CAC1B_RABIT - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: CAC1B_RABIT
• UniProt AC: Q05152
• Protein Name: Voltage-dependent N-type calcium channel subunit alpha-1B
• Gene Name: CACNA1B
• Organism: Oryctolagus cuniculus (Rabbit).
• Sequence Length: 2339
• Subcellular Localization: Membrane; Multi-pass membrane protein.
• 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-1B gives rise to N-type calcium currents. N-type calcium channels belong to the 'high-voltage activated' (HVA) group and are blocked by omega-conotoxin-GVIA (omega-CTx-GVIA) and by omega-agatoxin-IIIA (omega-Aga-IIIA). They are however insensitive to dihydropyridines (DHP), and omega-agatoxin-IVA (omega-Aga-IVA). Calcium channels containing alpha-1B subunit may play a role in directed migration of immature neurons..
• Protein Sequence: MVRFGDELGGRYGGAGGAERARGGGAGGAGGPGPGGLPPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKILALGFVLHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDPDPVGDFPCGKEAPARLCEGDTECREYWAGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDRNAEEKSPLDAVLKRAAAKKSRSDLIQAEEGEGRLTGLCAPGSPFARASLKSGKTESSSYFRRKEKMFRFFIRRMVKAQSFYWTVLCVVALNTLCVAMVHYNQPQRLTTALYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSIFEVVWAAVKPGTSFGISVLRALRLLRIFKVTKYWNSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFKDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSRGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRYATARHLRPDVKTHLDRPLVVEPGRDAPRGPPGGKSRPDGSEAPEGADPPRRHHRHRDKDKAPATVPSAGEQDRAEALRAEGGELGPREERGRPRRSRSKEAPGAPEVRSDRGRGPCPEGGRRHHRRGSPEEAAEREPRRHRAHRHGPDPGKEGPASGTRGERRARHRTGPRACPREAESSEEPARRHRARHKAPPTQETAEKDKEAAEKGGEATEAEKDKEARNHQPKELPCDLEAIGMLGVGAVHTLPSTCLQKVEEQPEDADNQRNVTRMGSQPPDTSTTVHIPVTLTGPPGETTVVPSGNVDLESQAEGKKEVETSDVMRSGPRPIVPYSSMFCLSPTNLLRRCCHYIVTMRYFEMVILVVIALSSIALAAEDPVRTDSPRNNALKYMDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSGSKGKDISTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGYRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISARPLTRYMPQNKQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSMECVLKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIANNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDDTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLSSRACDEHSNASECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYSDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISSEDMTVHFTSTLMALIRTALDIKLAPAGTKQHQCDAELRKEISCVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTSRDQTQQAPGGLSQLGPVSLFHPLKATLEQTQPALRGARAFLRQKSSASLSNGGAVQTQESGIKESVSWGTQRTQDVLCEARAPLERGHSAEIPVGQPGTLAVDVQMQNMTLSGPDAEPQPGLESQGRAASMPRLAAETQPAPDASPMKRSISTLAPRPHTARLGSTALDRPAPSQAPHHHHHRCHRRRDRKQRSLEKGPSLSADTDGAPDSTVGPGLPTGEGPPGCRRERERRQERGRSQERRQPSSSSSEKHRFYSCDRFGGREPPQPKPSLSSHPTSPTAGQEPGPHPQGSGSVHGSPLLSTSGASTPGRGRRQLPQTPLTPRPSVTYKTANSSPVHFAGAPSGLPAFSPGRLSRGLSEHNALLQRDPLSRPLAPGSRIGSDPYLGQRLDSEAPARALPEDAPAFEETAASNSGRSSRTSYVSSLTSQPPPLRRVPNGYHCTLGLGGGGRARRGCHHPDRDRRC

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
22	Methylation	AGGAERARGGGAGGA CCCCCCCCCCCCCCC	50.97	-
256	N-linked_Glycosylation	FHKACFPNSTDPDPV HHHHHCCCCCCCCCC	36.97	-
411	Phosphorylation	DRNAEEKSPLDAVLK CCCHHHCCHHHHHHH	33.69	-
447	Phosphorylation	TGLCAPGSPFARASL CCEECCCCCCHHHHH	18.78	-
746	Phosphorylation	AKEVAEVSPMSAANI HHHHHHHCCCCHHHH	13.34	-
749	Phosphorylation	VAEVSPMSAANISIA HHHHCCCCHHHHHHH	27.84	-
784	Phosphorylation	RLQNLRASCEALYSE HHHHHHHHHHHHHHC	13.17	-
1074	Phosphorylation	RNVTRMGSQPPDTST CCCCCCCCCCCCCCC	30.12	-
1566	N-linked_Glycosylation	EIANNFINLSFLRLF HHHHHCCCHHHHHHH	26.04	-
1678	N-linked_Glycosylation	RACDEHSNASECGSD CCCCCCCCHHHCCHH	49.76	-
1722	Phosphorylation	EYLTRDSSILGPHHL HHHHCCCCCCCCCCH	26.56	-
2067	Phosphorylation	RRDRKQRSLEKGPSL HHHHHHHHHCCCCCC	38.08	-
2224	Phosphorylation	PSGLPAFSPGRLSRG CCCCCCCCCCCCCCC	28.66	-
2233	Phosphorylation	GRLSRGLSEHNALLQ CCCCCCHHHCCHHHH	39.37	-
2256	Phosphorylation	APGSRIGSDPYLGQR CCCCCCCCCCCCHHC	32.80	-

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
411	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
411	S	Phosphorylation	Kinase	MAPK3	P27361	GPS
447	S	Phosphorylation	Kinase	MAPK1	P28482	GPS
447	S	Phosphorylation	Kinase	MAPK3	P27361	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of CAC1B_RABIT !!

Disease-associated PTM Sites based on SAP

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

Oops, there are no SNP-PTM records of CAC1B_RABIT !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
UBE3A_HUMAN	UBE3A	physical	28957379

Drug and Disease Associations

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