C1TC_MOUSE - dbPTM
C1TC_MOUSE - PTM Information in dbPTM
Basic Information of Protein
UniProt ID C1TC_MOUSE
UniProt AC Q922D8
Protein Name C-1-tetrahydrofolate synthase, cytoplasmic
Gene Name Mthfd1
Organism Mus musculus (Mouse).
Sequence Length 935
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MAPAGILNGKLVSAQIRDRLKNQVTRMQEQVPGFTPGLAILQVGDRDDSNLYINVKLKAAEEIGIKATHIKLPRTSTESEVLKYVISLNEDASVHGFIVQLPLDSENSINTEAVINAIAPEKDVDGLTSVSAGKLARGDLNDCFIPCTPKGCLELIKEAGVQIAGRHAVVVGRSKIVGAPMHDLLLWNNATVTTCHSKTANLDKEVNKGDILVVATGQPEMVKGEWIKPGAVVIDCGINYVPDDTKPNGRKVVGDVAYDEAKERASFITPVPGGVGPMTVAMLMQSTVESAQRFLQKFKPGKWTIQYNKLNLKTPVPSDIAISRSCKPKLIGNLAREIGLLTEEVELYGETKAKVLLSALDRLKHQPDGKYVVVTGITPTPLGEGKSTTTIGLVQALGAHLRQNVFACVRQPSQGPTFGIKGGAAGGGYSQVIPMEEFNLHLTGDIHAITAANNLVAAAIDARIFHELTQTDKALFNRLVPSVNGIRKFSDIQIRRLRRLGIEKTDPTTLTDDEINRFARLDIDPETITWQRVLDTNDRFLRKITIGQSPTEKGHTRTAQFDISVASEIMAVLALTSSLEDMRERLGRMVVASSKKGEPISCEDLGVSGALTVLMKDAIKPNLMQTLEGTPVFVHAGPFANIAHGNSSIIADRIALKLVGPEGFVVTEAGFGADIGMEKFFNIKCRYSGLQPHVVVLVATVRALKMHGGGPTVTAGLPLPKAYTEEDLDLVEKGFSNLRKQIENARMFGVPVVVAVNVFKTDTDAELDLVSRLSREHGAFDAVKCTHWAEGGQGALALAQAVQRASQAPSSFQLLYDLKLSIEDKIRIIAQRIYGADDIELLPEAQNKAEIYTKQGFGNLPICMAKTHLSLSHNPEQKGVPTGFVLPIRDIRASVGAGFLYPLVGTMSTMPGLPTRPCFYDIDLDPETEQVNGLF
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
1Acetylation-------MAPAGILN
-------CCCCCCCC
10.20-
10UbiquitinationPAGILNGKLVSAQIR
CCCCCCCEEEHHHHH
44.64-
10MalonylationPAGILNGKLVSAQIR
CCCCCCCEEEHHHHH
44.6426320211
56AcetylationSNLYINVKLKAAEEI
CCEEEEEEEEEHHHH
39.5223954790
58AcetylationLYINVKLKAAEEIGI
EEEEEEEEEHHHHCC
39.5723954790
58MalonylationLYINVKLKAAEEIGI
EEEEEEEEEHHHHCC
39.5726320211
79PhosphorylationLPRTSTESEVLKYVI
CCCCCCHHHHHHHHH
32.8528464351
128PhosphorylationEKDVDGLTSVSAGKL
CCCCCCCCCCCCCCC
32.3921183079
134UbiquitinationLTSVSAGKLARGDLN
CCCCCCCCCCCCCCC
38.39-
143S-palmitoylationARGDLNDCFIPCTPK
CCCCCCCCCCCCCCH
3.0328526873
147S-palmitoylationLNDCFIPCTPKGCLE
CCCCCCCCCCHHHHH
9.7028526873
157UbiquitinationKGCLELIKEAGVQIA
HHHHHHHHHHCCEEC
54.88-
191PhosphorylationLLLWNNATVTTCHSK
EEEECCCEEEECCCC
22.1023140645
193PhosphorylationLWNNATVTTCHSKTA
EECCCEEEECCCCCC
21.2523140645
194PhosphorylationWNNATVTTCHSKTAN
ECCCEEEECCCCCCC
12.1323140645
195GlutathionylationNNATVTTCHSKTANL
CCCEEEECCCCCCCC
2.2024333276
195S-palmitoylationNNATVTTCHSKTANL
CCCEEEECCCCCCCC
2.2028526873
197PhosphorylationATVTTCHSKTANLDK
CEEEECCCCCCCCCC
33.5725521595
204MalonylationSKTANLDKEVNKGDI
CCCCCCCCCCCCCCE
67.7226320211
208UbiquitinationNLDKEVNKGDILVVA
CCCCCCCCCCEEEEE
64.24-
246AcetylationNYVPDDTKPNGRKVV
CCCCCCCCCCCCEEE
43.4023201123
251UbiquitinationDTKPNGRKVVGDVAY
CCCCCCCEEECCEEC
42.54-
258PhosphorylationKVVGDVAYDEAKERA
EEECCEECHHHHHHH
17.73-
262UbiquitinationDVAYDEAKERASFIT
CEECHHHHHHHCEEE
45.76-
262AcetylationDVAYDEAKERASFIT
CEECHHHHHHHCEEE
45.7623236377
262MalonylationDVAYDEAKERASFIT
CEECHHHHHHHCEEE
45.7626320211
297AcetylationSAQRFLQKFKPGKWT
HHHHHHHHHCCCCEE
58.4623201123
299AcetylationQRFLQKFKPGKWTIQ
HHHHHHHCCCCEEEE
60.9523864654
302AcetylationLQKFKPGKWTIQYNK
HHHHCCCCEEEEEEE
50.0923864654
309AcetylationKWTIQYNKLNLKTPV
CEEEEEEECCCCCCC
33.5423954790
309MalonylationKWTIQYNKLNLKTPV
CEEEEEEECCCCCCC
33.5426320211
309UbiquitinationKWTIQYNKLNLKTPV
CEEEEEEECCCCCCC
33.54-
313UbiquitinationQYNKLNLKTPVPSDI
EEEECCCCCCCCCCE
50.11-
313MalonylationQYNKLNLKTPVPSDI
EEEECCCCCCCCCCE
50.1126320211
318PhosphorylationNLKTPVPSDIAISRS
CCCCCCCCCEEECCC
41.71-
329UbiquitinationISRSCKPKLIGNLAR
ECCCCCHHHHHHHHH
37.93-
348PhosphorylationLTEEVELYGETKAKV
CHHEEHHHCHHHHHH
10.2229899451
351PhosphorylationEVELYGETKAKVLLS
EEHHHCHHHHHHHHH
31.7529899451
352UbiquitinationVELYGETKAKVLLSA
EHHHCHHHHHHHHHH
41.74-
354UbiquitinationLYGETKAKVLLSALD
HHCHHHHHHHHHHHH
34.66-
364AcetylationLSALDRLKHQPDGKY
HHHHHHHHCCCCCCE
40.8823201123
370AcetylationLKHQPDGKYVVVTGI
HHCCCCCCEEEEEEC
42.1023954790
370UbiquitinationLKHQPDGKYVVVTGI
HHCCCCCCEEEEEEC
42.10-
380PhosphorylationVVTGITPTPLGEGKS
EEEECCCCCCCCCCC
23.6123984901
387PhosphorylationTPLGEGKSTTTIGLV
CCCCCCCCHHHHHHH
41.6723984901
388PhosphorylationPLGEGKSTTTIGLVQ
CCCCCCCHHHHHHHH
31.2923984901
389PhosphorylationLGEGKSTTTIGLVQA
CCCCCCHHHHHHHHH
24.4123984901
390PhosphorylationGEGKSTTTIGLVQAL
CCCCCHHHHHHHHHH
17.0923984901
408S-palmitoylationLRQNVFACVRQPSQG
HHHCEEEEEECCCCC
1.4428526873
413PhosphorylationFACVRQPSQGPTFGI
EEEEECCCCCCCCEE
39.1629514104
417PhosphorylationRQPSQGPTFGIKGGA
ECCCCCCCCEECCCC
41.1222802335
473UbiquitinationHELTQTDKALFNRLV
HHHHHHCHHHHHHHC
50.83-
473MalonylationHELTQTDKALFNRLV
HHHHHHCHHHHHHHC
50.8326320211
473AcetylationHELTQTDKALFNRLV
HHHHHHCHHHHHHHC
50.8323236377
488UbiquitinationPSVNGIRKFSDIQIR
CCCCCCCCCCHHHHH
47.50-
488MalonylationPSVNGIRKFSDIQIR
CCCCCCCCCCHHHHH
47.5026320211
488AcetylationPSVNGIRKFSDIQIR
CCCCCCCCCCHHHHH
47.5022826441
490PhosphorylationVNGIRKFSDIQIRRL
CCCCCCCCHHHHHHH
36.5224759943
504UbiquitinationLRRLGIEKTDPTTLT
HHHCCCCCCCCCCCC
57.20-
511PhosphorylationKTDPTTLTDDEINRF
CCCCCCCCHHHHHHH
39.0326525534
543UbiquitinationTNDRFLRKITIGQSP
CCCCCCHHEEECCCC
46.47-
543MalonylationTNDRFLRKITIGQSP
CCCCCCHHEEECCCC
46.4726320211
545PhosphorylationDRFLRKITIGQSPTE
CCCCHHEEECCCCCC
23.3023984901
549PhosphorylationRKITIGQSPTEKGHT
HHEEECCCCCCCCCC
28.6925521595
551PhosphorylationITIGQSPTEKGHTRT
EEECCCCCCCCCCCE
56.4222324799
553MalonylationIGQSPTEKGHTRTAQ
ECCCCCCCCCCCEEE
59.4726320211
553AcetylationIGQSPTEKGHTRTAQ
ECCCCCCCCCCCEEE
59.4723806337
553UbiquitinationIGQSPTEKGHTRTAQ
ECCCCCCCCCCCEEE
59.47-
595AcetylationRMVVASSKKGEPISC
CHHHCCCCCCCCCCH
63.407631103
601PhosphorylationSKKGEPISCEDLGVS
CCCCCCCCHHHCCCC
23.3628059163
612PhosphorylationLGVSGALTVLMKDAI
CCCCHHHHHHHHHCC
15.8528059163
616AcetylationGALTVLMKDAIKPNL
HHHHHHHHHCCCCCH
39.597631113
620UbiquitinationVLMKDAIKPNLMQTL
HHHHHCCCCCHHHHH
29.58-
684UbiquitinationMEKFFNIKCRYSGLQ
HHHEEEEEECCCCCC
17.48-
721UbiquitinationTAGLPLPKAYTEEDL
ECCCCCCCCCCHHHH
62.80-
733UbiquitinationEDLDLVEKGFSNLRK
HHHHHHHHHHHHHHH
58.75-
736PhosphorylationDLVEKGFSNLRKQIE
HHHHHHHHHHHHHHH
43.5629472430
784UbiquitinationHGAFDAVKCTHWAEG
HCCCCEEECCCHHCC
34.83-
786PhosphorylationAFDAVKCTHWAEGGQ
CCCEEECCCHHCCCH
18.0917203969
810PhosphorylationQRASQAPSSFQLLYD
HHHHCCCCHHHHHHE
46.9625195567
811PhosphorylationRASQAPSSFQLLYDL
HHHCCCCHHHHHHEE
18.8919060867
819AcetylationFQLLYDLKLSIEDKI
HHHHHEECCCHHHHH
36.9723954790
848UbiquitinationLLPEAQNKAEIYTKQ
HCHHHHHHHEEECCC
35.00-
854UbiquitinationNKAEIYTKQGFGNLP
HHHEEECCCCCCCCC
31.30-
863S-palmitoylationGFGNLPICMAKTHLS
CCCCCCEEEEEEEEC
1.7328526873

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_MOUSE !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of C1TC_MOUSE !!

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_MOUSE !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions

Oops, there are no PPI records of C1TC_MOUSE !!

Drug and Disease Associations
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of C1TC_MOUSE

loading...

Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"Protein phosphorylation and expression profiling by Yin-yangmultidimensional liquid chromatography (Yin-yang MDLC) massspectrometry.";
Dai J., Jin W.-H., Sheng Q.-H., Shieh C.-H., Wu J.-R., Zeng R.;
J. Proteome Res. 6:250-262(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-786, AND MASSSPECTROMETRY.

TOP