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P09488

- GSTM1_HUMAN

UniProt

P09488 - GSTM1_HUMAN

Protein

Glutathione S-transferase Mu 1

Gene

GSTM1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 3 (23 Jan 2007)
      Previous versions | rss
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    Functioni

    Conjugation of reduced glutathione to a wide number of exogenous and endogenous hydrophobic electrophiles.1 Publication

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.1 Publication

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei116 – 1161Substrate

    GO - Molecular functioni

    1. enzyme binding Source: BHF-UCL
    2. glutathione binding Source: BHF-UCL
    3. glutathione transferase activity Source: BHF-UCL
    4. protein homodimerization activity Source: BHF-UCL

    GO - Biological processi

    1. cellular detoxification of nitrogen compound Source: BHF-UCL
    2. glutathione derivative biosynthetic process Source: Reactome
    3. glutathione metabolic process Source: BHF-UCL
    4. nitrobenzene metabolic process Source: BHF-UCL
    5. small molecule metabolic process Source: Reactome
    6. xenobiotic catabolic process Source: BHF-UCL
    7. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_6926. Glutathione conjugation.
    SABIO-RKP09488.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase Mu 1 (EC:2.5.1.18)
    Alternative name(s):
    GST HB subunit 4
    GST class-mu 1
    GSTM1-1
    GSTM1a-1a
    GSTM1b-1b
    GTH4
    Gene namesi
    Name:GSTM1
    Synonyms:GST1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:4632. GSTM1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: BHF-UCL
    2. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi7 – 71Y → F: Reduces catalytic activity 100-fold. 1 Publication
    Mutagenesisi108 – 1081H → Q: Reduces catalytic activity by half. 2 Publications
    Mutagenesisi108 – 1081H → S: Changes the properties of the enzyme toward some substrates. 2 Publications
    Mutagenesisi109 – 1091M → I: Reduces catalytic activity by half. 1 Publication
    Mutagenesisi116 – 1161Y → A: Reduces catalytic activity 10-fold. 1 Publication
    Mutagenesisi116 – 1161Y → F: Slight increase of catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA182.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed6 Publications
    Chaini2 – 218217Glutathione S-transferase Mu 1PRO_0000185816Add
    BLAST

    Proteomic databases

    MaxQBiP09488.
    PaxDbiP09488.
    PRIDEiP09488.

    PTM databases

    PhosphoSiteiP09488.

    Expressioni

    Tissue specificityi

    Liver (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiP09488.
    BgeeiP09488.
    CleanExiHS_GSTM1.
    GenevestigatoriP09488.

    Organism-specific databases

    HPAiCAB022669.
    CAB047357.

    Interactioni

    Subunit structurei

    Homodimer.

    Protein-protein interaction databases

    BioGridi109199. 4 interactions.
    IntActiP09488. 6 interactions.
    STRINGi9606.ENSP00000311469.

    Structurei

    Secondary structure

    1
    218
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 119
    Helixi12 – 143
    Helixi15 – 239
    Beta strandi28 – 336
    Turni38 – 414
    Helixi44 – 507
    Beta strandi60 – 656
    Beta strandi68 – 725
    Helixi73 – 8311
    Helixi91 – 11525
    Helixi120 – 14223
    Beta strandi146 – 1527
    Helixi156 – 17015
    Turni172 – 1776
    Helixi179 – 18911
    Helixi192 – 1987
    Beta strandi200 – 2023
    Beta strandi214 – 2163

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1GTUX-ray2.68A/B/C/D2-218[»]
    1XW6X-ray1.90A/B/C/D1-218[»]
    1XWKX-ray2.30A/B/C1-218[»]
    1YJ6X-ray2.50A/B/C1-218[»]
    2F3MX-ray2.70A/B/C/D/E/F1-218[»]
    ProteinModelPortaliP09488.
    SMRiP09488. Positions 2-218.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP09488.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8887GST N-terminalAdd
    BLAST
    Domaini90 – 208119GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni7 – 82Glutathione binding
    Regioni46 – 505Glutathione binding
    Regioni59 – 602Glutathione binding
    Regioni72 – 732Glutathione binding

    Sequence similaritiesi

    Belongs to the GST superfamily. Mu family.Curated
    Contains 1 GST C-terminal domain.Curated
    Contains 1 GST N-terminal domain.Curated

    Phylogenomic databases

    eggNOGiNOG300089.
    HOGENOMiHOG000115735.
    HOVERGENiHBG106842.
    KOiK00799.
    PhylomeDBiP09488.
    TreeFamiTF353040.

    Family and domain databases

    Gene3Di1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProiIPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR003081. GST_mu.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    PRINTSiPR01267. GSTRNSFRASEM.
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    Sequence processingi: The displayed sequence is further processed into a mature form.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P09488-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MPMILGYWDI RGLAHAIRLL LEYTDSSYEE KKYTMGDAPD YDRSQWLNEK    50
    FKLGLDFPNL PYLIDGAHKI TQSNAILCYI ARKHNLCGET EEEKIRVDIL 100
    ENQTMDNHMQ LGMICYNPEF EKLKPKYLEE LPEKLKLYSE FLGKRPWFAG 150
    NKITFVDFLV YDVLDLHRIF EPKCLDAFPN LKDFISRFEG LEKISAYMKS 200
    SRFLPRPVFS KMAVWGNK 218
    Length:218
    Mass (Da):25,712
    Last modified:January 23, 2007 - v3
    Checksum:i98FB03E87B83A31B
    GO
    Isoform 2 (identifier: P09488-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         153-189: Missing.

    Show »
    Length:181
    Mass (Da):21,253
    Checksum:i1FB16A0418115A26
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti44 – 441S → T in CAA48636. (PubMed:8471052)Curated
    Sequence conflicti207 – 2071P → T in AAT06767. 1 PublicationCurated

    Polymorphismi

    There are two alleles; GSTM1A and GSTM1B which differ in position 173.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti173 – 1731K → N in allele GSTM1B. 2 Publications
    Corresponds to variant rs1065411 [ dbSNP | Ensembl ].
    VAR_003617
    Natural varianti210 – 2101S → T.
    Corresponds to variant rs449856 [ dbSNP | Ensembl ].
    VAR_014497

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei153 – 18937Missing in isoform 2. 2 PublicationsVSP_036618Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X08020 mRNA. Translation: CAA30821.1.
    J03817 mRNA. Translation: AAA59203.1.
    AY510272 mRNA. Translation: AAR85979.1.
    AY532926 mRNA. Translation: AAT06767.1.
    AY532927 mRNA. Translation: AAT06768.1.
    CR541868 mRNA. Translation: CAG46666.1.
    BC024005 mRNA. Translation: AAH24005.1.
    X68676 Genomic DNA. Translation: CAA48636.1.
    X51451 Genomic DNA. Translation: CAA35817.1.
    CCDSiCCDS809.1. [P09488-1]
    CCDS810.1. [P09488-2]
    PIRiS01719.
    RefSeqiNP_000552.2. NM_000561.3. [P09488-1]
    NP_666533.1. NM_146421.2. [P09488-2]
    UniGeneiHs.301961.

    Genome annotation databases

    EnsembliENST00000309851; ENSP00000311469; ENSG00000134184. [P09488-1]
    ENST00000349334; ENSP00000234981; ENSG00000134184. [P09488-2]
    GeneIDi2944.
    KEGGihsa:2944.
    UCSCiuc001dyk.3. human. [P09488-1]
    uc001dyl.3. human. [P09488-2]

    Polymorphism databases

    DMDMi121735.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    SHMPD

    The Singapore human mutation and polymorphism database

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X08020 mRNA. Translation: CAA30821.1 .
    J03817 mRNA. Translation: AAA59203.1 .
    AY510272 mRNA. Translation: AAR85979.1 .
    AY532926 mRNA. Translation: AAT06767.1 .
    AY532927 mRNA. Translation: AAT06768.1 .
    CR541868 mRNA. Translation: CAG46666.1 .
    BC024005 mRNA. Translation: AAH24005.1 .
    X68676 Genomic DNA. Translation: CAA48636.1 .
    X51451 Genomic DNA. Translation: CAA35817.1 .
    CCDSi CCDS809.1. [P09488-1 ]
    CCDS810.1. [P09488-2 ]
    PIRi S01719.
    RefSeqi NP_000552.2. NM_000561.3. [P09488-1 ]
    NP_666533.1. NM_146421.2. [P09488-2 ]
    UniGenei Hs.301961.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1GTU X-ray 2.68 A/B/C/D 2-218 [» ]
    1XW6 X-ray 1.90 A/B/C/D 1-218 [» ]
    1XWK X-ray 2.30 A/B/C 1-218 [» ]
    1YJ6 X-ray 2.50 A/B/C 1-218 [» ]
    2F3M X-ray 2.70 A/B/C/D/E/F 1-218 [» ]
    ProteinModelPortali P09488.
    SMRi P09488. Positions 2-218.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109199. 4 interactions.
    IntActi P09488. 6 interactions.
    STRINGi 9606.ENSP00000311469.

    Chemistry

    BindingDBi P09488.
    ChEMBLi CHEMBL2081.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P09488.

    Polymorphism databases

    DMDMi 121735.

    Proteomic databases

    MaxQBi P09488.
    PaxDbi P09488.
    PRIDEi P09488.

    Protocols and materials databases

    DNASUi 2944.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000309851 ; ENSP00000311469 ; ENSG00000134184 . [P09488-1 ]
    ENST00000349334 ; ENSP00000234981 ; ENSG00000134184 . [P09488-2 ]
    GeneIDi 2944.
    KEGGi hsa:2944.
    UCSCi uc001dyk.3. human. [P09488-1 ]
    uc001dyl.3. human. [P09488-2 ]

    Organism-specific databases

    CTDi 2944.
    GeneCardsi GC01P110232.
    HGNCi HGNC:4632. GSTM1.
    HPAi CAB022669.
    CAB047357.
    MIMi 138350. gene.
    neXtProti NX_P09488.
    PharmGKBi PA182.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300089.
    HOGENOMi HOG000115735.
    HOVERGENi HBG106842.
    KOi K00799.
    PhylomeDBi P09488.
    TreeFami TF353040.

    Enzyme and pathway databases

    Reactomei REACT_6926. Glutathione conjugation.
    SABIO-RK P09488.

    Miscellaneous databases

    ChiTaRSi GSTM1. human.
    EvolutionaryTracei P09488.
    GeneWikii Glutathione_S-transferase_Mu_1.
    GenomeRNAii 2944.
    NextBioi 11663.
    PROi P09488.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P09488.
    Bgeei P09488.
    CleanExi HS_GSTM1.
    Genevestigatori P09488.

    Family and domain databases

    Gene3Di 1.20.1050.10. 1 hit.
    3.40.30.10. 1 hit.
    InterProi IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR003081. GST_mu.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01267. GSTRNSFRASEM.
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS50405. GST_CTER. 1 hit.
    PS50404. GST_NTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The human liver glutathione S-transferase gene superfamily: expression and chromosome mapping of an Hb subunit cDNA."
      Dejong J.L., Chang C.M., Whang Peng J., Knutsen T., Tu C.-P.D.
      Nucleic Acids Res. 16:8541-8554(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Hereditary differences in the expression of the human glutathione transferase active on trans-stilbene oxide are due to a gene deletion."
      Seidegaard J., Vorachek W.R., Pero R.W., Pearson W.R.
      Proc. Natl. Acad. Sci. U.S.A. 85:7293-7297(1988) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. Chen P., Wu Y., Zhang C., Han L., Wu Y., Xie D., Chen L.
      Submitted (DEC-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ASN-173.
      Tissue: Liver.
    4. Chen P., Zhang C., Xie D., Wu Y., Han L., Chen L.
      Submitted (JAN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
      Tissue: Liver.
    5. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S., Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W., Korn B., Zuo D., Hu Y., LaBaer J.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ASN-173.
    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] (ISOFORM 2).
      Tissue: Testis.
    7. "Deduced amino acid sequence, gene structure and chromosomal location of a novel human class Mu glutathione S-transferase, GSTM4."
      Zhong S., Spurr N.K., Hayes J.D., Wolf C.R.
      Biochem. J. 291:41-50(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189 (ISOFORM 1).
    8. "Immunochemical evidence for the occurrence of Mu class glutathione S-transferase in human fetal livers."
      Mera N., Ohmori S., Itahashi K., Kiuchi M., Igarashi T., Rikihisa T., Kitada M.
      J. Biochem. 116:315-320(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-31, TISSUE SPECIFICITY.
      Tissue: Fetal liver.
    9. "Purification and characterization of glutathione transferases with an activity toward nitroglycerin from human aorta and heart. Multiplicity of the human class Mu forms."
      Tsuchida S., Maki T., Sato K.
      J. Biol. Chem. 265:7150-7157(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-25.
      Tissue: Aorta and Heart.
    10. "Structural evidence for three different types of glutathione transferase in human tissues."
      Alin P., Mannervik B., Joernvall H.
      FEBS Lett. 182:319-322(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-24.
    11. "Identification of three classes of cytosolic glutathione transferase common to several mammalian species: correlation between structural data and enzymatic properties."
      Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Joernvall H.
      Proc. Natl. Acad. Sci. U.S.A. 82:7202-7206(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-24.
    12. "Purification and characterization of human muscle glutathione S-transferases: evidence that glutathione S-transferase zeta corresponds to a locus distinct from GST1, GST2, and GST3."
      Singhal S.S., Ahmad H., Sharma R., Gupta S., Haque A.K., Awasthi Y.C.
      Arch. Biochem. Biophys. 285:64-73(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-15.
    13. "Gender related differences in the expression and characteristics of glutathione S-transferases of human colon."
      Singhal S.S., Saxena M., Awasthi S., Ahmad H., Sharma R., Awasthi Y.C.
      Biochim. Biophys. Acta 1171:19-26(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-13.
      Tissue: Colon.
    14. "Human ERp29: isolation, primary structural characterisation and two-dimensional gel mapping."
      Hubbard M.J., McHugh N.J.
      Electrophoresis 21:3785-3796(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 53-60, IDENTIFICATION BY MASS SPECTROMETRY.
      Tissue: Liver.
    15. "GST1 gene deletion determined by polymerase chain reaction."
      Comstock K.E., Sanderson B.J.S., Claflin G., Henner W.D.
      Nucleic Acids Res. 18:3670-3670(1990) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 60-118.
    16. "Identification of class-mu glutathione transferase genes GSTM1-GSTM5 on human chromosome 1p13."
      Pearson W.R., Vorachek W.R., Xu S.J., Berger R., Hart I., Vannais D., Patterson D.
      Am. J. Hum. Genet. 53:220-233(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 125-186.
    17. "Functions of His107 in the catalytic mechanism of human glutathione S-transferase hGSTM1a-1a."
      Patskovsky Y.V., Patskovska L.N., Listowsky I.
      Biochemistry 38:1193-1202(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.68 ANGSTROMS), MUTAGENESIS OF HIS-108.
    18. "Transition state model and mechanism of nucleophilic aromatic substitution reactions catalyzed by human glutathione S-transferase M1a-1a."
      Patskovsky Y., Patskovska L., Almo S.C., Listowsky I.
      Biochemistry 45:3852-3862(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) IN COMPLEXES WITH GLUTAHIONE ANALOGS, CATALYTIC ACTIVITY, FUNCTION, MUTAGENESIS OF TYR-7; HIS-108; MET-109 AND TYR-116.

    Entry informationi

    Entry nameiGSTM1_HUMAN
    AccessioniPrimary (citable) accession number: P09488
    Secondary accession number(s): Q5GHG0
    , Q6FH88, Q8TC98, Q9UC96
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 1, 1989
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 164 of the entry and version 3 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3