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P49767

- VEGFC_HUMAN

UniProt

P49767 - VEGFC_HUMAN

Protein

Vascular endothelial growth factor C

Gene

VEGFC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 134 (01 Oct 2014)
      Sequence version 1 (01 Oct 1996)
      Previous versions | rss
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    Functioni

    Growth factor active in angiogenesis, and endothelial cell growth, stimulating their proliferation and migration and also has effects on the permeability of blood vessels. May function in angiogenesis of the venous and lymphatic vascular systems during embryogenesis, and also in the maintenance of differentiated lymphatic endothelium in adults. Binds and activates VEGFR-2 (KDR/FLK1) and VEGFR-3 (FLT4) receptors.1 Publication

    GO - Molecular functioni

    1. chemoattractant activity Source: UniProtKB
    2. protein binding Source: IntAct

    GO - Biological processi

    1. angiogenesis Source: UniProtKB-KW
    2. blood coagulation Source: Reactome
    3. induction of positive chemotaxis Source: UniProtKB
    4. morphogenesis of embryonic epithelium Source: Ensembl
    5. negative regulation of blood pressure Source: Ensembl
    6. organ morphogenesis Source: Ensembl
    7. platelet activation Source: Reactome
    8. platelet degranulation Source: Reactome
    9. positive chemotaxis Source: GOC
    10. positive regulation of blood vessel endothelial cell migration Source: Ensembl
    11. positive regulation of cell division Source: UniProtKB-KW
    12. positive regulation of cell proliferation Source: ProtInc
    13. positive regulation of epithelial cell proliferation Source: Ensembl
    14. positive regulation of lymphangiogenesis Source: Ensembl
    15. positive regulation of mast cell chemotaxis Source: UniProtKB
    16. positive regulation of neuroblast proliferation Source: Ensembl
    17. positive regulation of protein autophosphorylation Source: Ensembl
    18. positive regulation of protein secretion Source: Ensembl
    19. regulation of vascular endothelial growth factor receptor signaling pathway Source: Ensembl
    20. response to drug Source: Ensembl
    21. signal transduction Source: ProtInc
    22. substrate-dependent cell migration Source: ProtInc
    23. vascular endothelial growth factor receptor signaling pathway Source: Reactome

    Keywords - Molecular functioni

    Developmental protein, Growth factor, Mitogen

    Keywords - Biological processi

    Angiogenesis, Differentiation

    Enzyme and pathway databases

    ReactomeiREACT_12380. VEGF ligand-receptor interactions.
    REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.

    Protein family/group databases

    TCDBi9.B.88.2.1. the selenoprotein p hydrogen selenide uptake protein (selp) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vascular endothelial growth factor C
    Short name:
    VEGF-C
    Alternative name(s):
    Flt4 ligand
    Short name:
    Flt4-L
    Vascular endothelial growth factor-related protein
    Short name:
    VRP
    Gene namesi
    Name:VEGFC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:12682. VEGFC.

    Subcellular locationi

    GO - Cellular componenti

    1. extracellular region Source: Reactome
    2. extracellular space Source: Ensembl
    3. membrane Source: InterPro
    4. platelet alpha granule lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi227 – 2271R → S: No proteolytic processing and lower effect on VEGFR-2 and VEGFR-3. 1 Publication

    Organism-specific databases

    Orphaneti79452. Milroy disease.
    PharmGKBiPA37304.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 31312 PublicationsAdd
    BLAST
    Propeptidei32 – 11180Or 1021 PublicationPRO_0000023400Add
    BLAST
    Chaini112 – 227116Vascular endothelial growth factor CPRO_0000023401Add
    BLAST
    Propeptidei228 – 419192PRO_0000023402Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi131 ↔ 1731 Publication
    Disulfide bondi156 – 156Interchain1 Publication
    Disulfide bondi162 ↔ 2091 Publication
    Disulfide bondi165 – 165Interchain1 Publication
    Disulfide bondi166 ↔ 2111 Publication
    Glycosylationi175 – 1751N-linked (GlcNAc...)1 Publication
    Glycosylationi205 – 2051N-linked (GlcNAc...)1 Publication
    Glycosylationi240 – 2401N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Undergoes a complex proteolytic maturation which generates a variety of processed secreted forms with increased activity toward VEGFR-3, but only the fully processed form could activate VEGFR-2. VEGF-C first form an antiparallel homodimer linked by disulfide bonds. Before secretion, a cleavage occurs between Arg-227 and Ser-228 producing a heterotetramer. The next extracellular step of the processing removes the N-terminal propeptide. Finally the mature VEGF-C is composed mostly of two VEGF homology domains (VHDs) bound by non-covalent interactions.

    Keywords - PTMi

    Cleavage on pair of basic residues, Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiP49767.
    PRIDEiP49767.

    PTM databases

    PhosphoSiteiP49767.

    Miscellaneous databases

    PMAP-CutDBP49767.

    Expressioni

    Tissue specificityi

    Spleen, lymph node, thymus, appendix, bone marrow, heart, placenta, ovary, skeletal muscle, prostate, testis, colon and small intestine and fetal liver, lung and kidney, but not in peripheral blood lymphocyte.

    Gene expression databases

    BgeeiP49767.
    CleanExiHS_VEGFC.
    GenevestigatoriP49767.

    Interactioni

    Subunit structurei

    Homodimer; non-covalent and antiparallel.1 Publication

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    FLT4P359162EBI-3405539,EBI-1005467

    Protein-protein interaction databases

    BioGridi113267. 2 interactions.
    DIPiDIP-5738N.
    IntActiP49767. 1 interaction.
    STRINGi9606.ENSP00000280193.

    Structurei

    Secondary structure

    1
    419
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi117 – 12913
    Beta strandi130 – 13910
    Turni140 – 1423
    Beta strandi151 – 16313
    Beta strandi167 – 1704
    Beta strandi172 – 18817
    Beta strandi190 – 1945
    Beta strandi197 – 21216

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2X1WX-ray2.70A/B/C/D112-215[»]
    2X1XX-ray3.10E112-215[»]
    4BSKX-ray4.20C103-215[»]
    ProteinModelPortaliP49767.
    SMRiP49767. Positions 117-215.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP49767.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati280 – 295161Add
    BLAST
    Repeati304 – 319162Add
    BLAST
    Repeati328 – 343163Add
    BLAST
    Repeati347 – 362164Add
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni280 – 362834 X 16 AA repeats of C-X(10)-C-X-C-X(1,3)-CAdd
    BLAST

    Sequence similaritiesi

    Belongs to the PDGF/VEGF growth factor family.Curated

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG79308.
    HOGENOMiHOG000231512.
    HOVERGENiHBG073119.
    InParanoidiP49767.
    KOiK05449.
    OrthoDBiEOG7J17ZS.
    PhylomeDBiP49767.
    TreeFamiTF319554.

    Family and domain databases

    Gene3Di2.10.90.10. 1 hit.
    InterProiIPR004153. CXCXC_repeat.
    IPR029034. Cystine-knot_cytokine.
    IPR023581. PD_growth_factor_CS.
    IPR000072. PDGF/VEGF_dom.
    [Graphical view]
    PfamiPF03128. CXCXC. 3 hits.
    PF00341. PDGF. 1 hit.
    [Graphical view]
    SMARTiSM00141. PDGF. 1 hit.
    [Graphical view]
    SUPFAMiSSF57501. SSF57501. 1 hit.
    PROSITEiPS00249. PDGF_1. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P49767-1 [UniParc]FASTAAdd to Basket

    « Hide

    MHLLGFFSVA CSLLAAALLP GPREAPAAAA AFESGLDLSD AEPDAGEATA    50
    YASKDLEEQL RSVSSVDELM TVLYPEYWKM YKCQLRKGGW QHNREQANLN 100
    SRTEETIKFA AAHYNTEILK SIDNEWRKTQ CMPREVCIDV GKEFGVATNT 150
    FFKPPCVSVY RCGGCCNSEG LQCMNTSTSY LSKTLFEITV PLSQGPKPVT 200
    ISFANHTSCR CMSKLDVYRQ VHSIIRRSLP ATLPQCQAAN KTCPTNYMWN 250
    NHICRCLAQE DFMFSSDAGD DSTDGFHDIC GPNKELDEET CQCVCRAGLR 300
    PASCGPHKEL DRNSCQCVCK NKLFPSQCGA NREFDENTCQ CVCKRTCPRN 350
    QPLNPGKCAC ECTESPQKCL LKGKKFHHQT CSCYRRPCTN RQKACEPGFS 400
    YSEEVCRCVP SYWKRPQMS 419
    Length:419
    Mass (Da):46,883
    Last modified:October 1, 1996 - v1
    Checksum:i9F598719DB3E014F
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94216 mRNA. Translation: CAA63907.1.
    U43142 mRNA. Translation: AAA85214.1.
    U58111 mRNA. Translation: AAB02909.1.
    AK313879 mRNA. Translation: BAG36605.1.
    AC092673 Genomic DNA. No translation available.
    AC093801 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04717.1.
    BC035212 mRNA. Translation: AAH35212.1.
    BC063685 mRNA. Translation: AAH63685.1.
    CCDSiCCDS43285.1.
    PIRiS69207.
    RefSeqiNP_005420.1. NM_005429.4.
    UniGeneiHs.435215.

    Genome annotation databases

    EnsembliENST00000280193; ENSP00000280193; ENSG00000150630.
    GeneIDi7424.
    KEGGihsa:7424.
    UCSCiuc003ius.1. human.

    Polymorphism databases

    DMDMi1718154.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X94216 mRNA. Translation: CAA63907.1 .
    U43142 mRNA. Translation: AAA85214.1 .
    U58111 mRNA. Translation: AAB02909.1 .
    AK313879 mRNA. Translation: BAG36605.1 .
    AC092673 Genomic DNA. No translation available.
    AC093801 Genomic DNA. No translation available.
    CH471056 Genomic DNA. Translation: EAX04717.1 .
    BC035212 mRNA. Translation: AAH35212.1 .
    BC063685 mRNA. Translation: AAH63685.1 .
    CCDSi CCDS43285.1.
    PIRi S69207.
    RefSeqi NP_005420.1. NM_005429.4.
    UniGenei Hs.435215.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2X1W X-ray 2.70 A/B/C/D 112-215 [» ]
    2X1X X-ray 3.10 E 112-215 [» ]
    4BSK X-ray 4.20 C 103-215 [» ]
    ProteinModelPortali P49767.
    SMRi P49767. Positions 117-215.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113267. 2 interactions.
    DIPi DIP-5738N.
    IntActi P49767. 1 interaction.
    STRINGi 9606.ENSP00000280193.

    Protein family/group databases

    TCDBi 9.B.88.2.1. the selenoprotein p hydrogen selenide uptake protein (selp) family.

    PTM databases

    PhosphoSitei P49767.

    Polymorphism databases

    DMDMi 1718154.

    Proteomic databases

    PaxDbi P49767.
    PRIDEi P49767.

    Protocols and materials databases

    DNASUi 7424.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000280193 ; ENSP00000280193 ; ENSG00000150630 .
    GeneIDi 7424.
    KEGGi hsa:7424.
    UCSCi uc003ius.1. human.

    Organism-specific databases

    CTDi 7424.
    GeneCardsi GC04M177604.
    HGNCi HGNC:12682. VEGFC.
    MIMi 601528. gene.
    neXtProti NX_P49767.
    Orphaneti 79452. Milroy disease.
    PharmGKBi PA37304.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG79308.
    HOGENOMi HOG000231512.
    HOVERGENi HBG073119.
    InParanoidi P49767.
    KOi K05449.
    OrthoDBi EOG7J17ZS.
    PhylomeDBi P49767.
    TreeFami TF319554.

    Enzyme and pathway databases

    Reactomei REACT_12380. VEGF ligand-receptor interactions.
    REACT_12583. VEGF binds to VEGFR leading to receptor dimerization.

    Miscellaneous databases

    EvolutionaryTracei P49767.
    GeneWikii Vascular_endothelial_growth_factor_C.
    GenomeRNAii 7424.
    NextBioi 29082.
    PMAP-CutDB P49767.
    PROi P49767.
    SOURCEi Search...

    Gene expression databases

    Bgeei P49767.
    CleanExi HS_VEGFC.
    Genevestigatori P49767.

    Family and domain databases

    Gene3Di 2.10.90.10. 1 hit.
    InterProi IPR004153. CXCXC_repeat.
    IPR029034. Cystine-knot_cytokine.
    IPR023581. PD_growth_factor_CS.
    IPR000072. PDGF/VEGF_dom.
    [Graphical view ]
    Pfami PF03128. CXCXC. 3 hits.
    PF00341. PDGF. 1 hit.
    [Graphical view ]
    SMARTi SM00141. PDGF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57501. SSF57501. 1 hit.
    PROSITEi PS00249. PDGF_1. 1 hit.
    PS50278. PDGF_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A novel vascular endothelial growth factor, VEGF-C, is a ligand for the Flt4 (VEGFR-3) and KDR (VEGFR-2) receptor tyrosine kinases."
      Joukov V., Pajusola K., Kaipainen A., Chilov D., Lahtinen I., Kukk E., Saksela O., Kalkkinen N., Alitalo K.
      EMBO J. 15:290-298(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 103-120.
    2. "Vascular endothelial growth factor-related protein: a ligand and specific activator of the tyrosine kinase receptor Flt4."
      Lee J., Gray A., Yuan J., Luoh S.-M., Avraham H., Wood W.I.
      Proc. Natl. Acad. Sci. U.S.A. 93:1988-1992(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Glial tumor.
    3. Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    4. "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: Trachea.
    5. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    7. "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: Skin and Urinary bladder.
    8. "Proteolytic processing regulates receptor specificity and activity of VEGF-C."
      Joukov V., Sorsa T., Kumar V., Jeltsch M., Claesson-Welsh L., Cao Y., Saksela O., Kalkkinen N., Alitalo K.
      EMBO J. 16:3898-3911(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-41; 112-121 AND 228-233, MUTAGENESIS OF ARG-227.
    9. "Signal peptide prediction based on analysis of experimentally verified cleavage sites."
      Zhang Z., Henzel W.J.
      Protein Sci. 13:2819-2824(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 32-46.
    10. Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 112-215 IN COMPLEX WITH KDR, FUNCTION, DISULFIDE BONDS, GLYCOSYLATION AT ASN-175 AND ASN-205, SUBUNIT.

    Entry informationi

    Entry nameiVEGFC_HUMAN
    AccessioniPrimary (citable) accession number: P49767
    Secondary accession number(s): B2R9Q8
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: October 1, 1996
    Last modified: October 1, 2014
    This is version 134 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    3. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    4. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3