CGL_HUMAN - dbPTM
CGL_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID CGL_HUMAN
UniProt AC P32929
Protein Name Cystathionine gamma-lyase
Gene Name CTH
Organism Homo sapiens (Human).
Sequence Length 405
Subcellular Localization Cytoplasm.
Protein Description Catalyzes the last step in the trans-sulfuration pathway from methionine to cysteine. Has broad substrate specificity. Converts cystathionine to cysteine, ammonia and 2-oxobutanoate. Converts two cysteine molecules to lanthionine and hydrogen sulfide. Can also accept homocysteine as substrate. Specificity depends on the levels of the endogenous substrates. Generates the endogenous signaling molecule hydrogen sulfide (H2S), and so contributes to the regulation of blood pressure. Acts as a cysteine-protein sulfhydrase by mediating sulfhydration of target proteins: sulfhydration consists of converting -SH groups into -SSH on specific cysteine residues of target proteins such as GAPDH, PTPN1 and NF-kappa-B subunit RELA, thereby regulating their function..
Protein Sequence MQEKDASSQGFLPHFQHFATQAIHVGQDPEQWTSRAVVPPISLSTTFKQGAPGQHSGFEYSRSGNPTRNCLEKAVAALDGAKYCLAFASGLAATVTITHLLKAGDQIICMDDVYGGTNRYFRQVASEFGLKISFVDCSKIKLLEAAITPETKLVWIETPTNPTQKVIDIEGCAHIVHKHGDIILVVDNTFMSPYFQRPLALGADISMYSATKYMNGHSDVVMGLVSVNCESLHNRLRFLQNSLGAVPSPIDCYLCNRGLKTLHVRMEKHFKNGMAVAQFLESNPWVEKVIYPGLPSHPQHELVKRQCTGCTGMVTFYIKGTLQHAEIFLKNLKLFTLAESLGGFESLAELPAIMTHASVLKNDRDVLGISDTLIRLSVGLEDEEDLLEDLDQALKAAHPPSGSHS
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
8PhosphorylationMQEKDASSQGFLPHF
CCHHHHHCCCCCHHH		35.7217525332
43UbiquitinationAVVPPISLSTTFKQG
CCCCCEEEECEECCC		5.6621963094
48UbiquitinationISLSTTFKQGAPGQH
EEEECEECCCCCCCC		45.8129967540
56PhosphorylationQGAPGQHSGFEYSRS
CCCCCCCCCCCCCCC		36.97-
60PhosphorylationGQHSGFEYSRSGNPT
CCCCCCCCCCCCCCC		13.7125159151
73UbiquitinationPTRNCLEKAVAALDG
CCCCHHHHHHHHHCH		34.9021890473
73UbiquitinationPTRNCLEKAVAALDG
CCCCHHHHHHHHHCH		34.9021963094
73 (in isoform 1)Ubiquitination-34.9021890473
73AcetylationPTRNCLEKAVAALDG
CCCCHHHHHHHHHCH		34.9026051181
73 (in isoform 2)Ubiquitination-34.9021890473
78UbiquitinationLEKAVAALDGAKYCL
HHHHHHHHCHHHHHH		4.5022817900
81UbiquitinationAVAALDGAKYCLAFA
HHHHHCHHHHHHHHH		10.1821963094
107UbiquitinationLLKAGDQIICMDDVY
HHHCCCEEEEECCCC		2.8929967540
109UbiquitinationKAGDQIICMDDVYGG
HCCCEEEEECCCCCC		2.3329967540
120UbiquitinationVYGGTNRYFRQVASE
CCCCCCHHHHHHHHH		12.7521963094
139UbiquitinationISFVDCSKIKLLEAA
EEEEEHHHCCHHHCC		50.6329967540
141UbiquitinationFVDCSKIKLLEAAIT
EEEHHHCCHHHCCCC		51.2429967540
152UbiquitinationAAITPETKLVWIETP
CCCCCCCEEEEEECC		39.1121963094
152 (in isoform 1)Ubiquitination-39.1121890473
159UbiquitinationKLVWIETPTNPTQKV
EEEEEECCCCCCCCE		19.8622817900
162UbiquitinationWIETPTNPTQKVIDI
EEECCCCCCCCEEEE		38.3921963094
212N6-(pyridoxal phosphate)lysineISMYSATKYMNGHSD
EEEEECCHHHCCCCC		42.07-
212AcetylationISMYSATKYMNGHSD
EEEEECCHHHCCCCC		42.077373219
212OtherISMYSATKYMNGHSD
EEEEECCHHHCCCCC		42.07-
224UbiquitinationHSDVVMGLVSVNCES
CCCCEEEEEECCHHH		1.0822817900
227UbiquitinationVVMGLVSVNCESLHN
CEEEEEECCHHHHHH		8.0821963094
236UbiquitinationCESLHNRLRFLQNSL
HHHHHHHHHHHHHCC		5.7222817900
239UbiquitinationLHNRLRFLQNSLGAV
HHHHHHHHHHCCCCC		3.6821963094
244UbiquitinationRFLQNSLGAVPSPID
HHHHHCCCCCCCCHH		25.0929967540
256UbiquitinationPIDCYLCNRGLKTLH
CHHHHCCCCCCCHHH		38.1629967540
268UbiquitinationTLHVRMEKHFKNGMA
HHHHHHHHHHCCCHH		45.0222817900
271UbiquitinationVRMEKHFKNGMAVAQ
HHHHHHHCCCHHHHH		52.9221963094
282PhosphorylationAVAQFLESNPWVEKV
HHHHHHHHCCCCCEE		50.7921082442
286UbiquitinationFLESNPWVEKVIYPG
HHHHCCCCCEEECCC		5.5629967540
288UbiquitinationESNPWVEKVIYPGLP
HHCCCCCEEECCCCC		25.0629967540
298UbiquitinationYPGLPSHPQHELVKR
CCCCCCCCHHHHHHH		41.3729967540
304UbiquitinationHPQHELVKRQCTGCT
CCHHHHHHHHCCCCC		49.75-
330UbiquitinationQHAEIFLKNLKLFTL
HHHHHHHHHHHHHHH		49.8629967540
333UbiquitinationEIFLKNLKLFTLAES
HHHHHHHHHHHHHHH		51.45-
351UbiquitinationFESLAELPAIMTHAS
CHHHHHHHHHHHHHH		15.9629967540
363UbiquitinationHASVLKNDRDVLGIS
HHHHHHCCCCHHCCC		46.7129967540
377PhosphorylationSDTLIRLSVGLEDEE
CHHHHHHHCCCCCHH		12.3219060867
395UbiquitinationEDLDQALKAAHPPSG
HHHHHHHHHHCCCCC		46.6829967540
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
377SPhosphorylationKinasePRKG2Q13237
GPS
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of CGL_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 CGL_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
CGL_HUMANCTHphysical
16189514
SDCB2_HUMANSDCBP2physical
21988832
PUR9_HUMANATICphysical
22863883
CAN2_HUMANCAPN2physical
22863883
PTMA_HUMANPTMAphysical
22863883
CGL_HUMANCTHphysical
25416956
RECK_HUMANRECKphysical
25416956
NTAQ1_HUMANWDYHV1physical
25416956
GUCD1_HUMANGUCD1physical
25416956
ACLY_HUMANACLYphysical
26344197
CTBP1_HUMANCTBP1physical
26344197
DUT_HUMANDUTphysical
26344197
ENOG_HUMANENO2physical
26344197
FPPS_HUMANFDPSphysical
26344197
CH10_HUMANHSPE1physical
26344197
PAPS2_HUMANPAPSS2physical
26344197
PPCE_HUMANPREPphysical
26344197
RPE_HUMANRPEphysical
26344197
SC31A_HUMANSEC31Aphysical
26344197
PRPK_HUMANTP53RKphysical
26344197
WDR1_HUMANWDR1physical
26344197
G3PT_HUMANGAPDHSphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
219500Cystathioninuria (CSTNU)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00151L-Cysteine
Regulatory Network of CGL_HUMAN

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"ATM and ATR substrate analysis reveals extensive protein networksresponsive to DNA damage.";
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
Science 316:1160-1166(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-8, AND MASSSPECTROMETRY.

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