SERA_HUMAN - dbPTM
SERA_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SERA_HUMAN
UniProt AC O43175
Protein Name D-3-phosphoglycerate dehydrogenase
Gene Name PHGDH
Organism Homo sapiens (Human).
Sequence Length 533
Subcellular Localization
Protein Description Catalyzes the reversible oxidation of 3-phospho-D-glycerate to 3-phosphonooxypyruvate, the first step of the phosphorylated L-serine biosynthesis pathway. Also catalyzes the reversible oxidation of 2-hydroxyglutarate to 2-oxoglutarate and the reversible oxidation of (S)-malate to oxaloacetate..
Protein Sequence MAFANLRKVLISDSLDPCCRKILQDGGLQVVEKQNLSKEELIAELQDCEGLIVRSATKVTADVINAAEKLQVVGRAGTGVDNVDLEAATRKGILVMNTPNGNSLSAAELTCGMIMCLARQIPQATASMKDGKWERKKFMGTELNGKTLGILGLGRIGREVATRMQSFGMKTIGYDPIISPEVSASFGVQQLPLEEIWPLCDFITVHTPLLPSTTGLLNDNTFAQCKKGVRVVNCARGGIVDEGALLRALQSGQCAGAALDVFTEEPPRDRALVDHENVISCPHLGASTKEAQSRCGEEIAVQFVDMVKGKSLTGVVNAQALTSAFSPHTKPWIGLAEALGTLMRAWAGSPKGTIQVITQGTSLKNAGNCLSPAVIVGLLKEASKQADVNLVNAKLLVKEAGLNVTTSHSPAAPGEQGFGECLLAVALAGAPYQAVGLVQGTTPVLQGLNGAVFRPEVPLRRDLPLLLFRTQTSDPAMLPTMIGLLAEAGVRLLSYQTSLVSDGETWHVMGISSLLPSLEAWKQHVTEAFQFHF
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------MAFANLRKV
------CCCCCHHHH
16.56-
7Methylation-MAFANLRKVLISDS
-CCCCCHHHHHHHCC
27.18115487443
82-HydroxyisobutyrylationMAFANLRKVLISDSL
CCCCCHHHHHHHCCC
44.55-
8AcetylationMAFANLRKVLISDSL
CCCCCHHHHHHHCCC
44.5527452117
8UbiquitinationMAFANLRKVLISDSL
CCCCCHHHHHHHCCC
44.5529967540
12PhosphorylationNLRKVLISDSLDPCC
CHHHHHHHCCCCHHH
19.5828450419
14PhosphorylationRKVLISDSLDPCCRK
HHHHHHCCCCHHHHH
28.0725159151
19GlutathionylationSDSLDPCCRKILQDG
HCCCCHHHHHHHHHC
6.3722555962
212-HydroxyisobutyrylationSLDPCCRKILQDGGL
CCCHHHHHHHHHCCC
33.58-
21AcetylationSLDPCCRKILQDGGL
CCCHHHHHHHHHCCC
33.58-
21MalonylationSLDPCCRKILQDGGL
CCCHHHHHHHHHCCC
33.5826320211
21SumoylationSLDPCCRKILQDGGL
CCCHHHHHHHHHCCC
33.5825114211
21UbiquitinationSLDPCCRKILQDGGL
CCCHHHHHHHHHCCC
33.5823000965
31UbiquitinationQDGGLQVVEKQNLSK
HHCCCEEEEECCCCH
4.9922817900
32UbiquitinationDGGLQVVEKQNLSKE
HCCCEEEEECCCCHH
50.5023000965
332-HydroxyisobutyrylationGGLQVVEKQNLSKEE
CCCEEEEECCCCHHH
32.64-
33AcetylationGGLQVVEKQNLSKEE
CCCEEEEECCCCHHH
32.6423954790
33UbiquitinationGGLQVVEKQNLSKEE
CCCEEEEECCCCHHH
32.6423000965
34UbiquitinationGLQVVEKQNLSKEEL
CCEEEEECCCCHHHH
42.4622817900
38UbiquitinationVEKQNLSKEELIAEL
EEECCCCHHHHHHHH
59.3723000965
43UbiquitinationLSKEELIAELQDCEG
CCHHHHHHHHHCCCC
24.8723000965
48GlutathionylationLIAELQDCEGLIVRS
HHHHHHCCCCEEECC
2.6322555962
48UbiquitinationLIAELQDCEGLIVRS
HHHHHHCCCCEEECC
2.6323000965
55PhosphorylationCEGLIVRSATKVTAD
CCCEEECCCCCCHHH
29.4228450419
57PhosphorylationGLIVRSATKVTADVI
CEEECCCCCCHHHHH
27.5628450419
582-HydroxyisobutyrylationLIVRSATKVTADVIN
EEECCCCCCHHHHHH
36.99-
58AcetylationLIVRSATKVTADVIN
EEECCCCCCHHHHHH
36.9925953088
58MalonylationLIVRSATKVTADVIN
EEECCCCCCHHHHHH
36.9926320211
58UbiquitinationLIVRSATKVTADVIN
EEECCCCCCHHHHHH
36.9923000965
60PhosphorylationVRSATKVTADVINAA
ECCCCCCHHHHHHHH
20.7828450419
692-HydroxyisobutyrylationDVINAAEKLQVVGRA
HHHHHHHHHHEECCC
39.22-
69AcetylationDVINAAEKLQVVGRA
HHHHHHHHHHEECCC
39.2225953088
69UbiquitinationDVINAAEKLQVVGRA
HHHHHHHHHHEECCC
39.2223000965
75MethylationEKLQVVGRAGTGVDN
HHHHEECCCCCCCCC
20.45115487459
78PhosphorylationQVVGRAGTGVDNVDL
HEECCCCCCCCCCCH
32.8029255136
89PhosphorylationNVDLEAATRKGILVM
CCCHHHHCCCCEEEE
39.7120068231
98PhosphorylationKGILVMNTPNGNSLS
CCEEEEECCCCCCCC
10.4721406692
103PhosphorylationMNTPNGNSLSAAELT
EECCCCCCCCHHHHH
25.7121406692
105PhosphorylationTPNGNSLSAAELTCG
CCCCCCCCHHHHHHH
25.8321406692
110PhosphorylationSLSAAELTCGMIMCL
CCCHHHHHHHHHHHH
9.8721406692
125PhosphorylationARQIPQATASMKDGK
HHHCCHHHHHCCCCC
17.6421406692
127PhosphorylationQIPQATASMKDGKWE
HCCHHHHHCCCCCCE
23.2421406692
128SulfoxidationIPQATASMKDGKWER
CCHHHHHCCCCCCEE
4.2130846556
1292-HydroxyisobutyrylationPQATASMKDGKWERK
CHHHHHCCCCCCEEH
61.91-
129UbiquitinationPQATASMKDGKWERK
CHHHHHCCCCCCEEH
61.9121906983
132UbiquitinationTASMKDGKWERKKFM
HHHCCCCCCEEHHHC
56.8922817900
136AcetylationKDGKWERKKFMGTEL
CCCCCEEHHHCCEEE
38.5625953088
136UbiquitinationKDGKWERKKFMGTEL
CCCCCEEHHHCCEEE
38.56-
137AcetylationDGKWERKKFMGTELN
CCCCEEHHHCCEEEC
46.9725953088
137MalonylationDGKWERKKFMGTELN
CCCCEEHHHCCEEEC
46.9726320211
137UbiquitinationDGKWERKKFMGTELN
CCCCEEHHHCCEEEC
46.9729967540
139SulfoxidationKWERKKFMGTELNGK
CCEEHHHCCEEECCE
9.9821406390
141PhosphorylationERKKFMGTELNGKTL
EEHHHCCEEECCEEE
26.05-
146UbiquitinationMGTELNGKTLGILGL
CCEEECCEEEEEECH
39.2323000965
147PhosphorylationGTELNGKTLGILGLG
CEEECCEEEEEECHH
31.4521712546
166PhosphorylationEVATRMQSFGMKTIG
HHHHHHHHCCCEECC
17.9027499020
166UbiquitinationEVATRMQSFGMKTIG
HHHHHHHHCCCEECC
17.9022817900
169UbiquitinationTRMQSFGMKTIGYDP
HHHHHCCCEECCCCC
3.0522817900
177UbiquitinationKTIGYDPIISPEVSA
EECCCCCCCCCHHHH
4.4422817900
180UbiquitinationGYDPIISPEVSASFG
CCCCCCCCHHHHHCC
35.2822817900
183UbiquitinationPIISPEVSASFGVQQ
CCCCCHHHHHCCCCC
19.2823000965
191UbiquitinationASFGVQQLPLEEIWP
HHCCCCCCCHHHHHH
2.6721963094
194UbiquitinationGVQQLPLEEIWPLCD
CCCCCCHHHHHHHCC
45.5623000965
203UbiquitinationIWPLCDFITVHTPLL
HHHHCCEEEECCCCC
2.2222817900
206UbiquitinationLCDFITVHTPLLPST
HCCEEEECCCCCCCC
17.0822817900
210UbiquitinationITVHTPLLPSTTGLL
EEECCCCCCCCCCCC
3.1121963094
212UbiquitinationVHTPLLPSTTGLLND
ECCCCCCCCCCCCCC
38.2722817900
220UbiquitinationTTGLLNDNTFAQCKK
CCCCCCCCCHHHHCC
35.7023000965
236MethylationVRVVNCARGGIVDEG
CEEEECCCCCCCCHH
46.18115487467
247MethylationVDEGALLRALQSGQC
CCHHHHHHHHHCCCC
33.82115487451
253UbiquitinationLRALQSGQCAGAALD
HHHHHCCCCCCEEEH
21.0927667366
254GlutathionylationRALQSGQCAGAALDV
HHHHCCCCCCEEEHC
4.2622555962
266UbiquitinationLDVFTEEPPRDRALV
EHCCCCCCCCCCCCC
24.0021963094
280PhosphorylationVDHENVISCPHLGAS
CCCCCCCCCCCCCCC
19.8127251275
281S-nitrosocysteineDHENVISCPHLGAST
CCCCCCCCCCCCCCH
1.37-
281GlutathionylationDHENVISCPHLGAST
CCCCCCCCCCCCCCH
1.3722555962
281S-nitrosylationDHENVISCPHLGAST
CCCCCCCCCCCCCCH
1.3722178444
282UbiquitinationHENVISCPHLGASTK
CCCCCCCCCCCCCHH
20.9621963094
286UbiquitinationISCPHLGASTKEAQS
CCCCCCCCCHHHHHH
22.0127667366
287PhosphorylationSCPHLGASTKEAQSR
CCCCCCCCHHHHHHH
37.9128857561
288PhosphorylationCPHLGASTKEAQSRC
CCCCCCCHHHHHHHH
32.1629083192
2892-HydroxyisobutyrylationPHLGASTKEAQSRCG
CCCCCCHHHHHHHHC
48.86-
289AcetylationPHLGASTKEAQSRCG
CCCCCCHHHHHHHHC
48.8626051181
289MalonylationPHLGASTKEAQSRCG
CCCCCCHHHHHHHHC
48.8626320211
289UbiquitinationPHLGASTKEAQSRCG
CCCCCCHHHHHHHHC
48.8621963094
295GlutathionylationTKEAQSRCGEEIAVQ
HHHHHHHHCHHHHHH
11.0222555962
296UbiquitinationKEAQSRCGEEIAVQF
HHHHHHHCHHHHHHH
34.1723000965
300UbiquitinationSRCGEEIAVQFVDMV
HHHCHHHHHHHHHCC
7.7323000965
306SulfoxidationIAVQFVDMVKGKSLT
HHHHHHHCCCCCCCC
2.5630846556
308UbiquitinationVQFVDMVKGKSLTGV
HHHHHCCCCCCCCCE
54.7221963094
310UbiquitinationFVDMVKGKSLTGVVN
HHHCCCCCCCCCEEE
36.2522817900
322PhosphorylationVVNAQALTSAFSPHT
EEEHHHHHHCCCCCC
22.4824719451
323PhosphorylationVNAQALTSAFSPHTK
EEHHHHHHCCCCCCC
28.3220068231
326PhosphorylationQALTSAFSPHTKPWI
HHHHHCCCCCCCCCH
18.5820068231
326UbiquitinationQALTSAFSPHTKPWI
HHHHHCCCCCCCCCH
18.5821963094
329PhosphorylationTSAFSPHTKPWIGLA
HHCCCCCCCCCHHHH
42.0329449344
330UbiquitinationSAFSPHTKPWIGLAE
HCCCCCCCCCHHHHH
35.0132015554
337UbiquitinationKPWIGLAEALGTLMR
CCCHHHHHHHHHHHH
49.8521963094
345UbiquitinationALGTLMRAWAGSPKG
HHHHHHHHHCCCCCC
6.1121963094
347UbiquitinationGTLMRAWAGSPKGTI
HHHHHHHCCCCCCEE
13.9622817900
349PhosphorylationLMRAWAGSPKGTIQV
HHHHHCCCCCCEEEE
18.7229396449
351AcetylationRAWAGSPKGTIQVIT
HHHCCCCCCEEEEEE
71.0826051181
351SuccinylationRAWAGSPKGTIQVIT
HHHCCCCCCEEEEEE
71.0823954790
351UbiquitinationRAWAGSPKGTIQVIT
HHHCCCCCCEEEEEE
71.0827667366
353PhosphorylationWAGSPKGTIQVITQG
HCCCCCCEEEEEECC
17.8628555341
356UbiquitinationSPKGTIQVITQGTSL
CCCCEEEEEECCCCC
4.5221963094
358PhosphorylationKGTIQVITQGTSLKN
CCEEEEEECCCCCCC
23.3020873877
358UbiquitinationKGTIQVITQGTSLKN
CCEEEEEECCCCCCC
23.3022817900
361PhosphorylationIQVITQGTSLKNAGN
EEEEECCCCCCCCCC
22.5220873877
362PhosphorylationQVITQGTSLKNAGNC
EEEECCCCCCCCCCC
44.1425159151
363UbiquitinationVITQGTSLKNAGNCL
EEECCCCCCCCCCCC
5.0821963094
364AcetylationITQGTSLKNAGNCLS
EECCCCCCCCCCCCC
44.5126051181
364UbiquitinationITQGTSLKNAGNCLS
EECCCCCCCCCCCCC
44.5121906983
369S-nitrosocysteineSLKNAGNCLSPAVIV
CCCCCCCCCCHHHHH
3.78-
369GlutathionylationSLKNAGNCLSPAVIV
CCCCCCCCCCHHHHH
3.7822555962
369S-nitrosylationSLKNAGNCLSPAVIV
CCCCCCCCCCHHHHH
3.7818335467
369S-palmitoylationSLKNAGNCLSPAVIV
CCCCCCCCCCHHHHH
3.7829575903
371PhosphorylationKNAGNCLSPAVIVGL
CCCCCCCCHHHHHHH
17.0225159151
380AcetylationAVIVGLLKEASKQAD
HHHHHHHHHHHHHCC
57.1726051181
380UbiquitinationAVIVGLLKEASKQAD
HHHHHHHHHHHHHCC
57.1721906983
382UbiquitinationIVGLLKEASKQADVN
HHHHHHHHHHHCCCC
22.0521963094
384MalonylationGLLKEASKQADVNLV
HHHHHHHHHCCCCHH
57.4626320211
384UbiquitinationGLLKEASKQADVNLV
HHHHHHHHHCCCCHH
57.4621906983
388UbiquitinationEASKQADVNLVNAKL
HHHHHCCCCHHHHHH
7.1827667366
3942-HydroxyisobutyrylationDVNLVNAKLLVKEAG
CCCHHHHHHHHHHHC
36.83-
394AcetylationDVNLVNAKLLVKEAG
CCCHHHHHHHHHHHC
36.8323236377
394MalonylationDVNLVNAKLLVKEAG
CCCHHHHHHHHHHHC
36.8326320211
394UbiquitinationDVNLVNAKLLVKEAG
CCCHHHHHHHHHHHC
36.8323000965
398UbiquitinationVNAKLLVKEAGLNVT
HHHHHHHHHHCCCCC
41.6423000965
399UbiquitinationNAKLLVKEAGLNVTT
HHHHHHHHHCCCCCC
40.2527667366
401UbiquitinationKLLVKEAGLNVTTSH
HHHHHHHCCCCCCCC
20.9021963094
412UbiquitinationTTSHSPAAPGEQGFG
CCCCCCCCCCCCCHH
18.9321963094
417UbiquitinationPAAPGEQGFGECLLA
CCCCCCCCHHHHHHH
28.3721963094
421UbiquitinationGEQGFGECLLAVALA
CCCCHHHHHHHHHHC
3.7427667366
425UbiquitinationFGECLLAVALAGAPY
HHHHHHHHHHCCCCE
4.5327667366
428UbiquitinationCLLAVALAGAPYQAV
HHHHHHHCCCCEEHH
11.4521963094
431UbiquitinationAVALAGAPYQAVGLV
HHHHCCCCEEHHHHC
22.3523000965
432UbiquitinationVALAGAPYQAVGLVQ
HHHCCCCEEHHHHCC
14.4727667366
435UbiquitinationAGAPYQAVGLVQGTT
CCCCEEHHHHCCCCC
3.4323000965
438UbiquitinationPYQAVGLVQGTTPVL
CEEHHHHCCCCCHHH
3.9721963094
442UbiquitinationVGLVQGTTPVLQGLN
HHHCCCCCHHHCCCC
20.4423000965
446UbiquitinationQGTTPVLQGLNGAVF
CCCCHHHCCCCCCCC
55.3423000965
454UbiquitinationGLNGAVFRPEVPLRR
CCCCCCCCCCCCCCC
21.6321963094
458UbiquitinationAVFRPEVPLRRDLPL
CCCCCCCCCCCCCCE
20.6327667366
468UbiquitinationRDLPLLLFRTQTSDP
CCCCEEEEECCCCCC
8.8423000965
470PhosphorylationLPLLLFRTQTSDPAM
CCEEEEECCCCCCCH
28.9428348404
472PhosphorylationLLLFRTQTSDPAMLP
EEEEECCCCCCCHHH
34.1928348404
472UbiquitinationLLLFRTQTSDPAMLP
EEEEECCCCCCCHHH
34.1923000965
473PhosphorylationLLFRTQTSDPAMLPT
EEEECCCCCCCHHHH
31.6028348404
477SulfoxidationTQTSDPAMLPTMIGL
CCCCCCCHHHHHHHH
5.8428183972
480PhosphorylationSDPAMLPTMIGLLAE
CCCCHHHHHHHHHHH
19.9120068231
481SulfoxidationDPAMLPTMIGLLAEA
CCCHHHHHHHHHHHH
1.8528183972
509SulfoxidationDGETWHVMGISSLLP
CCCCEEEEEHHHHHH
2.2628183972
522UbiquitinationLPSLEAWKQHVTEAF
HHHHHHHHHHHHHHH
37.26-

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
55SPhosphorylationKinasePRKCZQ05513
GPS
57TPhosphorylationKinasePRKCZQ05513
GPS
78TPhosphorylationKinasePRKCZQ05513
GPS
-KUbiquitinationE3 ubiquitin ligasePRKNO60260
PMID:32478681

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SERA_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 SERA_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
SURF4_HUMANSURF4physical
22939629
SRS10_HUMANSRSF10physical
22939629
TRA2A_HUMANTRA2Aphysical
22939629
SRS11_HUMANSRSF11physical
22939629
SMCA5_HUMANSMARCA5physical
22939629
U2AF1_HUMANU2AF1physical
22939629
SSRP1_HUMANSSRP1physical
22939629
TR150_HUMANTHRAP3physical
22939629
TRI55_HUMANTRIM55physical
22939629
VTNC_HUMANVTNphysical
22939629
TCRG1_HUMANTCERG1physical
22939629
TF3C1_HUMANGTF3C1physical
22939629
VASN_HUMANVASNphysical
22939629
U2AF2_HUMANU2AF2physical
22939629
SMU1_HUMANSMU1physical
22939629
SRSF1_HUMANSRSF1physical
22939629
STAT1_HUMANSTAT1physical
22939629
SRSF5_HUMANSRSF5physical
22939629
SON_HUMANSONphysical
22939629
UT14A_HUMANUTP14Aphysical
22939629
PIAS4_HUMANPIAS4physical
21988832
EPN1_HUMANEPN1physical
25036637
ROM1_HUMANROM1physical
25036637
ITSN1_HUMANITSN1physical
25036637
ADHX_HUMANADH5physical
26344197
ASNS_HUMANASNSphysical
26344197
ASSY_HUMANASS1physical
26344197
CCD25_HUMANCCDC25physical
26344197
GDPP1_HUMANGDPGP1physical
26344197
AATC_HUMANGOT1physical
26344197
GPD1L_HUMANGPD1Lphysical
26344197
ROA1_HUMANHNRNPA1physical
26344197
CH10_HUMANHSPE1physical
26344197
LDHB_HUMANLDHBphysical
26344197
C1TC_HUMANMTHFD1physical
26344197
MYL6_HUMANMYL6physical
26344197
NUDT9_HUMANNUDT9physical
26344197
PABP1_HUMANPABPC1physical
26344197
PABP4_HUMANPABPC4physical
26344197
PLIN3_HUMANPLIN3physical
26344197
PLPHP_HUMANPROSCphysical
26344197
SERC_HUMANPSAT1physical
26344197
RD23A_HUMANRAD23Aphysical
26344197
RD23B_HUMANRAD23Bphysical
26344197
STIP1_HUMANSTIP1physical
26344197
TYSY_HUMANTYMSphysical
26344197
UBE2N_HUMANUBE2Nphysical
26344197
UE2NL_HUMANUBE2NLphysical
26344197
UCRI_HUMANUQCRFS1physical
26344197
UBP7_HUMANUSP7physical
26344197

Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
601815Phosphoglycerate dehydrogenase deficiency (PHGDHD)
256520Neu-Laxova syndrome 1 (NLS1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SERA_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"A quantitative atlas of mitotic phosphorylation.";
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-371, AND MASSSPECTROMETRY.

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