VKGC_HUMAN - dbPTM
VKGC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID VKGC_HUMAN
UniProt AC P38435
Protein Name Vitamin K-dependent gamma-carboxylase
Gene Name GGCX
Organism Homo sapiens (Human).
Sequence Length 758
Subcellular Localization Endoplasmic reticulum membrane
Multi-pass membrane protein .
Protein Description Mediates the vitamin K-dependent carboxylation of glutamate residues to calcium-binding gamma-carboxyglutamate (Gla) residues with the concomitant conversion of the reduced hydroquinone form of vitamin K to vitamin K epoxide..
Protein Sequence MAVSAGSARTSPSSDKVQKDKAELISGPRQDSRIGKLLGFEWTDLSSWRRLVTLLNRPTDPASLAVFRFLFGFLMVLDIPQERGLSSLDRKYLDGLDVCRFPLLDALRPLPLDWMYLVYTIMFLGALGMMLGLCYRISCVLFLLPYWYVFLLDKTSWNNHSYLYGLLAFQLTFMDANHYWSVDGLLNAHRRNAHVPLWNYAVLRGQIFIVYFIAGVKKLDADWVEGYSMEYLSRHWLFSPFKLLLSEELTSLLVVHWGGLLLDLSAGFLLFFDVSRSIGLFFVSYFHCMNSQLFSIGMFSYVMLASSPLFCSPEWPRKLVSYCPRRLQQLLPLKAAPQPSVSCVYKRSRGKSGQKPGLRHQLGAAFTLLYLLEQLFLPYSHFLTQGYNNWTNGLYGYSWDMMVHSRSHQHVKITYRDGRTGELGYLNPGVFTQSRRWKDHADMLKQYATCLSRLLPKYNVTEPQIYFDIWVSINDRFQQRIFDPRVDIVQAAWSPFQRTSWVQPLLMDLSPWRAKLQEIKSSLDNHTEVVFIADFPGLHLENFVSEDLGNTSIQLLQGEVTVELVAEQKNQTLREGEKMQLPAGEYHKVYTTSPSPSCYMYVYVNTTELALEQDLAYLQELKEKVENGSETGPLPPELQPLLEGEVKGGPEPTPLVQTFLRRQQRLQEIERRRNTPFHERFFRFLLRKLYVFRRSFLMTCISLRNLILGRPSLEQLAQEVTYANLRPFEAVGELNPSNTDSSHSNPPESNPDPVHSEF
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
2Acetylation------MAVSAGSAR
------CCCCCCCCC		12.1721406692
4Phosphorylation----MAVSAGSARTS
----CCCCCCCCCCC		19.8520068231
4 (in isoform 2)Phosphorylation-19.8524719451
7Phosphorylation-MAVSAGSARTSPSS
-CCCCCCCCCCCCCC		17.8125159151
10PhosphorylationVSAGSARTSPSSDKV
CCCCCCCCCCCCHHH		44.7130266825
11PhosphorylationSAGSARTSPSSDKVQ
CCCCCCCCCCCHHHH		19.7530266825
13PhosphorylationGSARTSPSSDKVQKD
CCCCCCCCCHHHHHH		51.4330266825
13 (in isoform 2)Phosphorylation-51.4324719451
14PhosphorylationSARTSPSSDKVQKDK
CCCCCCCCHHHHHHH		44.8530266825
16UbiquitinationRTSPSSDKVQKDKAE
CCCCCCHHHHHHHHH		48.8129967540
19AcetylationPSSDKVQKDKAELIS
CCCHHHHHHHHHHHC		65.277673983
19UbiquitinationPSSDKVQKDKAELIS
CCCHHHHHHHHHHHC		65.27-
21UbiquitinationSDKVQKDKAELISGP
CHHHHHHHHHHHCCC		51.2829901268
26PhosphorylationKDKAELISGPRQDSR
HHHHHHHCCCCCCCH		56.20-
29 (in isoform 2)Phosphorylation-57.3624719451
29PhosphorylationAELISGPRQDSRIGK
HHHHCCCCCCCHHHH		57.3624719451
34UbiquitinationGPRQDSRIGKLLGFE
CCCCCCHHHHHHCCC		7.0821890473
34UbiquitinationGPRQDSRIGKLLGFE
CCCCCCHHHHHHCCC		7.0821890473
36UbiquitinationRQDSRIGKLLGFEWT
CCCCHHHHHHCCCCC		37.8621963094
60UbiquitinationTLLNRPTDPASLAVF
HHHCCCCCHHHHHHH		39.1821890473
91UbiquitinationGLSSLDRKYLDGLDV
CCCCCCHHHCCCCCC		50.2423000965
135PhosphorylationGMMLGLCYRISCVLF
HHHHHHHHHHHHHHH		18.9422817900
227PhosphorylationDADWVEGYSMEYLSR
CCCHHCCCCHHHHHH		7.4329759185
228PhosphorylationADWVEGYSMEYLSRH
CCHHCCCCHHHHHHH		18.9229759185
233PhosphorylationGYSMEYLSRHWLFSP
CCCHHHHHHHHHCCH		22.6129759185
261UbiquitinationVVHWGGLLLDLSAGF
HHHCHHHHHHCCCCH		3.8529901268
277UbiquitinationLFFDVSRSIGLFFVS
HHHHHHHHHHHHHHH		17.3221890473
277UbiquitinationLFFDVSRSIGLFFVS
HHHHHHHHHHHHHHH		17.3221963094
289UbiquitinationFVSYFHCMNSQLFSI
HHHHHHHHCCHHHHH		3.9829901268
318UbiquitinationCSPEWPRKLVSYCPR
CCCCCHHHHHHHCHH		49.5129901268
334UbiquitinationLQQLLPLKAAPQPSV
HHHHCCCCCCCCCCE		40.3321963094
346UbiquitinationPSVSCVYKRSRGKSG
CCEEEEEECCCCCCC		24.4129901268
351UbiquitinationVYKRSRGKSGQKPGL
EEECCCCCCCCCCCH		50.75-
381UbiquitinationQLFLPYSHFLTQGYN
HHHCCHHHHHCCCCC		18.8529967540
388UbiquitinationHFLTQGYNNWTNGLY
HHHCCCCCCCCCCCC		44.3729967540
438UbiquitinationFTQSRRWKDHADMLK
CCCCHHHHHHHHHHH		37.5129967540
445UbiquitinationKDHADMLKQYATCLS
HHHHHHHHHHHHHHH		34.3329967540
447PhosphorylationHADMLKQYATCLSRL
HHHHHHHHHHHHHHH		11.4228331001
458UbiquitinationLSRLLPKYNVTEPQI
HHHHHHHCCCCCCEE		16.9629967540
459N-linked_GlycosylationSRLLPKYNVTEPQIY
HHHHHHCCCCCCEEE		40.1219159218
494PhosphorylationDIVQAAWSPFQRTSW
CHHHHCCCCCCCCCC		15.8820068231
515UbiquitinationDLSPWRAKLQEIKSS
CCCHHHHHHHHHHHH		41.9729967540
521UbiquitinationAKLQEIKSSLDNHTE
HHHHHHHHHCCCCCE		41.6229967540
550N-linked_GlycosylationFVSEDLGNTSIQLLQ
HHCCCCCCCEEEEEE		37.6419159218
578UbiquitinationQTLREGEKMQLPAGE
CCHHCCCCEECCCCC		42.6829967540
653O-linked_GlycosylationVKGGPEPTPLVQTFL
CCCCCCCCHHHHHHH		27.8231492838
695PhosphorylationKLYVFRRSFLMTCIS
HHHHHHHHHHHHHHH		20.62-
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 VKGC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of VKGC_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 VKGC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of VKGC_HUMAN !!
Drug and Disease Associations
Kegg Disease
H00560 Pseudoxanthoma elasticum, including: Pseudoxanthoma elasticum (PXE); Pseudoxanthoma elasticum-like d
H00995 Combined deficiency of vitamin K-dependent clotting factors (VKCFD)
H01205 Coumarin resistance; Warfarin resistance
OMIM Disease
277450Combined deficiency of vitamin K-dependent clotting factors 1 (VKCFD1)
610842Pseudoxanthoma elasticum-like disorder with multiple coagulation factor deficiency (PXEL-MCFD)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of VKGC_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11, AND MASS SPECTROMETRY.
N-linked Glycosylation
ReferencePubMed
"Glycoproteomics analysis of human liver tissue by combination ofmultiple enzyme digestion and hydrazide chemistry.";
Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.;
J. Proteome Res. 8:651-661(2009).
Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-459 AND ASN-550, AND MASSSPECTROMETRY.
Phosphorylation
ReferencePubMed
"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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGESCALE ANALYSIS] AT SER-11, AND MASS SPECTROMETRY.

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