GCSP_HUMAN - dbPTM
GCSP_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID GCSP_HUMAN
UniProt AC P23378
Protein Name Glycine dehydrogenase (decarboxylating), mitochondrial {ECO:0000303|PubMed:15489334}
Gene Name GLDC {ECO:0000312|HGNC:HGNC:4313}
Organism Homo sapiens (Human).
Sequence Length 1020
Subcellular Localization Mitochondrion .
Protein Description The glycine cleavage system catalyzes the degradation of glycine. The P protein (GLDC) binds the alpha-amino group of glycine through its pyridoxal phosphate cofactor; CO(2) is released and the remaining methylamine moiety is then transferred to the lipoamide cofactor of the H protein (GCSH)..
Protein Sequence MQSCARAWGLRLGRGVGGGRRLAGGSGPCWAPRSRDSSSGGGDSAAAGASRLLERLLPRHDDFARRHIGPGDKDQREMLQTLGLASIDELIEKTVPANIRLKRPLKMEDPVCENEILATLHAISSKNQIWRSYIGMGYYNCSVPQTILRNLLENSGWITQYTPYQPEVSQGRLESLLNYQTMVCDITGLDMANASLLDEGTAAAEALQLCYRHNKRRKFLVDPRCHPQTIAVVQTRAKYTGVLTELKLPCEMDFSGKDVSGVLFQYPDTEGKVEDFTELVERAHQSGSLACCATDLLALCILRPPGEFGVDIALGSSQRFGVPLGYGGPHAAFFAVRESLVRMMPGRMVGVTRDATGKEVYRLALQTREQHIRRDKATSNICTAQALLANMAAMFAIYHGSHGLEHIARRVHNATLILSEGLKRAGHQLQHDLFFDTLKIQCGCSVKEVLGRAAQRQINFRLFEDGTLGISLDETVNEKDLDDLLWIFGCESSAELVAESMGEECRGIPGSVFKRTSPFLTHQVFNSYHSETNIVRYMKKLENKDISLVHSMIPLGSCTMKLNSSSELAPITWKEFANIHPFVPLDQAQGYQQLFRELEKDLCELTGYDQVCFQPNSGAQGEYAGLATIRAYLNQKGEGHRTVCLIPKSAHGTNPASAHMAGMKIQPVEVDKYGNIDAVHLKAMVDKHKENLAAIMITYPSTNGVFEENISDVCDLIHQHGGQVYLDGANMNAQVGICRPGDFGSDVSHLNLHKTFCIPHGGGGPGMGPIGVKKHLAPFLPNHPVISLKRNEDACPVGTVSAAPWGSSSILPISWAYIKMMGGKGLKQATETAILNANYMAKRLETHYRILFRGARGYVGHEFILDTRPFKKSANIEAVDVAKRLQDYGFHAPTMSWPVAGTLMVEPTESEDKAELDRFCDAMISIRQEIADIEEGRIDPRVNPLKMSPHSLTCVTSSHWDRPYSREVAAFPLPFVKPENKFWPTIARIDDIYGDQHLVCTCPPMEVYESPFSEQKRASS
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
34PhosphorylationGPCWAPRSRDSSSGG
CCCCCCCCCCCCCCC		39.1022210691
37PhosphorylationWAPRSRDSSSGGGDS
CCCCCCCCCCCCCCH		25.8722798277
38PhosphorylationAPRSRDSSSGGGDSA
CCCCCCCCCCCCCHH		36.9729255136
39PhosphorylationPRSRDSSSGGGDSAA
CCCCCCCCCCCCHHH		45.4629255136
44PhosphorylationSSSGGGDSAAAGASR
CCCCCCCHHHHHHHH		24.0729255136
50PhosphorylationDSAAAGASRLLERLL
CHHHHHHHHHHHHHC		23.6522210691
119PhosphorylationCENEILATLHAISSK
CCHHHHHHHHHHHCC		18.6826270265
124PhosphorylationLATLHAISSKNQIWR
HHHHHHHHCCCHHHH		35.7226270265
125PhosphorylationATLHAISSKNQIWRS
HHHHHHHCCCHHHHH		29.5226270265
218AcetylationYRHNKRRKFLVDPRC
HHHCCCCCEEECCCC		47.2727178108
225S-nitrosylationKFLVDPRCHPQTIAV
CEEECCCCCCCEEEE		7.1724105792
272UbiquitinationQYPDTEGKVEDFTEL
ECCCCCCCCCCHHHH		35.90-
358UbiquitinationVTRDATGKEVYRLAL
EEECCCCHHHHHHHH		39.38-
361PhosphorylationDATGKEVYRLALQTR
CCCCHHHHHHHHHHH		10.8623403867
423AcetylationLILSEGLKRAGHQLQ
HHCCHHHHHCCHHHC		51.5724886747
423UbiquitinationLILSEGLKRAGHQLQ
HHCCHHHHHCCHHHC		51.57-
447AcetylationIQCGCSVKEVLGRAA
HCCCCCHHHHHHHHH		26.30-
447UbiquitinationIQCGCSVKEVLGRAA
HCCCCCHHHHHHHHH		26.30-
514UbiquitinationGIPGSVFKRTSPFLT
CCCCCHHCCCCCCCC		53.24-
514AcetylationGIPGSVFKRTSPFLT
CCCCCHHCCCCCCCC		53.242380565
537PhosphorylationSETNIVRYMKKLENK
CHHHHHHHHHHHCCC		11.46-
636UbiquitinationIRAYLNQKGEGHRTV
HHHHHHHCCCCCCEE		58.8329967540
648AcetylationRTVCLIPKSAHGTNP
CEEEEEECCCCCCCC		53.967622737
664AcetylationSAHMAGMKIQPVEVD
HHHHCCCCEECEEEE		36.9524886755
672UbiquitinationIQPVEVDKYGNIDAV
EECEEEECCCCCCEE		61.3029967540
672AcetylationIQPVEVDKYGNIDAV
EECEEEECCCCCCEE		61.3023954790
687AcetylationHLKAMVDKHKENLAA
EHHHHHHHHHHCEEE		45.2027178108
754N6-(pyridoxal phosphate)lysineVSHLNLHKTFCIPHG
CCEEEECCEEEECCC		46.60-
754OtherVSHLNLHKTFCIPHG
CCEEEECCEEEECCC		46.60-
773AcetylationGMGPIGVKKHLAPFL
CCCCCCCHHHHCCCC		29.3024886763
773UbiquitinationGMGPIGVKKHLAPFL
CCCCCCCHHHHCCCC		29.3022505724
774UbiquitinationMGPIGVKKHLAPFLP
CCCCCCHHHHCCCCC		41.2529967540
787PhosphorylationLPNHPVISLKRNEDA
CCCCCEEEEECCCCC		28.2424719451
789AcetylationNHPVISLKRNEDACP
CCCEEEEECCCCCCC		46.5224886771
789UbiquitinationNHPVISLKRNEDACP
CCCEEEEECCCCCCC		46.52-
830PhosphorylationGKGLKQATETAILNA
CCCHHHHHHHHHHCH		31.23-
832PhosphorylationGLKQATETAILNANY
CHHHHHHHHHHCHHH		18.04-
839PhosphorylationTAILNANYMAKRLET
HHHHCHHHHHHHHHH		8.95-
871UbiquitinationILDTRPFKKSANIEA
EECCCCCCCCCCCEE		48.80-
871AcetylationILDTRPFKKSANIEA
EECCCCCCCCCCCEE		48.802402169
871SuccinylationILDTRPFKKSANIEA
EECCCCCCCCCCCEE		48.8023954790
872AcetylationLDTRPFKKSANIEAV
ECCCCCCCCCCCEEE		56.0027178108
872UbiquitinationLDTRPFKKSANIEAV
ECCCCCCCCCCCEEE		56.00-
873PhosphorylationDTRPFKKSANIEAVD
CCCCCCCCCCCEEEH		27.43-
883UbiquitinationIEAVDVAKRLQDYGF
CEEEHHHHHHHHCCC		54.1929967540
883AcetylationIEAVDVAKRLQDYGF
CEEEHHHHHHHHCCC		54.1924886779
8832-HydroxyisobutyrylationIEAVDVAKRLQDYGF
CEEEHHHHHHHHCCC		54.19-
925PhosphorylationRFCDAMISIRQEIAD
HHHHHHHHHHHHHHH		9.91-
977UbiquitinationAFPLPFVKPENKFWP
ECCCCCCCCCCCCCC		47.17-
981UbiquitinationPFVKPENKFWPTIAR
CCCCCCCCCCCCEEC		47.33-
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 GCSP_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of GCSP_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 GCSP_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
GCSP_HUMANGLDCphysical
6778858
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
605899Non-ketotic hyperglycinemia (NKH)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00145Glycine
Regulatory Network of GCSP_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Phosphoproteome of resting human platelets.";
Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,Schuetz C., Walter U., Gambaryan S., Sickmann A.;
J. Proteome Res. 7:526-534(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-38 AND SER-39, AND MASSSPECTROMETRY.

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