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Q8IVS2

- FABD_HUMAN

UniProt

Q8IVS2 - FABD_HUMAN

Protein

Malonyl-CoA-acyl carrier protein transacylase, mitochondrial

Gene

MCAT

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 109 (01 Oct 2014)
      Sequence version 2 (07 Jun 2004)
      Previous versions | rss
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    Functioni

    Catalyzes the transfer of a malonyl moiety from malonyl-CoA to the free thiol group of the phosphopantetheine arm of the mitochondrial ACP protein (NDUFAB1). This suggests the existence of the biosynthesis of fatty acids in mitochondrias.1 Publication

    Catalytic activityi

    Malonyl-CoA + an [acyl-carrier-protein] = CoA + a malonyl-[acyl-carrier-protein].1 Publication

    Pathwayi

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Active sitei153 – 1531By similarity
    Active sitei270 – 2701By similarity

    GO - Molecular functioni

    1. [acyl-carrier-protein] S-malonyltransferase activity Source: UniProtKB
    2. poly(A) RNA binding Source: UniProtKB
    3. transferase activity Source: UniProtKB

    GO - Biological processi

    1. fatty acid biosynthetic process Source: UniProtKB
    2. metabolic process Source: UniProtKB

    Keywords - Molecular functioni

    Transferase

    Keywords - Biological processi

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

    Enzyme and pathway databases

    BioCyciMetaCyc:HS02028-MONOMER.
    UniPathwayiUPA00094.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Malonyl-CoA-acyl carrier protein transacylase, mitochondrial (EC:2.3.1.39)
    Short name:
    MCT
    Alternative name(s):
    Mitochondrial malonyl CoA:ACP acyltransferase
    Mitochondrial malonyltransferase
    [Acyl-carrier-protein] malonyltransferase
    Gene namesi
    Name:MCAT
    Synonyms:MT
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 22

    Organism-specific databases

    HGNCiHGNC:29622. MCAT.

    Subcellular locationi

    Mitochondrion 1 Publication

    GO - Cellular componenti

    1. mitochondrion Source: UniProtKB

    Keywords - Cellular componenti

    Mitochondrion

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162395058.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transit peptidei1 – 2121MitochondrionSequence AnalysisAdd
    BLAST
    Chaini22 – 390369Malonyl-CoA-acyl carrier protein transacylase, mitochondrialPRO_0000000589Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei314 – 3141N6-succinyllysineBy similarity

    Proteomic databases

    MaxQBiQ8IVS2.
    PaxDbiQ8IVS2.
    PeptideAtlasiQ8IVS2.
    PRIDEiQ8IVS2.

    PTM databases

    PhosphoSiteiQ8IVS2.

    Expressioni

    Gene expression databases

    ArrayExpressiQ8IVS2.
    BgeeiQ8IVS2.
    CleanExiHS_MCAT.
    GenevestigatoriQ8IVS2.

    Organism-specific databases

    HPAiHPA035471.

    Interactioni

    Protein-protein interaction databases

    BioGridi118161. 15 interactions.
    IntActiQ8IVS2. 2 interactions.
    MINTiMINT-4828919.
    STRINGi9606.ENSP00000290429.

    Structurei

    Secondary structure

    1
    390
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi63 – 675
    Turni75 – 839
    Helixi87 – 9812
    Helixi102 – 1087
    Helixi111 – 1155
    Helixi117 – 13822
    Helixi140 – 1445
    Beta strandi146 – 1516
    Helixi155 – 1628
    Helixi168 – 18720
    Beta strandi191 – 1977
    Helixi204 – 21714
    Beta strandi225 – 2328
    Beta strandi235 – 2417
    Helixi242 – 2509
    Helixi252 – 2554
    Beta strandi259 – 2624
    Helixi272 – 2743
    Helixi275 – 28612
    Beta strandi294 – 2985
    Turni300 – 3023
    Beta strandi303 – 3053
    Helixi309 – 3113
    Helixi312 – 3198
    Helixi326 – 3338
    Beta strandi344 – 3529
    Helixi353 – 3619
    Helixi363 – 3664
    Beta strandi369 – 3724

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2C2NX-ray1.55A/B60-375[»]
    ProteinModelPortaliQ8IVS2.
    SMRiQ8IVS2. Positions 3-375.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ8IVS2.

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the type II malonyltransferase family.Curated

    Keywords - Domaini

    Transit peptide

    Phylogenomic databases

    eggNOGiCOG0331.
    HOGENOMiHOG000036504.
    HOVERGENiHBG051540.
    InParanoidiQ8IVS2.
    KOiK00645.
    OMAiMVFEEVD.
    OrthoDBiEOG7D85X6.
    PhylomeDBiQ8IVS2.
    TreeFamiTF313401.

    Family and domain databases

    Gene3Di3.40.366.10. 2 hits.
    InterProiIPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR016036. Malonyl_transacylase_ACP-bd.
    [Graphical view]
    PfamiPF00698. Acyl_transf_1. 1 hit.
    [Graphical view]
    SUPFAMiSSF52151. SSF52151. 2 hits.
    SSF55048. SSF55048. 1 hit.

    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: Q8IVS2-1) [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

    MSVRVARVAW VRGLGASYRR GASSFPVPPP GAQGVAELLR DATGAEEEAP    50
    WAATERRMPG QCSVLLFPGQ GSQVVGMGRG LLNYPRVREL YAAARRVLGY 100
    DLLELSLHGP QETLDRTVHC QPAIFVASLA AVEKLHHLQP SVIENCVAAA 150
    GFSVGEFAAL VFAGAMEFAE GLYAVKIRAE AMQEASEAVP SGMLSVLGQP 200
    QSKFNFACLE AREHCKSLGI ENPVCEVSNY LFPDCRVISG HQEALRFLQK 250
    NSSKFHFRRT RMLPVSGAFH TRLMEPAVEP LTQALKAVDI KKPLVSVYSN 300
    VHAHRYRHPG HIHKLLAQQL VSPVKWEQTM HAIYERKKGR GFPQTFEVGP 350
    GRQLGAILKS CNMQAWKSYS AVDVLQTLEH VDLDPQEPPR 390
    Length:390
    Mass (Da):42,962
    Last modified:June 7, 2004 - v2
    Checksum:i5CAF7AE9DFF36A21
    GO
    Isoform 2 (identifier: Q8IVS2-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         172-180: LYAVKIRAE → STVSPEEFL
         181-390: Missing.

    Show »
    Length:180
    Mass (Da):19,176
    Checksum:i8DA3FDA905D219C7
    GO

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti303 – 3031A → G.1 Publication
    Corresponds to variant rs13815 [ dbSNP | Ensembl ].
    VAR_048183

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei172 – 1809LYAVKIRAE → STVSPEEFL in isoform 2. 3 PublicationsVSP_010517
    Alternative sequencei181 – 390210Missing in isoform 2. 3 PublicationsVSP_010518Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL359401 mRNA. Translation: CAB94789.1.
    AL359403 mRNA. Translation: CAB94790.1.
    AK314059 mRNA. Translation: BAG36765.1.
    AL022237 Genomic DNA. Translation: CAQ07851.1.
    AL022237 Genomic DNA. Translation: CAA18261.1.
    CH471138 Genomic DNA. Translation: EAW73286.1.
    BC030985 mRNA. Translation: AAH30985.1.
    BC042195 mRNA. Translation: AAH42195.2.
    CCDSiCCDS14045.1. [Q8IVS2-2]
    CCDS33660.1. [Q8IVS2-1]
    RefSeqiNP_055322.1. NM_014507.3. [Q8IVS2-2]
    NP_775738.3. NM_173467.4. [Q8IVS2-1]
    UniGeneiHs.349111.

    Genome annotation databases

    EnsembliENST00000290429; ENSP00000290429; ENSG00000100294. [Q8IVS2-1]
    ENST00000327555; ENSP00000331306; ENSG00000100294. [Q8IVS2-2]
    GeneIDi27349.
    KEGGihsa:27349.
    UCSCiuc003bdl.1. human. [Q8IVS2-1]
    uc003bdm.1. human.

    Polymorphism databases

    DMDMi48428076.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AL359401 mRNA. Translation: CAB94789.1 .
    AL359403 mRNA. Translation: CAB94790.1 .
    AK314059 mRNA. Translation: BAG36765.1 .
    AL022237 Genomic DNA. Translation: CAQ07851.1 .
    AL022237 Genomic DNA. Translation: CAA18261.1 .
    CH471138 Genomic DNA. Translation: EAW73286.1 .
    BC030985 mRNA. Translation: AAH30985.1 .
    BC042195 mRNA. Translation: AAH42195.2 .
    CCDSi CCDS14045.1. [Q8IVS2-2 ]
    CCDS33660.1. [Q8IVS2-1 ]
    RefSeqi NP_055322.1. NM_014507.3. [Q8IVS2-2 ]
    NP_775738.3. NM_173467.4. [Q8IVS2-1 ]
    UniGenei Hs.349111.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2C2N X-ray 1.55 A/B 60-375 [» ]
    ProteinModelPortali Q8IVS2.
    SMRi Q8IVS2. Positions 3-375.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 118161. 15 interactions.
    IntActi Q8IVS2. 2 interactions.
    MINTi MINT-4828919.
    STRINGi 9606.ENSP00000290429.

    PTM databases

    PhosphoSitei Q8IVS2.

    Polymorphism databases

    DMDMi 48428076.

    Proteomic databases

    MaxQBi Q8IVS2.
    PaxDbi Q8IVS2.
    PeptideAtlasi Q8IVS2.
    PRIDEi Q8IVS2.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000290429 ; ENSP00000290429 ; ENSG00000100294 . [Q8IVS2-1 ]
    ENST00000327555 ; ENSP00000331306 ; ENSG00000100294 . [Q8IVS2-2 ]
    GeneIDi 27349.
    KEGGi hsa:27349.
    UCSCi uc003bdl.1. human. [Q8IVS2-1 ]
    uc003bdm.1. human.

    Organism-specific databases

    CTDi 27349.
    GeneCardsi GC22M043528.
    HGNCi HGNC:29622. MCAT.
    HPAi HPA035471.
    MIMi 614479. gene.
    neXtProti NX_Q8IVS2.
    PharmGKBi PA162395058.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0331.
    HOGENOMi HOG000036504.
    HOVERGENi HBG051540.
    InParanoidi Q8IVS2.
    KOi K00645.
    OMAi MVFEEVD.
    OrthoDBi EOG7D85X6.
    PhylomeDBi Q8IVS2.
    TreeFami TF313401.

    Enzyme and pathway databases

    UniPathwayi UPA00094 .
    BioCyci MetaCyc:HS02028-MONOMER.

    Miscellaneous databases

    EvolutionaryTracei Q8IVS2.
    GeneWikii MCAT_(gene).
    GenomeRNAii 27349.
    NextBioi 50446.
    PROi Q8IVS2.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q8IVS2.
    Bgeei Q8IVS2.
    CleanExi HS_MCAT.
    Genevestigatori Q8IVS2.

    Family and domain databases

    Gene3Di 3.40.366.10. 2 hits.
    InterProi IPR001227. Ac_transferase_dom.
    IPR014043. Acyl_transferase.
    IPR016035. Acyl_Trfase/lysoPLipase.
    IPR016036. Malonyl_transacylase_ACP-bd.
    [Graphical view ]
    Pfami PF00698. Acyl_transf_1. 1 hit.
    [Graphical view ]
    SUPFAMi SSF52151. SSF52151. 2 hits.
    SSF55048. SSF55048. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Reevaluating human gene annotation: a second-generation analysis of chromosome 22."
      Collins J.E., Goward M.E., Cole C.G., Smink L.J., Huckle E.J., Knowles S., Bye J.M., Beare D.M., Dunham I.
      Genome Res. 13:27-36(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    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 2).
      Tissue: Caudate nucleus.
    3. "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].
    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] (ISOFORMS 1 AND 2), VARIANT GLY-303.
      Tissue: Testis.
    6. "Cloning, expression, characterization, and interaction of two components of a human mitochondrial fatty acid synthase. Malonyltransferase and acyl carrier protein."
      Zhang L., Joshi A.K., Smith S.
      J. Biol. Chem. 278:40067-40074(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ENZYME ACTIVITY, SUBCELLULAR LOCATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    8. "Structure of human mitochondrial malonyltransferase."
      Structural genomics consortium (SGC)
      Submitted (SEP-2005) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (1.55 ANGSTROMS) OF 60-375.

    Entry informationi

    Entry nameiFABD_HUMAN
    AccessioniPrimary (citable) accession number: Q8IVS2
    Secondary accession number(s): B0QY72, O95510, O95511
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: June 7, 2004
    Last sequence update: June 7, 2004
    Last modified: October 1, 2014
    This is version 109 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 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. 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