MYL1_HUMAN - dbPTM
MYL1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MYL1_HUMAN
UniProt AC P05976
Protein Name Myosin light chain 1/3, skeletal muscle isoform
Gene Name MYL1
Organism Homo sapiens (Human).
Sequence Length 194
Subcellular Localization
Protein Description Regulatory light chain of myosin. Does not bind calcium..
Protein Sequence MAPKKDVKKPVAAAAAAPAPAPAPAPAPAPAKPKEEKIDLSAIKIEFSKEQQDEFKEAFLLFDRTGDSKITLSQVGDVLRALGTNPTNAEVRKVLGNPSNEELNAKKIEFEQFLPMMQAISNNKDQATYEDFVEGLRVFDKEGNGTVMGAELRHVLATLGEKMKEEEVEALMAGQEDSNGCINYEAFVKHIMSI
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
2 (in isoform 2)Acetylation-25.31-
2Methylation------MAPKKDVKK
------CCCHHHCCH
25.31-
41PhosphorylationKEEKIDLSAIKIEFS
CHHHCCHHEEECEEC
24.9726437602
65PhosphorylationAFLLFDRTGDSKITL
HHHHEECCCCCCEEH
47.3819764811
68PhosphorylationLFDRTGDSKITLSQV
HEECCCCCCEEHHHH
27.5719764811
71PhosphorylationRTGDSKITLSQVGDV
CCCCCCEEHHHHHHH
24.8826437602
73PhosphorylationGDSKITLSQVGDVLR
CCCCEEHHHHHHHHH
17.7320068231
84PhosphorylationDVLRALGTNPTNAEV
HHHHHHCCCCCCHHH
38.5826437602
87PhosphorylationRALGTNPTNAEVRKV
HHHCCCCCCHHHHHH
49.4826437602
97UbiquitinationEVRKVLGNPSNEELN
HHHHHHCCCCHHHHH
32.4421890473
97UbiquitinationEVRKVLGNPSNEELN
HHHHHHCCCCHHHHH
32.4421890473
99PhosphorylationRKVLGNPSNEELNAK
HHHHCCCCHHHHHHC
61.9619764811
121PhosphorylationLPMMQAISNNKDQAT
HHHHHHHHCCCCCCC
37.0520068231
141UbiquitinationEGLRVFDKEGNGTVM
HHEEEEEECCCCEEE
56.9323000965
141AcetylationEGLRVFDKEGNGTVM
HHEEEEEECCCCEEE
56.9321466224
146PhosphorylationFDKEGNGTVMGAELR
EEECCCCEEEHHHHH
16.0026437602
158PhosphorylationELRHVLATLGEKMKE
HHHHHHHHHHHHHCH
31.0026437602
162AcetylationVLATLGEKMKEEEVE
HHHHHHHHHCHHHHH
54.1719847527
178PhosphorylationLMAGQEDSNGCINYE
HHCCCCCCCCCCCHH
34.0819764811
181S-nitrosylationGQEDSNGCINYEAFV
CCCCCCCCCCHHHHH
1.8222178444
181S-nitrosocysteineGQEDSNGCINYEAFV
CCCCCCCCCCHHHHH
1.82-
184PhosphorylationDSNGCINYEAFVKHI
CCCCCCCHHHHHHHH
6.68-

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
-KUbiquitinationE3 ubiquitin ligaseTRIM63Q969Q1
PMID:22199232

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MYL1_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 MYL1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SEPT2_HUMANSEPT2physical
22939629
NU107_HUMANNUP107physical
22939629
SAE2_HUMANUBA2physical
22939629
IQGA1_HUMANIQGAP1physical
18587628

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 MYL1_HUMAN

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Related Literatures of Post-Translational Modification

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