C2D1B_HUMAN - dbPTM
C2D1B_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C2D1B_HUMAN
UniProt AC Q5T0F9
Protein Name Coiled-coil and C2 domain-containing protein 1B
Gene Name CC2D1B
Organism Homo sapiens (Human).
Sequence Length 858
Subcellular Localization Nucleus .
Protein Description Transcription factor that binds specifically to the DRE (dual repressor element) and represses HTR1A gene transcription in neuronal cells..
Protein Sequence MMPGPRPRKGPQARGQGVAAAKQMGLFMEFGPEDMLLGMDEAEDDEDLEAELLALTGEAQTTGKKPAPKGQAPLPMAHIEKLAADCMRDVEEEEEEEGLEEDAELLTELQEVLGVDEETEPLDGDEVADPGGSEEENGLEDTEPPVQTAVLTASAPAAQAGASQGLHALLEERIHNYREAAASAKEAGEAAKARRCERGLKTLESQLASVRRGRKINEDEIPPPVALGKRPLAPQEPANRSPETDPPAPPALESDNPSQPETSLPGISAQPVSDLDPDPRALLSSRQREYKVAALSAKRAGELDRARELMRIGKRFGAVLEALEKGQPVDLSAMPPAPEDLKPQQASQAPTAPSVIPPAVERVQPVMAPDVPATPVAPTESQTVLDALQQRLNKYREAGIQARSGGDERKARMHERIAKQYQDAIRAHRAGRKVNFAELPVPPGFPPIPGLESTMGVEEDAVAATLAAAEKLASAEDSAPADKDEDEPPGHLQGEPPAQAPVAKKPARPTVPSSQRLPEPRASSSKESPSPSVREQLALLEARKLQYQRAALQAKRSQDLEQAKAYLRVAKWLEAQIIQARSGRPVDLSKVPSPLTDEEGDFILIHHEDLRLSQKAEEVYAQLQKMLLEQQEKCLLFSKQFMHQGNVAETTRFEKLAQDRKKQLEILQLAQAQGLDPPTHHFELKTFQTVRIFSELNSTEMHLIIVRGMNLPAPPGVTPDDLDAFVRFEFHYPNSDQAQKSKTAVVKNTNSPEFDQLFKLNINRNHRGFKRVIQSKGIKFEIFHKGSFFRSDKLVGTAHLKLERLENECEIREIVEVLDGRKPTGGKLEVKVRLREPLSGQDVQMVTENWLVLEPRGL
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
14MethylationPRKGPQARGQGVAAA
CCCCCCCCCCHHHHH		32.49-
202O-linked_GlycosylationRCERGLKTLESQLAS
HHHHHHHHHHHHHHH		40.5830379171
209PhosphorylationTLESQLASVRRGRKI
HHHHHHHHHHCCCCC		25.4229978859
241PhosphorylationPQEPANRSPETDPPA
CCCCCCCCCCCCCCC		27.2229496963
244PhosphorylationPANRSPETDPPAPPA
CCCCCCCCCCCCCCC		58.1328464451
254PhosphorylationPAPPALESDNPSQPE
CCCCCCCCCCCCCCC		43.4624275569
263PhosphorylationNPSQPETSLPGISAQ
CCCCCCCCCCCCCCC		30.7928464451
284PhosphorylationPDPRALLSSRQREYK
CCHHHHHHHHHHHHH		25.0724719451
285PhosphorylationDPRALLSSRQREYKV
CHHHHHHHHHHHHHH		32.1924719451
298AcetylationKVAALSAKRAGELDR
HHHHHHHHHHCHHHH		39.1325953088
2982-HydroxyisobutyrylationKVAALSAKRAGELDR
HHHHHHHHHHCHHHH		39.13-
374PhosphorylationMAPDVPATPVAPTES
CCCCCCCCCCCCCCC		16.5428857561
379PhosphorylationPATPVAPTESQTVLD
CCCCCCCCCCHHHHH		38.2328555341
419MalonylationRMHERIAKQYQDAIR
HHHHHHHHHHHHHHH		47.3626320211
513PhosphorylationPARPTVPSSQRLPEP
CCCCCCCHHHCCCCC		34.4628555341
523PhosphorylationRLPEPRASSSKESPS
CCCCCCCCCCCCCCC		36.1023403867
524PhosphorylationLPEPRASSSKESPSP
CCCCCCCCCCCCCCH		44.4323403867
525PhosphorylationPEPRASSSKESPSPS
CCCCCCCCCCCCCHH		37.6426657352
528PhosphorylationRASSSKESPSPSVRE
CCCCCCCCCCHHHHH		34.1225159151
530PhosphorylationSSSKESPSPSVREQL
CCCCCCCCHHHHHHH		38.8026055452
532PhosphorylationSKESPSPSVREQLAL
CCCCCCHHHHHHHHH		37.8423403867
555UbiquitinationQRAALQAKRSQDLEQ
HHHHHHHHHHHCHHH		39.3529967540
564UbiquitinationSQDLEQAKAYLRVAK
HHCHHHHHHHHHHHH		36.9429967540
566PhosphorylationDLEQAKAYLRVAKWL
CHHHHHHHHHHHHHH		8.37-
582PhosphorylationAQIIQARSGRPVDLS
HHHHHHCCCCCCCHH		42.0122210691
589PhosphorylationSGRPVDLSKVPSPLT
CCCCCCHHHCCCCCC		27.4322210691
593PhosphorylationVDLSKVPSPLTDEEG
CCHHHCCCCCCCCCC		35.2129255136
596PhosphorylationSKVPSPLTDEEGDFI
HHCCCCCCCCCCCEE		44.7629255136
613PhosphorylationHHEDLRLSQKAEEVY
EECHHCHHHHHHHHH		24.1722210691
615UbiquitinationEDLRLSQKAEEVYAQ
CHHCHHHHHHHHHHH		55.1529967540
620PhosphorylationSQKAEEVYAQLQKML
HHHHHHHHHHHHHHH		7.6027642862
625UbiquitinationEVYAQLQKMLLEQQE
HHHHHHHHHHHHHHH		39.8629967540
638PhosphorylationQEKCLLFSKQFMHQG
HHHHHHHCHHHHHCC		26.0524719451
747UbiquitinationKSKTAVVKNTNSPEF
HHCEEEECCCCCHHH		52.0029967540
751PhosphorylationAVVKNTNSPEFDQLF
EEECCCCCHHHHHHH		24.6221815630
759UbiquitinationPEFDQLFKLNINRNH
HHHHHHHHCCCCCCC		49.5729967540
787PhosphorylationFEIFHKGSFFRSDKL
EEEEECCCCCCCCCE		26.4724719451
793UbiquitinationGSFFRSDKLVGTAHL
CCCCCCCCEEEEEHH		46.4429967540
797PhosphorylationRSDKLVGTAHLKLER
CCCCEEEEEHHHHHH		11.92-
801UbiquitinationLVGTAHLKLERLENE
EEEEEHHHHHHHHCC		38.1329967540
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 C2D1B_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C2D1B_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 C2D1B_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TLN1_HUMANTLN1physical
22863883
UGPA_HUMANUGP2physical
22863883
DCTN1_HUMANDCTN1physical
26344197
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of C2D1B_HUMAN

loading...

Related Literatures of Post-Translational Modification

TOP
© 2024 Institute of Bioinformatics and Systems Biology, NYCU | Designed by : BiOmics Laboratory