C2D1A_HUMAN - dbPTM
C2D1A_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C2D1A_HUMAN
UniProt AC Q6P1N0
Protein Name Coiled-coil and C2 domain-containing protein 1A
Gene Name CC2D1A
Organism Homo sapiens (Human).
Sequence Length 951
Subcellular Localization Cytoplasm . Nucleus . Cytoplasm, cytoskeleton, microtubule organizing center, centrosome .
Protein Description Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells. The combination of calcium and ATP specifically inactivates the binding with FRE. May play a role in the altered regulation of HTR1A associated with anxiety and major depression. Mediates HDAC-independent repression of HTR1A promoter in neuronal cell. Performs essential function in controlling functional maturation of synapses (By similarity). Plays distinct roles depending on its localization. When cytoplasmic, acts as a scaffold protein in the PI3K/PDK1/AKT pathway. Repressor of HTR1A when nuclear. In the centrosome, regulates spindle pole localization of the cohesin subunit SCC1/RAD21, thereby mediating centriole cohesion during mitosis..
Protein Sequence MHKRKGPPGPPGRGAAAARQLGLLVDLSPDGLMIPEDGANDEELEAEFLALVGGQPPALEKLKGKGPLPMEAIEKMASLCMRDPDEDEEEGTDEDDLEADDDLLAELNEVLGEEQKASETPPPVAQPKPEAPHPGLETTLQERLALYQTAIESARQAGDSAKMRRYDRGLKTLENLLASIRKGNAIDEADIPPPVAIGKGPASTPTYSPAPTQPAPRIASAPEPRVTLEGPSATAPASSPGLAKPQMPPGPCSPGPLAQLQSRQRDYKLAALHAKQQGDTTAAARHFRVAKSFDAVLEALSRGEPVDLSCLPPPPDQLPPDPPSPPSQPPTPATAPSTTEVPPPPRTLLEALEQRMERYQVAAAQAKSKGDQRKARMHERIVKQYQDAIRAHKAGRAVDVAELPVPPGFPPIQGLEATKPTQQSLVGVLETAMKLANQDEGPEDEEDEVPKKQNSPVAPTAQPKAPPSRTPQSGSAPTAKAPPKATSTRAQQQLAFLEGRKKQLLQAALRAKQKNDVEGAKMHLRQAKGLEPMLEASRNGLPVDITKVPPAPVNKDDFALVQRPGPGLSQEAARRYGELTKLIRQQHEMCLNHSNQFTQLGNITETTKFEKLAEDCKRSMDILKQAFVRGLPTPTARFEQRTFSVIKIFPDLSSNDMLLFIVKGINLPTPPGLSPGDLDVFVRFDFPYPNVEEAQKDKTSVIKNTDSPEFKEQFKLCINRSHRGFRRAIQTKGIKFEVVHKGGLFKTDRVLGTAQLKLDALEIACEVREILEVLDGRRPTGGRLEVMVRIREPLTAQQLETTTERWLVIDPVPAAVPTQVAGPKGKAPPVPAPARESGNRSARPLHSLSVLAFDQERLERKILALRQARRPVPPEVAQQYQDIMQRSQWQRAQLEQGGVGIRREYAAQLERQLQFYTEAARRLGNDGSRDAAKEALYRRNLVESELQRLRR
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
13MethylationGPPGPPGRGAAAARQ
CCCCCCCHHHHHHHH		37.03-
19MethylationGRGAAAARQLGLLVD
CHHHHHHHHHCCEEE		27.77-
78PhosphorylationEAIEKMASLCMRDPD
HHHHHHHHHHCCCCC		20.7127251275
92PhosphorylationDEDEEEGTDEDDLEA
CCCCCCCCCHHHHHC		39.2230278072
118PhosphorylationLGEEQKASETPPPVA
HCHHHHHCCCCCCCC		49.3823401153
120PhosphorylationEEQKASETPPPVAQP
HHHHHCCCCCCCCCC		38.3029255136
138PhosphorylationAPHPGLETTLQERLA
CCCCCHHHHHHHHHH		37.5424732914
139PhosphorylationPHPGLETTLQERLAL
CCCCHHHHHHHHHHH		19.6424732914
147PhosphorylationLQERLALYQTAIESA
HHHHHHHHHHHHHHH		9.7525159151
166PhosphorylationDSAKMRRYDRGLKTL
CHHHHHHHHHHHHHH		10.3026434552
172PhosphorylationRYDRGLKTLENLLAS
HHHHHHHHHHHHHHH		44.3326434552
179PhosphorylationTLENLLASIRKGNAI
HHHHHHHHHHCCCCC		23.9318491316
203PhosphorylationAIGKGPASTPTYSPA
EECCCCCCCCCCCCC		37.7421945579
204PhosphorylationIGKGPASTPTYSPAP
ECCCCCCCCCCCCCC		23.0421945579
206PhosphorylationKGPASTPTYSPAPTQ
CCCCCCCCCCCCCCC		36.4021945579
207PhosphorylationGPASTPTYSPAPTQP
CCCCCCCCCCCCCCC		17.5421945579
208PhosphorylationPASTPTYSPAPTQPA
CCCCCCCCCCCCCCC		19.6421945579
212PhosphorylationPTYSPAPTQPAPRIA
CCCCCCCCCCCCCCC		49.6521945579
220PhosphorylationQPAPRIASAPEPRVT
CCCCCCCCCCCCCEE		41.8220068231
227PhosphorylationSAPEPRVTLEGPSAT
CCCCCCEEEECCCCC		22.0022199227
232PhosphorylationRVTLEGPSATAPASS
CEEEECCCCCCCCCC		49.4626657352
234PhosphorylationTLEGPSATAPASSPG
EEECCCCCCCCCCCC		37.2022199227
238PhosphorylationPSATAPASSPGLAKP
CCCCCCCCCCCCCCC		35.6929255136
239PhosphorylationSATAPASSPGLAKPQ
CCCCCCCCCCCCCCC		25.7028355574
253PhosphorylationQMPPGPCSPGPLAQL
CCCCCCCCCCHHHHH		35.7025159151
262PhosphorylationGPLAQLQSRQRDYKL
CHHHHHHHHHCHHHH		38.6920068231
275UbiquitinationKLAALHAKQQGDTTA
HHHHHHHHHHCCCHH		32.1929967540
280PhosphorylationHAKQQGDTTAAARHF
HHHHHCCCHHHHHHH		25.7626699800
281PhosphorylationAKQQGDTTAAARHFR
HHHHCCCHHHHHHHH		21.0226699800
292PhosphorylationRHFRVAKSFDAVLEA
HHHHHHHHHHHHHHH		20.7226657352
309PhosphorylationRGEPVDLSCLPPPPD
CCCCCCCCCCCCCCC		14.7824275569
324PhosphorylationQLPPDPPSPPSQPPT
CCCCCCCCCCCCCCC		55.6328188228
327PhosphorylationPDPPSPPSQPPTPAT
CCCCCCCCCCCCCCC		59.7228188228
331PhosphorylationSPPSQPPTPATAPST
CCCCCCCCCCCCCCC		32.0427251275
334PhosphorylationSQPPTPATAPSTTEV
CCCCCCCCCCCCCCC		40.0627251275
347PhosphorylationEVPPPPRTLLEALEQ
CCCCCCHHHHHHHHH		41.2821406692
367UbiquitinationQVAAAQAKSKGDQRK
HHHHHHHHCHHHHHH		40.3924816145
418PhosphorylationPIQGLEATKPTQQSL
CCCCCCCCCCCHHHH		28.3422210691
431PhosphorylationSLVGVLETAMKLANQ
HHHHHHHHHHHHHCC		28.0822210691
455PhosphorylationEVPKKQNSPVAPTAQ
CCCCCCCCCCCCCCC		20.4629255136
460PhosphorylationQNSPVAPTAQPKAPP
CCCCCCCCCCCCCCC		28.3430266825
468PhosphorylationAQPKAPPSRTPQSGS
CCCCCCCCCCCCCCC		47.9625159151
470PhosphorylationPKAPPSRTPQSGSAP
CCCCCCCCCCCCCCC		29.9828985074
473PhosphorylationPPSRTPQSGSAPTAK
CCCCCCCCCCCCCCC		35.6025954137
475PhosphorylationSRTPQSGSAPTAKAP
CCCCCCCCCCCCCCC		36.0022468782
478PhosphorylationPQSGSAPTAKAPPKA
CCCCCCCCCCCCCCC		40.2720068231
479UbiquitinationQSGSAPTAKAPPKAT
CCCCCCCCCCCCCCC		12.6424816145
480UbiquitinationSGSAPTAKAPPKATS
CCCCCCCCCCCCCCC		65.0024816145
483UbiquitinationAPTAKAPPKATSTRA
CCCCCCCCCCCCHHH		43.7224816145
484UbiquitinationPTAKAPPKATSTRAQ
CCCCCCCCCCCHHHH		64.3424816145
486PhosphorylationAKAPPKATSTRAQQQ
CCCCCCCCCHHHHHH		36.4424275569
521UbiquitinationKNDVEGAKMHLRQAK
HCCHHHHHHHHHHHC		37.4029967540
555UbiquitinationVPPAPVNKDDFALVQ
CCCCCCCCCCEECCC		59.9329967540
581UbiquitinationRRYGELTKLIRQQHE
HHHHHHHHHHHHHHH		55.3229967540
608UbiquitinationGNITETTKFEKLAED
CCCCCCHHHHHHHHH		59.9729967540
624UbiquitinationKRSMDILKQAFVRGL
HHHHHHHHHHHHCCC		39.66-
669PhosphorylationVKGINLPTPPGLSPG
EECCCCCCCCCCCCC		45.3328102081
674PhosphorylationLPTPPGLSPGDLDVF
CCCCCCCCCCCCEEE		32.5229507054
707PhosphorylationSVIKNTDSPEFKEQF
CCCCCCCCHHHHHHH		25.0421815630
711UbiquitinationNTDSPEFKEQFKLCI
CCCCHHHHHHHHHHH		49.2829967540
715AcetylationPEFKEQFKLCINRSH
HHHHHHHHHHHCCCC		41.9925953088
741UbiquitinationIKFEVVHKGGLFKTD
CEEEEEECCCCCCCC		42.9629967540
746UbiquitinationVHKGGLFKTDRVLGT
EECCCCCCCCCEEEE		55.3429967540
837PhosphorylationVPAPARESGNRSARP
CCCCCCCCCCCCCCC		35.5028555341
849PhosphorylationARPLHSLSVLAFDQE
CCCCCCCHHEEECHH		20.3528857561
880PhosphorylationPPEVAQQYQDIMQRS
CHHHHHHHHHHHHHH		8.9627642862
916PhosphorylationLERQLQFYTEAARRL
HHHHHHHHHHHHHHH		7.24-
937PhosphorylationDAAKEALYRRNLVES
HHHHHHHHHHHHHHH		17.99-
944PhosphorylationYRRNLVESELQRLRR
HHHHHHHHHHHHHHC		35.8128857561
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
208SPhosphorylationKinaseCDK1P06493
Uniprot
208SPhosphorylationKinaseCDK2P24941
PSP
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
208SPhosphorylation

16964243
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 C2D1A_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
LRWD1_HUMANLRWD1physical
26344197
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
608443Mental retardation, autosomal recessive 3 (MRT3)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of C2D1A_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Mitotic phosphorylation of Aki1 at Ser208 by cyclin B1-Cdk1complex.";
Nakamura A., Naito M., Arai H., Fujita N.;
Biochem. Biophys. Res. Commun. 393:872-876(2010).
Cited for: FUNCTION, PHOSPHORYLATION AT SER-208 BY CDK1, AND SUBCELLULARLOCATION.
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-204 AND SER-208, ANDMASS SPECTROMETRY.
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-455, AND MASSSPECTROMETRY.
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT forefficient phosphoproteomic analysis.";
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,Yates J.R. III;
J. Proteome Res. 7:1346-1351(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.
"A probability-based approach for high-throughput proteinphosphorylation analysis and site localization.";
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
Nat. Biotechnol. 24:1285-1292(2006).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-208, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207, AND MASSSPECTROMETRY.

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