MLRV_HUMAN - dbPTM
MLRV_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MLRV_HUMAN
UniProt AC P10916
Protein Name Myosin regulatory light chain 2, ventricular/cardiac muscle isoform {ECO:0000305}
Gene Name MYL2 {ECO:0000312|HGNC:HGNC:7583}
Organism Homo sapiens (Human).
Sequence Length 166
Subcellular Localization Cytoplasm, myofibril, sarcomere, A band .
Protein Description Contractile protein that plays a role in heart development and function (By similarity). Following phosphorylation, plays a role in cross-bridge cycling kinetics and cardiac muscle contraction by increasing myosin lever arm stiffness and promoting myosin head diffusion; as a consequence of the increase in maximum contraction force and calcium sensitivity of contraction force. These events altogether slow down myosin kinetics and prolong duty cycle resulting in accumulated myosins being cooperatively recruited to actin binding sites to sustain thin filament activation as a means to fine-tune myofilament calcium sensitivity to force (By similarity). During cardiogenesis plays an early role in cardiac contractility by promoting cardiac myofibril assembly (By similarity)..
Protein Sequence MAPKKAKKRAGGANSNVFSMFEQTQIQEFKEAFTIMDQNRDGFIDKNDLRDTFAALGRVNVKNEEIDEMIKEAPGPINFTVFLTMFGEKLKGADPEETILNAFKVFDPEGKGVLKADYVREMLTTQAERFSKEEVDQMFAAFPPDVTGNLDYKNLVHIITHGEEKD
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
2Methylation------MAPKKAKKR
------CCCHHHHHH
25.31-
14Deamidated asparagineKKRAGGANSNVFSMF
HHHCCCCCCCHHHHH
37.07-
14DeamidationKKRAGGANSNVFSMF
HHHCCCCCCCHHHHH
37.0720445002
15PhosphorylationKRAGGANSNVFSMFE
HHCCCCCCCHHHHHH
33.5620038585
19PhosphorylationGANSNVFSMFEQTQI
CCCCCHHHHHHHHHH
20.489418861
24PhosphorylationVFSMFEQTQIQEFKE
HHHHHHHHHHHHHHH
22.0526437602
34PhosphorylationQEFKEAFTIMDQNRD
HHHHHHHHHHCCCCC
23.5726437602
52PhosphorylationDKNDLRDTFAALGRV
CHHHHHHHHHHHCCC
14.56-
80PhosphorylationAPGPINFTVFLTMFG
CCCCEEEEEEEECCC
13.0822673903
98PhosphorylationKGADPEETILNAFKV
CCCCHHHHHHHHHHH
29.1526437602
104AcetylationETILNAFKVFDPEGK
HHHHHHHHHCCCCCC
39.31160891
111AcetylationKVFDPEGKGVLKADY
HHCCCCCCCCCCHHH
44.1530584983
118PhosphorylationKGVLKADYVREMLTT
CCCCCHHHHHHHHHH
13.2819764811
124PhosphorylationDYVREMLTTQAERFS
HHHHHHHHHHHHHCC
18.6226437602
125PhosphorylationYVREMLTTQAERFSK
HHHHHHHHHHHHCCH
23.0926437602
152PhosphorylationDVTGNLDYKNLVHII
CCCCCCCHHCCEEEE
12.63-
153AcetylationVTGNLDYKNLVHIIT
CCCCCCHHCCEEEEC
43.3930584989
160PhosphorylationKNLVHIITHGEEKD-
HCCEEEECCCCCCC-
24.1926437602
165AcetylationIITHGEEKD------
EECCCCCCC------
65.528010075

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
15SPhosphorylationKinaseDAPK3O43293
Uniprot
15SPhosphorylationKinaseMYLKQ15746
GPS
15SPhosphorylationKinaseROCK2O75116
PSP
118YPhosphorylationKinasePKMP14618
PSP
-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 MLRV_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 MLRV_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
UBP6_HUMANUSP6physical
16555005
NHP2_HUMANNHP2physical
21988832
MYL5_HUMANMYL5physical
28514442
MYO5B_HUMANMYO5Bphysical
28514442
MYO19_HUMANMYO19physical
28514442
ASPM_HUMANASPMphysical
28514442
MYO5A_HUMANMYO5Aphysical
28514442
IL36G_HUMANIL36Gphysical
28514442
KPYM_HUMANPKMphysical
25412762

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608758Cardiomyopathy, familial hypertrophic 10 (CMH10)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of MLRV_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP