MLC1_YEAST - dbPTM
MLC1_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MLC1_YEAST
UniProt AC P53141
Protein Name Myosin light chain 1
Gene Name MLC1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 149
Subcellular Localization Bud neck . Bud tip . Concentrates to sites of polarized growth, namely to the incipient bud site in G1, to the bud tip during S and G2 phases of the cell cycle and to the bud neck during cytokinesis.
Protein Description Essential light chain for the class II conventional myosin MYO1. Acts also as light chain for the class V unconventional myosin MYO2 and for IQG1. Involved in the assembly of the contractile actomyosin ring at the bud neck during cytokinesis by recruiting IQG1 to the bud neck. Also required for chitin and MYO2-dependent secretory vesicle deposition to the center of the bud neck for septum formation. May stabilize MYO2 by binding to its IQ domains. Its major function is probably not to regulate MYO1 activity, but rather to coordinate actin ring formation and targeted membrane deposition during cytokinesis via its interactions with MYO1, IQG1 and MYO2..
Protein Sequence MSATRANKDIFTLFDKKGQGAIAKDSLGDYLRAIGYNPTNQLVQDIINADSSLRDASSLTLDQITGLIEVNEKELDATTKAKTEDFVKAFQVFDKESTGKVSVGDLRYMLTGLGEKLTDAEVDELLKGVEVDSNGEIDYKKFIEDVLRQ
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
2Phosphorylation------MSATRANKD
------CCCCCCCCC
38.0430377154
4Phosphorylation----MSATRANKDIF
----CCCCCCCCCCE
24.0230377154
8AcetylationMSATRANKDIFTLFD
CCCCCCCCCCEECCC
51.7424489116
16AcetylationDIFTLFDKKGQGAIA
CCEECCCCCCCCCHH
52.0124489116
17AcetylationIFTLFDKKGQGAIAK
CEECCCCCCCCCHHH
59.3124489116
24AcetylationKGQGAIAKDSLGDYL
CCCCCHHHCCHHHHH
41.5624489116
39PhosphorylationRAIGYNPTNQLVQDI
HHCCCCCHHHHHHHH
31.7724909858
51PhosphorylationQDIINADSSLRDASS
HHHHHCCCHHHHCHH
28.9430377154
57PhosphorylationDSSLRDASSLTLDQI
CCHHHHCHHCCHHHH
30.1228132839
58PhosphorylationSSLRDASSLTLDQIT
CHHHHCHHCCHHHHC
27.3928132839
60PhosphorylationLRDASSLTLDQITGL
HHHCHHCCHHHHCCE
30.1829734811
73AcetylationGLIEVNEKELDATTK
CEEEECHHHCCCCCC
59.3724489116
822-HydroxyisobutyrylationLDATTKAKTEDFVKA
CCCCCCCCHHHHHHH
54.74-
83PhosphorylationDATTKAKTEDFVKAF
CCCCCCCHHHHHHHH
45.7225752575
88UbiquitinationAKTEDFVKAFQVFDK
CCHHHHHHHHHEECC
43.4024961812
95AcetylationKAFQVFDKESTGKVS
HHHHEECCCCCCCEE
41.9424489116
102PhosphorylationKESTGKVSVGDLRYM
CCCCCCEEHHHHHHH
24.7030377154
108PhosphorylationVSVGDLRYMLTGLGE
EEHHHHHHHHHCCHH
12.0828889911
111PhosphorylationGDLRYMLTGLGEKLT
HHHHHHHHCCHHHCC
17.5228889911
116UbiquitinationMLTGLGEKLTDAEVD
HHHCCHHHCCHHHHH
55.6922106047
133PhosphorylationLKGVEVDSNGEIDYK
HCCCEECCCCCCCHH
52.4922369663
139PhosphorylationDSNGEIDYKKFIEDV
CCCCCCCHHHHHHHH
23.0322369663

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 MLC1_YEAST !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MLC1_YEAST !!

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 MLC1_YEAST !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MYO2_YEASTMYO2physical
12456647
SEC4_YEASTSEC4physical
12456647
IQG1_YEASTIQG1physical
11082046
MYO1_YEASTMYO1physical
11082046
MYO2_YEASTMYO2physical
12351846
MYO2_YEASTMYO2physical
12554638
MYO1_YEASTMYO1physical
15210731
MYO2_YEASTMYO2physical
16120677
MYO1_YEASTMYO1genetic
12456647
MYO2_YEASTMYO2genetic
12456647
MYO2_YEASTMYO2genetic
9700160
MYO4_YEASTMYO4physical
16554755
CALM_YEASTCMD1physical
16554755
HSP42_YEASTHSP42physical
16554755
RV167_YEASTRVS167physical
16554755
PIL1_YEASTPIL1physical
16554755
CORO_YEASTCRN1physical
16554755
IF4E_YEASTCDC33physical
16554755
MYO2_YEASTMYO2physical
16554755
LSP1_YEASTLSP1physical
16554755
BSP1_YEASTBSP1physical
16554755
MYO2_YEASTMYO2physical
16468996
IQG1_YEASTIQG1physical
10873803
MLC1_YEASTMLC1physical
18719252
MYO2_YEASTMYO2physical
18221262
MYO1_YEASTMYO1physical
21757693
MYO2_YEASTMYO2physical
21757693
IQG1_YEASTIQG1physical
24895401
CYK2_YEASTHOF1physical
24895401
IQGA1_HUMANIQGAP1physical
18587628
K1683_HUMANKIAA1683physical
27107014

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MLC1_YEAST

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Related Literatures of Post-Translational Modification

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