METK2_HUMAN - dbPTM
METK2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID METK2_HUMAN
UniProt AC P31153
Protein Name S-adenosylmethionine synthase isoform type-2
Gene Name MAT2A
Organism Homo sapiens (Human).
Sequence Length 395
Subcellular Localization
Protein Description Catalyzes the formation of S-adenosylmethionine from methionine and ATP. The reaction comprises two steps that are both catalyzed by the same enzyme: formation of S-adenosylmethionine (AdoMet) and triphosphate, and subsequent hydrolysis of the triphosphate..
Protein Sequence MNGQLNGFHEAFIEEGTFLFTSESVGEGHPDKICDQISDAVLDAHLQQDPDAKVACETVAKTGMILLAGEITSRAAVDYQKVVREAVKHIGYDDSSKGFDYKTCNVLVALEQQSPDIAQGVHLDRNEEDIGAGDQGLMFGYATDETEECMPLTIVLAHKLNAKLAELRRNGTLPWLRPDSKTQVTVQYMQDRGAVLPIRVHTIVISVQHDEEVCLDEMRDALKEKVIKAVVPAKYLDEDTIYHLQPSGRFVIGGPQGDAGLTGRKIIVDTYGGWGAHGGGAFSGKDYTKVDRSAAYAARWVAKSLVKGGLCRRVLVQVSYAIGVSHPLSISIFHYGTSQKSERELLEIVKKNFDLRPGVIVRDLDLKKPIYQRTAAYGHFGRDSFPWEVPKKLKY
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
18UbiquitinationAFIEEGTFLFTSESV
HHEECCCEEEEECCC		8.53-
25AcetylationFLFTSESVGEGHPDK
EEEEECCCCCCCCHH		7.70-
25UbiquitinationFLFTSESVGEGHPDK
EEEEECCCCCCCCHH		7.70-
34UbiquitinationEGHPDKICDQISDAV
CCCCHHHHHHHHHHH		3.7721890473
39UbiquitinationKICDQISDAVLDAHL
HHHHHHHHHHHHHHH		42.18-
53UbiquitinationLQQDPDAKVACETVA
HHCCCCCCHHHHHHH		37.43-
53AcetylationLQQDPDAKVACETVA
HHCCCCCCHHHHHHH		37.4326051181
61UbiquitinationVACETVAKTGMILLA
HHHHHHHHHCEEEEE		41.07-
62PhosphorylationACETVAKTGMILLAG
HHHHHHHHCEEEEEC		23.4220068231
64SulfoxidationETVAKTGMILLAGEI
HHHHHHCEEEEECEE		2.0628183972
812-HydroxyisobutyrylationRAAVDYQKVVREAVK
HHCCCHHHHHHHHHH		36.15-
81UbiquitinationRAAVDYQKVVREAVK
HHCCCHHHHHHHHHH		36.1521906983
81AcetylationRAAVDYQKVVREAVK
HHCCCHHHHHHHHHH		36.1519608861
882-HydroxyisobutyrylationKVVREAVKHIGYDDS
HHHHHHHHHHCCCCC		36.23-
88UbiquitinationKVVREAVKHIGYDDS
HHHHHHHHHHCCCCC		36.2321890473
88AcetylationKVVREAVKHIGYDDS
HHHHHHHHHHCCCCC		36.2323749302
96UbiquitinationHIGYDDSSKGFDYKT
HHCCCCCCCCCCHHH		43.74-
972-HydroxyisobutyrylationIGYDDSSKGFDYKTC
HCCCCCCCCCCHHHH		68.50-
97UbiquitinationIGYDDSSKGFDYKTC
HCCCCCCCCCCHHHH		68.5021890473
100UbiquitinationDDSSKGFDYKTCNVL
CCCCCCCCHHHHHEE		53.33-
101PhosphorylationDSSKGFDYKTCNVLV
CCCCCCCHHHHHEEE		13.1122817900
102UbiquitinationSSKGFDYKTCNVLVA
CCCCCCHHHHHEEEE		48.74-
103PhosphorylationSKGFDYKTCNVLVAL
CCCCCHHHHHEEEEE		11.7727080861
104S-palmitoylationKGFDYKTCNVLVALE
CCCCHHHHHEEEEEE		2.6529575903
114PhosphorylationLVALEQQSPDIAQGV
EEEEECCCCCHHHCE		25.0030266825
163AcetylationLAHKLNAKLAELRRN
HHHHHCHHHHHHHHC		47.3525953088
163UbiquitinationLAHKLNAKLAELRRN
HHHHHCHHHHHHHHC		47.35-
165UbiquitinationHKLNAKLAELRRNGT
HHHCHHHHHHHHCCC		17.05-
171AcetylationLAELRRNGTLPWLRP
HHHHHHCCCCCCCCC		27.15-
171UbiquitinationLAELRRNGTLPWLRP
HHHHHHCCCCCCCCC		27.1521890473
189SulfoxidationTQVTVQYMQDRGAVL
CEEEEEEECCCCCEE		1.5430846556
192MethylationTVQYMQDRGAVLPIR
EEEEECCCCCEEEEE		20.34115482647
222UbiquitinationLDEMRDALKEKVIKA
HHHHHHHHHHHHHHH		9.61-
226UbiquitinationRDALKEKVIKAVVPA
HHHHHHHHHHHHCCH		5.9421890473
228UbiquitinationALKEKVIKAVVPAKY
HHHHHHHHHHCCHHH		37.8121890473
2282-HydroxyisobutyrylationALKEKVIKAVVPAKY
HHHHHHHHHHCCHHH		37.81-
228AcetylationALKEKVIKAVVPAKY
HHHHHHHHHHCCHHH		37.8125953088
228SumoylationALKEKVIKAVVPAKY
HHHHHHHHHHCCHHH		37.8128112733
234AcetylationIKAVVPAKYLDEDTI
HHHHCCHHHCCCCCE		40.0323749302
2342-HydroxyisobutyrylationIKAVVPAKYLDEDTI
HHHHCCHHHCCCCCE		40.03-
234UbiquitinationIKAVVPAKYLDEDTI
HHHHCCHHHCCCCCE		40.0321890473
234SumoylationIKAVVPAKYLDEDTI
HHHHCCHHHCCCCCE		40.0328112733
235PhosphorylationKAVVPAKYLDEDTIY
HHHCCHHHCCCCCEE		22.8428152594
240UbiquitinationAKYLDEDTIYHLQPS
HHHCCCCCEEEECCC		22.76-
242PhosphorylationYLDEDTIYHLQPSGR
HCCCCCEEEECCCCC		9.89-
244UbiquitinationDEDTIYHLQPSGRFV
CCCCEEEECCCCCEE		4.4921890473
262PhosphorylationPQGDAGLTGRKIIVD
CCCCCCCCCCEEEEE		33.7420068231
285UbiquitinationGGGAFSGKDYTKVDR
CCCCCCCCCCCCCCH		46.49-
287UbiquitinationGAFSGKDYTKVDRSA
CCCCCCCCCCCCHHH		16.3721890473
288UbiquitinationAFSGKDYTKVDRSAA
CCCCCCCCCCCHHHH		34.4221890473
289UbiquitinationFSGKDYTKVDRSAAY
CCCCCCCCCCHHHHH		35.5921890473
293PhosphorylationDYTKVDRSAAYAARW
CCCCCCHHHHHHHHH		16.8829743597
296PhosphorylationKVDRSAAYAARWVAK
CCCHHHHHHHHHHHH		10.6622167270
303UbiquitinationYAARWVAKSLVKGGL
HHHHHHHHHHHHCCC		34.40-
303AcetylationYAARWVAKSLVKGGL
HHHHHHHHHHHHCCC		34.4025953088
307AcetylationWVAKSLVKGGLCRRV
HHHHHHHHCCCHHEE		53.1825953088
307UbiquitinationWVAKSLVKGGLCRRV
HHHHHHHHCCCHHEE		53.1821890473
319PhosphorylationRRVLVQVSYAIGVSH
HEEEEEHHHHHCCCC		7.55-
320PhosphorylationRVLVQVSYAIGVSHP
EEEEEHHHHHCCCCC		11.90-
340SumoylationFHYGTSQKSERELLE
EECCCCCCCHHHHHH		54.79-
340SumoylationFHYGTSQKSERELLE
EECCCCCCCHHHHHH		54.79-
350AcetylationRELLEIVKKNFDLRP
HHHHHHHHHCCCCCC		47.8925953088
350UbiquitinationRELLEIVKKNFDLRP
HHHHHHHHHCCCCCC		47.8921890473
351UbiquitinationELLEIVKKNFDLRPG
HHHHHHHHCCCCCCC		52.5321890473
351MalonylationELLEIVKKNFDLRPG
HHHHHHHHCCCCCCC		52.5326320211
367UbiquitinationIVRDLDLKKPIYQRT
EEEECCCCCCHHHHH		57.0521890473
3672-HydroxyisobutyrylationIVRDLDLKKPIYQRT
EEEECCCCCCHHHHH		57.05-
368SumoylationVRDLDLKKPIYQRTA
EEECCCCCCHHHHHC		43.90-
368SumoylationVRDLDLKKPIYQRTA
EEECCCCCCHHHHHC		43.90-
368UbiquitinationVRDLDLKKPIYQRTA
EEECCCCCCHHHHHC		43.90-
374PhosphorylationKKPIYQRTAAYGHFG
CCCHHHHHCCCCCCC		10.5023403867
377PhosphorylationIYQRTAAYGHFGRDS
HHHHHCCCCCCCCCC		14.5223403867
384PhosphorylationYGHFGRDSFPWEVPK
CCCCCCCCCCCCCCC		31.6719664994
3912-HydroxyisobutyrylationSFPWEVPKKLKY---
CCCCCCCCCCCC---		75.75-
392UbiquitinationFPWEVPKKLKY----
CCCCCCCCCCC----		44.11-
394SumoylationWEVPKKLKY------
CCCCCCCCC------		58.77-
394SumoylationWEVPKKLKY------
CCCCCCCCC------		58.77-
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 METK2_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of METK2_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 METK2_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
MAT2B_HUMANMAT2Bphysical
12671891
RS3A_HUMANRPS3Aphysical
22939629
RS3_HUMANRPS3physical
22939629
MAT2B_HUMANMAT2Bphysical
22863883
METK2_HUMANMAT2Aphysical
25416956
MAT2B_HUMANMAT2Bphysical
25416956
TM213_HUMANTMEM213physical
25416956
ABCB7_HUMANABCB7physical
26344197
ACSA_HUMANACSS2physical
26344197
ASNS_HUMANASNSphysical
26344197
NMD3_HUMANNMD3physical
26344197
SDHB_HUMANSDHBphysical
26344197
TBB5_HUMANTUBBphysical
26344197
MAT2B_HUMANMAT2Bphysical
27548429
METK2_HUMANMAT2Aphysical
27548429
CUL3_HUMANCUL3physical
27213918
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
DB00134L-Methionine
DB00118S-Adenosylmethionine
Regulatory Network of METK2_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-81, AND MASS SPECTROMETRY.
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-114, AND MASSSPECTROMETRY.

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