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Q00266

- METK1_HUMAN

UniProt

Q00266 - METK1_HUMAN

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Protein
S-adenosylmethionine synthase isoform type-1
Gene
MAT1A, AMS1, MATA1
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
Binding sitei29 – 291Substrate
Metal bindingi31 – 311Magnesium By similarity
Metal bindingi57 – 571Potassium By similarity
Binding sitei159 – 1591ATP Reviewed prediction
Binding sitei179 – 1791Substrate
Binding sitei247 – 2471Substrate
Binding sitei249 – 2491Substrate; via carbonyl oxygen
Binding sitei258 – 2581Substrate
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: ProtInc

GO - Biological processi

  1. S-adenosylmethionine biosynthetic process Source: UniProtKB-UniPathway
  2. cellular amino acid metabolic process Source: ProtInc
  3. cellular nitrogen compound metabolic process Source: Reactome
  4. methylation Source: Reactome
  5. one-carbon metabolic process Source: UniProtKB-KW
  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_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: 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) [MIM:250850]: An 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.4 Publications
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.

PTM / Processingi

Molecule processing

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

Amino acid modifications

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

Post-translational modificationi

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

Keywords - PTMi

Disulfide bond, S-nitrosylation

Proteomic databases

MaxQBiQ00266.
PaxDbiQ00266.
PRIDEiQ00266.

PTM databases

PhosphoSiteiQ00266.

Expressioni

Tissue specificityi

Expressed in liver.

Gene expression databases

ArrayExpressiQ00266.
BgeeiQ00266.
CleanExiHS_MAT1A.
GenevestigatoriQ00266.

Organism-specific databases

HPAiHPA048627.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi110313. 4 interactions.
STRINGi9606.ENSP00000361287.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2OBVX-ray2.05A16-395[»]
ProteinModelPortaliQ00266.
SMRiQ00266. Positions 14-395.

Miscellaneous databases

EvolutionaryTraceiQ00266.

Family & Domainsi

Sequence similaritiesi

Belongs to the AdoMet synthase family.

Phylogenomic databases

eggNOGiCOG0192.
HOGENOMiHOG000245710.
HOVERGENiHBG001562.
InParanoidiQ00266.
KOiK00789.
OMAiHEAVREQ.
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

MNGPVDGLCD HSLSEGVFMF TSESVGEGHP DKICDQISDA VLDAHLKQDP    50
NAKVACETVC KTGMVLLCGE ITSMAMVDYQ RVVRDTIKHI GYDDSAKGFD 100
FKTCNVLVAL EQQSPDIAQC VHLDRNEEDV GAGDQGLMFG YATDETEECM 150
PLTIILAHKL NARMADLRRS GLLPWLRPDS KTQVTVQYMQ DNGAVIPVRI 200
HTIVISVQHN EDITLEEMRR ALKEQVIRAV VPAKYLDEDT VYHLQPSGRF 250
VIGGPQGDAG VTGRKIIVDT YGGWGAHGGG AFSGKDYTKV DRSAAYAARW 300
VAKSLVKAGL CRRVLVQVSY AIGVAEPLSI SIFTYGTSQK TERELLDVVH 350
KNFDLRPGVI VRDLDLKKPI YQKTACYGHF GRSEFPWEVP RKLVF 395
Length:395
Mass (Da):43,648
Last modified:October 1, 1993 - v2
Checksum:iB3462A5670A5B0D4
GO

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 conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti272 – 2732GG → AA in BAA08355. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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_005269842.2.
UniGeneiHs.282670.

Genome annotation databases

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

Polymorphism databases

DMDMi417297.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS7365.1.
PIRi S27363.
RefSeqi NP_000420.1. NM_000429.2.
XP_005269899.1. XM_005269842.2.
UniGenei Hs.282670.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2OBV X-ray 2.05 A 16-395 [» ]
ProteinModelPortali Q00266.
SMRi Q00266. Positions 14-395.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110313. 4 interactions.
STRINGi 9606.ENSP00000361287.

Chemistry

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

PTM databases

PhosphoSitei Q00266.

Polymorphism databases

DMDMi 417297.

Proteomic databases

MaxQBi Q00266.
PaxDbi Q00266.
PRIDEi Q00266.

Protocols and materials databases

DNASUi 4143.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000372213 ; ENSP00000361287 ; ENSG00000151224 .
GeneIDi 4143.
KEGGi hsa:4143.
UCSCi uc001kbw.3. human.

Organism-specific databases

CTDi 4143.
GeneCardsi GC10M082021.
HGNCi HGNC:6903. MAT1A.
HPAi HPA048627.
MIMi 250850. phenotype.
610550. gene.
neXtProti NX_Q00266.
Orphaneti 168598. Brain demyelination due to methionine adenosyltransferase deficiency.
PharmGKBi PA30646.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0192.
HOGENOMi HOG000245710.
HOVERGENi HBG001562.
InParanoidi Q00266.
KOi K00789.
OMAi HEAVREQ.
OrthoDBi EOG7TF79H.
PhylomeDBi Q00266.
TreeFami TF300511.

Enzyme and pathway databases

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

Miscellaneous databases

EvolutionaryTracei Q00266.
GenomeRNAii 4143.
NextBioi 16272.
PROi Q00266.
SOURCEi Search...

Gene expression databases

ArrayExpressi Q00266.
Bgeei Q00266.
CleanExi HS_MAT1A.
Genevestigatori Q00266.

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. "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. "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.
  8. "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.
  9. "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.
  10. "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.
  11. "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: September 3, 2014
This is version 159 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

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