CHP1_HUMAN - dbPTM
CHP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CHP1_HUMAN
UniProt AC Q99653
Protein Name Calcineurin B homologous protein 1
Gene Name CHP1
Organism Homo sapiens (Human).
Sequence Length 195
Subcellular Localization Nucleus . Cytoplasm . Cytoplasm, cytoskeleton . Endomembrane system . Endoplasmic reticulum-Golgi intermediate compartment . Endoplasmic reticulum . Cell membrane . Membrane
Lipid-anchor . Localizes in cytoplasmic compartments in dividing cells. Lo
Protein Description Calcium-binding protein involved in different processes such as regulation of vesicular trafficking, plasma membrane Na(+)/H(+) exchanger and gene transcription. Involved in the constitutive exocytic membrane traffic. Mediates the association between microtubules and membrane-bound organelles of the endoplasmic reticulum and Golgi apparatus and is also required for the targeting and fusion of transcytotic vesicles (TCV) with the plasma membrane. Functions as an integral cofactor in cell pH regulation by controlling plasma membrane-type Na(+)/H(+) exchange activity. Affects the pH sensitivity of SLC9A1/NHE1 by increasing its sensitivity at acidic pH. Required for the stabilization and localization of SLC9A1/NHE1 at the plasma membrane. Inhibits serum- and GTPase-stimulated Na(+)/H(+) exchange. Plays a role as an inhibitor of ribosomal RNA transcription by repressing the nucleolar UBF1 transcriptional activity. May sequester UBF1 in the nucleoplasm and limit its translocation to the nucleolus. Associates to the ribosomal gene promoter. Acts as a negative regulator of the calcineurin/NFAT signaling pathway. Inhibits NFAT nuclear translocation and transcriptional activity by suppressing the calcium-dependent calcineurin phosphatase activity. Also negatively regulates the kinase activity of the apoptosis-induced kinase STK17B. Inhibits both STK17B auto- and substrate-phosphorylations in a calcium-dependent manner..
Protein Sequence MGSRASTLLRDEELEEIKKETGFSHSQITRLYSRFTSLDKGENGTLSREDFQRIPELAINPLGDRIINAFFPEGEDQVNFRGFMRTLAHFRPIEDNEKSKDVNGPEPLNSRSNKLHFAFRLYDLDKDEKISRDELLQVLRMMVGVNISDEQLGSIADRTIQEADQDGDSAISFTEFVKVLEKVDVEQKMSIRFLH
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
2N-myristoyl glycine------MGSRASTLL
------CCCHHHHHC
26.32-
2Myristoylation------MGSRASTLL
------CCCHHHHHC
26.3225255805
6Phosphorylation--MGSRASTLLRDEE
--CCCHHHHHCCHHH
20.6228348404
7Phosphorylation-MGSRASTLLRDEEL
-CCCHHHHHCCHHHH
28.9128355574
10MethylationSRASTLLRDEELEEI
CHHHHHCCHHHHHHH
53.02-
192-HydroxyisobutyrylationEELEEIKKETGFSHS
HHHHHHHHHHCCCHH
67.19-
19UbiquitinationEELEEIKKETGFSHS
HHHHHHHHHHCCCHH
67.19-
21PhosphorylationLEEIKKETGFSHSQI
HHHHHHHHCCCHHHH
53.0224719451
24PhosphorylationIKKETGFSHSQITRL
HHHHHCCCHHHHHHH
24.4723663014
26PhosphorylationKETGFSHSQITRLYS
HHHCCCHHHHHHHHH
23.2923663014
29PhosphorylationGFSHSQITRLYSRFT
CCCHHHHHHHHHHHH
13.6423663014
32PhosphorylationHSQITRLYSRFTSLD
HHHHHHHHHHHHCCC
8.4324719451
33PhosphorylationSQITRLYSRFTSLDK
HHHHHHHHHHHCCCC
26.0524719451
37PhosphorylationRLYSRFTSLDKGENG
HHHHHHHCCCCCCCC
31.68-
40UbiquitinationSRFTSLDKGENGTLS
HHHHCCCCCCCCCCC
73.7121906983
402-HydroxyisobutyrylationSRFTSLDKGENGTLS
HHHHCCCCCCCCCCC
73.71-
86PhosphorylationNFRGFMRTLAHFRPI
CHHHHHHHHHHCCCC
19.2620068231
98UbiquitinationRPIEDNEKSKDVNGP
CCCCCCCCCCCCCCC
69.89-
100UbiquitinationIEDNEKSKDVNGPEP
CCCCCCCCCCCCCCC
76.4221906983
114UbiquitinationPLNSRSNKLHFAFRL
CCCCCCCCCEEEEEE
44.58-
126UbiquitinationFRLYDLDKDEKISRD
EEECCCCCCCCCCHH
75.08-
1262-HydroxyisobutyrylationFRLYDLDKDEKISRD
EEECCCCCCCCCCHH
75.08-
1292-HydroxyisobutyrylationYDLDKDEKISRDELL
CCCCCCCCCCHHHHH
56.99-
154PhosphorylationISDEQLGSIADRTIQ
CCHHHHHHHHHHHHH
24.16-
178UbiquitinationISFTEFVKVLEKVDV
EEHHHHHHHHHHCCH
46.5621906983
182UbiquitinationEFVKVLEKVDVEQKM
HHHHHHHHCCHHHHH
39.3021906983
1822-HydroxyisobutyrylationEFVKVLEKVDVEQKM
HHHHHHHHCCHHHHH
39.30-
188UbiquitinationEKVDVEQKMSIRFLH
HHCCHHHHHCCEECC
22.55-

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 CHP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CHP1_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 CHP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
SL9A1_HUMANSLC9A1physical
12576672
SL9A2_HUMANSLC9A2physical
12576672
SL9A3_HUMANSLC9A3physical
12576672
SL9A4_HUMANSLC9A4physical
12576672
SL9A5_HUMANSLC9A5physical
12576672
SL9A1_HUMANSLC9A1physical
8901634
SL9A1_HUMANSLC9A1physical
11350981

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
D00107 Tacrolimus hydrate (JP16); Tacrolimus (USAN/INN); Prograf (TN); Protopic (TN)
D00184 Ciclosporin (JP16); Cyclosporine (USP); Gengraf (TN); Neoral (TN); Restasis (TN); Sandimmune (TN)
D05480 Pimecrolimus (JAN/USAN/INN); Elidel (TN)
D08556 Tacrolimus (INN); Prograf (TN)
D09033 Voclosporin (USAN/INN)
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CHP1_HUMAN

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Related Literatures of Post-Translational Modification

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