GCM2_HUMAN - dbPTM
GCM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCM2_HUMAN
UniProt AC O75603
Protein Name Chorion-specific transcription factor GCMb
Gene Name GCM2 {ECO:0000312|HGNC:HGNC:4198}
Organism Homo sapiens (Human).
Sequence Length 506
Subcellular Localization Nucleus .
Protein Description Transcription factor that binds specific sequences on gene promoters and activate their transcription. Through the regulation of gene transcription, may play a role in parathyroid gland development..
Protein Sequence MPAAAVQEAVGVCSYGMQLSWDINDPQMPQELALFDQFREWPDGYVRFIYSSDEKKAQRHLSGWAMRNTNNHNGHILKKSCLGVVVCTQACTLPDGSRLQLRPAICDKARLKQQKKACPNCHSALELIPCRGHSGYPVTNFWRLDGNAIFFQAKGVHDHPRPESKSETEARRSAIKRQMASFYQPQKKRIRESEAEENQDSSGHFSNIPPLENPEDFDIVTETSFPIPGQPCPSFPKSDVYKATCDLATFQGDKMPPFQKYSSPRIYLPRPPCSYELANPGYTNSSPYPTLYKDSTSIPNDTDWVHLNTLQCNVNSYSSYERSFDFTNKQHGWKPALGKPSLVERTNHGQFQAMATRPYYNPELPCRYLTTPPPGAPALQTVITTTTKVSYQAYQPPAMKYSDSVREVKSLSSCNYAPEDTGMSVYPEPWGPPVTVTRAASPSGPPPMKIAGDCRAIRPTVAIPHEPVSSRTDEAETWDVCLSGLGSAVSYSDRVGPFFTYNNEDF
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
166PhosphorylationHPRPESKSETEARRS
CCCCCCCCHHHHHHH
60.0622210691
168PhosphorylationRPESKSETEARRSAI
CCCCCCHHHHHHHHH
41.8722210691
193PhosphorylationQKKRIRESEAEENQD
HHHHHHHHHHHHCCC
32.0526330541
201PhosphorylationEAEENQDSSGHFSNI
HHHHCCCCCCCCCCC
28.5826330541
202PhosphorylationAEENQDSSGHFSNIP
HHHCCCCCCCCCCCC
44.5726330541
206PhosphorylationQDSSGHFSNIPPLEN
CCCCCCCCCCCCCCC
28.3326330541
221PhosphorylationPEDFDIVTETSFPIP
HHHCCEEEECCCCCC
33.6026330541
223PhosphorylationDFDIVTETSFPIPGQ
HCCEEEECCCCCCCC
26.7126330541
224PhosphorylationFDIVTETSFPIPGQP
CCEEEECCCCCCCCC
23.8526330541
234PhosphorylationIPGQPCPSFPKSDVY
CCCCCCCCCCHHHHE
61.9826330541
238PhosphorylationPCPSFPKSDVYKATC
CCCCCCHHHHEEEEE
32.3326330541
241PhosphorylationSFPKSDVYKATCDLA
CCCHHHHEEEEEEEE
10.4126330541
359PhosphorylationQAMATRPYYNPELPC
EEEECCCCCCCCCCC
16.7522817900
360PhosphorylationAMATRPYYNPELPCR
EEECCCCCCCCCCCE
27.2422817900
368PhosphorylationNPELPCRYLTTPPPG
CCCCCCEECCCCCCC
18.3423663014
370PhosphorylationELPCRYLTTPPPGAP
CCCCEECCCCCCCCC
28.4623663014
371PhosphorylationLPCRYLTTPPPGAPA
CCCEECCCCCCCCCC
31.0723663014
381PhosphorylationPGAPALQTVITTTTK
CCCCCCCEEEEECCC
18.0923663014
384PhosphorylationPALQTVITTTTKVSY
CCCCEEEEECCCEEE
17.4723663014
385PhosphorylationALQTVITTTTKVSYQ
CCCEEEEECCCEEEE
22.7323663014
386PhosphorylationLQTVITTTTKVSYQA
CCEEEEECCCEEEEE
18.9023663014
387PhosphorylationQTVITTTTKVSYQAY
CEEEEECCCEEEEEC
27.6223663014
435PhosphorylationEPWGPPVTVTRAASP
CCCCCCEEEEECCCC
23.1826434776

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 GCM2_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCM2_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 GCM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RBPMS_HUMANRBPMSphysical
25416956
HSFY1_HUMANHSFY1physical
25416956
CSTF1_HUMANCSTF1physical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
146200Hypoparathyroidism, familial isolated (FIH)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of GCM2_HUMAN

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Related Literatures of Post-Translational Modification

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