CSRP3_HUMAN - dbPTM
CSRP3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CSRP3_HUMAN
UniProt AC P50461
Protein Name Cysteine and glycine-rich protein 3
Gene Name CSRP3
Organism Homo sapiens (Human).
Sequence Length 194
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, cytoskeleton . Cytoplasm, myofibril, sarcomere, Z line . Cytoplasm, myofibril, sarcomere . Nucleocytoplasmic shuttling protein. Mainly cytoplasmic. In the Z line, found associated with GLRX3 (By similarity).
Isoform
Protein Description Positive regulator of myogenesis. Acts as cofactor for myogenic bHLH transcription factors such as MYOD1, and probably MYOG and MYF6. Enhances the DNA-binding activity of the MYOD1:TCF3 isoform E47 complex and may promote formation of a functional MYOD1:TCF3 isoform E47:MEF2A complex involved in myogenesis (By similarity). Plays a crucial and specific role in the organization of cytosolic structures in cardiomyocytes. Could play a role in mechanical stretch sensing. May be a scaffold protein that promotes the assembly of interacting proteins at Z-line structures. It is essential for calcineurin anchorage to the Z line. Required for stress-induced calcineurin-NFAT activation (By similarity). The role in regulation of cytoskeleton dynamics by association with CFL2 is reported conflictingly: Shown to enhance CFL2-mediated F-actin depolymerization dependent on the CSRP3:CFL2 molecular ratio, and also shown to reduce the ability of CLF1 and CFL2 to enhance actin depolymerization. [PubMed: 19752190]
Protein Sequence MPNWGGGAKCGACEKTVYHAEEIQCNGRSFHKTCFHCMACRKALDSTTVAAHESEIYCKVCYGRRYGPKGIGYGQGAGCLSTDTGEHLGLQFQQSPKPARSVTTSNPSKFTAKFGESEKCPRCGKSVYAAEKVMGGGKPWHKTCFRCAICGKSLESTNVTDKDGELYCKVCYAKNFGPTGIGFGGLTQQVEKKE
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
16PhosphorylationKCGACEKTVYHAEEI
CCCCCCCEEEECCEE
12.19-
18PhosphorylationGACEKTVYHAEEIQC
CCCCCEEEECCEEEE
10.67-
54PhosphorylationTTVAAHESEIYCKVC
CCEEEECCCEEEEEE
21.30-
57PhosphorylationAAHESEIYCKVCYGR
EEECCCEEEEEECCC
5.12-
69AcetylationYGRRYGPKGIGYGQG
CCCCCCCCCCCCCCC
59.819329223
73PhosphorylationYGPKGIGYGQGAGCL
CCCCCCCCCCCCCEE
12.3522673903
81PhosphorylationGQGAGCLSTDTGEHL
CCCCCEEECCCCCCC
28.4526437602
82PhosphorylationQGAGCLSTDTGEHLG
CCCCEEECCCCCCCE
25.3222673903
84PhosphorylationAGCLSTDTGEHLGLQ
CCEEECCCCCCCEEE
44.5522673903
95PhosphorylationLGLQFQQSPKPARSV
CEEEECCCCCCCCCC
24.9019764811
101PhosphorylationQSPKPARSVTTSNPS
CCCCCCCCCCCCCHH
26.3926437602
103PhosphorylationPKPARSVTTSNPSKF
CCCCCCCCCCCHHHE
26.2526437602
108PhosphorylationSVTTSNPSKFTAKFG
CCCCCCHHHEEEECC
44.6526437602
126PhosphorylationKCPRCGKSVYAAEKV
CCCCCCCCCHHHHHH
12.9726437602
128PhosphorylationPRCGKSVYAAEKVMG
CCCCCCCHHHHHHHC
13.7426437602
132UbiquitinationKSVYAAEKVMGGGKP
CCCHHHHHHHCCCCC
32.56-
153PhosphorylationRCAICGKSLESTNVT
EHHHCCCCEECCCCC
23.7423879269
156PhosphorylationICGKSLESTNVTDKD
HCCCCEECCCCCCCC
30.4926437602
167PhosphorylationTDKDGELYCKVCYAK
CCCCCCEEEEEEEEE
5.9728102081
172PhosphorylationELYCKVCYAKNFGPT
CEEEEEEEEECCCCC
24.4923879269

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 CSRP3_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CSRP3_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 CSRP3_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LDHD_HUMANLDHDphysical
12127981
MYOD1_HUMANMYOD1genetic
9234731
MYOD1_HUMANMYOD1physical
9234731
MYF6_HUMANMYF6physical
9234731
MYOG_HUMANMYOGphysical
9234731
HDAC4_HUMANHDAC4physical
18250163
KLF5_HUMANKLF5physical
22584587

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
607482Cardiomyopathy, dilated 1M (CMD1M)
612124Cardiomyopathy, familial hypertrophic 12 (CMH12)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CSRP3_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP