CAC1C_RAT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAC1C_RAT
• UniProt AC: P22002
• Protein Name: Voltage-dependent L-type calcium channel subunit alpha-1C
• Gene Name: Cacna1c
• Organism: Rattus norvegicus (Rat).
• Sequence Length: 2169
• 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. Binding of calmodulin or CABP1 at the same regulatory sites results in opposite effects on the channel function..
• Protein Sequence: MIRAFAQPSTPPYQPLSSCLSEDTERKFKGKVVHEAQLNCFYISPGGSNYGSPRPAHANMNANAAAGLAPEHIPTPGAALSWLAAIDAARQAKLMGSAGNATISTVSSTQRKRQQYGKPKKQGGTTATRPPRALLCLTLKNPIRRACISIVEWKPFEIIILLTIFANCVALAIYIPFPEDDSNATNSNLERVEYLFLIIFTVEAFLKVIAYGLLFHPNAYLRNGWNLLDFIIVVVGLFSAILEQATKADGANALGGKGAGFDVKALRAFRVLRPLRLVSGVPSLQVVLNSIIKAMVPLLHIALLVLFVIIIYAIIGLELFMGKMHKTCYNQEGIIDVPAEEDPSPCALETGHGRQCQNGTVCKPGWDGPKHGITNFDNFAFAMLTVFQCITMEGWTDVLYWMQDAMGYELPWVYFVSLVIFGSFFVLNLVLGVLSGEFSKEREKAKARGDFQKLREKQQLEEDLKGYLDWITQAEDIDPENEDEGMDEDKPRNMSMPTSETESVNTENVAGGDIEGENCGARLAHRISKSKFSRYWRRWNRFCRRKCRAAVKSNVFYWLVIFLVFLNTLTIASEHYNQPHWLTEVQDTANKALLALFTAEMLLKMYSLGLQAYFVSLFNRFDCFIVCGGILETILVETKIMSPLGISCWRCVRLLRIFKITRYWNSLSNLVASLLNSLRSIASLLLLLFLFIIIFSLLGMQLFGGKFNFDEMQTRRSTFDNFPQSLLTVFQILTGEDWNSVMYDGIMAYGGPSFPGMLVCIYFIILFISPNYILLNLFLAIAVDNLADAESLTSAQKEEEEEKERKKLARTASPEKKQEVMEKPAVEESKEEKIELKSITADGESPPTTKINMDDLQPSENEDKSPHSNPDTAGEEDEEEPEMPVGPRPRPLSELHLKEKAVPMPEASAFFIFSPNNRFRLQCHRIVNDTIFTNLILFFILLSSISLAAEDPVQHTSFRNHILFYFDIVFTTIFTIEIALKMTAYGAFLHKGSFCRNYFNILDLLVVSVSLISFGIQSSAINVVKILRVLRVLRPLRINRAKGLKHVVQCVFVAIRTIGNIVIVTTLLQFMFACIGVQLFKGKLYTCSDSSKQTEAESKGNYITYKTGEVDHPIIQPRSWENSKFDFDNVLAAMMALFTVSTFEGWPELLYRSIDSHTEDKGPIYNYRVEISIFFIIYIIIIAFFMMNIFVGFVIVTFQEQGEQEYKNCELDKNQRQCVEYALKARPLPRYIPKNQHQYKVWYVVNSTYFEYLMFVLILLNTICLAMQHYGQSCLFKIAMNILNMLFTGLFTVEMILKLIAFKPKHYFCDAWNTFDALIVVGSIVDIAITEVHPAEHTQCSPSMSAEENSRISITFFRLFRVMRLVKLLSRGEGIRTLLWTFIKSFQALPYVALLIVMLFFIYAVIGMQVFGKIALNDTTEINRNNNFQTFPQAVLLLFRCATGEAWQDIMLACMPGKKCAPESEPSNSTEGETPCGSSFAVFYFISFYMLCAFLIINLFVAVIMDNFDYLTRDWSILGPHHLDEFKRIWAEYDPEAKGRIKHLDVVTLLRRIQPPLGFGKLCPHRVACKRLVSMNMPLNSDGTVMFNATLFALVRTALRIKTEGNLEQANEELRAIIKKIWKRTSMKLLDQVVPPAGDDEVTVGKFYATFLIQEYFRKFKKRKEQGLVGKPSQRNALSLQAGLRTLHDIGPEIRRAISGDLTAEEELDKAMKEAVSAASEDDIFRRAGGLFGNHVSYYQSDSRSNFPQTFATQRPLHINKTGNNQADTESPSHEKLVDSTFTPSSYSSTGSNANINNANNTALGRFPHPAGYSSTVSTVEGHGPPLSPAVRVQEAAWKLSSKRCHSRESQGATVSQDMFPDETRSSVRLSEEVEYCSEPSLLSTDILSYQDDENRQLTCLEEDKREIQPCPKRSFLRSASLGRRASFHLECLKRQKDQGGDISQKTALPLHLVHHQALAVAGLSPLLQRSHSPSTFPRPRPTPPVTPGSRGRPLQPIPTLRLEGAESSEKLNSSFPSIHCSSWSEETTACSGGSSMARRARPVSLTVPSQAGAPGRQFHGSASSLVEAVLISEGLGQFAQDPKFIEVTTQELADACDMTIEEMENAADNILSGGAQQSPNGTLLPFVNCRDPGQDRAVVPEDESCVYALGRGRSEEALPDSRSYVSNL

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
9	Phosphorylation	IRAFAQPSTPPYQPL CCCCCCCCCCCCCCH	41.27	16641100
13	Phosphorylation	AQPSTPPYQPLSSCL CCCCCCCCCCHHHCC	24.78	16641100
17	Phosphorylation	TPPYQPLSSCLSEDT CCCCCCHHHCCCCCC	26.20	16641100
18	Phosphorylation	PPYQPLSSCLSEDTE CCCCCHHHCCCCCCC	27.10	16641100
93	Ubiquitination	IDAARQAKLMGSAGN HHHHHHHHHHCCCCC	30.57	-
125	Phosphorylation	KPKKQGGTTATRPPR CCCCCCCCCCCCCCC	21.78	23800682
126	Phosphorylation	PKKQGGTTATRPPRA CCCCCCCCCCCCCCE	29.34	23800682
128	Phosphorylation	KQGGTTATRPPRALL CCCCCCCCCCCCEEE	41.43	23800682
183	N-linked_Glycosylation	PFPEDDSNATNSNLE CCCCCCCCCCCCHHH	58.75	-
358	N-linked_Glycosylation	GHGRQCQNGTVCKPG CCCCCCCCCCCCCCC	56.58	-
472	Phosphorylation	KGYLDWITQAEDIDP HHHHHHHHHHHHCCC	19.92	19074150
499	Phosphorylation	RNMSMPTSETESVNT CCCCCCCCCCCCCCC	36.33	-
506	Phosphorylation	SETESVNTENVAGGD CCCCCCCCCCCCCCC	27.12	-
838	Phosphorylation	EEKIELKSITADGES HHCEEEEEEECCCCC	37.48	-
840	Phosphorylation	KIELKSITADGESPP CEEEEEEECCCCCCC	26.28	30240740
845	Phosphorylation	SITADGESPPTTKIN EEECCCCCCCCCCCC	41.53	25403869
848	Phosphorylation	ADGESPPTTKINMDD CCCCCCCCCCCCHHH	44.07	28432305
849	Phosphorylation	DGESPPTTKINMDDL CCCCCCCCCCCHHHC	35.38	22673903
1417	N-linked_Glycosylation	VFGKIALNDTTEINR HHHHHHCCCCCCCCC	35.24	-
1468	N-linked_Glycosylation	APESEPSNSTEGETP CCCCCCCCCCCCCCC	64.76	-
1516	Phosphorylation	DYLTRDWSILGPHHL HHHHCCCHHCCHHHH	16.54	-
1673	Phosphorylation	QGLVGKPSQRNALSL HCCCCCHHHHHHHHH	45.30	19527072
1699	Phosphorylation	PEIRRAISGDLTAEE HHHHHHHCCCCCHHH	25.85	28432305
1717	Phosphorylation	KAMKEAVSAASEDDI HHHHHHHHHHCCCHH	25.76	28432305
1720	Phosphorylation	KEAVSAASEDDIFRR HHHHHHHCCCHHHHH	41.07	25403869
1738	Phosphorylation	LFGNHVSYYQSDSRS CCCCCCHHCCCCCCC	12.39	-
1771	Phosphorylation	NNQADTESPSHEKLV CCCCCCCCCCCCHHH	33.52	28432305
1783	Phosphorylation	KLVDSTFTPSSYSST HHHCCCCCCCCCCCC	23.50	28432305
1785	Phosphorylation	VDSTFTPSSYSSTGS HCCCCCCCCCCCCCC	38.56	28432305
1786	Phosphorylation	DSTFTPSSYSSTGSN CCCCCCCCCCCCCCC	30.18	28432305
1787	Phosphorylation	STFTPSSYSSTGSNA CCCCCCCCCCCCCCC	15.81	28432305
1788	Phosphorylation	TFTPSSYSSTGSNAN CCCCCCCCCCCCCCC	24.30	28432305
1789	Phosphorylation	FTPSSYSSTGSNANI CCCCCCCCCCCCCCC	28.67	28432305
1790	Phosphorylation	TPSSYSSTGSNANIN CCCCCCCCCCCCCCC	38.39	28432305
1792	Phosphorylation	SSYSSTGSNANINNA CCCCCCCCCCCCCCC	32.62	28432305
1828	Phosphorylation	EGHGPPLSPAVRVQE CCCCCCCCHHHHHHH	19.31	15044319
1850	Phosphorylation	KRCHSRESQGATVSQ CCCCCCCCCCCCCCC	32.57	28432305
1854	Phosphorylation	SRESQGATVSQDMFP CCCCCCCCCCCCCCC	27.75	28432305
1856	Phosphorylation	ESQGATVSQDMFPDE CCCCCCCCCCCCCCC	18.99	28432305
1864	Phosphorylation	QDMFPDETRSSVRLS CCCCCCCCCCCCCCC	43.14	28432305
1919	Phosphorylation	PKRSFLRSASLGRRA CCHHHHHHHCCCHHH	25.10	-
1921	Phosphorylation	RSFLRSASLGRRASF HHHHHHHCCCHHHHH	32.38	25403869
1927	Phosphorylation	ASLGRRASFHLECLK HCCCHHHHHHHHHHH	16.04	15509562
2008	Phosphorylation	LRLEGAESSEKLNSS EEECCCCCHHHHHHC	43.17	28432305
2009	Phosphorylation	RLEGAESSEKLNSSF EECCCCCHHHHHHCC	30.20	28432305
2045	Phosphorylation	ARRARPVSLTVPSQA HCCCCCEEEECCCCC	22.47	28432305
2047	Phosphorylation	RARPVSLTVPSQAGA CCCCEEEECCCCCCC	23.90	28432305
2148	Phosphorylation	PEDESCVYALGRGRS CCCCHHHHHCCCCCC	10.63	10939336
2155	Phosphorylation	YALGRGRSEEALPDS HHCCCCCCCCCCCCC	42.48	28432305

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
1603	T	Phosphorylation	Kinase	CAMK2A	P11275	PSP
1738	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
1787	Y	Phosphorylation	Kinase	SRC	Q9WUD9	PSP
1927	S	Phosphorylation	Kinase	PKACA	P17612	PSP
1927	S	Phosphorylation	Kinase	PRKACA	P27791	GPS
1927	S	Phosphorylation	Kinase	PRKCA	P17252	GPS
1927	S	Phosphorylation	Kinase	PKC-FAMILY	-	GPS
1927	S	Phosphorylation	Kinase	PKA	-	Uniprot
1927	S	Phosphorylation	Kinase	PKC_GROUP	-	PhosphoELM
2148	Y	Phosphorylation	Kinase	SRC	P12931	PSP

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
1927	S	Phosphorylation	Phosphorylation by PKA at Ser-1927 activates the channel (By similarity).	8396138

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CAC1C_RAT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
TERA_RAT	Vcp	physical	21186355

Drug and Disease Associations

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