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Q96GX9

- MTNB_HUMAN

UniProt

Q96GX9 - MTNB_HUMAN

Protein

Methylthioribulose-1-phosphate dehydratase

Gene

APIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 108 (01 Oct 2014)
      Sequence version 1 (01 Dec 2001)
      Previous versions | rss
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    Functioni

    Catalyzes the dehydration of methylthioribulose-1-phosphate (MTRu-1-P) into 2,3-diketo-5-methylthiopentyl-1-phosphate (DK-MTP-1-P). Functions in the methionine salvage pathway, which plays a key role in cancer, apoptosis, microbial proliferation and inflammation. May inhibit the CASP1-related inflammatory response (pyroptosis), the CASP9-dependent apoptotic pathway and the cytochrome c-dependent and APAF1-mediated cell death.3 PublicationsUniRule annotation

    Catalytic activityi

    S-methyl-5-thio-D-ribulose 1-phosphate = 5-(methylthio)-2,3-dioxopentyl phosphate + H2O.UniRule annotation

    Cofactori

    Binds 1 zinc ion per subunit.UniRule annotation

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi115 – 1151ZincCurated
    Metal bindingi117 – 1171ZincCurated

    GO - Molecular functioni

    1. identical protein binding Source: IntAct
    2. methylthioribulose 1-phosphate dehydratase activity Source: Reactome
    3. protein binding Source: IntAct
    4. zinc ion binding Source: UniProtKB-HAMAP

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. cellular nitrogen compound metabolic process Source: Reactome
    3. L-methionine biosynthetic process from methylthioadenosine Source: UniProtKB
    4. L-methionine biosynthetic process from S-adenosylmethionine Source: UniProtKB-HAMAP
    5. negative regulation of apoptotic process Source: UniProtKB
    6. polyamine metabolic process Source: Reactome
    7. regulation of ERK1 and ERK2 cascade Source: UniProtKB
    8. small molecule metabolic process Source: Reactome
    9. sulfur amino acid metabolic process Source: Reactome

    Keywords - Molecular functioni

    Lyase

    Keywords - Biological processi

    Amino-acid biosynthesis, Apoptosis, Methionine biosynthesis

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_75881. Methionine salvage pathway.
    UniPathwayiUPA00904; UER00875.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Methylthioribulose-1-phosphate dehydrataseUniRule annotation (EC:4.2.1.109UniRule annotation)
    Short name:
    MTRu-1-P dehydrataseUniRule annotation
    Alternative name(s):
    APAF1-interacting proteinUniRule annotation
    Short name:
    hAPIP
    Gene namesi
    Name:APIPUniRule annotation
    ORF Names:CGI-29
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 11

    Organism-specific databases

    HGNCiHGNC:17581. APIP.

    Subcellular locationi

    Cytoplasm 2 PublicationsUniRule annotation

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi84 – 841S → A or D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-87 and A,D-89. 1 Publication
    Mutagenesisi87 – 871S → A or D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-89. 1 Publication
    Mutagenesisi89 – 891S → A or D: Does not affect ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A,D-84 and A,D-87. 1 Publication
    Mutagenesisi97 – 971C → A: Acts as a dominant negative mutant; unable to use 5'-methylthioadenosine as source of methionine. Does not affect the ability to bind CASP1 and to inhibit cell death induced by CASP9 overexpression. 1 Publication
    Mutagenesisi115 – 1151H → A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-117 and A-195. Unable to inhibit both CASP1 and CASP9 mediated cell death. 2 Publications
    Mutagenesisi117 – 1171H → A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with A-115 and A-195. 1 Publication
    Mutagenesisi195 – 1951H → A: Impaired ability of cells to grow in media where methionine is replaced by 5-methylthioadenosine; when associated with 87-A--A-89. 1 Publication

    Organism-specific databases

    PharmGKBiPA142672601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 242242Methylthioribulose-1-phosphate dehydratasePRO_0000239022Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei87 – 871Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ96GX9.
    PaxDbiQ96GX9.
    PeptideAtlasiQ96GX9.
    PRIDEiQ96GX9.

    PTM databases

    PhosphoSiteiQ96GX9.

    Expressioni

    Tissue specificityi

    Isoform 1 is ubiquitously expressed. Isoform 2 is expressed at lower levels and detected in heart, brain, pancreas, liver, placenta, skeletal muscle and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ96GX9.
    BgeeiQ96GX9.
    CleanExiHS_APIP.
    GenevestigatoriQ96GX9.

    Organism-specific databases

    HPAiHPA021188.
    HPA024131.

    Interactioni

    Subunit structurei

    Interacts with APAF1. May interact with CASP1.2 PublicationsUniRule annotation

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself4EBI-359248,EBI-359248
    NUDT18Q6ZVK83EBI-359248,EBI-740486

    Protein-protein interaction databases

    BioGridi119265. 12 interactions.
    IntActiQ96GX9. 14 interactions.
    MINTiMINT-1156691.
    STRINGi9606.ENSP00000278359.

    Structurei

    Secondary structure

    1
    242
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi24 – 3714
    Helixi42 – 443
    Beta strandi47 – 526
    Beta strandi55 – 584
    Helixi65 – 673
    Helixi70 – 723
    Beta strandi74 – 763
    Beta strandi82 – 843
    Helixi88 – 903
    Helixi98 – 10811
    Beta strandi111 – 1166
    Helixi119 – 1279
    Beta strandi130 – 1378
    Helixi139 – 1435
    Turni147 – 1493
    Beta strandi157 – 1648
    Helixi170 – 18314
    Beta strandi188 – 1925
    Turni193 – 1953
    Beta strandi196 – 2038
    Helixi204 – 22623

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    4M6RX-ray2.00A/B/C/D20-242[»]
    ProteinModelPortaliQ96GX9.
    SMRiQ96GX9. Positions 20-242.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the aldolase class II family. MtnB subfamily.UniRule annotation

    Phylogenomic databases

    eggNOGiCOG0235.
    HOGENOMiHOG000192424.
    HOVERGENiHBG080536.
    InParanoidiQ96GX9.
    KOiK08964.
    OrthoDBiEOG74TX0H.
    PhylomeDBiQ96GX9.
    TreeFamiTF105632.

    Family and domain databases

    Gene3Di3.40.225.10. 1 hit.
    HAMAPiMF_03116. Salvage_MtnB_euk.
    InterProiIPR001303. Aldolase_II/adducin_N.
    IPR017714. MethylthioRu-1-P_deHdtase_MtnB.
    IPR027514. Salvage_MtnB_euk.
    [Graphical view]
    PANTHERiPTHR10640. PTHR10640. 1 hit.
    PfamiPF00596. Aldolase_II. 1 hit.
    [Graphical view]
    SMARTiSM01007. Aldolase_II. 1 hit.
    [Graphical view]
    SUPFAMiSSF53639. SSF53639. 1 hit.
    TIGRFAMsiTIGR03328. salvage_mtnB. 1 hit.

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q96GX9-1) [UniParc]FASTAAdd to Basket

    Also known as: Long

    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

    MSGCDAREGD CCSRRCGAQD KEHPRYLIPE LCKQFYHLGW VTGTGGGISL    50
    KHGDEIYIAP SGVQKERIQP EDMFVCDINE KDISGPSPSK KLKKSQCTPL 100
    FMNAYTMRGA GAVIHTHSKA AVMATLLFPG REFKITHQEM IKGIKKCTSG 150
    GYYRYDDMLV VPIIENTPEE KDLKDRMAHA MNEYPDSCAV LVRRHGVYVW 200
    GETWEKAKTM CECYDYLFDI AVSMKKVGLD PSQLPVGENG IV 242
    Length:242
    Mass (Da):27,125
    Last modified:December 1, 2001 - v1
    Checksum:i9B8D5D1435D6775A
    GO
    Isoform 2 (identifier: Q96GX9-3) [UniParc]FASTAAdd to Basket

    Also known as: Short

    The sequence of this isoform differs from the canonical sequence as follows:
         1-53: MSGCDAREGDCCSRRCGAQDKEHPRYLIPELCKQFYHLGWVTGTGGGISLKHG → MLGRETVVPGDAARS

    Show »
    Length:204
    Mass (Da):22,858
    Checksum:i82FC4E97BC6C2853
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71R → G in AAD27738. (PubMed:10810093)Curated
    Sequence conflicti172 – 1721D → T in AAD27738. (PubMed:10810093)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti7 – 71R → W.2 Publications
    Corresponds to variant rs2956114 [ dbSNP | Ensembl ].
    VAR_026575
    Natural varianti23 – 231H → R.1 Publication
    Corresponds to variant rs17850326 [ dbSNP | Ensembl ].
    VAR_026576
    Natural varianti76 – 761C → Y.2 Publications
    Corresponds to variant rs1977420 [ dbSNP | Ensembl ].
    VAR_026577
    Natural varianti181 – 1811M → V.1 Publication
    Corresponds to variant rs17850327 [ dbSNP | Ensembl ].
    VAR_026578

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 5353MSGCD…SLKHG → MLGRETVVPGDAARS in isoform 2. CuratedVSP_044403Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132963 mRNA. Translation: AAD27738.1.
    AK292648 mRNA. Translation: BAF85337.1.
    AC107928 Genomic DNA. No translation available.
    BC008440 mRNA. Translation: AAH08440.1.
    BC009077 mRNA. Translation: AAH09077.1.
    BC017594 mRNA. Translation: AAH17594.1.
    CCDSiCCDS7895.1. [Q96GX9-1]
    RefSeqiNP_057041.2. NM_015957.3. [Q96GX9-1]
    UniGeneiHs.447794.

    Genome annotation databases

    EnsembliENST00000395787; ENSP00000379133; ENSG00000149089. [Q96GX9-1]
    GeneIDi51074.
    KEGGihsa:51074.
    UCSCiuc001mvs.2. human. [Q96GX9-1]

    Polymorphism databases

    DMDMi74731866.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF132963 mRNA. Translation: AAD27738.1 .
    AK292648 mRNA. Translation: BAF85337.1 .
    AC107928 Genomic DNA. No translation available.
    BC008440 mRNA. Translation: AAH08440.1 .
    BC009077 mRNA. Translation: AAH09077.1 .
    BC017594 mRNA. Translation: AAH17594.1 .
    CCDSi CCDS7895.1. [Q96GX9-1 ]
    RefSeqi NP_057041.2. NM_015957.3. [Q96GX9-1 ]
    UniGenei Hs.447794.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    4M6R X-ray 2.00 A/B/C/D 20-242 [» ]
    ProteinModelPortali Q96GX9.
    SMRi Q96GX9. Positions 20-242.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119265. 12 interactions.
    IntActi Q96GX9. 14 interactions.
    MINTi MINT-1156691.
    STRINGi 9606.ENSP00000278359.

    PTM databases

    PhosphoSitei Q96GX9.

    Polymorphism databases

    DMDMi 74731866.

    Proteomic databases

    MaxQBi Q96GX9.
    PaxDbi Q96GX9.
    PeptideAtlasi Q96GX9.
    PRIDEi Q96GX9.

    Protocols and materials databases

    DNASUi 51074.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000395787 ; ENSP00000379133 ; ENSG00000149089 . [Q96GX9-1 ]
    GeneIDi 51074.
    KEGGi hsa:51074.
    UCSCi uc001mvs.2. human. [Q96GX9-1 ]

    Organism-specific databases

    CTDi 51074.
    GeneCardsi GC11M034861.
    HGNCi HGNC:17581. APIP.
    HPAi HPA021188.
    HPA024131.
    MIMi 612491. gene.
    neXtProti NX_Q96GX9.
    PharmGKBi PA142672601.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0235.
    HOGENOMi HOG000192424.
    HOVERGENi HBG080536.
    InParanoidi Q96GX9.
    KOi K08964.
    OrthoDBi EOG74TX0H.
    PhylomeDBi Q96GX9.
    TreeFami TF105632.

    Enzyme and pathway databases

    UniPathwayi UPA00904 ; UER00875 .
    Reactomei REACT_75881. Methionine salvage pathway.

    Miscellaneous databases

    GeneWikii APIP.
    GenomeRNAii 51074.
    NextBioi 53699.
    PROi Q96GX9.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q96GX9.
    Bgeei Q96GX9.
    CleanExi HS_APIP.
    Genevestigatori Q96GX9.

    Family and domain databases

    Gene3Di 3.40.225.10. 1 hit.
    HAMAPi MF_03116. Salvage_MtnB_euk.
    InterProi IPR001303. Aldolase_II/adducin_N.
    IPR017714. MethylthioRu-1-P_deHdtase_MtnB.
    IPR027514. Salvage_MtnB_euk.
    [Graphical view ]
    PANTHERi PTHR10640. PTHR10640. 1 hit.
    Pfami PF00596. Aldolase_II. 1 hit.
    [Graphical view ]
    SMARTi SM01007. Aldolase_II. 1 hit.
    [Graphical view ]
    SUPFAMi SSF53639. SSF53639. 1 hit.
    TIGRFAMsi TIGR03328. salvage_mtnB. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
      Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
      Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    2. "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] (ISOFORM 1), VARIANTS TRP-7 AND TYR-76.
      Tissue: Thymus.
    3. 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] (ISOFORM 1), VARIANTS TRP-7; ARG-23; TYR-76 AND VAL-181.
      Tissue: Bone marrow, Colon and Eye.
    5. "Induced inhibition of ischemic/hypoxic injury by APIP, a novel Apaf-1-interacting protein."
      Cho D.-H., Hong Y.-M., Lee H.-J., Woo H.-N., Pyo J.-O., Mak T.W., Jung Y.-K.
      J. Biol. Chem. 279:39942-39950(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH APAF1, TISSUE SPECIFICITY, SUBCELLULAR LOCATION, ALTERNATIVE SPLICING (ISOFORM 2).
    6. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    7. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-87, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Functional identification of APIP as human mtnB, a key enzyme in the methionine salvage pathway."
      Mary C., Duek P., Salleron L., Tienz P., Bumann D., Bairoch A., Lane L.
      PLoS ONE 7:E52877-E52877(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, PATHWAY, ALTERNATIVE SPLICING (ISOFORM 2), SUBCELLULAR LOCATION, TISSUE SPECIFICITY, MUTAGENESIS OF SER-84; SER-87; SER-89; HIS-115; HIS-117 AND HIS-195.
    9. "Functional genetic screen of human diversity reveals that a methionine salvage enzyme regulates inflammatory cell death."
      Ko D.C., Gamazon E.R., Shukla K.P., Pfuetzner R.A., Whittington D., Holden T.D., Brittnacher M.J., Fong C., Radey M., Ogohara C., Stark A.L., Akey J.M., Dolan M.E., Wurfel M.M., Miller S.I.
      Proc. Natl. Acad. Sci. U.S.A. 109:E2343-E2352(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CASP1, MUTAGENESIS OF CYS-97 AND HIS-115.

    Entry informationi

    Entry nameiMTNB_HUMAN
    AccessioniPrimary (citable) accession number: Q96GX9
    Secondary accession number(s): A8K9D3
    , Q6PJX6, Q8WVU2, Q96HK2, Q9Y318
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 30, 2006
    Last sequence update: December 1, 2001
    Last modified: October 1, 2014
    This is version 108 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

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 11
      Human chromosome 11: 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