SERC_HUMAN - dbPTM
SERC_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID SERC_HUMAN
UniProt AC Q9Y617
Protein Name Phosphoserine aminotransferase
Gene Name PSAT1
Organism Homo sapiens (Human).
Sequence Length 370
Subcellular Localization
Protein Description Catalyzes the reversible conversion of 3-phosphohydroxypyruvate to phosphoserine and of 3-hydroxy-2-oxo-4-phosphonooxybutanoate to phosphohydroxythreonine..
Protein Sequence MDAPRQVVNFGPGPAKLPHSVLLEIQKELLDYKGVGISVLEMSHRSSDFAKIINNTENLVRELLAVPDNYKVIFLQGGGCGQFSAVPLNLIGLKAGRCADYVVTGAWSAKAAEEAKKFGTINIVHPKLGSYTKIPDPSTWNLNPDASYVYYCANETVHGVEFDFIPDVKGAVLVCDMSSNFLSKPVDVSKFGVIFAGAQKNVGSAGVTVVIVRDDLLGFALRECPSVLEYKVQAGNSSLYNTPPCFSIYVMGLVLEWIKNNGGAAAMEKLSSIKSQTIYEIIDNSQGFYVCPVEPQNRSKMNIPFRIGNAKGDDALEKRFLDKALELNMLSLKGHRSVGGIRASLYNAVTIEDVQKLAAFMKKFLEMHQL
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-------MDAPRQVV
-------CCCCCEEE		10.0119413330
5Methylation---MDAPRQVVNFGP
---CCCCCEEEECCC		43.58115489283
16UbiquitinationNFGPGPAKLPHSVLL
ECCCCCCCCCHHHHH		66.7321906983
16 (in isoform 2)Ubiquitination-66.7321890473
16 (in isoform 1)Ubiquitination-66.7321890473
16AcetylationNFGPGPAKLPHSVLL
ECCCCCCCCCHHHHH		66.7325953088
20PhosphorylationGPAKLPHSVLLEIQK
CCCCCCHHHHHHHHH		16.7225159151
27UbiquitinationSVLLEIQKELLDYKG
HHHHHHHHHHHCCCC		56.8621906983
27 (in isoform 2)Ubiquitination-56.8621890473
27 (in isoform 1)Ubiquitination-56.8621890473
32PhosphorylationIQKELLDYKGVGISV
HHHHHHCCCCCCEEE		15.04-
33UbiquitinationQKELLDYKGVGISVL
HHHHHCCCCCCEEEE		46.95-
33AcetylationQKELLDYKGVGISVL
HHHHHCCCCCCEEEE		46.9527452117
332-HydroxyisobutyrylationQKELLDYKGVGISVL
HHHHHCCCCCCEEEE		46.95-
38PhosphorylationDYKGVGISVLEMSHR
CCCCCCEEEEEECCC		18.0823401153
42SulfoxidationVGISVLEMSHRSSDF
CCEEEEEECCCCCHH		3.4130846556
43PhosphorylationGISVLEMSHRSSDFA
CEEEEEECCCCCHHH		13.3320068231
45MethylationSVLEMSHRSSDFAKI
EEEEECCCCCHHHHH		30.46115489277
46PhosphorylationVLEMSHRSSDFAKII
EEEECCCCCHHHHHH		28.9229514088
47PhosphorylationLEMSHRSSDFAKIIN
EEECCCCCHHHHHHH		36.3829514088
51 (in isoform 2)Acetylation-44.08-
51 (in isoform 2)Ubiquitination-44.0821890473
51AcetylationHRSSDFAKIINNTEN
CCCCHHHHHHHCHHH		44.0819608861
51 (in isoform 1)Ubiquitination-44.0821890473
51UbiquitinationHRSSDFAKIINNTEN
CCCCHHHHHHHCHHH		44.0821906983
70PhosphorylationLLAVPDNYKVIFLQG
HHCCCCCEEEEEECC		17.6327642862
71UbiquitinationLAVPDNYKVIFLQGG
HCCCCCEEEEEECCC		34.80-
94UbiquitinationPLNLIGLKAGRCADY
CHHHHCCCCCCCCCE		43.5121906983
94 (in isoform 1)Ubiquitination-43.5121890473
94 (in isoform 2)Ubiquitination-43.5121890473
97MethylationLIGLKAGRCADYVVT
HHCCCCCCCCCEEEC		19.81115489259
101PhosphorylationKAGRCADYVVTGAWS
CCCCCCCEEECCCCC		4.3628152594
110AcetylationVTGAWSAKAAEEAKK
ECCCCCHHHHHHHHH		42.4823749302
110UbiquitinationVTGAWSAKAAEEAKK
ECCCCCHHHHHHHHH		42.48-
117AcetylationKAAEEAKKFGTINIV
HHHHHHHHHCCEEEE		56.9525953088
117UbiquitinationKAAEEAKKFGTINIV
HHHHHHHHHCCEEEE		56.95-
127MalonylationTINIVHPKLGSYTKI
CEEEECCCCCCCCCC		51.0726320211
127AcetylationTINIVHPKLGSYTKI
CEEEECCCCCCCCCC		51.0723954790
127UbiquitinationTINIVHPKLGSYTKI
CEEEECCCCCCCCCC		51.0719608861
127 (in isoform 2)Acetylation-51.07-
130PhosphorylationIVHPKLGSYTKIPDP
EECCCCCCCCCCCCC		39.8126091039
177SulfoxidationGAVLVCDMSSNFLSK
CEEEEEECCCCCCCC		3.9130846556
178 (in isoform 2)Phosphorylation-14.63-
178PhosphorylationAVLVCDMSSNFLSKP
EEEEEECCCCCCCCC		14.6320068231
179PhosphorylationVLVCDMSSNFLSKPV
EEEEECCCCCCCCCC		25.5920068231
179 (in isoform 2)Phosphorylation-25.59-
183PhosphorylationDMSSNFLSKPVDVSK
ECCCCCCCCCCCHHH		30.6720068231
184AcetylationMSSNFLSKPVDVSKF
CCCCCCCCCCCHHHC		51.7326051181
184UbiquitinationMSSNFLSKPVDVSKF
CCCCCCCCCCCHHHC		51.73-
190 (in isoform 2)Ubiquitination-46.0821890473
190 (in isoform 1)Ubiquitination-46.0821890473
190UbiquitinationSKPVDVSKFGVIFAG
CCCCCHHHCEEEEEE		46.081906983
200OtherVIFAGAQKNVGSAGV
EEEEECCCCCCCCCE		53.73-
200N6-(pyridoxal phosphate)lysineVIFAGAQKNVGSAGV
EEEEECCCCCCCCCE		53.73-
222MethylationDLLGFALRECPSVLE
CHHHHHHHCCCCEEE		39.79115489265
226PhosphorylationFALRECPSVLEYKVQ
HHHHCCCCEEEEEEE		51.5023312004
269 (in isoform 2)Acetylation-40.35-
269UbiquitinationGGAAAMEKLSSIKSQ
CHHHHHHHHHHCCCC		40.3521906983
269AcetylationGGAAAMEKLSSIKSQ
CHHHHHHHHHHCCCC		40.3519608861
269 (in isoform 1)Ubiquitination-40.3521890473
269 (in isoform 2)Ubiquitination-40.3521890473
271PhosphorylationAAAMEKLSSIKSQTI
HHHHHHHHHCCCCCC		40.8824719451
274UbiquitinationMEKLSSIKSQTIYEI
HHHHHHCCCCCCEEE		38.16-
279PhosphorylationSIKSQTIYEIIDNSQ
HCCCCCCEEEECCCC		12.40-
298 (in isoform 2)Phosphorylation-32.19-
300 (in isoform 2)Phosphorylation-32.50-
300UbiquitinationVEPQNRSKMNIPFRI
CCCCCCCCCCCCEEE		32.50-
311 (in isoform 1)Ubiquitination-67.8621890473
311SuccinylationPFRIGNAKGDDALEK
CEEECCCCCCHHHHH		67.8623954790
3112-HydroxyisobutyrylationPFRIGNAKGDDALEK
CEEECCCCCCHHHHH		67.86-
311AcetylationPFRIGNAKGDDALEK
CEEECCCCCCHHHHH		67.8623749302
311UbiquitinationPFRIGNAKGDDALEK
CEEECCCCCCHHHHH		67.86-
317 (in isoform 2)Ubiquitination-43.8621890473
318MalonylationKGDDALEKRFLDKAL
CCCHHHHHHHHHHHH		49.6626320211
318AcetylationKGDDALEKRFLDKAL
CCCHHHHHHHHHHHH		49.6619608861
318UbiquitinationKGDDALEKRFLDKAL
CCCHHHHHHHHHHHH		49.6619608861
318 (in isoform 1)Ubiquitination-49.6621890473
3232-HydroxyisobutyrylationLEKRFLDKALELNML
HHHHHHHHHHHHHCC		57.95-
323 (in isoform 1)Ubiquitination-57.9521890473
323AcetylationLEKRFLDKALELNML
HHHHHHHHHHHHHCC		57.9519608861
323UbiquitinationLEKRFLDKALELNML
HHHHHHHHHHHHHCC		57.9521906983
329SulfoxidationDKALELNMLSLKGHR
HHHHHHHCCCCCCCC		4.1530846556
331PhosphorylationALELNMLSLKGHRSV
HHHHHCCCCCCCCCC		19.7829255136
333MalonylationELNMLSLKGHRSVGG
HHHCCCCCCCCCCHH		49.6626320211
333UbiquitinationELNMLSLKGHRSVGG
HHHCCCCCCCCCCHH		49.6619608861
333 (in isoform 1)Ubiquitination-49.6621890473
333AcetylationELNMLSLKGHRSVGG
HHHCCCCCCCCCCHH		49.6619608861
333MethylationELNMLSLKGHRSVGG
HHHCCCCCCCCCCHH		49.6619608861
336MethylationMLSLKGHRSVGGIRA
CCCCCCCCCCHHHHH		41.53115489271
344PhosphorylationSVGGIRASLYNAVTI
CCHHHHHHHCCCCCH		22.8719664994
346PhosphorylationGGIRASLYNAVTIED
HHHHHHHCCCCCHHH		9.8930266825
350PhosphorylationASLYNAVTIEDVQKL
HHHCCCCCHHHHHHH		19.0824719451
356UbiquitinationVTIEDVQKLAAFMKK
CCHHHHHHHHHHHHH		39.68-
3622-HydroxyisobutyrylationQKLAAFMKKFLEMHQ
HHHHHHHHHHHHHHC		33.64-
362AcetylationQKLAAFMKKFLEMHQ
HHHHHHHHHHHHHHC		33.6426051181
363AcetylationKLAAFMKKFLEMHQL
HHHHHHHHHHHHHCC		43.3125953088
363 (in isoform 1)Ubiquitination-43.3121890473
3632-HydroxyisobutyrylationKLAAFMKKFLEMHQL
HHHHHHHHHHHHHCC		43.31-
363MalonylationKLAAFMKKFLEMHQL
HHHHHHHHHHHHHCC		43.3126320211
363UbiquitinationKLAAFMKKFLEMHQL
HHHHHHHHHHHHHCC		43.312189047
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 SERC_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of SERC_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 SERC_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
A4_HUMANAPPphysical
21832049
THIC_HUMANACAT2physical
22939629
SHOT1_HUMANKIAA1598physical
22939629
THADA_HUMANTHADAphysical
22939629
TTC1_HUMANTTC1physical
22939629
TALDO_HUMANTALDO1physical
22939629
STAT6_HUMANSTAT6physical
22939629
TBB6_HUMANTUBB6physical
22939629
PSD10_HUMANPSMD10physical
21988832
MPRIP_HUMANMPRIPphysical
26186194
CAB39_HUMANCAB39physical
26344197
PGBM_HUMANHSPG2physical
26344197
PCBP1_HUMANPCBP1physical
26344197
SGPL1_HUMANSGPL1physical
26344197
MPRIP_HUMANMPRIPphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
610992Phosphoserine aminotransferase deficiency (PSATD)
616038Neu-Laxova syndrome 2 (NLS2)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of SERC_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 MET-1, 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-51; LYS-269; LYS-318;LYS-323 AND LYS-333, AND MASS SPECTROMETRY.

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