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Q9H7Z7

- PGES2_HUMAN

UniProt

Q9H7Z7 - PGES2_HUMAN

Protein

Prostaglandin E synthase 2

Gene

PTGES2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 125 (01 Oct 2014)
      Sequence version 1 (01 Mar 2001)
      Previous versions | rss
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    Functioni

    Dual function enzyme which exhibits both isomerase and lyase activities. Its catalytic activity is altered by the presence or absence of the cofactors glutathione (GSH) and heme. The GSH-heme complex-bound enzyme (mPGES-2h) acts as a lyase and catalyzes the degradation of prostaglandin E2 H2 (PGH2) to 12(S)-hydroxy-5(Z),8(E),10(E)-heptadecatrienoic acid (HHT) and malondialdehyde (MDA) while the GSH-heme complex-free enzyme (mPGES-2) acts as an isomerase and catalyzes the isomerization of PGH2 into the more stable prostaglandin E2 (PGE2) form By similarity.By similarity

    Catalytic activityi

    (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = (5Z,13E)-(15S)-11-alpha,15-dihydroxy-9-oxoprosta-5,13-dienoate.
    (5Z,13E)-(15S)-9-alpha,11-alpha-epidioxy-15-hydroxyprosta-5,13-dienoate = malonaldehyde + (5Z,8E,10E)-(12S)-hydroxyheptadeca-5,8,10-trienoate.

    Cofactori

    Dihydrolipoic acid; required for isomerase activity.1 Publication
    Glutathione (GSH). Required for lyase activity By similarity.By similarity
    Heme. Required for lyase activity By similarity.By similarity

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei87 – 882CleavageBy similarity
    Binding sitei148 – 1481Glutathione; via amide nitrogen and carbonyl oxygenBy similarity

    GO - Molecular functioni

    1. DNA binding Source: Ensembl
    2. electron carrier activity Source: InterPro
    3. glutathione binding Source: UniProtKB
    4. heme binding Source: UniProtKB
    5. lyase activity Source: UniProtKB
    6. prostaglandin-E synthase activity Source: UniProtKB-EC
    7. protein disulfide oxidoreductase activity Source: InterPro

    GO - Biological processi

    1. cell redox homeostasis Source: InterPro
    2. positive regulation of transcription, DNA-templated Source: Ensembl
    3. prostaglandin biosynthetic process Source: UniProtKB-UniPathway
    4. secretion Source: Ensembl

    Keywords - Molecular functioni

    Isomerase, Lyase

    Keywords - Biological processi

    Fatty acid biosynthesis, Fatty acid metabolism, Lipid biosynthesis, Lipid metabolism, Prostaglandin biosynthesis, Prostaglandin metabolism

    Enzyme and pathway databases

    BioCyciMetaCyc:HS07514-MONOMER.
    BRENDAi5.3.99.3. 2681.
    UniPathwayiUPA00662.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Prostaglandin E synthase 2 (EC:4.1.2.-, EC:5.3.99.3)
    Alternative name(s):
    Microsomal prostaglandin E synthase 2
    Short name:
    mPGES-2
    Cleaved into the following chain:
    Gene namesi
    Name:PTGES2
    Synonyms:C9orf15, PGES2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 9

    Organism-specific databases

    HGNCiHGNC:17822. PTGES2.

    Subcellular locationi

    Golgi apparatus membrane 1 Publication; Single-pass membrane protein 1 Publication
    Chain Prostaglandin E synthase 2 truncated form : Cytoplasmperinuclear region
    Note: Synthesized as a Golgi membrane-bound protein, which is further cleaved into the predominant soluble truncated form. The truncated form is cytoplasmic and is enriched in the perinuclear region.

    GO - Cellular componenti

    1. cytosol Source: Ensembl
    2. Golgi membrane Source: UniProtKB-SubCell
    3. integral component of membrane Source: UniProtKB-KW
    4. mitochondrion Source: LIFEdb
    5. nucleus Source: Ensembl
    6. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi110 – 1101C → S: Loss of function. 1 Publication
    Mutagenesisi113 – 1131C → S: Does not strongly affect enzyme activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA33949.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 377377Prostaglandin E synthase 2PRO_0000013127Add
    BLAST
    Chaini88 – 377290Prostaglandin E synthase 2 truncated formBy similarityPRO_0000013128Add
    BLAST

    Proteomic databases

    MaxQBiQ9H7Z7.
    PaxDbiQ9H7Z7.
    PRIDEiQ9H7Z7.

    PTM databases

    PhosphoSiteiQ9H7Z7.

    Expressioni

    Tissue specificityi

    Widely expressed. Expressed in the heart, including apex, inter-ventricular septum, both atria and ventricles, but not in the aorta. Also expressed in fetal heart. Detected in various regions of the brain: cerebellum; occipital, frontal and parietal lobes. Also expressed in the lymph nodes, skeletal muscle, kidney and trachea, but not in the thymus or lung. Overexpressed in colorectal cancer.1 Publication

    Gene expression databases

    ArrayExpressiQ9H7Z7.
    BgeeiQ9H7Z7.
    CleanExiHS_PTGES2.
    GenevestigatoriQ9H7Z7.

    Organism-specific databases

    HPAiHPA020631.

    Interactioni

    Subunit structurei

    Homodimer. May interact with CEBPB By similarity. Interacts with EXOSC10.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi123135. 7 interactions.
    IntActiQ9H7Z7. 6 interactions.
    STRINGi9606.ENSP00000345341.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9H7Z7.
    SMRiQ9H7Z7. Positions 100-373.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini1 – 5757LumenalSequence AnalysisAdd
    BLAST
    Topological domaini75 – 377303CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei58 – 7417HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini90 – 193104GlutaredoxinPROSITE-ProRule annotationAdd
    BLAST
    Domaini263 – 377115GST C-terminalAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni164 – 1652Glutathione bindingBy similarity

    Sequence similaritiesi

    Belongs to the GST superfamily.Curated
    Contains 1 glutaredoxin domain.PROSITE-ProRule annotation
    Contains 1 GST C-terminal domain.Curated

    Keywords - Domaini

    Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG316980.
    HOGENOMiHOG000231901.
    HOVERGENiHBG069136.
    InParanoidiQ9H7Z7.
    KOiK05309.
    OMAiAMYFISK.
    OrthoDBiEOG7060R5.
    PhylomeDBiQ9H7Z7.
    TreeFamiTF314304.

    Family and domain databases

    Gene3Di1.20.1050.10. 2 hits.
    3.40.30.10. 1 hit.
    InterProiIPR002109. Glutaredoxin.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view]
    PfamiPF14497. GST_C_3. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view]
    SUPFAMiSSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEiPS00195. GLUTAREDOXIN_1. 1 hit.
    PS51354. GLUTAREDOXIN_2. 1 hit.
    PS50405. GST_CTER. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9H7Z7-1 [UniParc]FASTAAdd to Basket

    « Hide

    MDPAARVVRA LWPGGCALAW RLGGRPQPLL PTQSRAGFAG AAGGPSPVAA    50
    ARKGSPRLLG AAALALGGAL GLYHTARWHL RAQDLHAERS AAQLSLSSRL 100
    QLTLYQYKTC PFCSKVRAFL DFHALPYQVV EVNPVRRAEI KFSSYRKVPI 150
    LVAQEGESSQ QLNDSSVIIS ALKTYLVSGQ PLEEIITYYP AMKAVNEQGK 200
    EVTEFGNKYW LMLNEKEAQQ VYGGKEARTE EMKWRQWADD WLVHLISPNV 250
    YRTPTEALAS FDYIVREGKF GAVEGAVAKY MGAAAMYLIS KRLKSRHRLQ 300
    DNVREDLYEA ADKWVAAVGK DRPFMGGQKP NLADLAVYGV LRVMEGLDAF 350
    DDLMQHTHIQ PWYLRVERAI TEASPAH 377
    Length:377
    Mass (Da):41,943
    Last modified:March 1, 2001 - v1
    Checksum:i82F2DF867BB8337C
    GO

    Sequence cautioni

    The sequence CAI13822.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti319 – 3191G → S in BAD97240. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti298 – 2981R → H.
    Corresponds to variant rs13283456 [ dbSNP | Ensembl ].
    VAR_049494

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK024100 mRNA. Translation: BAB14826.1.
    AK223520 mRNA. Translation: BAD97240.1.
    AL590708 Genomic DNA. Translation: CAI13821.1.
    AL590708 Genomic DNA. Translation: CAI13822.1. Sequence problems.
    BC009397 mRNA. Translation: AAH09397.2.
    BC009456 mRNA. Translation: AAH09456.1.
    BC011613 mRNA. Translation: AAH11613.1.
    CCDSiCCDS6891.1.
    RefSeqiNP_001243264.1. NM_001256335.1.
    NP_079348.1. NM_025072.6.
    NP_945176.1. NM_198938.2.
    UniGeneiHs.495219.

    Genome annotation databases

    EnsembliENST00000338961; ENSP00000345341; ENSG00000148334.
    GeneIDi80142.
    KEGGihsa:80142.
    UCSCiuc004bti.4. human.

    Polymorphism databases

    DMDMi73921741.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK024100 mRNA. Translation: BAB14826.1 .
    AK223520 mRNA. Translation: BAD97240.1 .
    AL590708 Genomic DNA. Translation: CAI13821.1 .
    AL590708 Genomic DNA. Translation: CAI13822.1 . Sequence problems.
    BC009397 mRNA. Translation: AAH09397.2 .
    BC009456 mRNA. Translation: AAH09456.1 .
    BC011613 mRNA. Translation: AAH11613.1 .
    CCDSi CCDS6891.1.
    RefSeqi NP_001243264.1. NM_001256335.1.
    NP_079348.1. NM_025072.6.
    NP_945176.1. NM_198938.2.
    UniGenei Hs.495219.

    3D structure databases

    ProteinModelPortali Q9H7Z7.
    SMRi Q9H7Z7. Positions 100-373.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 123135. 7 interactions.
    IntActi Q9H7Z7. 6 interactions.
    STRINGi 9606.ENSP00000345341.

    Chemistry

    BindingDBi Q9H7Z7.
    ChEMBLi CHEMBL4411.

    PTM databases

    PhosphoSitei Q9H7Z7.

    Polymorphism databases

    DMDMi 73921741.

    Proteomic databases

    MaxQBi Q9H7Z7.
    PaxDbi Q9H7Z7.
    PRIDEi Q9H7Z7.

    Protocols and materials databases

    DNASUi 80142.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000338961 ; ENSP00000345341 ; ENSG00000148334 .
    GeneIDi 80142.
    KEGGi hsa:80142.
    UCSCi uc004bti.4. human.

    Organism-specific databases

    CTDi 80142.
    GeneCardsi GC09M130882.
    HGNCi HGNC:17822. PTGES2.
    HPAi HPA020631.
    MIMi 608152. gene.
    neXtProti NX_Q9H7Z7.
    PharmGKBi PA33949.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG316980.
    HOGENOMi HOG000231901.
    HOVERGENi HBG069136.
    InParanoidi Q9H7Z7.
    KOi K05309.
    OMAi AMYFISK.
    OrthoDBi EOG7060R5.
    PhylomeDBi Q9H7Z7.
    TreeFami TF314304.

    Enzyme and pathway databases

    UniPathwayi UPA00662 .
    BioCyci MetaCyc:HS07514-MONOMER.
    BRENDAi 5.3.99.3. 2681.

    Miscellaneous databases

    ChiTaRSi PTGES2. human.
    GeneWikii PTGES2.
    GenomeRNAii 80142.
    NextBioi 70401.
    PROi Q9H7Z7.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9H7Z7.
    Bgeei Q9H7Z7.
    CleanExi HS_PTGES2.
    Genevestigatori Q9H7Z7.

    Family and domain databases

    Gene3Di 1.20.1050.10. 2 hits.
    3.40.30.10. 1 hit.
    InterProi IPR002109. Glutaredoxin.
    IPR010987. Glutathione-S-Trfase_C-like.
    IPR004045. Glutathione_S-Trfase_N.
    IPR004046. GST_C.
    IPR012336. Thioredoxin-like_fold.
    [Graphical view ]
    Pfami PF14497. GST_C_3. 1 hit.
    PF13417. GST_N_3. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47616. SSF47616. 1 hit.
    SSF52833. SSF52833. 1 hit.
    PROSITEi PS00195. GLUTAREDOXIN_1. 1 hit.
    PS51354. GLUTAREDOXIN_2. 1 hit.
    PS50405. GST_CTER. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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].
      Tissue: Embryo.
    2. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    3. "DNA sequence and analysis of human chromosome 9."
      Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
      , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
      Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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: Brain and Lung.
    5. "Identification and characterization of a novel type of membrane-associated prostaglandin E synthase."
      Tanikawa N., Ohmiya Y., Ohkubo H., Hashimoto K., Kangawa K., Kojima M., Ito S., Watanabe K.
      Biochem. Biophys. Res. Commun. 291:884-889(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "Essential 110Cys in active site of membrane-associated prostaglandin E synthase-2."
      Watanabe K., Ohkubo H., Niwa H., Tanikawa N., Koda N., Ito S., Ohmiya Y.
      Biochem. Biophys. Res. Commun. 306:577-581(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: COFACTOR, MUTAGENESIS OF CYS-110 AND CYS-113.
    7. "Cellular prostaglandin E2 production by membrane-bound prostaglandin E synthase-2 via both cyclooxygenases-1 and -2."
      Murakami M., Nakashima K., Kamei D., Masuda S., Ishikawa Y., Ishii T., Ohmiya Y., Watanabe K., Kudo I.
      J. Biol. Chem. 278:37937-37947(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: CLEAVAGE, SUBCELLULAR LOCATION.
    8. "A protein interaction framework for human mRNA degradation."
      Lehner B., Sanderson C.M.
      Genome Res. 14:1315-1323(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH EXOSC10.
    9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiPGES2_HUMAN
    AccessioniPrimary (citable) accession number: Q9H7Z7
    Secondary accession number(s): Q53EW9
    , Q5SYV6, Q96GI0, Q96GL2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: August 30, 2005
    Last sequence update: March 1, 2001
    Last modified: October 1, 2014
    This is version 125 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

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 9
      Human chromosome 9: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3