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P31153

- METK2_HUMAN

UniProt

P31153 - METK2_HUMAN

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Protein

S-adenosylmethionine synthase isoform type-2

Gene
MAT2A, AMS2, MATA2
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Catalyzes the formation of S-adenosylmethionine from methionine and ATP.UniRule annotation

Catalytic activityi

ATP + L-methionine + H2O = phosphate + diphosphate + S-adenosyl-L-methionine.UniRule annotation

Cofactori

Binds 2 divalent ions per subunit. Magnesium or cobalt By similarity.
Binds 1 potassium ion per subunit By similarity.UniRule annotation

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi31 – 311Magnesium By similarity
Metal bindingi57 – 571Potassium By similarity
Binding sitei159 – 1591ATP Reviewed prediction
Metal bindingi283 – 2831Potassium By similarity
Metal bindingi291 – 2911Magnesium By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 1366ATP Reviewed prediction

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. metal ion binding Source: UniProtKB-KW
  3. methionine adenosyltransferase activity Source: UniProt
  4. protein binding Source: UniProtKB

GO - Biological processi

  1. cellular nitrogen compound metabolic process Source: Reactome
  2. methylation Source: Reactome
  3. one-carbon metabolic process Source: UniProtKB-KW
  4. S-adenosylmethionine biosynthetic process Source: UniProt
  5. small molecule metabolic process Source: Reactome
  6. sulfur amino acid metabolic process Source: Reactome
  7. xenobiotic metabolic process Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Transferase

Keywords - Biological processi

One-carbon metabolism

Keywords - Ligandi

ATP-binding, Cobalt, Magnesium, Metal-binding, Nucleotide-binding, Potassium

Enzyme and pathway databases

ReactomeiREACT_115639. Sulfur amino acid metabolism.
REACT_6946. Methylation.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-2 (EC:2.5.1.6)
Short name:
AdoMet synthase 2
Alternative name(s):
Methionine adenosyltransferase 2
Short name:
MAT 2
Methionine adenosyltransferase II
Short name:
MAT-II
Gene namesi
Name:MAT2A
Synonyms:AMS2, MATA2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 2

Organism-specific databases

HGNCiHGNC:6904. MAT2A.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. methionine adenosyltransferase complex Source: UniProt
Complete GO annotation...

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30647.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395S-adenosylmethionine synthase isoform type-2UniRule annotationPRO_0000174435Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei81 – 811N6-acetyllysine1 Publication
Modified residuei114 – 1141Phosphoserine1 Publication

Post-translational modificationi

The alpha' subunit is a post-translationally modified version of MAT2A.UniRule annotation

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiP31153.
PaxDbiP31153.
PeptideAtlasiP31153.
PRIDEiP31153.

2D gel databases

REPRODUCTION-2DPAGEIPI00010157.

PTM databases

PhosphoSiteiP31153.

Expressioni

Gene expression databases

ArrayExpressiP31153.
BgeeiP31153.
CleanExiHS_MAT2A.
GenevestigatoriP31153.

Organism-specific databases

HPAiCAB009968.
HPA043028.

Interactioni

Subunit structurei

Heterotetramer composed of 2 catalytic alpha subunits (alpha and alpha') (MAT2A) and 1 copy of beta subunit (MAT2B).1 Publication

Protein-protein interaction databases

BioGridi110314. 22 interactions.
IntActiP31153. 17 interactions.
STRINGi9606.ENSP00000303147.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi17 – 259
Helixi30 – 4819
Beta strandi53 – 619
Beta strandi64 – 729
Helixi79 – 9012
Helixi95 – 973
Turni101 – 1033
Beta strandi104 – 1118
Helixi115 – 1217
Turni122 – 1243
Helixi127 – 1293
Beta strandi132 – 1343
Beta strandi136 – 1438
Helixi152 – 16918
Beta strandi176 – 19116
Beta strandi194 – 20916
Helixi215 – 22410
Helixi227 – 2304
Helixi233 – 2353
Beta strandi241 – 2455
Helixi254 – 2563
Turni266 – 2738
Helixi290 – 30718
Beta strandi312 – 3209
Beta strandi328 – 3336
Helixi342 – 35211
Helixi357 – 3648
Turni365 – 3673
Helixi371 – 3744
Beta strandi375 – 3773
Beta strandi379 – 3824
Helixi386 – 3883

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2P02X-ray1.21A1-395[»]
ProteinModelPortaliP31153.
SMRiP31153. Positions 16-395.

Miscellaneous databases

EvolutionaryTraceiP31153.

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.

Phylogenomic databases

eggNOGiCOG0192.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiP31153.
KOiK00789.
OMAiDETEESM.
PhylomeDBiP31153.
TreeFamiTF300511.

Family and domain databases

HAMAPiMF_00086. S_AdoMet_synth1.
InterProiIPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view]
PANTHERiPTHR11964. PTHR11964. 1 hit.
PfamiPF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view]
PIRSFiPIRSF000497. MAT. 1 hit.
SUPFAMiSSF55973. SSF55973. 3 hits.
TIGRFAMsiTIGR01034. metK. 1 hit.
PROSITEiPS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P31153-1 [UniParc]FASTAAdd to Basket

« Hide

MNGQLNGFHE AFIEEGTFLF TSESVGEGHP DKICDQISDA VLDAHLQQDP    50
DAKVACETVA KTGMILLAGE ITSRAAVDYQ KVVREAVKHI GYDDSSKGFD 100
YKTCNVLVAL EQQSPDIAQG VHLDRNEEDI GAGDQGLMFG YATDETEECM 150
PLTIVLAHKL NAKLAELRRN GTLPWLRPDS KTQVTVQYMQ DRGAVLPIRV 200
HTIVISVQHD EEVCLDEMRD ALKEKVIKAV VPAKYLDEDT IYHLQPSGRF 250
VIGGPQGDAG LTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 300
VAKSLVKGGL CRRVLVQVSY AIGVSHPLSI SIFHYGTSQK SERELLEIVK 350
KNFDLRPGVI VRDLDLKKPI YQRTAAYGHF GRDSFPWEVP KKLKY 395
Length:395
Mass (Da):43,661
Last modified:July 1, 1993 - v1
Checksum:i2E7D1B91CC4F7BDD
GO

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68836 mRNA. Translation: CAA48726.1.
DQ083239 mRNA. Translation: AAY85355.1.
AK291126 mRNA. Translation: BAF83815.1.
AC016753 Genomic DNA. Translation: AAY24339.1.
CH471053 Genomic DNA. Translation: EAW99511.1.
CH471053 Genomic DNA. Translation: EAW99513.1.
BC001686 mRNA. Translation: AAH01686.1.
BC001854 mRNA. Translation: AAH01854.1.
CCDSiCCDS1977.1.
PIRiS27257.
RefSeqiNP_005902.1. NM_005911.5.
UniGeneiHs.516157.

Genome annotation databases

EnsembliENST00000306434; ENSP00000303147; ENSG00000168906.
GeneIDi4144.
KEGGihsa:4144.
UCSCiuc002spr.3. human.

Polymorphism databases

DMDMi400245.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X68836 mRNA. Translation: CAA48726.1 .
DQ083239 mRNA. Translation: AAY85355.1 .
AK291126 mRNA. Translation: BAF83815.1 .
AC016753 Genomic DNA. Translation: AAY24339.1 .
CH471053 Genomic DNA. Translation: EAW99511.1 .
CH471053 Genomic DNA. Translation: EAW99513.1 .
BC001686 mRNA. Translation: AAH01686.1 .
BC001854 mRNA. Translation: AAH01854.1 .
CCDSi CCDS1977.1.
PIRi S27257.
RefSeqi NP_005902.1. NM_005911.5.
UniGenei Hs.516157.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2P02 X-ray 1.21 A 1-395 [» ]
ProteinModelPortali P31153.
SMRi P31153. Positions 16-395.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110314. 22 interactions.
IntActi P31153. 17 interactions.
STRINGi 9606.ENSP00000303147.

Chemistry

DrugBanki DB00134. L-Methionine.
DB00118. S-Adenosylmethionine.

PTM databases

PhosphoSitei P31153.

Polymorphism databases

DMDMi 400245.

2D gel databases

REPRODUCTION-2DPAGE IPI00010157.

Proteomic databases

MaxQBi P31153.
PaxDbi P31153.
PeptideAtlasi P31153.
PRIDEi P31153.

Protocols and materials databases

DNASUi 4144.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000306434 ; ENSP00000303147 ; ENSG00000168906 .
GeneIDi 4144.
KEGGi hsa:4144.
UCSCi uc002spr.3. human.

Organism-specific databases

CTDi 4144.
GeneCardsi GC02P085766.
H-InvDB HIX0117562.
HGNCi HGNC:6904. MAT2A.
HPAi CAB009968.
HPA043028.
MIMi 601468. gene.
neXtProti NX_P31153.
PharmGKBi PA30647.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0192.
HOGENOMi HOG000245710.
HOVERGENi HBG001562.
InParanoidi P31153.
KOi K00789.
OMAi DETEESM.
PhylomeDBi P31153.
TreeFami TF300511.

Enzyme and pathway databases

UniPathwayi UPA00315 ; UER00080 .
Reactomei REACT_115639. Sulfur amino acid metabolism.
REACT_6946. Methylation.

Miscellaneous databases

ChiTaRSi MAT2A. human.
EvolutionaryTracei P31153.
GenomeRNAii 4144.
NextBioi 16276.
PROi P31153.
SOURCEi Search...

Gene expression databases

ArrayExpressi P31153.
Bgeei P31153.
CleanExi HS_MAT2A.
Genevestigatori P31153.

Family and domain databases

HAMAPi MF_00086. S_AdoMet_synth1.
InterProi IPR022631. ADOMET_SYNTHASE_CS.
IPR022630. S-AdoMet_synt_C.
IPR022629. S-AdoMet_synt_central.
IPR022628. S-AdoMet_synt_N.
IPR002133. S-AdoMet_synthetase.
IPR022636. S-AdoMet_synthetase_sfam.
[Graphical view ]
PANTHERi PTHR11964. PTHR11964. 1 hit.
Pfami PF02773. S-AdoMet_synt_C. 1 hit.
PF02772. S-AdoMet_synt_M. 1 hit.
PF00438. S-AdoMet_synt_N. 1 hit.
[Graphical view ]
PIRSFi PIRSF000497. MAT. 1 hit.
SUPFAMi SSF55973. SSF55973. 3 hits.
TIGRFAMsi TIGR01034. metK. 1 hit.
PROSITEi PS00376. ADOMET_SYNTHASE_1. 1 hit.
PS00377. ADOMET_SYNTHASE_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning and developmental expression of a human kidney S-adenosylmethionine synthetase."
    Horikawa S., Tsukada K.
    FEBS Lett. 312:37-41(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Kidney.
  2. "Activation of a novel isoform of methionine adenosyl transferase 2A and increased S-adenosylmethionine turnover in lung epithelial cells exposed to hyperoxia."
    Panayiotidis M.I., Stabler S.P., Ahmad A., Pappa A., Legros L.H. Jr., Hernandez-Saavedra D., Schneider B.K., Allen R.H., Vasiliou V., McCord J.M., Kotb M., White C.W.
    Free Radic. Biol. Med. 40:348-358(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Lung.
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Muscle.
  7. "Cloning, expression, and functional characterization of the beta regulatory subunit of human methionine adenosyltransferase (MAT II)."
    LeGros H.L., Halim A.-B., Geller A.M., Kotb M.
    J. Biol. Chem. 275:2359-2366(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-81, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMETK2_HUMAN
AccessioniPrimary (citable) accession number: P31153
Secondary accession number(s): A8K511, D6W5L1, Q53SP5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1993
Last sequence update: July 1, 1993
Last modified: September 3, 2014
This is version 150 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  4. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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