CANB1_HUMAN - dbPTM
CANB1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CANB1_HUMAN
UniProt AC P63098
Protein Name Calcineurin subunit B type 1
Gene Name PPP3R1
Organism Homo sapiens (Human).
Sequence Length 170
Subcellular Localization Cytoplasm, cytosol . Cell membrane . Cell membrane, sarcolemma . Cell membrane
Lipid-anchor . Translocates from the cytosol to the sarcolemma in a CIB1-dependent manner during cardiomyocyte hypertrophy.
Protein Description Regulatory subunit of calcineurin, a calcium-dependent, calmodulin stimulated protein phosphatase. Confers calcium sensitivity..
Protein Sequence MGNEASYPLEMCSHFDADEIKRLGKRFKKLDLDNSGSLSVEEFMSLPELQQNPLVQRVIDIFDTDGNGEVDFKEFIEGVSQFSVKGDKEQKLRFAFRIYDMDKDGYISNGELFQVLKMMVGNNLKDTQLQQIVDKTIINADKDGDGRISFEEFCAVVGGLDIHKKMVVDV
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
2Myristoylation------MGNEASYPL
------CCCCCCCCH
40.4625255805
7Phosphorylation-MGNEASYPLEMCSH
-CCCCCCCCHHHHCC
20.9124719451
13PhosphorylationSYPLEMCSHFDADEI
CCCHHHHCCCCHHHH
26.3624719451
29UbiquitinationRLGKRFKKLDLDNSG
HHHHHHHHCCCCCCC
44.5121906983
35PhosphorylationKKLDLDNSGSLSVEE
HHCCCCCCCCCCHHH
29.4425159151
37PhosphorylationLDLDNSGSLSVEEFM
CCCCCCCCCCHHHHH
19.7925159151
39PhosphorylationLDNSGSLSVEEFMSL
CCCCCCCCHHHHHCC
29.2218669648
45PhosphorylationLSVEEFMSLPELQQN
CCHHHHHCCHHHHCC
46.2027251275
64PhosphorylationRVIDIFDTDGNGEVD
HHHEEECCCCCCEEC
34.7520068231
85UbiquitinationGVSQFSVKGDKEQKL
CCCEEEECCCHHHHE
61.2632015554
103UbiquitinationFRIYDMDKDGYISNG
EEEEECCCCCCCCHH
46.55-
106PhosphorylationYDMDKDGYISNGELF
EECCCCCCCCHHHHH
16.0021082442
108PhosphorylationMDKDGYISNGELFQV
CCCCCCCCHHHHHHH
30.23-
125UbiquitinationMMVGNNLKDTQLQQI
HHHCCCCCHHHHHHH
61.9321906983
135UbiquitinationQLQQIVDKTIINADK
HHHHHHCCEEECCCC
30.6329967540
142UbiquitinationKTIINADKDGDGRIS
CEEECCCCCCCCCCC
62.2929967540
164UbiquitinationVGGLDIHKKMVVDV-
HCCCCCCCCCEECC-
42.7932015554
165UbiquitinationGGLDIHKKMVVDV--
CCCCCCCCCEECC--
23.8221906983

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 CANB1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CANB1_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 CANB1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CABP2_HUMANCABP2physical
11108966
CABP5_HUMANCABP5physical
11108966
CABP1_HUMANCABP1physical
11108966
PSA7_HUMANPSMA7physical
21256111
PDE4D_HUMANPDE4Dphysical
20647544
PP2BA_HUMANPPP3CAphysical
22939629

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 CANB1_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP