CAC1B_HUMAN - dbPTM
CAC1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CAC1B_HUMAN
UniProt AC Q00975
Protein Name Voltage-dependent N-type calcium channel subunit alpha-1B
Gene Name CACNA1B
Organism Homo sapiens (Human).
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 MVRFGDELGGRYGGPGGGERARGGGAGGAGGPGPGGLQPGQRVLYKQSIAQRARTMALYNPIPVKQNCFTVNRSLFVFSEDNVVRKYAKRITEWPPFEYMILATIIANCIVLALEQHLPDGDKTPMSERLDDTEPYFIGIFCFEAGIKIIALGFVFHKGSYLRNGWNVMDFVVVLTGILATAGTDFDLRTLRAVRVLRPLKLVSGIPSLQVVLKSIMKAMVPLLQIGLLLFFAILMFAIIGLEFYMGKFHKACFPNSTDAEPVGDFPCGKEAPARLCEGDTECREYWPGPNFGITNFDNILFAILTVFQCITMEGWTDILYNTNDAAGNTWNWLYFIPLIIIGSFFMLNLVLGVLSGEFAKERERVENRRAFLKLRRQQQIERELNGYLEWIFKAEEVMLAEEDRNAEEKSPLDVLKRAATKKSRNDLIHAEEGEDRFADLCAVGSPFARASLKSGKTESSSYFRRKEKMFRFFIRRMVKAQSFYWVVLCVVALNTLCVAMVHYNQPRRLTTTLYFAEFVFLGLFLTEMSLKMYGLGPRSYFRSSFNCFDFGVIVGSVFEVVWAAIKPGSSFGISVLRALRLLRIFKVTKYWSSLRNLVVSLLNSMKSIISLLFLLFLFIVVFALLGMQLFGGQFNFQDETPTTNFDTFPAAILTVFQILTGEDWNAVMYHGIESQGGVSKGMFSSFYFIVLTLFGNYTLLNVFLAIAVDNLANAQELTKDEEEMEEAANQKLALQKAKEVAEVSPMSAANISIAARQQNSAKARSVWEQRASQLRLQNLRASCEALYSEMDPEERLRFATTRHLRPDMKTHLDRPLVVELGRDGARGPVGGKARPEAAEAPEGVDPPRRHHRHRDKDKTPAAGDQDRAEAPKAESGEPGAREERPRPHRSHSKEAAGPPEARSERGRGPGPEGGRRHHRRGSPEEAAEREPRRHRAHRHQDPSKECAGAKGERRARHRGGPRAGPREAESGEEPARRHRARHKAQPAHEAVEKETTEKEATEKEAEIVEADKEKELRNHQPREPHCDLETSGTVTVGPMHTLPSTCLQKVEEQPEDADNQRNVTRMGSQPPDPNTIVHIPVMLTGPLGEATVVPSGNVDLESQAEGKKEVEADDVMRSGPRPIVPYSSMFCLSPTNLLRRFCHYIVTMRYFEVVILVVIALSSIALAAEDPVRTDSPRNNALKYLDYIFTGVFTFEMVIKMIDLGLLLHPGAYFRDLWNILDFIVVSGALVAFAFSGSKGKDINTIKSLRVLRVLRPLKTIKRLPKLKAVFDCVVNSLKNVLNILIVYMLFMFIFAVIAVQLFKGKFFYCTDESKELERDCRGQYLDYEKEEVEAQPRQWKKYDFHYDNVLWALLTLFTVSTGEGWPMVLKHSVDATYEEQGPSPGYRMELSIFYVVYFVVFPFFFVNIFVALIIITFQEQGDKVMSECSLEKNERACIDFAISAKPLTRYMPQNRQSFQYKTWTFVVSPPFEYFIMAMIALNTVVLMMKFYDAPYEYELMLKCLNIVFTSMFSMECVLKIIAFGVLNYFRDAWNVFDFVTVLGSITDILVTEIAETNNFINLSFLRLFRAARLIKLLRQGYTIRILLWTFVQSFKALPYVCLLIAMLFFIYAIIGMQVFGNIALDDDTSINRHNNFRTFLQALMLLFRSATGEAWHEIMLSCLSNQACDEQANATECGSDFAYFYFVSFIFLCSFLMLNLFVAVIMDNFEYLTRDSSILGPHHLDEFIRVWAEYDPAACGRISYNDMFEMLKHMSPPLGLGKKCPARVAYKRLVRMNMPISNEDMTVHFTSTLMALIRTALEIKLAPAGTKQHQCDAELRKEISVVWANLPQKTLDLLVPPHKPDEMTVGKVYAALMIFDFYKQNKTTRDQMQQAPGGLSQMGPVSLFHPLKATLEQTQPAVLRGARVFLRQKSSTSLSNGGAIQNQESGIKESVSWGTQRTQDAPHEARPPLERGHSTEIPVGRSGALAVDVQMQSITRRGPDGEPQPGLESQGRAASMPRLAAETQPVTDASPMKRSISTLAQRPRGTHLCSTTPDRPPPSQASSHHHHHRCHRRRDRKQRSLEKGPSLSADMDGAPSSAVGPGLPPGEGPTGCRRERERRQERGRSQERRQPSSSSSEKQRFYSCDRFGGREPPKPKPSLSSHPTSPTAGQEPGPHPQGSGSVNGSPLLSTSGASTPGRGGRRQLPQTPLTPRPSITYKTANSSPIHFAGAQTSLPAFSPGRLSRGLSEHNALLQRDPLSQPLAPGSRIGSDPYLGQRLDSEASVHALPEDTLTFEEAVATNSGRSSRTSYVSSLTSQSHPLRRVPNGYHCTLGLSSGGRARHSYHHPDQDHWC
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
22MethylationPGGGERARGGGAGGA
CCCCCCCCCCCCCCC		50.97-
176PhosphorylationMDFVVVLTGILATAG
HHHHHHHHHHHHHCC		15.5725332170
181PhosphorylationVLTGILATAGTDFDL
HHHHHHHHCCCCCCH		23.3625332170
201UbiquitinationVRVLRPLKLVSGIPS
HHHHHCHHHHCCCCH		49.9123503661
208PhosphorylationKLVSGIPSLQVVLKS
HHHCCCCHHHHHHHH		29.52-
245PhosphorylationAIIGLEFYMGKFHKA
HHHHHHHHHCCHHHH		8.79-
256N-linked_GlycosylationFHKACFPNSTDAEPV
HHHHHCCCCCCCCCC		36.97UniProtKB CARBOHYD
374UbiquitinationENRRAFLKLRRQQQI
HHHHHHHHHHHHHHH		33.23-
411PhosphorylationDRNAEEKSPLDVLKR
CCCCHHCCHHHHHHH		33.6924076635
417UbiquitinationKSPLDVLKRAATKKS
CCHHHHHHHHHCCCC		39.5832142685
421PhosphorylationDVLKRAATKKSRNDL
HHHHHHHCCCCHHHC		37.7111053424
455PhosphorylationFARASLKSGKTESSS
HHHHHHHCCCCCCCH		51.3017081983
460PhosphorylationLKSGKTESSSYFRRK
HHCCCCCCCHHHHHH		29.8028787133
463PhosphorylationGKTESSSYFRRKEKM
CCCCCCHHHHHHHHH		11.7628787133
745PhosphorylationAKEVAEVSPMSAANI
HHHHHHHCCCCHHHH		13.3424076635
748PhosphorylationVAEVSPMSAANISIA
HHHHCCCCHHHHHHH		27.8430622161
753PhosphorylationPMSAANISIAARQQN
CCCHHHHHHHHHHHC		13.1430622161
761PhosphorylationIAARQQNSAKARSVW
HHHHHHCCHHHHHHH		27.1530622161
766PhosphorylationQNSAKARSVWEQRAS
HCCHHHHHHHHHHHH		36.1227251275
783PhosphorylationRLQNLRASCEALYSE
HHHHHHHHHHHHHHC		13.1727732954
876PhosphorylationAEAPKAESGEPGARE
HHCCCCCCCCCCCCC		54.0029449344
923PhosphorylationRRHHRRGSPEEAAER
CCCCCCCCHHHHHHH		27.5925307156
971PhosphorylationAGPREAESGEEPARR
CCCCCCCCCCCHHHH		59.56-
1069PhosphorylationRNVTRMGSQPPDPNT
CCCCCCCCCCCCCCC		30.12-
1085PhosphorylationVHIPVMLTGPLGEAT
EEEEEEEECCCCEEE		20.7519690332
1134PhosphorylationYSSMFCLSPTNLLRR
CCCCEECCHHHHHHH		30.7530576142
1136PhosphorylationSMFCLSPTNLLRRFC
CCEECCHHHHHHHHH		34.8130576142
1242UbiquitinationAFSGSKGKDINTIKS
HHCCCCCCCHHHHHH		60.20-
1247UbiquitinationKGKDINTIKSLRVLR
CCCCHHHHHHHHHHH		2.1722817900
1248UbiquitinationGKDINTIKSLRVLRV
CCCHHHHHHHHHHHH		41.2022817900
1248 (in isoform 2)Ubiquitination-41.2021906983
1249UbiquitinationKDINTIKSLRVLRVL
CCHHHHHHHHHHHHH		19.9822817900
1249 (in isoform 1)Ubiquitination-19.9821906983
1252UbiquitinationNTIKSLRVLRVLRPL
HHHHHHHHHHHHHCH		4.9222817900
1253UbiquitinationTIKSLRVLRVLRPLK
HHHHHHHHHHHHCHH		2.2422817900
1330UbiquitinationRGQYLDYEKEEVEAQ
HCCCCCCCHHHHHCC		54.3722817900
1331UbiquitinationGQYLDYEKEEVEAQP
CCCCCCCHHHHHCCC		53.6022817900
1331 (in isoform 2)Ubiquitination-53.6021906983
1332UbiquitinationQYLDYEKEEVEAQPR
CCCCCCHHHHHCCCC		56.1622817900
1332 (in isoform 1)Ubiquitination-56.1621906983
1335UbiquitinationDYEKEEVEAQPRQWK
CCCHHHHHCCCCCCC		44.8822817900
1336UbiquitinationYEKEEVEAQPRQWKK
CCHHHHHCCCCCCCC		29.8322817900
1445PhosphorylationACIDFAISAKPLTRY
HHHHHHHCCCCCCCC		27.15-
1447UbiquitinationIDFAISAKPLTRYMP
HHHHHCCCCCCCCCC		33.502190698
1447 (in isoform 2)Ubiquitination-33.5021906983
1448 (in isoform 1)Ubiquitination-38.3921906983
1450PhosphorylationAISAKPLTRYMPQNR
HHCCCCCCCCCCCCC		28.42-
1493PhosphorylationVVLMMKFYDAPYEYE
HHHHHHHCCCCHHHH		12.9926074081
1563N-linked_GlycosylationAETNNFINLSFLRLF
HHHCCCCCHHHHHHH		26.04UniProtKB CARBOHYD
1584PhosphorylationKLLRQGYTIRILLWT
HHHHCCCCHHHHHHH		15.5924719451
1675N-linked_GlycosylationQACDEQANATECGSD
CHHHHHCCHHHCCHH		47.27UniProtKB CARBOHYD
1719PhosphorylationEYLTRDSSILGPHHL
HHHHCCCCCCCCCCH		26.56-
1736PhosphorylationFIRVWAEYDPAACGR
HHHHHHHCCHHHCCC		21.3418083107
1762UbiquitinationHMSPPLGLGKKCPAR
HCCCCCCCCCCCHHH		13.8123503661
1763UbiquitinationMSPPLGLGKKCPARV
CCCCCCCCCCCHHHH		26.1023503661
1764UbiquitinationSPPLGLGKKCPARVA
CCCCCCCCCCHHHHH		57.1323503661
1765UbiquitinationPPLGLGKKCPARVAY
CCCCCCCCCHHHHHH		43.5923503661
1766UbiquitinationPLGLGKKCPARVAYK
CCCCCCCCHHHHHHH		3.4723503661
1767UbiquitinationLGLGKKCPARVAYKR
CCCCCCCHHHHHHHH		31.7923503661
1768UbiquitinationGLGKKCPARVAYKRL
CCCCCCHHHHHHHHH		28.2223503661
1769UbiquitinationLGKKCPARVAYKRLV
CCCCCHHHHHHHHHH		9.9523503661
1770UbiquitinationGKKCPARVAYKRLVR
CCCCHHHHHHHHHHH		8.0923503661
1783PhosphorylationVRMNMPISNEDMTVH
HHCCCCCCCCCCCHH		28.4422210691
1788PhosphorylationPISNEDMTVHFTSTL
CCCCCCCCHHHHHHH		24.1329978859
1792PhosphorylationEDMTVHFTSTLMALI
CCCCHHHHHHHHHHH		13.1129978859
1793PhosphorylationDMTVHFTSTLMALIR
CCCHHHHHHHHHHHH		20.7122210691
1794PhosphorylationMTVHFTSTLMALIRT
CCHHHHHHHHHHHHH		19.9322210691
1869PhosphorylationDFYKQNKTTRDQMQQ
HHHHCCCCCHHHHHH		34.31-
1870PhosphorylationFYKQNKTTRDQMQQA
HHHCCCCCHHHHHHC		33.58-
1916PhosphorylationRVFLRQKSSTSLSNG
EEEEECCCCCCCCCC		30.4328348404
1917PhosphorylationVFLRQKSSTSLSNGG
EEEECCCCCCCCCCC		29.1128348404
1918PhosphorylationFLRQKSSTSLSNGGA
EEECCCCCCCCCCCC		40.5524719451
1919PhosphorylationLRQKSSTSLSNGGAI
EECCCCCCCCCCCCC		31.5728348404
1941PhosphorylationKESVSWGTQRTQDAP
CCCCCCCCCCCCCCC		14.49-
1944PhosphorylationVSWGTQRTQDAPHEA
CCCCCCCCCCCCCCC		22.45-
1960PhosphorylationPPLERGHSTEIPVGR
CCCCCCCCCCCCCCC		30.4725307156
1961PhosphorylationPLERGHSTEIPVGRS
CCCCCCCCCCCCCCC		32.0624719451
1968PhosphorylationTEIPVGRSGALAVDV
CCCCCCCCCCEEEEE		23.6118187866
2001PhosphorylationESQGRAASMPRLAAE
HHCCCCCCCCCHHHC		28.4724719451
2009PhosphorylationMPRLAAETQPVTDAS
CCCHHHCCCCCCCCC		33.18-
2016PhosphorylationTQPVTDASPMKRSIS
CCCCCCCCCCCCHHH		28.4724719451
2023PhosphorylationSPMKRSISTLAQRPR
CCCCCHHHHHHCCCC		20.7224719451
2024PhosphorylationPMKRSISTLAQRPRG
CCCCHHHHHHCCCCC		25.1723312004
2066PhosphorylationRRDRKQRSLEKGPSL
HHHHHHHHHCCCCCC		38.08-
2119PhosphorylationQERRQPSSSSSEKQR
CCCCCCCCCCHHHHH		40.71-
2128PhosphorylationSSEKQRFYSCDRFGG
CHHHHHHHCCCCCCC		15.5825884760
2129PhosphorylationSEKQRFYSCDRFGGR
HHHHHHHCCCCCCCC		13.5624719451
2193PhosphorylationGRRQLPQTPLTPRPS
CCCCCCCCCCCCCCC		20.5124043423
2205PhosphorylationRPSITYKTANSSPIH
CCCEEEEECCCCCCE		22.2127732954
2208PhosphorylationITYKTANSSPIHFAG
EEEEECCCCCCEECC		34.7227732954
2209PhosphorylationTYKTANSSPIHFAGA
EEEECCCCCCEECCC		27.9027732954
2218PhosphorylationIHFAGAQTSLPAFSP
CEECCCCCCCCCCCC		31.5327732954
2219PhosphorylationHFAGAQTSLPAFSPG
EECCCCCCCCCCCCC		21.9227732954
2224PhosphorylationQTSLPAFSPGRLSRG
CCCCCCCCCCCCCCC		28.6627732954
2233PhosphorylationGRLSRGLSEHNALLQ
CCCCCCHHHCCHHHC		39.3727732954
2256PhosphorylationAPGSRIGSDPYLGQR
CCCCCCCCCCCCCCC		32.8027732954
2259PhosphorylationSRIGSDPYLGQRLDS
CCCCCCCCCCCCCCC		28.5825884760
2266PhosphorylationYLGQRLDSEASVHAL
CCCCCCCCCCCCCCC		39.3924719451
2294PhosphorylationNSGRSSRTSYVSSLT
CCCCCCCHHHHHHHH		26.7626471730
2295PhosphorylationSGRSSRTSYVSSLTS
CCCCCCHHHHHHHHC		23.5626471730
2296PhosphorylationGRSSRTSYVSSLTSQ
CCCCCHHHHHHHHCC		12.0726471730
2298PhosphorylationSSRTSYVSSLTSQSH
CCCHHHHHHHHCCCC		16.0526471730
2299PhosphorylationSRTSYVSSLTSQSHP
CCHHHHHHHHCCCCC		26.1426471730
2301PhosphorylationTSYVSSLTSQSHPLR
HHHHHHHHCCCCCCC		27.0326471730
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_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CAC1B_HUMAN !!
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_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GBB2_HUMANGNB2physical
9238069
MLP3B_HUMANMAP1LC3Bphysical
24566975
UB2L3_HUMANUBE2L3physical
24566975
UB2L3_HUMANUBE2L3physical
25483588
MAP1B_HUMANMAP1Bphysical
25483588
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
614860Dystonia 23 (DYT23)
Kegg Drug
D01173 Cilnidipine (JAN/INN); Atelec (TN)
D06363 Ziconotide (USAN/INN); Prialt (TN)
D08686 Ziconotide acetate; Prialt (TN)
DrugBank
DB00381Amlodipine
DB00996Gabapentin
DB01202Levetiracetam
DB00421Spironolactone
DB00661Verapamil
Regulatory Network of CAC1B_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
Anal. Sci. 24:161-166(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1968, AND MASSSPECTROMETRY.
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks.";
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.;
Cell 127:635-648(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASSSPECTROMETRY.

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