CAC1B_MOUSE - dbPTM
CAC1B_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1B_MOUSE
UniProt AC O55017
Protein Name Voltage-dependent N-type calcium channel subunit alpha-1B
Gene Name Cacna1b
Organism Mus musculus (Mouse).
Sequence Length 2327
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 MVRFGDELGGRYGGTGGGERARGGGAGGAGGPGQGGLPPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDTEPVGDFPCGKDPPARQCDGDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDKNAEEKSPLDVLKRAATKKSRNDLIHAEEGEDRFVDLCAVGSPFARASLKSGKTESSSYFRRKEKMFRFFIRRMVKAQSFYWVVLCVVALNTLCVAMVHYNQPQRLTTALYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSIFEVVWAAIKPGTSFGISVLRALRLLRIFKVTKYWNSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFQDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSKGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRYASTRHVRPDMKTHMDRPLVVEPGRDGLRGPVGSKSKPEGTEATESADLPRRHHRHRDRDKTSATAPAGGEQDRTESTETGAREERARPRRSHSKETPGADTQVRCERSRRHHRRGSPEEATEREPRRHRAHRHAQDSSKEGTAPVLVPKGERRARHRGPRTGPREAENNEEPTRRHRARHKVPPTLQPPEREAAEKESNAVEGDKETRNHQPKEPHCDLEAIAVTGVGPLHMLPSTCLQKVDEQPEDADNQRNVTRMGSQPSDPSTTVHVPVTLTGPPGETPVVPSGNMNLEGQAEGKKEAEADDVLRRGPRPIVPYSSMFCLSPTNLLRRFCHYIVTMRYFEMVILVVIALSSIALAAEDPVRTDSFRNNALKYMDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSSFMGGSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGFRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISAKPLTRYMPQNKQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSMECILKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIANNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDDTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLGNRACDPHANASECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYNDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISNEDMTVHFTSTLMALIRTALEIKLAPAGTKQHQCDAELRKEISSVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTTRDQTHQAPGGLSQMGPVSLFHPLKATLEQTQPAVLRGARVFLRQKSATSLSNGGAIQTQESGIKESLSWGTQRTQDALYEARAPLERGHSAEIPVGQSGTLAVDVQMQNMTLRGPDGEPQPGLESQGRAASMPRLAAETQPAPNASPMKRSISTLAPRPHGTQLCSTVLDRPPPSQASHHHHHRCHRRRDKKQRSLEKGPSLSVDPEGAPSTAAGPGLPHGEGSTACRRDRKQERGRSQERRQPSSSSSEKQRFYSCDRFGSREPPQLMPSLSSHPTSPTAALEPAPHPQGSGSVNGSPLMSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPVHFAEGQSGLPAFSPGRLSRGLSEHNALLQKEPLSQPLAPGSRIGSDPYLGQRLDSEASAHTLPEDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSTGVRARHSYHHPDQDHWC
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
22MethylationTGGGERARGGGAGGA
CCCCCCCCCCCCCCC		50.9724129315
46UbiquitinationPGQRVLYKQSIAQRA
CCCCHHHHHHHHHHH		33.15-
48PhosphorylationQRVLYKQSIAQRART
CCHHHHHHHHHHHHH		18.7529899451
65UbiquitinationLYNPIPVKQNCFTVN
HHCCCCCCCCCEEEC		30.36-
160PhosphorylationGFVFHKGSYLRNGWN
ECCCCCCCHHHCCCC		26.29-
161PhosphorylationFVFHKGSYLRNGWNV
CCCCCCCHHHCCCCH		20.53-
256N-linked_GlycosylationFHKACFPNSTDTEPV
HHHHHCCCCCCCCCC		36.97-
411PhosphorylationDKNAEEKSPLDVLKR
CCCCCCCCHHHHHHH		33.6922324799
424PhosphorylationKRAATKKSRNDLIHA
HHHHCCCCHHHCCCC		37.5620415495
446PhosphorylationVDLCAVGSPFARASL
EEEEECCCHHHHHHH		15.3920415495
452PhosphorylationGSPFARASLKSGKTE
CCHHHHHHHHCCCCC		30.6721082442
455PhosphorylationFARASLKSGKTESSS
HHHHHHHCCCCCCCH		51.3021082442
745 (in isoform 2)Phosphorylation-13.3422807455
745PhosphorylationAKEVAEVSPMSAANI
HHHHHHHCCCCHHHH		13.3425521595
748PhosphorylationVAEVSPMSAANISIA
HHHHCCCCHHHHHHH		27.8422324799
748 (in isoform 2)Phosphorylation-27.8421183079
753PhosphorylationPMSAANISIAARQQN
CCCHHHHHHHHHHHC		13.1420415495
753 (in isoform 2)Phosphorylation-13.1426239621
761 (in isoform 2)Phosphorylation-27.1529899451
766PhosphorylationQNSAKARSVWEQRAS
HCCHHHHHHHHHHHH		36.1229472430
766 (in isoform 2)Phosphorylation-36.1229899451
768 (in isoform 2)Phosphorylation-9.3929899451
769 (in isoform 2)Phosphorylation-28.2129899451
770 (in isoform 2)Phosphorylation-30.4428066266
772 (in isoform 2)Phosphorylation-11.0028066266
773PhosphorylationSVWEQRASQLRLQNL
HHHHHHHHHHHHHHH		31.7528285833
773 (in isoform 2)Phosphorylation-31.7528066266
776 (in isoform 2)Phosphorylation-26.9628066266
783PhosphorylationRLQNLRASCEALYSE
HHHHHHHHHHHHHHC		13.1725521595
787 (in isoform 2)Phosphorylation-1.9525266776
789PhosphorylationASCEALYSEMDPEER
HHHHHHHHCCCHHHH		27.5629899451
801PhosphorylationEERLRYASTRHVRPD
HHHHHHHHHCCCCCC		19.6229899451
802PhosphorylationERLRYASTRHVRPDM
HHHHHHHHCCCCCCC		19.3429899451
811PhosphorylationHVRPDMKTHMDRPLV
CCCCCCCCCCCCCEE		18.7828576409
873PhosphorylationAGGEQDRTESTETGA
CCCCCCCCCCCCCHH		42.4529899451
875PhosphorylationGEQDRTESTETGARE
CCCCCCCCCCCHHHH		30.8229899451
876PhosphorylationEQDRTESTETGAREE
CCCCCCCCCCHHHHH		31.1929899451
878PhosphorylationDRTESTETGAREERA
CCCCCCCCHHHHHHC		35.9129899451
890PhosphorylationERARPRRSHSKETPG
HHCCCCCCCCCCCCC		33.1323335269
892PhosphorylationARPRRSHSKETPGAD
CCCCCCCCCCCCCCC		33.1730372032
895PhosphorylationRRSHSKETPGADTQV
CCCCCCCCCCCCHHH		30.6620415495
915PhosphorylationRRHHRRGSPEEATER
HHHHCCCCHHHHHHH		27.5925521595
920PhosphorylationRGSPEEATEREPRRH
CCCHHHHHHHCHHHH		38.5625521595
1024O-linked_GlycosylationDLEAIAVTGVGPLHM
CCEEEEEECCCCHHC		19.6855411447
1058PhosphorylationRNVTRMGSQPSDPST
CCCCCCCCCCCCCCC		29.5819060867
1121S-palmitoylationVPYSSMFCLSPTNLL
CCCCCCCCCCHHHHH		2.4828680068
1253AcetylationLRVLRPLKTIKRLPK
HHHHHCHHHHHCCHH		51.3821728379
1440UbiquitinationIDFAISAKPLTRYMP
HHHHHCCCCCCCCCC		33.50-
1554N-linked_GlycosylationEIANNFINLSFLRLF
HHHHHCCCHHHHHHH		26.04-
1666N-linked_GlycosylationRACDPHANASECGSD
CCCCCCCCHHHCCCH		40.75-
1710PhosphorylationEYLTRDSSILGPHHL
HHHHCCCCCCCCCCH		26.56-
1814UbiquitinationQCDAELRKEISSVWA
CCCHHHHHHHHHHHH		72.52-
1907PhosphorylationRVFLRQKSATSLSNG
EEEEECCCCCHHCCC		28.5725521595
1909PhosphorylationFLRQKSATSLSNGGA
EEECCCCCHHCCCCC		36.9729899451
1910PhosphorylationLRQKSATSLSNGGAI
EECCCCCHHCCCCCC		29.5329899451
1912PhosphorylationQKSATSLSNGGAIQT
CCCCCHHCCCCCCCC		32.9429899451
1927PhosphorylationQESGIKESLSWGTQR
CCCCHHCHHCCCCHH		23.7722324799
1929PhosphorylationSGIKESLSWGTQRTQ
CCHHCHHCCCCHHHH		32.5122324799
1932PhosphorylationKESLSWGTQRTQDAL
HCHHCCCCHHHHHHH		14.4922324799
1951PhosphorylationAPLERGHSAEIPVGQ
CCHHCCCCCCCCCCC		30.3525521595
1959PhosphorylationAEIPVGQSGTLAVDV
CCCCCCCCCCEEEEE		28.0229899451
1961PhosphorylationIPVGQSGTLAVDVQM
CCCCCCCCEEEEEEE		19.4520415495
1992PhosphorylationESQGRAASMPRLAAE
HHCCCCCCCHHHHHH		28.4722324799
2007PhosphorylationTQPAPNASPMKRSIS
CCCCCCCCCCCCCHH		31.9729899451
2014PhosphorylationSPMKRSISTLAPRPH
CCCCCCHHHCCCCCC		20.7220415495
2015PhosphorylationPMKRSISTLAPRPHG
CCCCCHHHCCCCCCC		25.8520415495
2056PhosphorylationRRDKKQRSLEKGPSL
HCCHHHHHHCCCCCC		38.0820047950
2059AcetylationKKQRSLEKGPSLSVD
HHHHHHCCCCCCCCC		79.857719443
2062PhosphorylationRSLEKGPSLSVDPEG
HHHCCCCCCCCCCCC		41.7819060867
2064PhosphorylationLEKGPSLSVDPEGAP
HCCCCCCCCCCCCCC		28.8929899451
2117PhosphorylationSEKQRFYSCDRFGSR
HHHHHHHCCCCCCCC		13.56-
2184PhosphorylationQLPQTPLTPRPSITY
CCCCCCCCCCCCEEE		20.60-
2188PhosphorylationTPLTPRPSITYKTAN
CCCCCCCCEEEEECC		28.9229899451
2190PhosphorylationLTPRPSITYKTANSS
CCCCCCEEEEECCCC		24.2529899451
2193PhosphorylationRPSITYKTANSSPVH
CCCEEEEECCCCCCC		22.2129899451
2196PhosphorylationITYKTANSSPVHFAE
EEEEECCCCCCCCCC		33.2922807455
2197PhosphorylationTYKTANSSPVHFAEG
EEEECCCCCCCCCCC		30.6521183079
2206PhosphorylationVHFAEGQSGLPAFSP
CCCCCCCCCCCCCCC		53.8329899451
2212PhosphorylationQSGLPAFSPGRLSRG
CCCCCCCCCCCCCCC		28.6621183079
2217PhosphorylationAFSPGRLSRGLSEHN
CCCCCCCCCCHHHHC		23.96-
2221PhosphorylationGRLSRGLSEHNALLQ
CCCCCCHHHHCHHHC		39.3725521595
2244PhosphorylationAPGSRIGSDPYLGQR
CCCCCCCCCCCCHHH		32.8025521595
2317PhosphorylationTGVRARHSYHHPDQD
CCCCCCCCCCCCCCC		22.1729899451
2318PhosphorylationGVRARHSYHHPDQDH
CCCCCCCCCCCCCCC		9.68-
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

Oops, there are no upstream regulatory protein records of CAC1B_MOUSE !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAC1B_MOUSE !!
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 CAC1B_MOUSE !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CACB1_MOUSECacnb1physical
10328888
CACB3_MOUSECacnb3physical
10328888
CACB4_MOUSECacnb4physical
10328888
CACB2_MOUSECacnb2physical
16787652
CACB3_MOUSECacnb3physical
16787652
MLP3B_MOUSEMap1lc3bphysical
24566975
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of CAC1B_MOUSE

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"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-745; SER-783 ANDSER-2244, AND MASS SPECTROMETRY.
"Comprehensive identification of phosphorylation sites in postsynapticdensity preparations.";
Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R.,Burlingame A.L.;
Mol. Cell. Proteomics 5:914-922(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-783, AND MASSSPECTROMETRY.

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