C1TC_YEAST - dbPTM
C1TC_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C1TC_YEAST
UniProt AC P07245
Protein Name C-1-tetrahydrofolate synthase, cytoplasmic
Gene Name ADE3
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 946
Subcellular Localization Cytoplasm . Nucleus .
Protein Description
Protein Sequence MAGQVLDGKACAQQFRSNIANEIKSIQGHVPGFAPNLAIIQVGNRPDSATYVRMKRKAAEEAGIVANFIHLDESATEFEVLRYVDQLNEDPHTHGIIVQLPLPAHLDEDRITSRVLAEKDVDGFGPTNIGELNKKNGHPFFLPCTPKGIIELLHKANVTIEGSRSVVIGRSDIVGSPVAELLKSLNSTVTITHSKTRDIASYLHDADIVVVAIGQPEFVKGEWFKPRDGTSSDKKTVVIDVGTNYVADPSKKSGFKCVGDVEFNEAIKYVHLITPVPGGVGPMTVAMLMQNTLIAAKRQMEESSKPLQIPPLPLKLLTPVPSDIDISRAQQPKLINQLAQELGIYSHELELYGHYKAKISPKVIERLQTRQNGKYILVSGITPTPLGEGKSTTTMGLVQALTAHLGKPAIANVRQPSLGPTLGVKGGAAGGGYSQVIPMDEFNLHLTGDIHAIGAANNLLAAAIDTRMFHETTQKNDATFYNRLVPRKNGKRKFTPSMQRRLNRLGIQKTNPDDLTPEEINKFARLNIDPDTITIKRVVDINDRMLRQITIGQAPTEKNHTRVTGFDITVASELMAILALSKDLRDMKERIGRVVVAADVNRSPVTVEDVGCTGALTALLRDAIKPNLMQTLEGTPVLVHAGPFANISIGASSVIADRVALKLVGTEPEAKTEAGYVVTEAGFDFTMGGERFFNIKCRSSGLTPNAVVLVATVRALKSHGGAPDVKPGQPLPSAYTEENIEFVEKGAANMCKQIANIKQFGVPVVVAINKFETDTEGEIAAIRKAALEAGAFEAVTSNHWAEGGKGAIDLAKAVIEASNQPVDFHFLYDVNSSVEDKLTTIVQKMYGGAAIDILPEAQRKIDMYKEQGFGNLPICIAKTQYSLSHDATLKGVPTGFTFPIRDVRLSNGAGYLYALAAEIQTIPGLATYAGYMAVEVDDDGEIDGLF
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
17PhosphorylationACAQQFRSNIANEIK
HHHHHHHHHHHHHHH		33.6028889911
24AcetylationSNIANEIKSIQGHVP
HHHHHHHHHHCCCCC		35.0124489116
25PhosphorylationNIANEIKSIQGHVPG
HHHHHHHHHCCCCCC		26.3021440633
119AcetylationTSRVLAEKDVDGFGP
HHHEEEECCCCCCCC		58.4024489116
155AcetylationGIIELLHKANVTIEG
HHHHHHHHCCCEEEC		41.4424489116
176PhosphorylationGRSDIVGSPVAELLK
ECCCCCCCHHHHHHH		12.8122369663
184PhosphorylationPVAELLKSLNSTVTI
HHHHHHHHCCCEEEE		32.5221440633
194PhosphorylationSTVTITHSKTRDIAS
CEEEEEECCHHHHHH		27.3721440633
1952-HydroxyisobutyrylationTVTITHSKTRDIASY
EEEEEECCHHHHHHH		39.72-
236PhosphorylationGTSSDKKTVVIDVGT
CCCCCCCEEEEECCC		26.2522369663
243PhosphorylationTVVIDVGTNYVADPS
EEEEECCCCCCCCCC		24.1922369663
245PhosphorylationVIDVGTNYVADPSKK
EEECCCCCCCCCCCC		9.2422369663
250PhosphorylationTNYVADPSKKSGFKC
CCCCCCCCCCCCCEE		53.9522369663
251AcetylationNYVADPSKKSGFKCV
CCCCCCCCCCCCEEE		57.2424489116
274PhosphorylationIKYVHLITPVPGGVG
EEEEEEEECCCCCCC		25.2923749301
297UbiquitinationQNTLIAAKRQMEESS
HHHHHHHHHHHHHCC		33.8523749301
315UbiquitinationQIPPLPLKLLTPVPS
CCCCCCCHHCCCCCC		39.2424961812
318PhosphorylationPLPLKLLTPVPSDID
CCCCHHCCCCCCCCC		32.4522369663
322PhosphorylationKLLTPVPSDIDISRA
HHCCCCCCCCCCCHH		47.6422369663
327PhosphorylationVPSDIDISRAQQPKL
CCCCCCCCHHHCHHH		20.1629136822
362UbiquitinationYKAKISPKVIERLQT
ECCCCCHHHHHHHHH		49.4023749301
374UbiquitinationLQTRQNGKYILVSGI
HHHHCCCCEEEEEEC		36.3523749301
384PhosphorylationLVSGITPTPLGEGKS
EEEECCCCCCCCCCC		23.6128889911
407UbiquitinationALTAHLGKPAIANVR
HHHHHHCCCEECCCC		37.3223749301
417PhosphorylationIANVRQPSLGPTLGV
ECCCCCCCCCCCCCC		37.3022369663
421PhosphorylationRQPSLGPTLGVKGGA
CCCCCCCCCCCCCCC		34.0522369663
434PhosphorylationGAAGGGYSQVIPMDE
CCCCCCCCCEEECCC		22.6528889911
475AcetylationMFHETTQKNDATFYN
HHCHHCCCCCCCHHH		55.4924489116
495PhosphorylationKNGKRKFTPSMQRRL
CCCCCCCCHHHHHHH		19.9319779198
497PhosphorylationGKRKFTPSMQRRLNR
CCCCCCHHHHHHHHH		25.2125752575
510PhosphorylationNRLGIQKTNPDDLTP
HHHCCCCCCCCCCCH		35.2924909858
522UbiquitinationLTPEEINKFARLNID
CCHHHHHHHHHCCCC		46.1723749301
522AcetylationLTPEEINKFARLNID
CCHHHHHHHHHCCCC		46.1724489116
550PhosphorylationDRMLRQITIGQAPTE
HHHHHCCEECCCCCC		15.6622369663
556PhosphorylationITIGQAPTEKNHTRV
CEECCCCCCCCCCCC		63.7122369663
558AcetylationIGQAPTEKNHTRVTG
ECCCCCCCCCCCCCC		57.4124489116
662AcetylationIADRVALKLVGTEPE
HHHHHHHHHHCCCCC		31.2424489116
662UbiquitinationIADRVALKLVGTEPE
HHHHHHHHHHCCCCC		31.2423749301
860AcetylationILPEAQRKIDMYKEQ
HCHHHHHHHHHHHHC		30.8624489116
884PhosphorylationAKTQYSLSHDATLKG
EECEEECCCCCCCCC		17.2423749301
894PhosphorylationATLKGVPTGFTFPIR
CCCCCCCCCEEEEEC		42.3928889911
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 C1TC_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C1TC_YEAST !!
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 C1TC_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
HIP1_YEASTHIP1genetic
12684846
GLYM_YEASTSHM1genetic
12684846
C1TM_YEASTMIS1physical
16554755
MPG1_YEASTPSA1physical
16429126
RS3A1_YEASTRPS1Aphysical
16429126
FTHC_YEASTFAU1genetic
15744050
METE_YEASTMET6genetic
15744050
GLYC_YEASTSHM2genetic
15744050
PMU1_YEASTPMU1genetic
15744050
SSB1_YEASTSSB1physical
19536198
C1TC_YEASTADE3physical
19343713
ADK_YEASTADO1genetic
21757731
PNPP_YEASTPHO13genetic
21757731
I23O_YEASTBNA2genetic
24997118
PTE1_YEASTTES1genetic
24997118
FTHC_YEASTFAU1genetic
25893566
METE_YEASTMET6genetic
25893566
BAS1_YEASTBAS1genetic
25893566
GLYC_YEASTSHM2genetic
25893566
MRL1_YEASTMRL1genetic
27708008
SIW14_YEASTSIW14genetic
27708008
PMP1_YEASTPMP1physical
26404137
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of C1TC_YEAST

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A multidimensional chromatography technology for in-depthphosphoproteome analysis.";
Albuquerque C.P., Smolka M.B., Payne S.H., Bafna V., Eng J., Zhou H.;
Mol. Cell. Proteomics 7:1389-1396(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176; THR-318; SER-322;THR-384 AND THR-894, AND MASS SPECTROMETRY.

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