C1TM_YEAST - dbPTM
C1TM_YEAST - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C1TM_YEAST
UniProt AC P09440
Protein Name C-1-tetrahydrofolate synthase, mitochondrial
Gene Name MIS1
Organism Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast).
Sequence Length 975
Subcellular Localization Mitochondrion .
Protein Description
Protein Sequence MLSRLSLLSNSRAFQQARWRIYRLKVSPTVHASQYHILSGRKLAQSIREKANDEIQAIKLKHPNFKPTLKIIQVGARPDSSTYVRMKLKASKDSNVDCIIEKLPAEITEVELLKKISDINDDDSIHGLLIQLPLPRHLDETTITNAVDFKKDVDGFHRYNAGELAKKGGKPYFIPCTPYGCMKLLEEAHVKLDGKNAVVLGRSSIVGNPIASLLKNANATVTVCHSHTRNIAEVVSQADIVIAACGIPQYVKSDWIKEGAVVIDVGINYVPDISKKSGQKLVGDVDFDSVKEKTSYITPVPGGVGPMTVAMLVSNVLLAAKRQFVESEKLPVIKPLPLHLESPVPSDIDISRAQSPKHIKQVAEELGIHSHELELYGHYKAKISPNIFKRLESRENGKYVLVAGITPTPLGEGKSTTTMGLVQALSAHLGKPSIANVRQPSLGPTLGVKGGAAGGGYAQVIPMDEFNLHLTGDIHAISAANNLLAAAIDTRMFHEATQKNDSTFYKRLVPRKKGIRKFTPSMQRRLKRLDIEKEDPDALTPEEVKRFARLNINPDTITIRRVVDINDRMLRQITIGEAATEKGFTRTTGFDITVASELMAILALSKSLHEMKERIGRMVIGADYDNKPVTVEDIGCTGALTALLRDAIKPNLMQTLEGTPVMVHAGPFANISIGASSVIADLMALKLVGSEKNPLNDKNIHEPGYVVTEAGFDFAMGGERFFDIKCRSSGLVPDAVVLVATVRALKSHGGAPNVKPGQSLPKEYTEENIDFVAKGVSNLVKQIENIKTFGIPVVVAINRFETDSQAEIEVIKKAALNAGASHAVTSNHWMEGGKGAVELAHAVVDATKEPKNFNFLYDVNSSIEDKLTSIVQKMYGGAKIEVSPEAQKKIDTYKKQGFGNLPICIAKTQYSLSHDPSLKGVPRGFTFPIRDVRASIGAGYLYALAAEIQTIPGLSTYAGYMAVEVDDDGEIEGLF
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
27PhosphorylationRIYRLKVSPTVHASQ
HEEEEEECCCEEHHH		17.1728889911
29PhosphorylationYRLKVSPTVHASQYH
EEEEECCCEEHHHEE		19.8828889911
39PhosphorylationASQYHILSGRKLAQS
HHHEEHHHCHHHHHH		35.6328889911
59AcetylationNDEIQAIKLKHPNFK
HHHHHHHHCCCCCCC		55.2724489116
92AcetylationRMKLKASKDSNVDCI
EEEEECCCCCCCCEE		70.7725381059
114AcetylationITEVELLKKISDIND
CEEHHHHHHHHCCCC		61.7624489116
124PhosphorylationSDINDDDSIHGLLIQ
HCCCCCCCCEEEEEE		24.3921440633
150AcetylationITNAVDFKKDVDGFH
ECCCCCCCCCCCCCC		43.5324489116
191AcetylationLLEEAHVKLDGKNAV
HHHHHCEEECCCCEE		30.8724489116
280AcetylationISKKSGQKLVGDVDF
CCHHCCCCEECCCCH		48.9824489116
289PhosphorylationVGDVDFDSVKEKTSY
ECCCCHHHHCCCCCE		34.7719795423
291AcetylationDVDFDSVKEKTSYIT
CCCHHHHCCCCCEEE		58.4024489116
329AcetylationRQFVESEKLPVIKPL
HHHHHCCCCCCCCCC		68.3322865919
334AcetylationSEKLPVIKPLPLHLE
CCCCCCCCCCCCCCC		40.5124489116
346PhosphorylationHLESPVPSDIDISRA
CCCCCCCCCCCCHHC		47.64-
351PhosphorylationVPSDIDISRAQSPKH
CCCCCCCHHCCCHHH		20.1620377248
355PhosphorylationIDISRAQSPKHIKQV
CCCHHCCCHHHHHHH		34.6220377248
399PhosphorylationESRENGKYVLVAGIT
HHCCCCCEEEEEEEC		10.6229688323
406PhosphorylationYVLVAGITPTPLGEG
EEEEEEECCCCCCCC		21.8629688323
408PhosphorylationLVAGITPTPLGEGKS
EEEEECCCCCCCCCC		23.6129688323
426PhosphorylationMGLVQALSAHLGKPS
HHHHHHHHHHCCCCC		19.3623749301
431AcetylationALSAHLGKPSIANVR
HHHHHCCCCCCCCCC		41.7924489116
431UbiquitinationALSAHLGKPSIANVR
HHHHHCCCCCCCCCC		41.7923749301
441PhosphorylationIANVRQPSLGPTLGV
CCCCCCCCCCCCCCC		37.3022369663
445PhosphorylationRQPSLGPTLGVKGGA
CCCCCCCCCCCCCCC		34.0522369663
499AcetylationMFHEATQKNDSTFYK
HHHHHHCCCCCCHHH		59.3724489116
506SuccinylationKNDSTFYKRLVPRKK
CCCCCHHHHHCCCCC		34.7623954790
506AcetylationKNDSTFYKRLVPRKK
CCCCCHHHHHCCCCC		34.7624489116
519PhosphorylationKKGIRKFTPSMQRRL
CCCHHHCCHHHHHHH		19.9319779198
521PhosphorylationGIRKFTPSMQRRLKR
CHHHCCHHHHHHHHH		25.2125752575
533AcetylationLKRLDIEKEDPDALT
HHHCCCCCCCCCCCC		68.6924489116
540PhosphorylationKEDPDALTPEEVKRF
CCCCCCCCHHHHHHH		30.3028889911
545AcetylationALTPEEVKRFARLNI
CCCHHHHHHHHHCCC		45.1124489116
556PhosphorylationRLNINPDTITIRRVV
HCCCCCCCEEEEEEE		22.6821440633
574PhosphorylationDRMLRQITIGEAATE
HHHEEEEEHHHHHHH		18.0022369663
580PhosphorylationITIGEAATEKGFTRT
EEHHHHHHHCCCCCC		45.3222369663
582AcetylationIGEAATEKGFTRTTG
HHHHHHHCCCCCCCC		55.7824489116
587PhosphorylationTEKGFTRTTGFDITV
HHCCCCCCCCCCHHH		28.3629688323
588PhosphorylationEKGFTRTTGFDITVA
HCCCCCCCCCCHHHH		32.3429688323
593PhosphorylationRTTGFDITVASELMA
CCCCCCHHHHHHHHH		16.3229688323
596PhosphorylationGFDITVASELMAILA
CCCHHHHHHHHHHHH		27.2529688323
605PhosphorylationLMAILALSKSLHEMK
HHHHHHHHHHHHHHH		18.0029688323
612AcetylationSKSLHEMKERIGRMV
HHHHHHHHHHHHCEE		40.6425381059
802PhosphorylationVAINRFETDSQAEIE
EEEECCCCCCHHHHH		37.9328889911
804PhosphorylationINRFETDSQAEIEVI
EECCCCCCHHHHHHH		38.4228889911
879AcetylationQKMYGGAKIEVSPEA
HHHHCCCEEEECHHH		42.5524489116
895AcetylationKKIDTYKKQGFGNLP
HHHHHHHHCCCCCCC		45.2822865919
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 C1TM_YEAST !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C1TM_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 C1TM_YEAST !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
RLA3_YEASTRPP1Bphysical
16554755
SPT16_YEASTSPT16physical
16554755
LONM_YEASTPIM1physical
16429126
RL10_YEASTRPL10physical
16429126
RL17A_YEASTRPL17Aphysical
16429126
RL27A_YEASTRPL27Aphysical
16429126
RL6B_YEASTRPL6Bphysical
16429126
RS3A2_YEASTRPS1Bphysical
16429126
RLA0_YEASTRPP0physical
16429126
GBLP_YEASTASC1physical
16429126
RL5_YEASTRPL5physical
16429126
AEP3_YEASTAEP3genetic
19843529
CRD1_YEASTCRD1genetic
21623372
PDE2_YEASTPDE2genetic
21623372
MGR1_YEASTMGR1genetic
27708008
RIM1_YEASTRIM1genetic
27708008
GUAD_YEASTGUD1genetic
27708008
RAV2_YEASTRAV2genetic
27708008
DON1_YEASTDON1genetic
27708008
VAM7_YEASTVAM7genetic
27708008
YIA6_YEASTYIA6genetic
27708008
ITPA_YEASTHAM1genetic
27708008
AMPD_YEASTAMD1genetic
27708008
ATP18_YEASTATP18genetic
27708008
BUL2_YEASTBUL2genetic
27708008
IZH4_YEASTIZH4genetic
27708008
MPD1_YEASTMPD1genetic
27708008
GNT1_YEASTGNT1genetic
27708008
YP148_YEASTYPR148Cgenetic
27708008
VPS8_YEASTVPS8genetic
27708008
ATS1_YEASTATS1genetic
27708008
GFD2_YEASTGFD2genetic
27708008
MTU1_YEASTSLM3genetic
27708008
HOSM_YEASTLYS21genetic
27708008
CRD1_YEASTCRD1genetic
27708008
UGA4_YEASTUGA4genetic
27708008
DPP1_YEASTDPP1genetic
27708008
YSP2_YEASTYSP2genetic
27708008
LSM6_YEASTLSM6genetic
27708008
RSM28_YEASTRSM28genetic
27708008
WWM1_YEASTWWM1genetic
27708008
DLDH_YEASTLPD1genetic
27708008
ARO8_YEASTARO8genetic
27708008
EFM5_YEASTAML1genetic
27708008
MSP1_YEASTMSP1genetic
27708008
BIOB_YEASTBIO2genetic
27708008
YIC9_YEASTYIL029Cgenetic
27708008
YIF4_YEASTYIL054Wgenetic
27708008
MAD2_YEASTMAD2genetic
27708008
YJT3_YEASTYJL193Wgenetic
27708008
AIM24_YEASTAIM24genetic
27708008
RGT1_YEASTRGT1genetic
27708008
ZRT3_YEASTZRT3genetic
27708008
BAS1_YEASTBAS1genetic
27708008
NMD4_YEASTNMD4genetic
27708008
PP2B1_YEASTCNA1genetic
27708008
SST2_YEASTSST2genetic
27708008
RCF1_YEASTRCF1genetic
27708008
ASND1_YEASTYML096Wgenetic
27708008
YM100_YEASTYML100W-Agenetic
27708008
YM085_YEASTYMR085Wgenetic
27708008
YM22_YEASTYMR144Wgenetic
27708008
ERG2_YEASTERG2genetic
27708008
ADH6_YEASTADH6genetic
27708008
SPO1_YEASTSPO1genetic
27708008
PUB1_YEASTPUB1genetic
27708008
BOP3_YEASTBOP3genetic
27708008
AF9_YEASTYAF9genetic
27708008
TAT2_YEASTTAT2genetic
27708008
INO4_YEASTINO4genetic
27708008
MDY2_YEASTMDY2genetic
27708008
VPS68_YEASTVPS68genetic
27708008
PDP1_YEASTPTC5genetic
27708008
RS28A_YEASTRPS28Agenetic
27708008
BUD7_YEASTBUD7genetic
27708008
MSC6_YEASTMSC6genetic
27708008
VTS1_YEASTVTS1genetic
27708008
CHL1_YEASTCHL1genetic
27708008
OAZ_YEASTOAZ1genetic
27708008
YP225_YEASTYPL225Wgenetic
27708008
PUF2_YEASTPUF2genetic
27708008
Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of C1TM_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-521, AND MASSSPECTROMETRY.

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