MTDC_HUMAN - dbPTM
MTDC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MTDC_HUMAN
UniProt AC P13995
Protein Name Bifunctional methylenetetrahydrofolate dehydrogenase/cyclohydrolase, mitochondrial
Gene Name MTHFD2
Organism Homo sapiens (Human).
Sequence Length 350
Subcellular Localization Mitochondrion.
Protein Description Although its dehydrogenase activity is NAD-specific, it can also utilize NADP at a reduced efficiency..
Protein Sequence MAATSLMSALAARLLQPAHSCSLRLRPFHLAAVRNEAVVISGRKLAQQIKQEVRQEVEEWVASGNKRPHLSVILVGENPASHSYVLNKTRAAAVVGINSETIMKPASISEEELLNLINKLNNDDNVDGLLVQLPLPEHIDERRICNAVSPDKDVDGFHVINVGRMCLDQYSMLPATPWGVWEIIKRTGIPTLGKNVVVAGRSKNVGMPIAMLLHTDGAHERPGGDATVTISHRYTPKEQLKKHTILADIVISAAGIPNLITADMIKEGAAVIDVGINRVHDPVTAKPKLVGDVDFEGVRQKAGYITPVPGGVGPMTVAMLMKNTIIAAKKVLRLEEREVLKSKELGVATN
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
4Phosphorylation----MAATSLMSALA
----CHHHHHHHHHH		16.9224043423
5Phosphorylation---MAATSLMSALAA
---CHHHHHHHHHHH		19.8324043423
8PhosphorylationMAATSLMSALAARLL
CHHHHHHHHHHHHHH		25.9824043423
20PhosphorylationRLLQPAHSCSLRLRP
HHHCCHHHCCEECCC		13.9124043423
22PhosphorylationLQPAHSCSLRLRPFH
HCCHHHCCEECCCCC		21.3824043423
44SuccinylationAVVISGRKLAQQIKQ
EEEECHHHHHHHHHH		52.2627452117
44UbiquitinationAVVISGRKLAQQIKQ
EEEECHHHHHHHHHH		52.2627667366
50AcetylationRKLAQQIKQEVRQEV
HHHHHHHHHHHHHHH		35.7519608861
50SuccinylationRKLAQQIKQEVRQEV
HHHHHHHHHHHHHHH		35.7527452117
50SumoylationRKLAQQIKQEVRQEV
HHHHHHHHHHHHHHH		35.7528112733
50UbiquitinationRKLAQQIKQEVRQEV
HHHHHHHHHHHHHHH		35.7524816145
50MalonylationRKLAQQIKQEVRQEV
HHHHHHHHHHHHHHH		35.7526320211
71PhosphorylationGNKRPHLSVILVGEN
CCCCCCEEEEEECCC		12.2228270605
81PhosphorylationLVGENPASHSYVLNK
EECCCCCCCHHHCCC		17.7728270605
83PhosphorylationGENPASHSYVLNKTR
CCCCCCCHHHCCCCC		17.9128270605
84PhosphorylationENPASHSYVLNKTRA
CCCCCCHHHCCCCCC		11.9728270605
88UbiquitinationSHSYVLNKTRAAAVV
CCHHHCCCCCCEEEE		34.9223503661
88AcetylationSHSYVLNKTRAAAVV
CCHHHCCCCCCEEEE		34.9225953088
89PhosphorylationHSYVLNKTRAAAVVG
CHHHCCCCCCEEEEE		25.1928270605
92UbiquitinationVLNKTRAAAVVGINS
HCCCCCCEEEEECCC		9.4827667366
104UbiquitinationINSETIMKPASISEE
CCCCCCCCCCCCCHH		33.31-
119UbiquitinationELLNLINKLNNDDNV
HHHHHHHHHCCCCCC		45.6729967540
135UbiquitinationGLLVQLPLPEHIDER
EEEEECCCCCCCCCC		12.0627667366
143MethylationPEHIDERRICNAVSP
CCCCCCCCCCCCCCC		35.45115484051
149PhosphorylationRRICNAVSPDKDVDG
CCCCCCCCCCCCCCC		25.6028464451
152UbiquitinationCNAVSPDKDVDGFHV
CCCCCCCCCCCCEEE		64.1424816145
152AcetylationCNAVSPDKDVDGFHV
CCCCCCCCCCCCEEE		64.1425825284
184UbiquitinationPWGVWEIIKRTGIPT
CCCHHHHHHHHCCCC		1.3521890473
184UbiquitinationPWGVWEIIKRTGIPT
CCCHHHHHHHHCCCC		1.3522817900
186UbiquitinationGVWEIIKRTGIPTLG
CHHHHHHHHCCCCCC		27.9822817900
187PhosphorylationVWEIIKRTGIPTLGK
HHHHHHHHCCCCCCC		34.1721406692
191PhosphorylationIKRTGIPTLGKNVVV
HHHHCCCCCCCCEEE		46.3421406692
194UbiquitinationTGIPTLGKNVVVAGR
HCCCCCCCCEEEEEC		50.0827667366
194MalonylationTGIPTLGKNVVVAGR
HCCCCCCCCEEEEEC		50.0826320211
199UbiquitinationLGKNVVVAGRSKNVG
CCCCEEEEECCCCCC		8.9621963094
227UbiquitinationERPGGDATVTISHRY
CCCCCCCEEEEEECC		23.9527667366
229PhosphorylationPGGDATVTISHRYTP
CCCCCEEEEEECCCC		16.6532142685
234PhosphorylationTVTISHRYTPKEQLK
EEEEEECCCCHHHHH		23.2129496907
237UbiquitinationISHRYTPKEQLKKHT
EEECCCCHHHHHHCC		50.7427667366
239UbiquitinationHRYTPKEQLKKHTIL
ECCCCHHHHHHCCHH		65.7821890473
239UbiquitinationHRYTPKEQLKKHTIL
ECCCCHHHHHHCCHH		65.7821890473
241UbiquitinationYTPKEQLKKHTILAD
CCCHHHHHHCCHHHH		42.0521890473
241UbiquitinationYTPKEQLKKHTILAD
CCCHHHHHHCCHHHH		42.0522817900
286AcetylationVHDPVTAKPKLVGDV
CCCCCCCCCCEECCC		33.0623236377
286UbiquitinationVHDPVTAKPKLVGDV
CCCCCCCCCCEECCC		33.0621906983
288UbiquitinationDPVTAKPKLVGDVDF
CCCCCCCCEECCCCC		55.9122817900
301UbiquitinationDFEGVRQKAGYITPV
CCCCHHHHCCEEECC		32.9621963094
306PhosphorylationRQKAGYITPVPGGVG
HHHCCEEECCCCCCC		15.11-
324PhosphorylationVAMLMKNTIIAAKKV
HHHHHHHHHHHHHHH		14.29-
329UbiquitinationKNTIIAAKKVLRLEE
HHHHHHHHHHHHHHH		34.1027667366
329AcetylationKNTIIAAKKVLRLEE
HHHHHHHHHHHHHHH		34.1030582777
341UbiquitinationLEEREVLKSKELGVA
HHHHHHHHHHHHCCC		65.7321906983
342PhosphorylationEEREVLKSKELGVAT
HHHHHHHHHHHCCCC		27.4822468782
343UbiquitinationEREVLKSKELGVATN
HHHHHHHHHHCCCCC		56.2021906983
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 MTDC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of MTDC_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 MTDC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
NAGK_HUMANNAGKphysical
25416956
CLIC1_HUMANCLIC1physical
26344197
NAGK_HUMANNAGKphysical
21516116
MTD2L_HUMANMTHFD2Lphysical
28514442
ACADL_HUMANACADLphysical
28514442
TFCP2_HUMANTFCP2physical
28514442
RASH_HUMANHRASphysical
28514442
UBIP1_HUMANUBP1physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
There are no disease associations of PTM sites.
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
DB00116Tetrahydrofolic acid
Regulatory Network of MTDC_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-50, AND MASS SPECTROMETRY.

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