGTY
HHHHHHHHCCCCCCH		61.2625953088
79 (in isoform 1)Ubiquitination-61.2621890473
79UbiquitinationPMLQTVAKNKDQGTY
HHHHHHHHCCCCCCH		61.2623000965
81AcetylationLQTVAKNKDQGTYED
HHHHHHCCCCCCHHH		51.2019608861
81 (in isoform 1)Ubiquitination-51.2021890473
81UbiquitinationLQTVAKNKDQGTYED
HHHHHHCCCCCCHHH		51.2023000965
81 (in isoform 2)Ubiquitination-51.2021890473
81MalonylationLQTVAKNKDQGTYED
HHHHHHCCCCCCHHH		51.2026320211
85PhosphorylationAKNKDQGTYEDYVEG
HHCCCCCCHHHHCCE		20.3628796482
86PhosphorylationKNKDQGTYEDYVEGL
HCCCCCCHHHHCCEE		17.3923911959
89PhosphorylationDQGTYEDYVEGLRVF
CCCCHHHHCCEEEEE		6.6128674151
94MethylationEDYVEGLRVFDKEGN
HHHCCEEEEEEECCC		37.60115484215
98 (in isoform 1)Ubiquitination-56.9321890473
98 (in isoform 2)Ubiquitination-56.9321890473
98UbiquitinationEGLRVFDKEGNGTVM
CEEEEEEECCCCEEE		56.9323000965
98AcetylationEGLRVFDKEGNGTVM
CEEEEEEECCCCEEE		56.9330590603
103PhosphorylationFDKEGNGTVMGAEIR
EEECCCCEEECHHHH		16.0020068231
105SulfoxidationKEGNGTVMGAEIRHV
ECCCCEEECHHHHEE		4.1721406390
115PhosphorylationEIRHVLVTLGEKMTE
HHHEEEEECCCCCCH		25.5323911959
120SulfoxidationLVTLGEKMTEEEVEM
EEECCCCCCHHHHHH		5.0530846556
121PhosphorylationVTLGEKMTEEEVEML
EECCCCCCHHHHHHH		51.8429116813
121 (in isoform 2)Phosphorylation-51.8428450419
127SulfoxidationMTEEEVEMLVAGHED
CCHHHHHHHHHCCCC		4.3930846556
135PhosphorylationLVAGHEDSNGCINYE
HHHCCCCCCCCCCHH		31.9430266825
135 (in isoform 2)Phosphorylation-31.9430266825
141PhosphorylationDSNGCINYEAFVRHI
CCCCCCCHHHHHHHH		6.6830266825
141 (in isoform 2)Phosphorylation-6.6823663014
150PhosphorylationAFVRHILSG------
HHHHHHHCC------		41.6824719451
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 MYL6_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYL6_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 MYL6_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CPSF5_HUMANNUDT21physical
16189514
ATS12_HUMANADAMTS12physical
25416956
SAHH2_HUMANAHCYL1physical
26344197
AHNK_HUMANAHNAKphysical
26344197
CY1_HUMANCYC1physical
26344197
RAB2A_HUMANRAB2Aphysical
26344197
STMN1_HUMANSTMN1physical
26344197
TPM2_HUMANTPM2physical
26344197
MY18A_HUMANMYO18Aphysical
28514442
IQGA1_HUMANIQGAP1physical
28514442
MYH14_HUMANMYH14physical
28514442
NEB1_HUMANPPP1R9Aphysical
28514442
LIMA1_HUMANLIMA1physical
28514442
IQGA3_HUMANIQGAP3physical
28514442
RANG_HUMANRANBP1physical
28514442
MYH10_HUMANMYH10physical
28514442
MYL6B_HUMANMYL6Bphysical
28514442
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 MYL6_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50 AND LYS-81, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-29, AND MASSSPECTROMETRY.

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