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P30711

- GSTT1_HUMAN

UniProt

P30711 - GSTT1_HUMAN

Protein

Glutathione S-transferase theta-1

Gene

GSTT1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 159 (01 Oct 2014)
      Sequence version 4 (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. Acts on 1,2-epoxy-3-(4-nitrophenoxy)propane, phenethylisothiocyanate 4-nitrobenzyl chloride and 4-nitrophenethyl bromide. Displays glutathione peroxidase activity with cumene hydroperoxide.2 Publications

    Catalytic activityi

    RX + glutathione = HX + R-S-glutathione.2 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei40 – 401Glutathione

    GO - Molecular functioni

    1. glutathione peroxidase activity Source: UniProtKB
    2. glutathione transferase activity Source: UniProtKB

    GO - Biological processi

    1. glutathione derivative biosynthetic process Source: Reactome
    2. glutathione metabolic process Source: UniProtKB
    3. oxidation-reduction process Source: GOC
    4. response to drug Source: Ensembl
    5. response to organic cyclic compound Source: Ensembl
    6. small molecule metabolic process Source: Reactome
    7. xenobiotic metabolic process Source: Reactome

    Keywords - Molecular functioni

    Transferase

    Enzyme and pathway databases

    ReactomeiREACT_6926. Glutathione conjugation.
    SABIO-RKP30711.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Glutathione S-transferase theta-1 (EC:2.5.1.18)
    Alternative name(s):
    GST class-theta-1
    Glutathione transferase T1-1
    Gene namesi
    Name:GSTT1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:4641. GSTT1.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: UniProtKB
    2. extracellular vesicular exosome Source: UniProt

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi176 – 1761H → Q: Increases activity towards alkylhalogenides, but not hydroperoxides. 1 Publication
    Mutagenesisi234 – 2341W → R: Facilitates binding of substrates and increases catalytic activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA183.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 240239Glutathione S-transferase theta-1PRO_0000185938Add
    BLAST

    Proteomic databases

    MaxQBiP30711.
    PaxDbiP30711.
    PRIDEiP30711.

    PTM databases

    PhosphoSiteiP30711.

    Expressioni

    Tissue specificityi

    Found in erythrocyte. Expressed at low levels in liver. In lung, expressed at low levels in Clara cells and ciliated cells at the alveolar/bronchiolar junction. Absent from epithelial cells of larger bronchioles.1 Publication

    Gene expression databases

    ArrayExpressiP30711.
    BgeeiP30711.
    CleanExiHS_GSTT1.
    GenevestigatoriP30711.

    Interactioni

    Subunit structurei

    Homodimer.1 Publication

    Protein-protein interaction databases

    BioGridi109207. 1 interaction.
    IntActiP30711. 1 interaction.
    STRINGi9606.ENSP00000248935.

    Structurei

    Secondary structure

    1
    240
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi3 – 75
    Helixi12 – 2312
    Beta strandi29 – 324
    Helixi35 – 373
    Helixi39 – 413
    Helixi43 – 486
    Beta strandi56 – 594
    Beta strandi62 – 654
    Helixi67 – 7711
    Helixi82 – 843
    Helixi89 – 10113
    Helixi102 – 1043
    Helixi106 – 11712
    Helixi118 – 1236
    Helixi130 – 15021
    Turni151 – 1544
    Beta strandi155 – 1628
    Helixi165 – 17915
    Helixi189 – 20214
    Helixi204 – 2107
    Helixi212 – 2154
    Helixi216 – 2194
    Helixi225 – 23915

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C3NX-ray1.50A/B/C/D2-240[»]
    2C3QX-ray1.85A/B/C/D2-240[»]
    2C3TX-ray2.40A/B/C/D2-240[»]
    ProteinModelPortaliP30711.
    SMRiP30711. Positions 2-240.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30711.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini2 – 8281GST N-terminalAdd
    BLAST
    Domaini88 – 220133GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni53 – 542Glutathione binding
    Regioni66 – 672Glutathione binding

    Sequence similaritiesi

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

    Phylogenomic databases

    eggNOGiCOG0625.
    HOGENOMiHOG000125747.
    HOVERGENiHBG051854.
    InParanoidiP30711.
    KOiK00799.
    OMAiTVKQKLM.
    PhylomeDBiP30711.
    TreeFamiTF325759.

    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.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view]
    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: P30711-1) [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

    MGLELYLDLL SQPCRAVYIF AKKNDIPFEL RIVDLIKGQH LSDAFAQVNP    50
    LKKVPALKDG DFTLTESVAI LLYLTRKYKV PDYWYPQDLQ ARARVDEYLA 100
    WQHTTLRRSC LRALWHKVMF PVFLGEPVSP QTLAATLAEL DVTLQLLEDK 150
    FLQNKAFLTG PHISLADLVA ITELMHPVGA GCQVFEGRPK LATWRQRVEA 200
    AVGEDLFQEA HEVILKAKDF PPADPTIKQK LMPWVLAMIR 240
    Length:240
    Mass (Da):27,335
    Last modified:January 23, 2007 - v4
    Checksum:iBD19F2BFDEF9F619
    GO
    Isoform 2 (identifier: P30711-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-118: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:122
    Mass (Da):13,517
    Checksum:i13F6A21E9D214D56
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti43 – 442DA → SD AA sequence (PubMed:1848757)Curated
    Sequence conflicti45 – 451F → C in AAH07065. (PubMed:15489334)Curated
    Sequence conflicti126 – 1261E → G in CAA55935. (PubMed:8198545)Curated

    Polymorphismi

    The GSTT1 gene is absent from 38% of the population. The presence or absence of the GSTT1 gene is coincident with the conjugator (GSST1+) and non-conjugator (GSTT1-) phenotypes respectively. The GSTT1+ phenotype can catalyze the glutathione conjugation of dichloromethane.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti21 – 211A → T.
    Corresponds to variant rs2266635 [ dbSNP | Ensembl ].
    VAR_014501
    Natural varianti141 – 1411D → N.
    Corresponds to variant rs2266633 [ dbSNP | Ensembl ].
    VAR_014502
    Natural varianti169 – 1691V → I.1 Publication
    Corresponds to variant rs2266637 [ dbSNP | Ensembl ].
    VAR_014503
    Natural varianti173 – 1731E → K.
    Corresponds to variant rs2234953 [ dbSNP | Ensembl ].
    VAR_014504

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 118118Missing in isoform 2. 1 PublicationVSP_056474Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X79389 mRNA. Translation: CAA55935.1.
    AF435971 mRNA. Translation: AAL31549.1.
    AF240786 Genomic DNA. Translation: AAG02374.1.
    AB057594 Genomic DNA. Translation: BAB39498.1.
    CR456499 mRNA. Translation: CAG30385.1.
    BT019951 mRNA. Translation: AAV38754.1.
    AP000351 Genomic DNA. No translation available.
    Z84718 Genomic DNA. No translation available.
    BC007065 mRNA. Translation: AAH07065.1.
    CCDSiCCDS13822.1.
    PIRiS44358.
    RefSeqiNP_000844.2. NM_000853.2.
    XP_005261645.1. XM_005261588.1.
    UniGeneiHs.268573.
    Hs.738514.

    Genome annotation databases

    EnsembliENST00000439996; ENSP00000401632; ENSG00000184674.
    GeneIDi2952.
    KEGGihsa:2952.
    UCSCiuc002zze.4. human.

    Polymorphism databases

    DMDMi21264427.

    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
    X79389 mRNA. Translation: CAA55935.1 .
    AF435971 mRNA. Translation: AAL31549.1 .
    AF240786 Genomic DNA. Translation: AAG02374.1 .
    AB057594 Genomic DNA. Translation: BAB39498.1 .
    CR456499 mRNA. Translation: CAG30385.1 .
    BT019951 mRNA. Translation: AAV38754.1 .
    AP000351 Genomic DNA. No translation available.
    Z84718 Genomic DNA. No translation available.
    BC007065 mRNA. Translation: AAH07065.1 .
    CCDSi CCDS13822.1.
    PIRi S44358.
    RefSeqi NP_000844.2. NM_000853.2.
    XP_005261645.1. XM_005261588.1.
    UniGenei Hs.268573.
    Hs.738514.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C3N X-ray 1.50 A/B/C/D 2-240 [» ]
    2C3Q X-ray 1.85 A/B/C/D 2-240 [» ]
    2C3T X-ray 2.40 A/B/C/D 2-240 [» ]
    ProteinModelPortali P30711.
    SMRi P30711. Positions 2-240.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 109207. 1 interaction.
    IntActi P30711. 1 interaction.
    STRINGi 9606.ENSP00000248935.

    Chemistry

    ChEMBLi CHEMBL2141.
    DrugBanki DB00143. Glutathione.

    PTM databases

    PhosphoSitei P30711.

    Polymorphism databases

    DMDMi 21264427.

    Proteomic databases

    MaxQBi P30711.
    PaxDbi P30711.
    PRIDEi P30711.

    Protocols and materials databases

    DNASUi 2952.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000439996 ; ENSP00000401632 ; ENSG00000184674 .
    GeneIDi 2952.
    KEGGi hsa:2952.
    UCSCi uc002zze.4. human.

    Organism-specific databases

    CTDi 2952.
    GeneCardsi GC22M024952.
    H-InvDB HIX0019638.
    HGNCi HGNC:4641. GSTT1.
    MIMi 600436. gene.
    neXtProti NX_P30711.
    PharmGKBi PA183.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0625.
    HOGENOMi HOG000125747.
    HOVERGENi HBG051854.
    InParanoidi P30711.
    KOi K00799.
    OMAi TVKQKLM.
    PhylomeDBi P30711.
    TreeFami TF325759.

    Enzyme and pathway databases

    Reactomei REACT_6926. Glutathione conjugation.
    SABIO-RK P30711.

    Miscellaneous databases

    EvolutionaryTracei P30711.
    GeneWikii GSTT1.
    GenomeRNAii 2952.
    NextBioi 11698.
    PROi P30711.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30711.
    Bgeei P30711.
    CleanExi HS_GSTT1.
    Genevestigatori P30711.

    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.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF00043. GST_C. 1 hit.
    PF02798. GST_N. 1 hit.
    [Graphical view ]
    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. "Human glutathione S-transferase theta (GSTT1): cDNA cloning and the characterization of a genetic polymorphism."
      Pemble S., Schroeder K.R., Spencer S.R., Meyer D.J., Hallier E., Bolt H.M., Ketterer B., Taylor J.B.
      Biochem. J. 300:271-276(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    2. "Kinetic characterization of recombinant human glutathione transferase T1-1, a polymorphic detoxication enzyme."
      Jemth P., Mannervik B.
      Arch. Biochem. Biophys. 348:247-254(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), CHARACTERIZATION.
    3. "Characterization of the glutathione S-transferase GSTT1 deletion: discrimination of all genotypes by polymerase chain reaction indicates a trimodular genotype-phenotype correlation."
      Sprenger R., Schlagenhaufer R., Kerb R., Bruhn C., Brockmoeller J., Roots I., Brinkmann U.
      Pharmacogenetics 10:557-565(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    4. "Complete genomic structure of human glutathione S-transferase TT1."
      Iida A., Kondo K., Kitamura Y., Mishima C., Osawa S., Kitamoto T., Harigae C., Nakamura Y.
      Submitted (MAR-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
      Tissue: Thymus.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    6. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
      Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
      Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT ILE-169.
    7. "The DNA sequence of human chromosome 22."
      Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
      , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
      Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    8. "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 1).
      Tissue: Urinary bladder.
    9. "Theta, a new class of glutathione transferases purified from rat and man."
      Meyer D.J., Coles B., Pemble S.E., Gilmore K.S., Fraser G.M., Ketterer B.
      Biochem. J. 274:409-414(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 2-47.
      Tissue: Liver.
    10. "The distribution of theta-class glutathione S-transferases in the liver and lung of mouse, rat and human."
      Mainwaring G.W., Williams S.M., Foster J.R., Tugwood J., Green T.
      Biochem. J. 318:297-303(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
      Tissue: Liver and Lung.
    11. "Residue 234 is a master switch of the alternative-substrate activity profile of human and rodent theta class glutathione transferase T1-1."
      Shokeer A., Mannervik B.
      Biochim. Biophys. Acta 1800:466-473(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. "Structural basis of the suppressed catalytic activity of wild-type human glutathione transferase T1-1 compared to its W234R mutant."
      Tars K., Larsson A.K., Shokeer A., Olin B., Mannervik B., Kleywegt G.J.
      J. Mol. Biol. 355:96-105(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.5 ANGSTROMS) OF WILD-TYPE AND MUTANT ARG-234 IN COMPLEX WITH HEXYLGLUTATHIONE, CATALYTIC ACTIVITY, FUNCTION, SUBUNIT, MUTAGENESIS OF HIS-176 AND TRP-234.

    Entry informationi

    Entry nameiGSTT1_HUMAN
    AccessioniPrimary (citable) accession number: P30711
    Secondary accession number(s): O00226
    , Q5TZY2, Q6IC69, Q969K8, Q96IY3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 159 of the entry and version 4 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 22
      Human chromosome 22: 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