LDHA_HUMAN - dbPTM
LDHA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID LDHA_HUMAN
UniProt AC P00338
Protein Name L-lactate dehydrogenase A chain
Gene Name LDHA
Organism Homo sapiens (Human).
Sequence Length 332
Subcellular Localization Cytoplasm.
Protein Description
Protein Sequence MATLKDQLIYNLLKEEQTPQNKITVVGVGAVGMACAISILMKDLADELALVDVIEDKLKGEMMDLQHGSLFLRTPKIVSGKDYNVTANSKLVIITAGARQQEGESRLNLVQRNVNIFKFIIPNVVKYSPNCKLLIVSNPVDILTYVAWKISGFPKNRVIGSGCNLDSARFRYLMGERLGVHPLSCHGWVLGEHGDSSVPVWSGMNVAGVSLKTLHPDLGTDKDKEQWKEVHKQVVESAYEVIKLKGYTSWAIGLSVADLAESIMKNLRRVHPVSTMIKGLYGIKDDVFLSVPCILGQNGISDLVKVTLTSEEEARLKKSADTLWGIQKELQF
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------MATLKDQLI
------CCCHHHHHH
22.9522223895
3Phosphorylation-----MATLKDQLIY
-----CCCHHHHHHH
32.8028857561
5Ubiquitination---MATLKDQLIYNL
---CCCHHHHHHHHH
38.7921890473
5Acetylation---MATLKDQLIYNL
---CCCHHHHHHHHH
38.7919608861
5Methylation---MATLKDQLIYNL
---CCCHHHHHHHHH
38.7919608861
5Succinylation---MATLKDQLIYNL
---CCCHHHHHHHHH
38.79-
5Succinylation---MATLKDQLIYNL
---CCCHHHHHHHHH
38.7923954790
5Ubiquitination---MATLKDQLIYNL
---CCCHHHHHHHHH
38.7921890473
10NitrationTLKDQLIYNLLKEEQ
CHHHHHHHHHHHHCC
14.35-
10PhosphorylationTLKDQLIYNLLKEEQ
CHHHHHHHHHHHHCC
14.3521945579
14UbiquitinationQLIYNLLKEEQTPQN
HHHHHHHHHCCCCCC
63.4721890473
14AcetylationQLIYNLLKEEQTPQN
HHHHHHHHHCCCCCC
63.4719608861
14SuccinylationQLIYNLLKEEQTPQN
HHHHHHHHHCCCCCC
63.4723954790
14SumoylationQLIYNLLKEEQTPQN
HHHHHHHHHCCCCCC
63.4719608861
14UbiquitinationQLIYNLLKEEQTPQN
HHHHHHHHHCCCCCC
63.4721890473
14 (in isoform 1)Ubiquitination-63.4721890473
14 (in isoform 2)Ubiquitination-63.4721890473
18PhosphorylationNLLKEEQTPQNKITV
HHHHHCCCCCCCEEE
30.0721945579
22AcetylationEEQTPQNKITVVGVG
HCCCCCCCEEEEECH
34.2169955
24PhosphorylationQTPQNKITVVGVGAV
CCCCCCEEEEECHHH
15.6820860994
27UbiquitinationQNKITVVGVGAVGMA
CCCEEEEECHHHHHH
14.06-
27 (in isoform 3)Ubiquitination-14.06-
34 (in isoform 3)Ubiquitination-3.60-
39PhosphorylationGMACAISILMKDLAD
HHHHHHHHHHHHHHH
3.4027642862
43AcetylationAISILMKDLADELAL
HHHHHHHHHHHHHHH
32.8819608861
43UbiquitinationAISILMKDLADELAL
HHHHHHHHHHHHHHH
32.8819608861
43 (in isoform 3)Ubiquitination-32.88-
57AcetylationLVDVIEDKLKGEMMD
HHHHHHHHHCCCCEE
39.0319608861
57SumoylationLVDVIEDKLKGEMMD
HHHHHHHHHCCCCEE
39.0328112733
57UbiquitinationLVDVIEDKLKGEMMD
HHHHHHHHHCCCCEE
39.0321906983
57 (in isoform 2)Ubiquitination-39.0321890473
59UbiquitinationDVIEDKLKGEMMDLQ
HHHHHHHCCCCEECC
59.5721890473
59AcetylationDVIEDKLKGEMMDLQ
HHHHHHHCCCCEECC
59.5726051181
59MalonylationDVIEDKLKGEMMDLQ
HHHHHHHCCCCEECC
59.5733225896
59UbiquitinationDVIEDKLKGEMMDLQ
HHHHHHHCCCCEECC
59.5721890473
59 (in isoform 1)Ubiquitination-59.5721890473
59 (in isoform 2)Ubiquitination-59.5721890473
62SulfoxidationEDKLKGEMMDLQHGS
HHHHCCCCEECCCCC
3.2728465586
63SulfoxidationDKLKGEMMDLQHGSL
HHHCCCCEECCCCCE
3.9628465586
69O-linked_GlycosylationMMDLQHGSLFLRTPK
CEECCCCCEEEECCC
17.5231373491
69PhosphorylationMMDLQHGSLFLRTPK
CEECCCCCEEEECCC
17.5227080861
74PhosphorylationHGSLFLRTPKIVSGK
CCCEEEECCCCCCCC
30.95-
76UbiquitinationSLFLRTPKIVSGKDY
CEEEECCCCCCCCCC
55.9421890473
76 (in isoform 1)Ubiquitination-55.9421890473
76 (in isoform 2)Ubiquitination-55.9421890473
79PhosphorylationLRTPKIVSGKDYNVT
EECCCCCCCCCCEEC
43.5328152594
81AcetylationTPKIVSGKDYNVTAN
CCCCCCCCCCEECCC
49.9219608861
81MalonylationTPKIVSGKDYNVTAN
CCCCCCCCCCEECCC
49.9233225896
81UbiquitinationTPKIVSGKDYNVTAN
CCCCCCCCCCEECCC
49.9220639865
81 (in isoform 1)Ubiquitination-49.9221890473
81 (in isoform 2)Ubiquitination-49.9221890473
83PhosphorylationKIVSGKDYNVTANSK
CCCCCCCCEECCCCE
18.2828152594
86AcetylationSGKDYNVTANSKLVI
CCCCCEECCCCEEEE
19.2419608861
86PhosphorylationSGKDYNVTANSKLVI
CCCCCEECCCCEEEE
19.2426437602
86UbiquitinationSGKDYNVTANSKLVI
CCCCCEECCCCEEEE
19.2419608861
88UbiquitinationKDYNVTANSKLVIIT
CCCEECCCCEEEEEE
30.2521890473
88 (in isoform 3)Ubiquitination-30.25-
89PhosphorylationDYNVTANSKLVIITA
CCEECCCCEEEEEEC
25.5428152594
90UbiquitinationYNVTANSKLVIITAG
CEECCCCEEEEEECC
46.7390473
90 (in isoform 2)Ubiquitination-46.7321890473
95PhosphorylationNSKLVIITAGARQQE
CCEEEEEECCCCCCH
14.1228857561
97UbiquitinationKLVIITAGARQQEGE
EEEEEECCCCCCHHC
16.7921890473
105UbiquitinationARQQEGESRLNLVQR
CCCCHHCHHHHHHHH
53.5821890473
105PhosphorylationARQQEGESRLNLVQR
CCCCHHCHHHHHHHH
53.5830622161
105 (in isoform 3)Ubiquitination-53.58-
110UbiquitinationGESRLNLVQRNVNIF
HCHHHHHHHHHHCCH
4.9721890473
110AcetylationGESRLNLVQRNVNIF
HCHHHHHHHHHHCCH
4.9719608861
110UbiquitinationGESRLNLVQRNVNIF
HCHHHHHHHHHHCCH
4.9719608861
110 (in isoform 3)Ubiquitination-4.97-
112PhosphorylationSRLNLVQRNVNIFKF
HHHHHHHHHHCCHHH
41.4027642862
115PhosphorylationNLVQRNVNIFKFIIP
HHHHHHHCCHHHHCC
37.2127251275
118AcetylationQRNVNIFKFIIPNVV
HHHHCCHHHHCCCCE
31.6819608861
118MethylationQRNVNIFKFIIPNVV
HHHHCCHHHHCCCCE
31.6888375
118SuccinylationQRNVNIFKFIIPNVV
HHHHCCHHHHCCCCE
31.68-
118SuccinylationQRNVNIFKFIIPNVV
HHHHCCHHHHCCCCE
31.6823954790
118UbiquitinationQRNVNIFKFIIPNVV
HHHHCCHHHHCCCCE
31.6819608861
118 (in isoform 1)Ubiquitination-31.6821890473
118 (in isoform 2)Ubiquitination-31.6821890473
124PhosphorylationFKFIIPNVVKYSPNC
HHHHCCCCEEECCCC
3.0927251275
126AcetylationFIIPNVVKYSPNCKL
HHCCCCEEECCCCEE
35.4119608861
126MalonylationFIIPNVVKYSPNCKL
HHCCCCEEECCCCEE
35.4126320211
126UbiquitinationFIIPNVVKYSPNCKL
HHCCCCEEECCCCEE
35.4121890473
126 (in isoform 1)Ubiquitination-35.4121890473
126 (in isoform 2)Ubiquitination-35.4121890473
127PhosphorylationIIPNVVKYSPNCKLL
HCCCCEEECCCCEEE
20.1126437602
128PhosphorylationIPNVVKYSPNCKLLI
CCCCEEECCCCEEEE
12.15-
131S-palmitoylationVVKYSPNCKLLIVSN
CEEECCCCEEEEECC
3.5929575903
132AcetylationVKYSPNCKLLIVSNP
EEECCCCEEEEECCC
53.6321466224
132UbiquitinationVKYSPNCKLLIVSNP
EEECCCCEEEEECCC
53.6321906983
132 (in isoform 2)Ubiquitination-53.6321890473
137O-linked_GlycosylationNCKLLIVSNPVDILT
CCEEEEECCCHHHHH
28.5531373491
144PhosphorylationSNPVDILTYVAWKIS
CCCHHHHHHHHHHCC
19.1128348404
145PhosphorylationNPVDILTYVAWKISG
CCHHHHHHHHHHCCC
5.6825147952
147UbiquitinationVDILTYVAWKISGFP
HHHHHHHHHHCCCCC
7.4521890473
147AcetylationVDILTYVAWKISGFP
HHHHHHHHHHCCCCC
7.4519608861
147UbiquitinationVDILTYVAWKISGFP
HHHHHHHHHHCCCCC
7.4519608861
147 (in isoform 3)Ubiquitination-7.45-
149AcetylationILTYVAWKISGFPKN
HHHHHHHHCCCCCCC
19.7721466224
155UbiquitinationWKISGFPKNRVIGSG
HHCCCCCCCCEECCC
55.9421890473
155AcetylationWKISGFPKNRVIGSG
HHCCCCCCCCEECCC
55.9419608861
155UbiquitinationWKISGFPKNRVIGSG
HHCCCCCCCCEECCC
55.9421890473
155 (in isoform 1)Ubiquitination-55.9421890473
155 (in isoform 2)Ubiquitination-55.9421890473
155 (in isoform 3)Ubiquitination-55.94-
157MethylationISGFPKNRVIGSGCN
CCCCCCCCEECCCCC
27.79-
161PhosphorylationPKNRVIGSGCNLDSA
CCCCEECCCCCCCHH
29.1124114839
163S-palmitoylationNRVIGSGCNLDSARF
CCEECCCCCCCHHHH
4.9729575903
164AcetylationRVIGSGCNLDSARFR
CEECCCCCCCHHHHH
50.8619608861
164UbiquitinationRVIGSGCNLDSARFR
CEECCCCCCCHHHHH
50.8619608861
167PhosphorylationGSGCNLDSARFRYLM
CCCCCCCHHHHHHHH
25.2221712546
169MethylationGCNLDSARFRYLMGE
CCCCCHHHHHHHHCC
22.11-
172PhosphorylationLDSARFRYLMGERLG
CCHHHHHHHHCCCCC
9.7925147952
174UbiquitinationSARFRYLMGERLGVH
HHHHHHHHCCCCCCC
3.7721890473
184UbiquitinationRLGVHPLSCHGWVLG
CCCCCEEECCCEEEC
14.4421890473
184PhosphorylationRLGVHPLSCHGWVLG
CCCCCEEECCCEEEC
14.44-
185UbiquitinationLGVHPLSCHGWVLGE
CCCCEEECCCEEECC
4.5421890473
196PhosphorylationVLGEHGDSSVPVWSG
EECCCCCCCCCCCCC
37.5228348404
197PhosphorylationLGEHGDSSVPVWSGM
ECCCCCCCCCCCCCC
34.8728348404
204SulfoxidationSVPVWSGMNVAGVSL
CCCCCCCCCCCCEEE
2.8130846556
212AcetylationNVAGVSLKTLHPDLG
CCCCEEECCCCCCCC
41.3526051181
212UbiquitinationNVAGVSLKTLHPDLG
CCCCEEECCCCCCCC
41.35-
213PhosphorylationVAGVSLKTLHPDLGT
CCCEEECCCCCCCCC
35.2826437602
220UbiquitinationTLHPDLGTDKDKEQW
CCCCCCCCCCCHHHH
47.3621890473
220AcetylationTLHPDLGTDKDKEQW
CCCCCCCCCCCHHHH
47.3619608861
220UbiquitinationTLHPDLGTDKDKEQW
CCCCCCCCCCCHHHH
47.3619608861
222AcetylationHPDLGTDKDKEQWKE
CCCCCCCCCHHHHHH
71.2223954790
222UbiquitinationHPDLGTDKDKEQWKE
CCCCCCCCCHHHHHH
71.2221906983
222 (in isoform 2)Ubiquitination-71.2221890473
224AcetylationDLGTDKDKEQWKEVH
CCCCCCCHHHHHHHH
58.5123749302
224UbiquitinationDLGTDKDKEQWKEVH
CCCCCCCHHHHHHHH
58.51-
228AcetylationDKDKEQWKEVHKQVV
CCCHHHHHHHHHHHH
49.9422424773
228SuccinylationDKDKEQWKEVHKQVV
CCCHHHHHHHHHHHH
49.9423954790
228UbiquitinationDKDKEQWKEVHKQVV
CCCHHHHHHHHHHHH
49.94-
232AcetylationEQWKEVHKQVVESAY
HHHHHHHHHHHHHHH
50.3823954790
232MalonylationEQWKEVHKQVVESAY
HHHHHHHHHHHHHHH
50.3826320211
232UbiquitinationEQWKEVHKQVVESAY
HHHHHHHHHHHHHHH
50.3821890473
232 (in isoform 1)Ubiquitination-50.3821890473
232 (in isoform 2)Phosphorylation-50.3824719451
233 (in isoform 2)Phosphorylation-29.6124719451
237PhosphorylationVHKQVVESAYEVIKL
HHHHHHHHHHHHHHH
25.2521945579
239PhosphorylationKQVVESAYEVIKLKG
HHHHHHHHHHHHHCC
21.7325159151
243AcetylationESAYEVIKLKGYTSW
HHHHHHHHHCCCCHH
49.6923954790
243UbiquitinationESAYEVIKLKGYTSW
HHHHHHHHHCCCCHH
49.6921890473
243 (in isoform 1)Ubiquitination-49.6921890473
245UbiquitinationAYEVIKLKGYTSWAI
HHHHHHHCCCCHHHH
44.89-
247PhosphorylationEVIKLKGYTSWAIGL
HHHHHCCCCHHHHHC
8.9420068231
248PhosphorylationVIKLKGYTSWAIGLS
HHHHCCCCHHHHHCC
26.8520068231
249PhosphorylationIKLKGYTSWAIGLSV
HHHCCCCHHHHHCCH
13.1620068231
251AcetylationLKGYTSWAIGLSVAD
HCCCCHHHHHCCHHH
5.9219608861
251UbiquitinationLKGYTSWAIGLSVAD
HCCCCHHHHHCCHHH
5.9219608861
251 (in isoform 3)Ubiquitination-5.92-
253 (in isoform 3)Ubiquitination-12.26-
255PhosphorylationTSWAIGLSVADLAES
CHHHHHCCHHHHHHH
15.2820068231
260AcetylationGLSVADLAESIMKNL
HCCHHHHHHHHHHHH
14.7219608861
260UbiquitinationGLSVADLAESIMKNL
HCCHHHHHHHHHHHH
14.7219608861
261UbiquitinationLSVADLAESIMKNLR
CCHHHHHHHHHHHHC
48.3621890473
261 (in isoform 3)Ubiquitination-48.36-
262PhosphorylationSVADLAESIMKNLRR
CHHHHHHHHHHHHCC
23.5220068231
264SulfoxidationADLAESIMKNLRRVH
HHHHHHHHHHHCCCC
3.0730846556
266PhosphorylationLAESIMKNLRRVHPV
HHHHHHHHHCCCCCH
22.7727251275
268PhosphorylationESIMKNLRRVHPVST
HHHHHHHCCCCCHHH
48.2227642862
269MethylationSIMKNLRRVHPVSTM
HHHHHHCCCCCHHHH
33.97115481941
270UbiquitinationIMKNLRRVHPVSTMI
HHHHHCCCCCHHHHH
4.9021890473
272UbiquitinationKNLRRVHPVSTMIKG
HHHCCCCCHHHHHHH
20.9221890473
272 (in isoform 3)Ubiquitination-20.92-
274PhosphorylationLRRVHPVSTMIKGLY
HCCCCCHHHHHHHHH
19.4029802988
274 (in isoform 3)Ubiquitination-19.40-
275PhosphorylationRRVHPVSTMIKGLYG
CCCCCHHHHHHHHHC
24.1329802988
276SulfoxidationRVHPVSTMIKGLYGI
CCCCHHHHHHHHHCC
2.0230846556
278AcetylationHPVSTMIKGLYGIKD
CCHHHHHHHHHCCCC
31.8523954790
278MalonylationHPVSTMIKGLYGIKD
CCHHHHHHHHHCCCC
31.8526320211
278MethylationHPVSTMIKGLYGIKD
CCHHHHHHHHHCCCC
31.8522639955
278UbiquitinationHPVSTMIKGLYGIKD
CCHHHHHHHHHCCCC
31.8521890473
278 (in isoform 1)Ubiquitination-31.8521890473
284SuccinylationIKGLYGIKDDVFLSV
HHHHHCCCCCEEEEC
43.4423954790
284UbiquitinationIKGLYGIKDDVFLSV
HHHHHCCCCCEEEEC
43.44-
284 (in isoform 2)Ubiquitination-43.4421890473
305UbiquitinationNGISDLVKVTLTSEE
CCCCCCEEEECCCHH
36.48-
307UbiquitinationISDLVKVTLTSEEEA
CCCCEEEECCCHHHH
20.7121890473
307AcetylationISDLVKVTLTSEEEA
CCCCEEEECCCHHHH
20.7119608861
307PhosphorylationISDLVKVTLTSEEEA
CCCCEEEECCCHHHH
20.7121815630
307UbiquitinationISDLVKVTLTSEEEA
CCCCEEEECCCHHHH
20.7119608861
307 (in isoform 3)Ubiquitination-20.71-
309PhosphorylationDLVKVTLTSEEEARL
CCEEEECCCHHHHHH
25.4029255136
310PhosphorylationLVKVTLTSEEEARLK
CEEEECCCHHHHHHH
46.2329255136
317UbiquitinationSEEEARLKKSADTLW
CHHHHHHHHHHHHHH
38.85-
318AcetylationEEEARLKKSADTLWG
HHHHHHHHHHHHHHH
56.3119608861
318MalonylationEEEARLKKSADTLWG
HHHHHHHHHHHHHHH
56.3126320211
318SuccinylationEEEARLKKSADTLWG
HHHHHHHHHHHHHHH
56.31-
318SuccinylationEEEARLKKSADTLWG
HHHHHHHHHHHHHHH
56.31-
318UbiquitinationEEEARLKKSADTLWG
HHHHHHHHHHHHHHH
56.3119608861
318 (in isoform 2)Ubiquitination-56.3121890473
319PhosphorylationEEARLKKSADTLWGI
HHHHHHHHHHHHHHH
29.7722777824
322PhosphorylationRLKKSADTLWGIQKE
HHHHHHHHHHHHHHH
24.9120873877
328AcetylationDTLWGIQKELQF---
HHHHHHHHHHCC---
59.4822424773
328SuccinylationDTLWGIQKELQF---
HHHHHHHHHHCC---
59.4823954790
328SumoylationDTLWGIQKELQF---
HHHHHHHHHHCC---
59.48-
328UbiquitinationDTLWGIQKELQF---
HHHHHHHHHHCC---
59.4821890473
328 (in isoform 1)Ubiquitination-59.4821890473
328 (in isoform 2)Ubiquitination-59.4821890473
338PhosphorylationQF-------------
CC-------------
27251275
346 (in isoform 3)Ubiquitination--
347Acetylation----------------------
----------------------
19608861
347Ubiquitination----------------------
----------------------
19608861
347 (in isoform 3)Ubiquitination--
357Ubiquitination--------------------------------
--------------------------------
21890473
357 (in isoform 3)Ubiquitination--

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
3TPhosphorylationKinaseMAP3K7O43318
GPS
10YPhosphorylationKinaseERBB2P04626
GPS
10YPhosphorylationKinaseFGFR1P11362
PSP
10YPhosphorylationKinaseSRCP12931
PSP
83YPhosphorylationKinaseFGFR1P11362
PSP
248TPhosphorylationKinaseCDK1P06493
PSP

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of LDHA_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 LDHA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KCJ11_HUMANKCNJ11physical
12145195
ABCC9_HUMANABCC9physical
12145195
MDHC_HUMANMDH1physical
22939629
LDHB_HUMANLDHBphysical
22939629
LDHA_HUMANLDHAphysical
21988832
LDHB_HUMANLDHBphysical
21988832
BZW1_HUMANBZW1physical
22863883
CNDP2_HUMANCNDP2physical
22863883
GNAI3_HUMANGNAI3physical
22863883
GSHR_HUMANGSRphysical
22863883
6PGD_HUMANPGDphysical
22863883
KS6A1_HUMANRPS6KA1physical
22863883
DHSO_HUMANSORDphysical
22863883
LDHB_HUMANLDHBphysical
25416956
MK10_HUMANMAPK10physical
25416956
GABT_HUMANABATphysical
26344197
ACADM_HUMANACADMphysical
26344197
ADK_HUMANADKphysical
26344197
AL1B1_HUMANALDH1B1physical
26344197
ALDH2_HUMANALDH2physical
26344197
AL4A1_HUMANALDH4A1physical
26344197
APT_HUMANAPRTphysical
26344197
ARF4_HUMANARF4physical
26344197
ARF5_HUMANARF5physical
26344197
CATA_HUMANCATphysical
26344197
TCPG_HUMANCCT3physical
26344197
TCPW_HUMANCCT6Bphysical
26344197
CATD_HUMANCTSDphysical
26344197
ENOA_HUMANENO1physical
26344197
ETFA_HUMANETFAphysical
26344197
FAAA_HUMANFAHphysical
26344197
FAHD1_HUMANFAHD1physical
26344197
FUMH_HUMANFHphysical
26344197
LYAG_HUMANGAAphysical
26344197
GSTO1_HUMANGSTO1physical
26344197
IDE_HUMANIDEphysical
26344197
MIF_HUMANMIFphysical
26344197
NDKB_HUMANNME2physical
26344197
PARK7_HUMANPARK7physical
26344197
ODPA_HUMANPDHA1physical
26344197
PEPD_HUMANPEPDphysical
26344197
PGK1_HUMANPGK1physical
26344197
PGM1_HUMANPGM1physical
26344197
KPYM_HUMANPKMphysical
26344197
PPIA_HUMANPPIAphysical
26344197
PPT1_HUMANPPT1physical
26344197
PCP_HUMANPRCPphysical
26344197
PRDX2_HUMANPRDX2physical
26344197
PRDX5_HUMANPRDX5physical
26344197
GLU2B_HUMANPRKCSHphysical
26344197
PRS7_HUMANPSMC2physical
26344197
RAB5A_HUMANRAB5Aphysical
26344197
RAB6B_HUMANRAB6Bphysical
26344197
SDHB_HUMANSDHBphysical
26344197
DHSO_HUMANSORDphysical
26344197
SPRE_HUMANSPRphysical
26344197
TALDO_HUMANTALDO1physical
26344197
TPIS_HUMANTPI1physical
26344197
UFD1_HUMANUFD1Lphysical
26344197
LDHB_HUMANLDHBphysical
21516116
LDHC_HUMANLDHCphysical
28514442
LDHB_HUMANLDHBphysical
28514442

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
612933Glycogen storage disease 11 (GSD11)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of LDHA_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
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: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, AND MASS SPECTROMETRY.
"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-5; LYS-14; LYS-57; LYS-81;LYS-118; LYS-126; LYS-222; LYS-278 AND LYS-318, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"Quantitative phosphoproteomic analysis of T cell receptor signalingreveals system-wide modulation of protein-protein interactions.";
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,Rodionov V., Han D.K.;
Sci. Signal. 2:RA46-RA46(2009).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-10 AND TYR-239, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASSSPECTROMETRY.
"Immunoaffinity profiling of tyrosine phosphorylation in cancercells.";
Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,Zha X.-M., Polakiewicz R.D., Comb M.J.;
Nat. Biotechnol. 23:94-101(2005).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-239, AND MASSSPECTROMETRY.

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