MDHC_HUMAN - dbPTM
MDHC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID MDHC_HUMAN
UniProt AC P40925
Protein Name Malate dehydrogenase, cytoplasmic
Gene Name MDH1
Organism Homo sapiens (Human).
Sequence Length 334
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MSEPIRVLVTGAAGQIAYSLLYSIGNGSVFGKDQPIILVLLDITPMMGVLDGVLMELQDCALPLLKDVIATDKEDVAFKDLDVAILVGSMPRREGMERKDLLKANVKIFKSQGAALDKYAKKSVKVIVVGNPANTNCLTASKSAPSIPKENFSCLTRLDHNRAKAQIALKLGVTANDVKNVIIWGNHSSTQYPDVNHAKVKLQGKEVGVYEALKDDSWLKGEFVTTVQQRGAAVIKARKLSSAMSAAKAICDHVRDIWFGTPEGEFVSMGVISDGNSYGVPDDLLYSFPVVIKNKTWKFVEGLPINDFSREKMDLTAKELTEEKESAFEFLSSA
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
2Acetylation------MSEPIRVLV
------CCCCEEEEE
52.6725944712
5 (in isoform 3)Phosphorylation-4.1126437602
14AcetylationVLVTGAAGQIAYSLL
EEEECCHHHHHHHHH
20.9219608861
22PhosphorylationQIAYSLLYSIGNGSV
HHHHHHHHHCCCCCC
11.9722673903
23PhosphorylationIAYSLLYSIGNGSVF
HHHHHHHHCCCCCCC
24.8022673903
29AcetylationYSIGNGSVFGKDQPI
HHCCCCCCCCCCCCE
8.5419608861
29UbiquitinationYSIGNGSVFGKDQPI
HHCCCCCCCCCCCCE
8.5419608861
44PhosphorylationILVLLDITPMMGVLD
EEEEEECHHHCCHHH
12.5624043423
71PhosphorylationLLKDVIATDKEDVAF
HHHHHHCCCHHHCCC
36.1623911959
73AcetylationKDVIATDKEDVAFKD
HHHHCCCHHHCCCCC
52.0023954790
73UbiquitinationKDVIATDKEDVAFKD
HHHHCCCHHHCCCCC
52.0021906983
89PhosphorylationDVAILVGSMPRREGM
CEEEEECCCCCCCCC
20.3822673903
90SulfoxidationVAILVGSMPRREGME
EEEEECCCCCCCCCC
2.1721406390
103AcetylationMERKDLLKANVKIFK
CCHHHHHHHHHHHHH
45.2519608861
103SuccinylationMERKDLLKANVKIFK
CCHHHHHHHHHHHHH
45.2523954790
103UbiquitinationMERKDLLKANVKIFK
CCHHHHHHHHHHHHH
45.2519608861
107AcetylationDLLKANVKIFKSQGA
HHHHHHHHHHHHCCC
42.0823749302
107SuccinylationDLLKANVKIFKSQGA
HHHHHHHHHHHHCCC
42.0823954790
107UbiquitinationDLLKANVKIFKSQGA
HHHHHHHHHHHHCCC
42.08-
107 (in isoform 3)Phosphorylation-42.0827251275
110AcetylationKANVKIFKSQGAALD
HHHHHHHHHCCCHHH
45.3925953088
110MalonylationKANVKIFKSQGAALD
HHHHHHHHHCCCHHH
45.3926320211
110MethylationKANVKIFKSQGAALD
HHHHHHHHHCCCHHH
45.3938025153
110SuccinylationKANVKIFKSQGAALD
HHHHHHHHHCCCHHH
45.39-
110SuccinylationKANVKIFKSQGAALD
HHHHHHHHHCCCHHH
45.3927452117
110UbiquitinationKANVKIFKSQGAALD
HHHHHHHHHCCCHHH
45.39-
111PhosphorylationANVKIFKSQGAALDK
HHHHHHHHCCCHHHH
24.0926657352
118AcetylationSQGAALDKYAKKSVK
HCCCHHHHHCCCCCE
48.2122693256
118UbiquitinationSQGAALDKYAKKSVK
HCCCHHHHHCCCCCE
48.2122693256
119PhosphorylationQGAALDKYAKKSVKV
CCCHHHHHCCCCCEE
24.2628152594
121AcetylationAALDKYAKKSVKVIV
CHHHHHCCCCCEEEE
42.3522693256
121UbiquitinationAALDKYAKKSVKVIV
CHHHHHCCCCCEEEE
42.35-
122UbiquitinationALDKYAKKSVKVIVV
HHHHHCCCCCEEEEE
52.92-
125UbiquitinationKYAKKSVKVIVVGNP
HHCCCCCEEEEECCC
33.0821890473
129 (in isoform 3)Phosphorylation-4.1624719451
135PhosphorylationVVGNPANTNCLTASK
EECCCCCCCCCCCCC
29.4328348404
136UbiquitinationVGNPANTNCLTASKS
ECCCCCCCCCCCCCC
20.7121890473
136UbiquitinationVGNPANTNCLTASKS
ECCCCCCCCCCCCCC
20.7121890473
136AcetylationVGNPANTNCLTASKS
ECCCCCCCCCCCCCC
20.7119608861
136UbiquitinationVGNPANTNCLTASKS
ECCCCCCCCCCCCCC
20.7119608861
137S-nitrosocysteineGNPANTNCLTASKSA
CCCCCCCCCCCCCCC
3.17-
137S-nitrosylationGNPANTNCLTASKSA
CCCCCCCCCCCCCCC
3.1718335467
137S-palmitoylationGNPANTNCLTASKSA
CCCCCCCCCCCCCCC
3.1726865113
139PhosphorylationPANTNCLTASKSAPS
CCCCCCCCCCCCCCC
30.9628348404
141PhosphorylationNTNCLTASKSAPSIP
CCCCCCCCCCCCCCC
23.1629507054
142AcetylationTNCLTASKSAPSIPK
CCCCCCCCCCCCCCC
48.4426051181
142UbiquitinationTNCLTASKSAPSIPK
CCCCCCCCCCCCCCC
48.44-
143UbiquitinationNCLTASKSAPSIPKE
CCCCCCCCCCCCCCC
42.8021890473
143UbiquitinationNCLTASKSAPSIPKE
CCCCCCCCCCCCCCC
42.8021890473
143PhosphorylationNCLTASKSAPSIPKE
CCCCCCCCCCCCCCC
42.8026437602
143UbiquitinationNCLTASKSAPSIPKE
CCCCCCCCCCCCCCC
42.8021890473
146PhosphorylationTASKSAPSIPKENFS
CCCCCCCCCCCCCCC
51.7628188228
149AcetylationKSAPSIPKENFSCLT
CCCCCCCCCCCCHHH
64.7226051181
149UbiquitinationKSAPSIPKENFSCLT
CCCCCCCCCCCCHHH
64.72-
153PhosphorylationSIPKENFSCLTRLDH
CCCCCCCCHHHHCCC
21.5726437602
154S-nitrosylationIPKENFSCLTRLDHN
CCCCCCCHHHHCCCH
3.8324105792
157 (in isoform 3)Phosphorylation-25.7727251275
164UbiquitinationRLDHNRAKAQIALKL
HCCCHHHHHHHHHHH
37.2721890473
170UbiquitinationAKAQIALKLGVTAND
HHHHHHHHHCCCHHH
33.89-
174PhosphorylationIALKLGVTANDVKNV
HHHHHCCCHHHCCEE
20.2522673903
179AcetylationGVTANDVKNVIIWGN
CCCHHHCCEEEEECC
48.6525953088
179UbiquitinationGVTANDVKNVIIWGN
CCCHHHCCEEEEECC
48.65-
188PhosphorylationVIIWGNHSSTQYPDV
EEEECCCCCCCCCCC
38.8023401153
189PhosphorylationIIWGNHSSTQYPDVN
EEECCCCCCCCCCCC
16.3928152594
190PhosphorylationIWGNHSSTQYPDVNH
EECCCCCCCCCCCCC
34.8328152594
192PhosphorylationGNHSSTQYPDVNHAK
CCCCCCCCCCCCCCE
11.0728152594
199AcetylationYPDVNHAKVKLQGKE
CCCCCCCEEEECCEE
32.1425953088
199UbiquitinationYPDVNHAKVKLQGKE
CCCCCCCEEEECCEE
32.14-
201UbiquitinationDVNHAKVKLQGKEVG
CCCCCEEEECCEEEE
34.09-
205AcetylationAKVKLQGKEVGVYEA
CEEEECCEEEEEEEE
35.9426051181
205UbiquitinationAKVKLQGKEVGVYEA
CEEEECCEEEEEEEE
35.9421890473
207 (in isoform 3)Phosphorylation-7.7724719451
208 (in isoform 3)Phosphorylation-19.8527251275
209AcetylationLQGKEVGVYEALKDD
ECCEEEEEEEECCCC
4.7619608861
209UbiquitinationLQGKEVGVYEALKDD
ECCEEEEEEEECCCC
4.7619608861
210PhosphorylationQGKEVGVYEALKDDS
CCEEEEEEEECCCCC
6.9125159151
214AcetylationVGVYEALKDDSWLKG
EEEEEECCCCCCCCC
67.5426822725
214SuccinylationVGVYEALKDDSWLKG
EEEEEECCCCCCCCC
67.54-
214SuccinylationVGVYEALKDDSWLKG
EEEEEECCCCCCCCC
67.5423954790
214UbiquitinationVGVYEALKDDSWLKG
EEEEEECCCCCCCCC
67.5421890473
217PhosphorylationYEALKDDSWLKGEFV
EEECCCCCCCCCCEE
44.4328857561
220UbiquitinationLKDDSWLKGEFVTTV
CCCCCCCCCCEEEEH
50.5721890473
223UbiquitinationDSWLKGEFVTTVQQR
CCCCCCCEEEEHHHH
8.9021890473
223UbiquitinationDSWLKGEFVTTVQQR
CCCCCCCEEEEHHHH
8.9021890473
223UbiquitinationDSWLKGEFVTTVQQR
CCCCCCCEEEEHHHH
8.9021890473
228 (in isoform 3)Phosphorylation-25.7627642862
230MethylationFVTTVQQRGAAVIKA
EEEEHHHHCHHHHHH
21.4558858501
232UbiquitinationTTVQQRGAAVIKARK
EEHHHHCHHHHHHHH
10.7621890473
232UbiquitinationTTVQQRGAAVIKARK
EEHHHHCHHHHHHHH
10.7621890473
232UbiquitinationTTVQQRGAAVIKARK
EEHHHHCHHHHHHHH
10.7621890473
235 (in isoform 3)Phosphorylation-2.1827251275
236AcetylationQRGAAVIKARKLSSA
HHCHHHHHHHHHHHH
35.2225953088
236UbiquitinationQRGAAVIKARKLSSA
HHCHHHHHHHHHHHH
35.22-
239AcetylationAAVIKARKLSSAMSA
HHHHHHHHHHHHHHH
58.5425953088
239UbiquitinationAAVIKARKLSSAMSA
HHHHHHHHHHHHHHH
58.54-
241PhosphorylationVIKARKLSSAMSAAK
HHHHHHHHHHHHHHH
21.0629255136
242PhosphorylationIKARKLSSAMSAAKA
HHHHHHHHHHHHHHH
38.1330266825
244SulfoxidationARKLSSAMSAAKAIC
HHHHHHHHHHHHHHH
2.7930846556
245PhosphorylationRKLSSAMSAAKAICD
HHHHHHHHHHHHHHH
25.4530266825
248AcetylationSSAMSAAKAICDHVR
HHHHHHHHHHHHHHH
37.6925953088
259 (in isoform 3)Phosphorylation-8.7924719451
277PhosphorylationGVISDGNSYGVPDDL
EEECCCCCCCCCCCC
28.8830576142
278PhosphorylationVISDGNSYGVPDDLL
EECCCCCCCCCCCCE
26.5830576142
296PhosphorylationPVVIKNKTWKFVEGL
CEEEECCCEEEECCC
43.1922673903
298AcetylationVIKNKTWKFVEGLPI
EEECCCEEEECCCCC
44.7722693256
298SuccinylationVIKNKTWKFVEGLPI
EEECCCEEEECCCCC
44.77-
298SuccinylationVIKNKTWKFVEGLPI
EEECCCEEEECCCCC
44.7719608861
298UbiquitinationVIKNKTWKFVEGLPI
EEECCCEEEECCCCC
44.7722693256
309PhosphorylationGLPINDFSREKMDLT
CCCCCCCCHHHCCCC
42.2521712546
312AcetylationINDFSREKMDLTAKE
CCCCCHHHCCCCHHH
36.2825953088
312UbiquitinationINDFSREKMDLTAKE
CCCCCHHHCCCCHHH
36.28-
316UbiquitinationSREKMDLTAKELTEE
CHHHCCCCHHHHHHH
31.2721890473
316UbiquitinationSREKMDLTAKELTEE
CHHHCCCCHHHHHHH
31.2721890473
316AcetylationSREKMDLTAKELTEE
CHHHCCCCHHHHHHH
31.2719608861
316PhosphorylationSREKMDLTAKELTEE
CHHHCCCCHHHHHHH
31.2728634298
316UbiquitinationSREKMDLTAKELTEE
CHHHCCCCHHHHHHH
31.2719608861
318SuccinylationEKMDLTAKELTEEKE
HHCCCCHHHHHHHHH
48.28-
318SuccinylationEKMDLTAKELTEEKE
HHCCCCHHHHHHHHH
48.2823954790
318UbiquitinationEKMDLTAKELTEEKE
HHCCCCHHHHHHHHH
48.2821890473
321PhosphorylationDLTAKELTEEKESAF
CCCHHHHHHHHHHHH
43.0921712546
324UbiquitinationAKELTEEKESAFEFL
HHHHHHHHHHHHHHH
51.2221890473
326PhosphorylationELTEEKESAFEFLSS
HHHHHHHHHHHHHHC
49.6928176443
332PhosphorylationESAFEFLSSA-----
HHHHHHHHCC-----
29.5530108239
333PhosphorylationSAFEFLSSA------
HHHHHHHCC------
39.9028176443
336UbiquitinationEFLSSA---------
HHHHCC---------
21890473
336UbiquitinationEFLSSA---------
HHHHCC---------
21890473
350 (in isoform 3)Phosphorylation-27251275
351 (in isoform 3)Phosphorylation-24719451

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 MDHC_HUMAN !!

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
118KAcetylation

19608861

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 MDHC_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
P53_HUMANTP53physical
19229245
PRDX6_HUMANPRDX6physical
22939629
NHRF1_HUMANSLC9A3R1physical
22939629
PRDX5_HUMANPRDX5physical
22939629
PGM1_HUMANPGM1physical
22939629
ESTD_HUMANESDphysical
26344197
GLRX1_HUMANGLRXphysical
26344197
AATC_HUMANGOT1physical
26344197
PDXK_HUMANPDXKphysical
26344197
PGM1_HUMANPGM1physical
26344197
PGM2_HUMANPGM2physical
26344197
SCPDL_HUMANSCCPDHphysical
26344197

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
There are no disease associations of PTM sites.
Regulatory Network of MDHC_HUMAN

loading...

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-103; LYS-118 AND LYS-298,AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach.";
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.;
Anal. Chem. 81:4493-4501(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-241, AND MASSSPECTROMETRY.

TOP