KCC1A_MOUSE - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: KCC1A_MOUSE
• UniProt AC: Q91YS8
• Protein Name: Calcium/calmodulin-dependent protein kinase type 1
• Gene Name: Camk1
• Organism: Mus musculus (Mouse).
• Sequence Length: 374
• 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-673', 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. 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 (By similarity)..
• Protein Sequence: MPGAVEGPRWKQAEDIRDIYDFRDVLGTGAFSEVILAEDKRTQKLVAIKCIAKKALEGKEGSMENEIAVLHKIKHPNIVALDDIYESGGHLYLIMQLVSGGELFDRIVEKGFYTERDASRLIFQVLDAVKYLHDLGIVHRDLKPENLLYYSLDEDSKIMISDFGLSKMEDPGSVLSTACGTPGYVAPEVLAQKPYSKAVDCWSIGVIAYILLCGYPPFYDENDAKLFEQILKAEYEFDSPYWDDISDSAKDFIRHLMEKDPEKRFTCEQALQHPWIAGDTALDKNIHQSVSEQIKKNFAKSKWKQAFNATAVVRHMRKLQLGTSQEGQGQTGSHGELLTPTAGGPAAGCCCRDCCVEPGSELPPAPPPSSRAMD

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
110	Acetylation	LFDRIVEKGFYTERD HHHHHHHCCCCCHHH	43.35	22826441
150	Phosphorylation	KPENLLYYSLDEDSK CHHHCEEEECCCCCC	11.61	22817900
151	Phosphorylation	PENLLYYSLDEDSKI HHHCEEEECCCCCCE	18.78	29899451
173	Phosphorylation	SKMEDPGSVLSTACG CCCCCCCCHHHHCCC	25.85	25619855
176	Phosphorylation	EDPGSVLSTACGTPG CCCCCHHHHCCCCCC	16.29	25619855
177	Phosphorylation	DPGSVLSTACGTPGY CCCCHHHHCCCCCCC	23.08	22322096
179	Glutathionylation	GSVLSTACGTPGYVA CCHHHHCCCCCCCCC	6.72	22833525
181	Phosphorylation	VLSTACGTPGYVAPE HHHHCCCCCCCCCHH	17.27	25619855
184	Phosphorylation	TACGTPGYVAPEVLA HCCCCCCCCCHHHHC	8.47	25619855
195	Phosphorylation	EVLAQKPYSKAVDCW HHHCCCCCCCHHHHH	29.82	25619855
196	Phosphorylation	VLAQKPYSKAVDCWS HHCCCCCCCHHHHHH	23.75	25619855
259	Acetylation	FIRHLMEKDPEKRFT HHHHHHHHCHHHCCC	65.70	22826441
310	Phosphorylation	WKQAFNATAVVRHMR HHHHHHHHHHHHHHH	22.53	25777480
323	Phosphorylation	MRKLQLGTSQEGQGQ HHHCCCCCCCCCCCC	35.51	25521595
324	Phosphorylation	RKLQLGTSQEGQGQT HHCCCCCCCCCCCCC	25.16	25521595
331	Phosphorylation	SQEGQGQTGSHGELL CCCCCCCCCCCCEEC	47.69	26643407
333	Phosphorylation	EGQGQTGSHGELLTP CCCCCCCCCCEECCC	31.54	24453211
339	Phosphorylation	GSHGELLTPTAGGPA CCCCEECCCCCCCCC	31.08	24453211
341	Phosphorylation	HGELLTPTAGGPAAG CCEECCCCCCCCCCC	32.47	20415495

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
177	T	Phosphorylation	Kinase	CAMKK1	Q8VBY2	Uniprot
177	T	Phosphorylation	Kinase	CAMKK2	Q8C078	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
177	T	Phosphorylation	Phosphorylated by CaMKK1 and CaMKK2 on Thr-177.	-

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of KCC1A_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
FXL12_MOUSE	Fbxl12	physical	23707388

Drug and Disease Associations

• Kegg Drug
• DrugBank
• There are no disease associations of PTM sites.