dbPTM

CAC1C_MOUSE - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	CAC1C_MOUSE
UniProt AC	Q01815
Protein Name	Voltage-dependent L-type calcium channel subunit alpha-1C
Gene Name	Cacna1c
Organism	Mus musculus (Mouse).
Sequence Length	2139
Subcellular Localization	Membrane Multi-pass membrane protein . Cell membrane . The interaction between RRAD and CACNB2 regulates its trafficking to the cell membrane.
Protein Description	Voltage-sensitive calcium channels (VSCC) mediate the entry of calcium ions into excitable cells and are also involved in a variety of calcium-dependent processes, including muscle contraction, hormone or neurotransmitter release, gene expression, cell motility, cell division and cell death. The isoform alpha-1C gives rise to L-type calcium currents. Long-lasting (L-type) calcium channels belong to the 'high-voltage activated' (HVA) group. They are blocked by dihydropyridines (DHP), phenylalkylamines, benzothiazepines, and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to omega-conotoxin-GVIA (omega-CTx-GVIA) and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing the alpha-1C subunit play an important role in excitation-contraction coupling in the heart. The various isoforms display marked differences in the sensitivity to DHP compounds. Binding of calmodulin or CABP1 at the same regulatory sites results in opposite effects on the channel function..
Protein Sequence	MVNENTRMYVPEENHQGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWQAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGGTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIIDVPAEEDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEDKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPHWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFIVCGGILETILVETKIMSPLGISVLRCVRLLRIFKITRYWNSLSNLVASLLNSVRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFICGNYILLNVFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQEVMEKPAVEESKEEKIELKSITADGESPPTTKINMDDLQPSENEDKSPHSNPDTAGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSPNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILGNADYVFTSIFTLEIILKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRAINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAECKGNYITYKDGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLRRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKGYFSDPWNVFDFLIVIGSIIDVILSETNPAEHTQCSPSMSAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVTYYQSDSRGNFPQTFATQRPLHINKTGNNQADTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRFPHPAGYSSTVSTVEGHGPPLSPAVRVQEAAWKLSSKRCHSRESQGATVNQEIFPDETRSVRMSEEAEYCSEPSLLSTDMFSYQEDEHRQLTCPEEDKREIQPSPKRSFLRSASLGRRASFHLECLKRQKDQGGDISQKTALPLHLVHHQALAVAGLSPLLQRSHSPTTFPRPCPTPPVTPGSRGRPLRPIPTLRLEGAESSEKLNSSFPSIHCSSWSEETTACSGSSSMARRARPVSLTVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMENAADNILSGGAQQSPNGTLLPFVNCRDPGQDRAVAPEDESCAYALGRGRSEEALADSRSYVSNL

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
63	Ubiquitination	IDAARQAKLMGSAGN HHHHHHHHHHCCCCC	30.57	-
72	Phosphorylation	MGSAGNATISTVSST HCCCCCCEEEECCCH	21.33	26239621
77	Phosphorylation	NATISTVSSTQRKRQ CCEEEECCCHHHHHH	27.96	23737553
78	Phosphorylation	ATISTVSSTQRKRQQ CEEEECCCHHHHHHH	24.99	23737553
79	Phosphorylation	TISTVSSTQRKRQQY EEEECCCHHHHHHHH	25.53	23737553
106	S-palmitoylation	RPPRALLCLTLKNPI CCCCEEEHHCCCCHH	2.58	28680068
153	N-linked_Glycosylation	PFPEDDSNATNSNLE CCCCCCCCCCCCHHH	58.75	-
171	Phosphorylation	YLFLIIFTVEAFLKV HHHHHHHHHHHHHHH	13.66	-
328	N-linked_Glycosylation	GHGRQCQNGTVCKPG CCCCCCCCCCCCCCC	56.58	-
469	Phosphorylation	RNMSMPTSETESVNT CCCCCCCCCCCCCCC	36.33	22817900
471	Phosphorylation	MSMPTSETESVNTEN CCCCCCCCCCCCCCC	33.07	22817900
473	Phosphorylation	MPTSETESVNTENVA CCCCCCCCCCCCCCC	28.25	19060867
476	Phosphorylation	SETESVNTENVAGGD CCCCCCCCCCCCCCC	27.12	22817900
783	Phosphorylation	KKLARTASPEKKQEV HHHHHHCCHHHHHHH	32.74	16155576
808	Phosphorylation	EEKIELKSITADGES HHCEEEEEEECCCCC	37.48	22817900
810	Phosphorylation	KIELKSITADGESPP CEEEEEEECCCCCCC	26.28	22807455
815	Phosphorylation	SITADGESPPTTKIN EEECCCCCCCCCCCC	41.53	25521595
818	Phosphorylation	ADGESPPTTKINMDD CCCCCCCCCCCCHHH	44.07	23737553
819	Phosphorylation	DGESPPTTKINMDDL CCCCCCCCCCCHHHC	35.38	23737553
829	Phosphorylation	NMDDLQPSENEDKSP CHHHCCCCCCCCCCC	39.84	25338131
835	Phosphorylation	PSENEDKSPHSNPDT CCCCCCCCCCCCCCC	39.92	21082442
838	Phosphorylation	NEDKSPHSNPDTAGE CCCCCCCCCCCCCCC	54.14	25338131
842	Phosphorylation	SPHSNPDTAGEEDEE CCCCCCCCCCCCCCC	37.51	21082442
1184	Ubiquitination	YKNCELDKNQRQCVE HHCCCCCHHHHHHHH	68.55	-
1388	N-linked_Glycosylation	VFGKIALNDTTEINR HHHHHHCCCCCCCCC	35.24	-
1439	N-linked_Glycosylation	APESEPSNSTEGETP CCCCCCCCCCCCCCC	64.76	-
1487	Phosphorylation	DYLTRDWSILGPHHL HHHHCCCHHCCHHHH	16.54	20479240
1509	Ubiquitination	AEYDPEAKGRIKHLD HHCCHHCCCCCCCHH	47.24	-
1545	Phosphorylation	VACKRLVSMNMPLNS HHHHHHHHCCCCCCC	14.72	20479240
1635	Acetylation	FRKFKKRKEQGLVGK HHHHHHHHHHCCCCC	64.37	11789845
1642	Ubiquitination	KEQGLVGKPSQRNAL HHHCCCCCHHHHHHH	33.73	-
1644	Phosphorylation	QGLVGKPSQRNALSL HCCCCCHHHHHHHHH	45.30	27742792
1650	Phosphorylation	PSQRNALSLQAGLRT HHHHHHHHHHHHHHH	18.94	23737553
1670	Phosphorylation	PEIRRAISGDLTAEE HHHHHHHCCCCCHHH	25.85	26824392
1674	Phosphorylation	RAISGDLTAEEELDK HHHCCCCCHHHHHHH	36.44	27742792
1688	Phosphorylation	KAMKEAVSAASEDDI HHHHHHHHHHCCCHH	25.76	22324799
1691	Phosphorylation	KEAVSAASEDDIFRR HHHHHHHCCCHHHHH	41.07	25521595
1714	Phosphorylation	VTYYQSDSRGNFPQT EEEEECCCCCCCCCC	47.54	22817900
1733	Phosphorylation	RPLHINKTGNNQADT CCCEECCCCCCCCCC	40.42	29899451
1740	Phosphorylation	TGNNQADTESPSHEK CCCCCCCCCCCCCCH	41.18	29899451
1742	Phosphorylation	NNQADTESPSHEKLV CCCCCCCCCCCCHHH	33.52	25521595
1744	Phosphorylation	QADTESPSHEKLVDS CCCCCCCCCCHHHCC	54.26	23737553
1756	Phosphorylation	VDSTFTPSSYSSTGS HCCCCCCCCCCCCCC	38.56	25338131
1763	Phosphorylation	SSYSSTGSNANINNA CCCCCCCCCCCCCCC	32.62	25338131
1799	Phosphorylation	EGHGPPLSPAVRVQE CCCCCCCCHHHHHHH	19.31	29514104
1812	Phosphorylation	QEAAWKLSSKRCHSR HHHHHHHHCCCCCCC	30.04	25338131
1818	Phosphorylation	LSSKRCHSRESQGAT HHCCCCCCCCCCCCC	41.17	29899451
1821	Phosphorylation	KRCHSRESQGATVNQ CCCCCCCCCCCCCCC	32.57	29899451
1835	Phosphorylation	QEIFPDETRSVRMSE CHHCCCCCCCCCCCH	35.31	30635358
1889	Phosphorylation	PKRSFLRSASLGRRA CCHHHHHHHHCCHHH	25.10	-
1897	Phosphorylation	ASLGRRASFHLECLK HHCCHHHHHHHHHHH	16.04	7814415
1978	Phosphorylation	LRLEGAESSEKLNSS EEECCCCCHHHHHHC	43.17	26824392
1979	Phosphorylation	RLEGAESSEKLNSSF EECCCCCHHHHHHCC	30.20	23737553
2015	Phosphorylation	ARRARPVSLTVPSQA HCCCCCEEEECCCCC	22.47	26824392
2020	Phosphorylation	PVSLTVPSQAGAPGR CEEEECCCCCCCCCC	28.46	-
2034	Phosphorylation	RQFHGSASSLVEAVL CCCCCCHHHHHHHHH	26.38	25338131
2035	Phosphorylation	QFHGSASSLVEAVLI CCCCCHHHHHHHHHH	35.83	25338131
2125	Phosphorylation	YALGRGRSEEALADS HHCCCCCCHHHHHHC	42.48	26824392

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
783	S	Phosphorylation	Kinase	CDK5	P49615	PSP
1487	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
1487	S	Phosphorylation	Kinase	CAMK2A	P11798	PSP
1545	S	Phosphorylation	Kinase	CAMK2A	Q9UQM7	PSP
1545	S	Phosphorylation	Kinase	CAMK2A	P11798	PSP
1644	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
1897	S	Phosphorylation	Kinase	PKACA	P17612	PSP
1897	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
1897	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
1897	S	Phosphorylation	Kinase	PKA-FAMILY	-	GPS
1897	S	Phosphorylation	Kinase	PKA	-	Uniprot

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1897	S	Phosphorylation		25368181
Phosphorylation by PKA at Ser-1897 activates the channel.

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 CAC1C_MOUSE !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TRI13_MOUSE	Trim13	physical	21186355
RYR2_MOUSE	Ryr2	physical	16352659
CACB3_MOUSE	Cacnb3	physical	16787652
IL16_MOUSE	Il16	physical	10479680

Drug and Disease Associations

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

Regulatory Network of CAC1C_MOUSE

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Qualitative and quantitative analyses of protein phosphorylation innaive and stimulated mouse synaptosomal preparations."; Munton R.P., Tweedie-Cullen R., Livingstone-Zatchej M., Weinandy F.,Waidelich M., Longo D., Gehrig P., Potthast F., Rutishauser D.,Gerrits B., Panse C., Schlapbach R., Mansuy I.M.; Mol. Cell. Proteomics 6:283-293(2007). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-815, AND MASSSPECTROMETRY.	17114649 [Abstract]

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