KCC1A_HUMAN - dbPTM
KCC1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID KCC1A_HUMAN
UniProt AC Q14012
Protein Name Calcium/calmodulin-dependent protein kinase type 1
Gene Name CAMK1
Organism Homo sapiens (Human).
Sequence Length 370
Subcellular Localization Cytoplasm. Nucleus. Predominantly cytoplasmic..
Protein Description Calcium/calmodulin-dependent protein kinase that operates in the calcium-triggered CaMKK-CaMK1 signaling cascade and, upon calcium influx, regulates transcription activators activity, cell cycle, hormone production, cell differentiation, actin filament organization and neurite outgrowth. Recognizes the substrate consensus sequence [MVLIF]-x-R-x(2)-[ST]-x(3)-[MVLIF]. Regulates axonal extension and growth cone motility in hippocampal and cerebellar nerve cells. Upon NMDA receptor-mediated Ca(2+) elevation, promotes dendritic growth in hippocampal neurons and is essential in synapses for full long-term potentiation (LTP) and ERK2-dependent translational activation. Downstream of NMDA receptors, promotes the formation of spines and synapses in hippocampal neurons by phosphorylating ARHGEF7/BETAPIX on 'Ser-694', which results in the enhancement of ARHGEF7 activity and activation of RAC1. Promotes neuronal differentiation and neurite outgrowth by activation and phosphorylation of MARK2 on 'Ser-91', 'Ser-92', 'Ser-93' and 'Ser-294'. Promotes nuclear export of HDAC5 and binding to 14-3-3 by phosphorylation of 'Ser-259' and 'Ser-498' in the regulation of muscle cell differentiation. Regulates NUMB-mediated endocytosis by phosphorylation of NUMB on 'Ser-276' and 'Ser-295'. Involved in the regulation of basal and estrogen-stimulated migration of medulloblastoma cells through ARHGEF7/BETAPIX phosphorylation (By similarity). Is required for proper activation of cyclin-D1/CDK4 complex during G1 progression in diploid fibroblasts. Plays a role in K(+) and ANG2-mediated regulation of the aldosterone synthase (CYP11B2) to produce aldosterone in the adrenal cortex. Phosphorylates EIF4G3/eIF4GII. In vitro phosphorylates CREB1, ATF1, CFTR, MYL9 and SYN1/synapsin I..
Protein Sequence MLGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKEALEGKEGSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAKSKWKQAFNATAVVRHMRKLQLGTSQEGQGQTASHGELLTPVAGGPAAGCCCRDCCVEPGTELSPTLPHQL
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
20PhosphorylationAEDIRDIYDFRDVLG
HHHHHHHHCHHHHHC		17.2021951684
59UbiquitinationAKEALEGKEGSMENE
HHHHHCCCCCCCHHH		49.9123707388
131PhosphorylationQVLDAVKYLHDLGIV
HHHHHHHHHHHCCCC		11.5818083107
143UbiquitinationGIVHRDLKPENLLYY
CCCCCCCCHHHCEEE		55.35-
149PhosphorylationLKPENLLYYSLDEDS
CCHHHCEEEECCCCC		8.3227642862
173PhosphorylationSKMEDPGSVLSTACG
CCCCCCCCHHHHCCC		25.8527486199
176PhosphorylationEDPGSVLSTACGTPG
CCCCCHHHHCCCCCC		16.2923401153
177PhosphorylationDPGSVLSTACGTPGY
CCCCHHHHCCCCCCC		23.0821712546
181PhosphorylationVLSTACGTPGYVAPE
HHHHCCCCCCCCCHH		17.2728857561
184PhosphorylationTACGTPGYVAPEVLA
HCCCCCCCCCHHHHC		8.4727486199
235PhosphorylationEQILKAEYEFDSPYW
HHHHHHHCCCCCCCC		27.1021951684
301PhosphorylationIKKNFAKSKWKQAFN
HHHHHHHHHHHHHHH		40.0823285258
310PhosphorylationWKQAFNATAVVRHMR
HHHHHHHHHHHHHHH		22.5328857561
323PhosphorylationMRKLQLGTSQEGQGQ
HHHCCCCCCCCCCCC		35.5128450419
324PhosphorylationRKLQLGTSQEGQGQT
HHCCCCCCCCCCCCC		25.1626657352
331PhosphorylationSQEGQGQTASHGELL
CCCCCCCCCCCCEEE		36.6328450419
333PhosphorylationEGQGQTASHGELLTP
CCCCCCCCCCEEECC		35.1028450419
339PhosphorylationASHGELLTPVAGGPA
CCCCEEECCCCCCCC		28.4828857561
360PhosphorylationDCCVEPGTELSPTLP
HCCCCCCCCCCCCCC		44.4629396449
363PhosphorylationVEPGTELSPTLPHQL
CCCCCCCCCCCCCCC		15.0323707388
365PhosphorylationPGTELSPTLPHQL--
CCCCCCCCCCCCC--		49.9328450419
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
177TPhosphorylationKinaseKCC1AQ14012
PhosphoELM
177TPhosphorylationKinaseCAMKK1Q8N5S9
Uniprot
177TPhosphorylationKinaseCAMKK2Q96RR4
Uniprot
177TPhosphorylationKinaseCAMK1-FAMILY-GPS
177TPhosphorylationKinaseCAM-KI_GROUP-PhosphoELM
-KUbiquitinationE3 ubiquitin ligaseFBXL12Q9NXK8
PMID:22199232
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
177TPhosphorylation

7641687
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 KCC1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KKCC2_HUMANCAMKK2physical
10187789
GCM1_HUMANGCM1physical
21791615
A4_HUMANAPPphysical
21832049
CDN1B_HUMANCDKN1Bphysical
23707388
CCND1_HUMANCCND1physical
23707388
CDK4_HUMANCDK4physical
23707388
MARK2_HUMANMARK2physical
17442826
BLK_HUMANBLKphysical
26186194
PPME1_HUMANPPME1physical
24841198
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 KCC1A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Human calcium-calmodulin dependent protein kinase I: cDNA cloning,domain structure and activation by phosphorylation at threonine-177 bycalcium-calmodulin dependent protein kinase I kinase.";
Haribabu B., Hook S.S., Selbert M.A., Goldstein E.G., Tomhave E.D.,Edelman A.M., Snyderman R., Means A.R.;
EMBO J. 14:3679-3686(1995).
Cited for: NUCLEOTIDE SEQUENCE [MRNA], PHOSPHORYLATION AT THR-177, MUTAGENESIS OFLYS-49 AND THR-177, AND ENZYME REGULATION.

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