CABP1_HUMAN - dbPTM
CABP1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CABP1_HUMAN
UniProt AC Q9NZU7
Protein Name Calcium-binding protein 1
Gene Name CABP1
Organism Homo sapiens (Human).
Sequence Length 370
Subcellular Localization Cytoplasm, cytoskeleton . Cytoplasm, perinuclear region . Cell membrane
Lipid-anchor
Cytoplasmic side. Golgi apparatus . Cell junction, synapse, postsynaptic cell membrane, postsynaptic density . L-CaBP1 is associated most likely with the cytoskel
Protein Description Modulates calcium-dependent activity of inositol 1,4,5-triphosphate receptors (ITPRs)(PubMed:14570872). Inhibits agonist-induced intracellular calcium signaling. [PubMed: 15980432 Enhances inactivation and does not support calcium-dependent facilitation of voltage-dependent P/Q-type calcium channels]
Protein Sequence MGGGDGAAFKRPGDGARLQRVLGLGSRREPRSLPAGGPAPRRTAPPPPGHASAGPAAMSSHIAKSESKTSLLKAAAAAASGGSRAPRHGPARDPGLPSRRLPGSCPATPQSSGDPSSRRPLCRPAPREEGARGSQRVLPQAHCRPREALPAAASRPSPSSPLPPARGRDGEERGLSPALGLRGSLRARGRGDSVPAAASEADPFLHRLRPMLSSAFGQDRSLRPEEIEELREAFREFDKDKDGYINCRDLGNCMRTMGYMPTEMELIELSQQINMNLGGHVDFDDFVELMGPKLLAETADMIGVKELRDAFREFDTNGDGEISTSELREAMRKLLGHQVGHRDIEEIIRDVDLNGDGRVDFEEFVRMMSR
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------MGGGDGAAF
------CCCCCCCCC
49.11-
2 (in isoform 1)Myristoylation-49.1110625670
2 (in isoform 2)Myristoylation-49.1110625670
4 (in isoform 1)S-palmitoylation-25.1710625670
4 (in isoform 2)S-palmitoylation-25.1710625670
31MethylationLGSRREPRSLPAGGP
CCCCCCCCCCCCCCC
46.18-
70PhosphorylationAKSESKTSLLKAAAA
HCCCCHHHHHHHHHH
35.1324719451
87DimethylationSGGSRAPRHGPARDP
HCCCCCCCCCCCCCC
46.54-
92DimethylationAPRHGPARDPGLPSR
CCCCCCCCCCCCCCC
54.51-
98PhosphorylationARDPGLPSRRLPGSC
CCCCCCCCCCCCCCC
34.77-
176PhosphorylationDGEERGLSPALGLRG
CCCCCCCCHHHCHHH
15.7928857561
180PhosphorylationRGLSPALGLRGSLRA
CCCCHHHCHHHHHHH
18.5514685260
190MethylationGSLRARGRGDSVPAA
HHHHHCCCCCCCCHH
39.94-
323PhosphorylationTNGDGEISTSELREA
CCCCCCCCHHHHHHH
22.9010625670

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 CABP1_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CABP1_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 CABP1_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CAC1C_HUMANCACNA1Cphysical
15140941
CAC1A_HUMANCACNA1Aphysical
14570872
CAC1A_HUMANCACNA1Aphysical
11865310
GRK5_HUMANGRK5physical
10625670
ITPR1_HUMANITPR1physical
12032348
UBP4_HUMANUSP4physical
28514442

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 CABP1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Regulation of InsP3 receptor activity by neuronal Ca2+-bindingproteins.";
Kasri N.N., Holmes A.M., Bultynck G., Parys J.B., Bootman M.D.,Rietdorf K., Missiaen L., McDonald F., De Smedt H., Conway S.J.,Holmes A.B., Berridge M.J., Roderick H.L.;
EMBO J. 23:312-321(2004).
Cited for: PHOSPHORYLATION AT SER-323, MUTAGENESIS OF SER-323, SUBCELLULARLOCATION, AND INTERACTION WITH ITPR1.

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