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Protein

S-adenosylmethionine synthase isoform type-1

Gene

MAT1A

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

Functioni

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

Catalytic activityi

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

Cofactori

Protein has several cofactor binding sites:
  • Mg2+By similarity, Co2+By similarityNote: Binds 2 divalent ions per subunit. Magnesium or cobalt.By similarity
  • K(+)By similarityNote: Binds 1 potassium ion per subunit.By similarity

Pathwayi

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei29 – 291Substrate1 Publication
Metal bindingi31 – 311MagnesiumBy similarity
Metal bindingi57 – 571PotassiumBy similarity
Binding sitei159 – 1591ATPSequence Analysis
Binding sitei179 – 1791Substrate1 Publication
Binding sitei247 – 2471Substrate1 Publication
Binding sitei249 – 2491Substrate; via carbonyl oxygen1 Publication
Binding sitei258 – 2581Substrate1 Publication
Metal bindingi283 – 2831PotassiumBy similarity
Metal bindingi291 – 2911MagnesiumBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi131 – 1366ATPSequence Analysis

GO - Molecular functioni

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

GO - Biological processi

  1. cellular amino acid metabolic process Source: ProtInc
  2. cellular nitrogen compound metabolic process Source: Reactome
  3. methylation Source: Reactome
  4. one-carbon metabolic process Source: UniProtKB-KW
  5. S-adenosylmethionine biosynthetic process Source: UniProtKB-UniPathway
  6. small molecule metabolic process Source: Reactome
  7. sulfur amino acid metabolic process Source: Reactome
  8. 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_268063. Defective MAT1A causes Methionine adenosyltransferase deficiency (MATD).
REACT_6946. Methylation.
UniPathwayiUPA00315; UER00080.

Names & Taxonomyi

Protein namesi
Recommended name:
S-adenosylmethionine synthase isoform type-1 (EC:2.5.1.6)
Short name:
AdoMet synthase 1
Alternative name(s):
Methionine adenosyltransferase 1
Short name:
MAT 1
Methionine adenosyltransferase I/III
Short name:
MAT-I/III
Gene namesi
Name:MAT1A
Synonyms:AMS1, MATA1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:6903. MAT1A.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
Complete GO annotation...

Pathology & Biotechi

Involvement in diseasei

Methionine adenosyltransferase deficiency (MATD)4 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn inborn error of metabolism resulting in isolated hypermethioninemia. Most patients have no clinical abnormalities, although some neurologic symptoms may be present in rare cases with severe loss of methionine adenosyltransferase activity.

See also OMIM:250850
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381S → N in MATD; abolishes enzyme activity. 1 Publication
VAR_031242
Natural varianti55 – 551A → D in MATD. 1 Publication
VAR_006935
Natural varianti199 – 1991R → C in MATD; retains 11% of wild-type activity. 1 Publication
VAR_006936
Natural varianti264 – 2641R → C in MATD; has virtually no enzymatic activity. 1 Publication
VAR_031243
Natural varianti264 – 2641R → H in MATD; dominant mutation. 2 Publications
VAR_006937
Natural varianti305 – 3051L → P in MATD. 1 Publication
VAR_006938
Natural varianti322 – 3221I → M in MATD; diminishes but do not completely abolishes enzyme activity; 46% of the level of the wild-type enzyme. 2 Publications
VAR_006939
Natural varianti336 – 3361G → R in MATD; retains significant enzymatic activity; 23% of the level of the wild-type enzyme. 1 Publication
VAR_031244
Natural varianti344 – 3441E → A in MATD; diminishes but do not completely abolishes enzyme activity; 12% of the level of the wild-type enzyme. 1 Publication
VAR_031245
Natural varianti356 – 3561R → Q in MATD. 1 Publication
Corresponds to variant rs138742870 [ dbSNP | Ensembl ].
VAR_006940
Natural varianti357 – 3571P → L in MATD. 1 Publication
VAR_006941
Natural varianti378 – 3781G → S in MATD. 1 Publication
VAR_006942

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi250850. phenotype.
Orphaneti168598. Brain demyelination due to methionine adenosyltransferase deficiency.
PharmGKBiPA30646.

Chemistry

DrugBankiDB00134. L-Methionine.
DB00118. S-Adenosylmethionine.

Polymorphism and mutation databases

BioMutaiMAT1A.
DMDMi417297.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 395395S-adenosylmethionine synthase isoform type-1PRO_0000174432Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi34 ↔ 60By similarity
Modified residuei120 – 1201S-nitrosocysteineBy similarity

Post-translational modificationi

S-nitrosylation of Cys-120 inactivates the enzyme.By similarity

Keywords - PTMi

Disulfide bond, S-nitrosylation

Proteomic databases

MaxQBiQ00266.
PaxDbiQ00266.
PRIDEiQ00266.

PTM databases

PhosphoSiteiQ00266.

Expressioni

Tissue specificityi

Expressed in liver.

Gene expression databases

BgeeiQ00266.
CleanExiHS_MAT1A.
ExpressionAtlasiQ00266. baseline and differential.
GenevestigatoriQ00266.

Organism-specific databases

HPAiHPA048627.

Interactioni

Subunit structurei

Homotetramer (MAT-I) or homodimer (MAT-III).1 Publication

Protein-protein interaction databases

BioGridi110313. 7 interactions.
STRINGi9606.ENSP00000361287.

Structurei

Secondary structure

1
395
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi18 – 258Combined sources
Helixi30 – 4819Combined sources
Beta strandi53 – 619Combined sources
Beta strandi64 – 729Combined sources
Helixi79 – 9012Combined sources
Helixi95 – 973Combined sources
Turni101 – 1033Combined sources
Beta strandi105 – 1117Combined sources
Helixi115 – 1217Combined sources
Turni122 – 1243Combined sources
Helixi127 – 1293Combined sources
Beta strandi132 – 1343Combined sources
Beta strandi136 – 1438Combined sources
Helixi152 – 17019Combined sources
Beta strandi171 – 1733Combined sources
Beta strandi176 – 19116Combined sources
Beta strandi194 – 20916Combined sources
Beta strandi211 – 2133Combined sources
Helixi215 – 22410Combined sources
Helixi227 – 2304Combined sources
Helixi233 – 2353Combined sources
Beta strandi241 – 2455Combined sources
Helixi254 – 2563Combined sources
Turni266 – 2738Combined sources
Helixi290 – 30718Combined sources
Beta strandi312 – 3209Combined sources
Beta strandi328 – 3336Combined sources
Helixi342 – 35211Combined sources
Helixi357 – 3637Combined sources
Turni364 – 3674Combined sources
Helixi371 – 3744Combined sources
Beta strandi375 – 3773Combined sources
Beta strandi379 – 3813Combined sources
Helixi386 – 3883Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OBVX-ray2.05A16-395[»]
ProteinModelPortaliQ00266.
SMRiQ00266. Positions 14-395.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ00266.

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.Curated

Phylogenomic databases

eggNOGiCOG0192.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ00266.
KOiK00789.
OMAiSEFPWEI.
OrthoDBiEOG7TF79H.
PhylomeDBiQ00266.
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.

Q00266-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MNGPVDGLCD HSLSEGVFMF TSESVGEGHP DKICDQISDA VLDAHLKQDP
60 70 80 90 100
NAKVACETVC KTGMVLLCGE ITSMAMVDYQ RVVRDTIKHI GYDDSAKGFD
110 120 130 140 150
FKTCNVLVAL EQQSPDIAQC VHLDRNEEDV GAGDQGLMFG YATDETEECM
160 170 180 190 200
PLTIILAHKL NARMADLRRS GLLPWLRPDS KTQVTVQYMQ DNGAVIPVRI
210 220 230 240 250
HTIVISVQHN EDITLEEMRR ALKEQVIRAV VPAKYLDEDT VYHLQPSGRF
260 270 280 290 300
VIGGPQGDAG VTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW
310 320 330 340 350
VAKSLVKAGL CRRVLVQVSY AIGVAEPLSI SIFTYGTSQK TERELLDVVH
360 370 380 390
KNFDLRPGVI VRDLDLKKPI YQKTACYGHF GRSEFPWEVP RKLVF
Length:395
Mass (Da):43,648
Last modified:October 1, 1993 - v2
Checksum:iB3462A5670A5B0D4
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti272 – 2732GG → AA in BAA08355 (PubMed:1772450).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti38 – 381S → N in MATD; abolishes enzyme activity. 1 Publication
VAR_031242
Natural varianti55 – 551A → D in MATD. 1 Publication
VAR_006935
Natural varianti119 – 1191Q → H.
Corresponds to variant rs1143693 [ dbSNP | Ensembl ].
VAR_028944
Natural varianti199 – 1991R → C in MATD; retains 11% of wild-type activity. 1 Publication
VAR_006936
Natural varianti264 – 2641R → C in MATD; has virtually no enzymatic activity. 1 Publication
VAR_031243
Natural varianti264 – 2641R → H in MATD; dominant mutation. 2 Publications
VAR_006937
Natural varianti305 – 3051L → P in MATD. 1 Publication
VAR_006938
Natural varianti322 – 3221I → M in MATD; diminishes but do not completely abolishes enzyme activity; 46% of the level of the wild-type enzyme. 2 Publications
VAR_006939
Natural varianti336 – 3361G → R in MATD; retains significant enzymatic activity; 23% of the level of the wild-type enzyme. 1 Publication
VAR_031244
Natural varianti344 – 3441E → A in MATD; diminishes but do not completely abolishes enzyme activity; 12% of the level of the wild-type enzyme. 1 Publication
VAR_031245
Natural varianti356 – 3561R → Q in MATD. 1 Publication
Corresponds to variant rs138742870 [ dbSNP | Ensembl ].
VAR_006940
Natural varianti357 – 3571P → L in MATD. 1 Publication
VAR_006941
Natural varianti378 – 3781G → S in MATD. 1 Publication
VAR_006942

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49357 mRNA. Translation: BAA08355.1.
X69078 mRNA. Translation: CAA48822.1.
AL359195 Genomic DNA. Translation: CAI13695.1.
CH471142 Genomic DNA. Translation: EAW80396.1.
CH471142 Genomic DNA. Translation: EAW80397.1.
BC018359 mRNA. Translation: AAH18359.1.
CCDSiCCDS7365.1.
PIRiS27363.
RefSeqiNP_000420.1. NM_000429.2.
XP_005269899.1. XM_005269842.3.
UniGeneiHs.282670.

Genome annotation databases

EnsembliENST00000372213; ENSP00000361287; ENSG00000151224.
GeneIDi4143.
KEGGihsa:4143.
UCSCiuc001kbw.3. human.

Polymorphism and mutation databases

BioMutaiMAT1A.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D49357 mRNA. Translation: BAA08355.1.
X69078 mRNA. Translation: CAA48822.1.
AL359195 Genomic DNA. Translation: CAI13695.1.
CH471142 Genomic DNA. Translation: EAW80396.1.
CH471142 Genomic DNA. Translation: EAW80397.1.
BC018359 mRNA. Translation: AAH18359.1.
CCDSiCCDS7365.1.
PIRiS27363.
RefSeqiNP_000420.1. NM_000429.2.
XP_005269899.1. XM_005269842.3.
UniGeneiHs.282670.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OBVX-ray2.05A16-395[»]
ProteinModelPortaliQ00266.
SMRiQ00266. Positions 14-395.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi110313. 7 interactions.
STRINGi9606.ENSP00000361287.

Chemistry

DrugBankiDB00134. L-Methionine.
DB00118. S-Adenosylmethionine.

PTM databases

PhosphoSiteiQ00266.

Polymorphism and mutation databases

BioMutaiMAT1A.
DMDMi417297.

Proteomic databases

MaxQBiQ00266.
PaxDbiQ00266.
PRIDEiQ00266.

Protocols and materials databases

DNASUi4143.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000372213; ENSP00000361287; ENSG00000151224.
GeneIDi4143.
KEGGihsa:4143.
UCSCiuc001kbw.3. human.

Organism-specific databases

CTDi4143.
GeneCardsiGC10M082021.
HGNCiHGNC:6903. MAT1A.
HPAiHPA048627.
MIMi250850. phenotype.
610550. gene.
neXtProtiNX_Q00266.
Orphaneti168598. Brain demyelination due to methionine adenosyltransferase deficiency.
PharmGKBiPA30646.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0192.
GeneTreeiENSGT00500000044811.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ00266.
KOiK00789.
OMAiSEFPWEI.
OrthoDBiEOG7TF79H.
PhylomeDBiQ00266.
TreeFamiTF300511.

Enzyme and pathway databases

UniPathwayiUPA00315; UER00080.
ReactomeiREACT_115639. Sulfur amino acid metabolism.
REACT_268063. Defective MAT1A causes Methionine adenosyltransferase deficiency (MATD).
REACT_6946. Methylation.

Miscellaneous databases

EvolutionaryTraceiQ00266.
GenomeRNAii4143.
NextBioi16272.
PROiQ00266.
SOURCEiSearch...

Gene expression databases

BgeeiQ00266.
CleanExiHS_MAT1A.
ExpressionAtlasiQ00266. baseline and differential.
GenevestigatoriQ00266.

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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a full-length cDNA encoding human liver S-adenosylmethionine synthetase: tissue-specific gene expression and mRNA levels in hepatopathies."
    Alvarez L., Corrales F., Mato J.M.
    Biochem. J. 293:481-486(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Molecular cloning and nucleotide sequence of cDNA encoding the human liver S-adenosylmethionine synthetase."
    Horikawa S., Tsukada K.
    Biochem. Int. 25:81-90(1991) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Liver.
  3. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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: Lymph.
  6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  7. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  8. "Crystal structure of the human s-adenosylmethionine synthetase 1 in complex with the product."
    Structural genomics consortium (SGC)
    Submitted (JUL-2007) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) OF 14-395 IN COMPLEX WITH SUBSTRATE.
  9. "Molecular mechanisms of an inborn error of methionine pathway. Methionine adenosyltransferase deficiency."
    Ubagai T., Lei K.-J., Huang S., Mudd S.H., Levy H.L., Chou J.Y.
    J. Clin. Invest. 96:1943-1947(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MATD ASP-55; PRO-305; MET-322 AND LEU-357.
  10. "Demyelination of the brain is associated with methionine adenosyltransferase I/III deficiency."
    Chamberlin M.E., Ubagai T., Mudd S.H., Wilson W.G., Leonard J.V., Chou J.Y.
    J. Clin. Invest. 98:1021-1027(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MATD CYS-199; GLN-356 AND SER-378.
  11. "Dominant inheritance of isolated hypermethioninemia is associated with a mutation in the human methionine adenosyltransferase 1A gene."
    Chamberlin M.E., Ubagai T., Mudd S.H., Levy H.L., Chou J.Y.
    Am. J. Hum. Genet. 60:540-546(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANT MATD HIS-264.
  12. "Methionine adenosyltransferase I/III deficiency: novel mutations and clinical variations."
    Chamberlin M.E., Ubagai T., Mudd S.H., Thomas J., Pao V.Y., Nguyen T.K., Levy H.L., Greene C., Freehauf C., Chou J.Y.
    Am. J. Hum. Genet. 66:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322; ARG-336 AND ALA-344, CHARACTERIZATION OF VARIANTS MATD ASN-38; CYS-264; HIS-264; MET-322; ARG-336 AND ALA-344.

Entry informationi

Entry nameiMETK1_HUMAN
AccessioniPrimary (citable) accession number: Q00266
Secondary accession number(s): D3DWD5, Q5QP09
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: October 1, 1993
Last modified: April 29, 2015
This is version 167 of the entry and version 2 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 10
    Human chromosome 10: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PATHWAY comments
    Index of metabolic and biosynthesis pathways
  6. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  7. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.