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P02774

- VTDB_HUMAN

UniProt

P02774 - VTDB_HUMAN

Protein

Vitamin D-binding protein

Gene

GC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 168 (01 Oct 2014)
      Sequence version 1 (21 Jul 1986)
      Previous versions | rss
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    Functioni

    Multifunctional protein found in plasma, ascitic fluid, cerebrospinal fluid, and urine and on the surface of many cell types. In plasma, it carries the vitamin D sterols and prevents polymerization of actin by binding its monomers. DBP associates with membrane-bound immunoglobulin on the surface of B-lymphocytes and with IgG Fc receptor on the membranes of T-lymphocytes.

    GO - Molecular functioni

    1. actin binding Source: UniProtKB
    2. calcidiol binding Source: UniProtKB
    3. vitamin D binding Source: ProtInc
    4. vitamin transporter activity Source: InterPro

    GO - Biological processi

    1. small molecule metabolic process Source: Reactome
    2. steroid metabolic process Source: Reactome
    3. vitamin D metabolic process Source: Reactome
    4. vitamin transport Source: ProtInc

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Actin-binding, Vitamin D

    Enzyme and pathway databases

    ReactomeiREACT_13523. Vitamin D (calciferol) metabolism.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Vitamin D-binding protein
    Short name:
    DBP
    Short name:
    VDB
    Alternative name(s):
    Gc-globulin
    Group-specific component
    Gene namesi
    Name:GC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:4187. GC.

    Subcellular locationi

    GO - Cellular componenti

    1. blood microparticle Source: UniProt
    2. cytosol Source: Reactome
    3. extracellular region Source: UniProtKB
    4. extracellular space Source: UniProt
    5. extracellular vesicular exosome Source: UniProt
    6. lysosomal lumen Source: Reactome

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Organism-specific databases

    MIMi139200. gene+phenotype.
    PharmGKBiPA28601.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 16162 PublicationsAdd
    BLAST
    Chaini17 – 474458Vitamin D-binding proteinPRO_0000001102Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 75
    Disulfide bondi74 ↔ 83PROSITE-ProRule annotation
    Disulfide bondi96 ↔ 112
    Disulfide bondi111 ↔ 122
    Disulfide bondi145 ↔ 190
    Disulfide bondi189 ↔ 198
    Disulfide bondi220 ↔ 266
    Disulfide bondi265 ↔ 273
    Disulfide bondi286 ↔ 300
    Glycosylationi288 – 2881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi299 ↔ 311
    Disulfide bondi335 ↔ 376
    Disulfide bondi375 ↔ 384
    Disulfide bondi407 ↔ 453
    Disulfide bondi452 ↔ 462

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiP02774.
    PaxDbiP02774.
    PeptideAtlasiP02774.
    PRIDEiP02774.

    2D gel databases

    DOSAC-COBS-2DPAGEP02774.
    REPRODUCTION-2DPAGEIPI00555812.
    P02774.
    SWISS-2DPAGEP02774.

    PTM databases

    PhosphoSiteiP02774.
    UniCarbKBiP02774.

    Expressioni

    Gene expression databases

    ArrayExpressiP02774.
    BgeeiP02774.
    CleanExiHS_GC.
    GenevestigatoriP02774.

    Organism-specific databases

    HPAiCAB008596.
    HPA001526.
    HPA019855.

    Interactioni

    Protein-protein interaction databases

    BioGridi108908. 10 interactions.
    DIPiDIP-17038N.
    IntActiP02774. 7 interactions.
    MINTiMINT-239255.
    STRINGi9606.ENSP00000273951.

    Structurei

    Secondary structure

    1
    474
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi23 – 3513
    Helixi37 – 5115
    Helixi57 – 7418
    Beta strandi76 – 794
    Helixi83 – 9412
    Beta strandi97 – 993
    Helixi108 – 1114
    Helixi116 – 12510
    Helixi141 – 15010
    Helixi152 – 16615
    Helixi172 – 19019
    Beta strandi192 – 1943
    Helixi195 – 22632
    Helixi228 – 24215
    Helixi248 – 26518
    Helixi273 – 28917
    Turni290 – 2923
    Helixi294 – 2996
    Beta strandi302 – 3043
    Helixi305 – 31410
    Helixi331 – 3355
    Beta strandi336 – 3383
    Helixi340 – 35112
    Helixi358 – 37316
    Turni374 – 3774
    Helixi381 – 40626
    Turni407 – 4126
    Helixi415 – 42915
    Helixi435 – 45218
    Helixi459 – 47012

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1J78X-ray2.31A/B17-474[»]
    1J7EX-ray2.55A/B17-474[»]
    1KW2X-ray2.15A/B17-474[»]
    1KXPX-ray2.10D17-474[»]
    1LOTX-ray2.50A17-474[»]
    1MA9X-ray2.40A17-474[»]
    ProteinModelPortaliP02774.
    SMRiP02774. Positions 20-474.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP02774.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini17 – 208192Albumin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini209 – 394186Albumin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini395 – 47480Albumin 3PROSITE-ProRule annotationAdd
    BLAST

    Sequence similaritiesi

    Belongs to the ALB/AFP/VDB family.PROSITE-ProRule annotation
    Contains 3 albumin domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal

    Phylogenomic databases

    eggNOGiNOG40465.
    HOGENOMiHOG000140946.
    HOVERGENiHBG009729.
    InParanoidiP02774.
    KOiK12258.
    OrthoDBiEOG7B05CR.
    PhylomeDBiP02774.
    TreeFamiTF335561.

    Family and domain databases

    InterProiIPR000264. ALB/AFP/VDB.
    IPR020858. Serum_albumin-like.
    IPR020857. Serum_albumin_CS.
    IPR014760. Serum_albumin_N.
    IPR000213. VitD-bd.
    IPR015247. VitD-bind_III.
    [Graphical view]
    PfamiPF00273. Serum_albumin. 2 hits.
    PF09164. VitD-bind_III. 1 hit.
    [Graphical view]
    PRINTSiPR00802. SERUMALBUMIN.
    PR00804. VITAMNDBNDNG.
    SMARTiSM00103. ALBUMIN. 2 hits.
    [Graphical view]
    SUPFAMiSSF48552. SSF48552. 3 hits.
    PROSITEiPS00212. ALBUMIN_1. 1 hit.
    PS51438. ALBUMIN_2. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

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

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P02774-1) [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

    MKRVLVLLLA VAFGHALERG RDYEKNKVCK EFSHLGKEDF TSLSLVLYSR    50
    KFPSGTFEQV SQLVKEVVSL TEACCAEGAD PDCYDTRTSA LSAKSCESNS 100
    PFPVHPGTAE CCTKEGLERK LCMAALKHQP QEFPTYVEPT NDEICEAFRK 150
    DPKEYANQFM WEYSTNYGQA PLSLLVSYTK SYLSMVGSCC TSASPTVCFL 200
    KERLQLKHLS LLTTLSNRVC SQYAAYGEKK SRLSNLIKLA QKVPTADLED 250
    VLPLAEDITN ILSKCCESAS EDCMAKELPE HTVKLCDNLS TKNSKFEDCC 300
    QEKTAMDVFV CTYFMPAAQL PELPDVELPT NKDVCDPGNT KVMDKYTFEL 350
    SRRTHLPEVF LSKVLEPTLK SLGECCDVED STTCFNAKGP LLKKELSSFI 400
    DKGQELCADY SENTFTEYKK KLAERLKAKL PDATPKELAK LVNKRSDFAS 450
    NCCSINSPPL YCDSEIDAEL KNIL 474
    Length:474
    Mass (Da):52,964
    Last modified:July 21, 1986 - v1
    Checksum:i6AD8F163B551F1E4
    GO
    Isoform 2 (identifier: P02774-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-122: Missing.

    Note: May be produced at very low levels due to a premature stop codon in the mRNA, leading to nonsense-mediated mRNA decay.

    Show »
    Length:352
    Mass (Da):39,542
    Checksum:i13170DD8F989B341
    GO
    Isoform 3 (identifier: P02774-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-1: M → MLWSWSEERGGAARLSGRKM

    Note: No experimental confirmation available.

    Show »
    Length:493
    Mass (Da):55,123
    Checksum:iC4738F41F3B76713
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti168 – 1681G → E in AAA52173. (PubMed:2416779)Curated
    Sequence conflicti183 – 1831L → P in AK309595. (PubMed:14702039)Curated
    Sequence conflicti327 – 3271E → R in AAA52173. (PubMed:2416779)Curated

    Polymorphismi

    Over 80 variants of human DBP have been identified. The three most common alleles are called GC*1F, GC*1S, and GC*2. The sequence shown is that of the GC*2 allele.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti432 – 4321D → E in allele GC*1S. 6 Publications
    Corresponds to variant rs7041 [ dbSNP | Ensembl ].
    VAR_000548
    Natural varianti436 – 4361K → T in allele GC*1F, allele GC*1A1 and allele GC*1S. 9 Publications
    Corresponds to variant rs4588 [ dbSNP | Ensembl ].
    VAR_000549
    Natural varianti445 – 4451R → C in allele GC*2A9. 1 Publication
    VAR_014120
    Natural varianti445 – 4451R → H in allele GC*1A1. 3 Publications
    Corresponds to variant rs9016 [ dbSNP | Ensembl ].
    VAR_014121

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 122122Missing in isoform 2. 1 PublicationVSP_038427Add
    BLAST
    Alternative sequencei1 – 11M → MLWSWSEERGGAARLSGRKM in isoform 3. 1 PublicationVSP_044523

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12654 mRNA. Translation: AAA52173.1.
    X03178 mRNA. Translation: CAA26938.1.
    S67480
    , S67474, S67476, S67478, S67479, S67526 Genomic DNA. Translation: AAB29423.1.
    L10641 Genomic DNA. Translation: AAA61704.1.
    AK290827 mRNA. Translation: BAF83516.1.
    AK298433 mRNA. Translation: BAG60654.1. Sequence problems.
    AK309595 mRNA. No translation available.
    AK315853 mRNA. Translation: BAF98744.1.
    AK223458 mRNA. Translation: BAD97178.1.
    AC024722 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05645.1.
    BC057228 mRNA. Translation: AAH57228.1.
    M17156 Genomic DNA. Translation: AAA19662.2.
    S77129 Genomic DNA. Translation: AAD14249.1. Sequence problems.
    S77130 Genomic DNA. Translation: AAD14250.1. Sequence problems.
    CCDSiCCDS3550.1. [P02774-1]
    CCDS56332.1. [P02774-3]
    PIRiA94076. VYHUD.
    RefSeqiNP_000574.2. NM_000583.3.
    NP_001191235.1. NM_001204306.1.
    NP_001191236.1. NM_001204307.1.
    UniGeneiHs.418497.

    Genome annotation databases

    EnsembliENST00000273951; ENSP00000273951; ENSG00000145321.
    ENST00000504199; ENSP00000421725; ENSG00000145321.
    GeneIDi2638.
    KEGGihsa:2638.

    Polymorphism databases

    DMDMi139641.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M12654 mRNA. Translation: AAA52173.1 .
    X03178 mRNA. Translation: CAA26938.1 .
    S67480
    , S67474 , S67476 , S67478 , S67479 , S67526 Genomic DNA. Translation: AAB29423.1 .
    L10641 Genomic DNA. Translation: AAA61704.1 .
    AK290827 mRNA. Translation: BAF83516.1 .
    AK298433 mRNA. Translation: BAG60654.1 . Sequence problems.
    AK309595 mRNA. No translation available.
    AK315853 mRNA. Translation: BAF98744.1 .
    AK223458 mRNA. Translation: BAD97178.1 .
    AC024722 Genomic DNA. No translation available.
    CH471057 Genomic DNA. Translation: EAX05645.1 .
    BC057228 mRNA. Translation: AAH57228.1 .
    M17156 Genomic DNA. Translation: AAA19662.2 .
    S77129 Genomic DNA. Translation: AAD14249.1 . Sequence problems.
    S77130 Genomic DNA. Translation: AAD14250.1 . Sequence problems.
    CCDSi CCDS3550.1. [P02774-1 ]
    CCDS56332.1. [P02774-3 ]
    PIRi A94076. VYHUD.
    RefSeqi NP_000574.2. NM_000583.3.
    NP_001191235.1. NM_001204306.1.
    NP_001191236.1. NM_001204307.1.
    UniGenei Hs.418497.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1J78 X-ray 2.31 A/B 17-474 [» ]
    1J7E X-ray 2.55 A/B 17-474 [» ]
    1KW2 X-ray 2.15 A/B 17-474 [» ]
    1KXP X-ray 2.10 D 17-474 [» ]
    1LOT X-ray 2.50 A 17-474 [» ]
    1MA9 X-ray 2.40 A 17-474 [» ]
    ProteinModelPortali P02774.
    SMRi P02774. Positions 20-474.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 108908. 10 interactions.
    DIPi DIP-17038N.
    IntActi P02774. 7 interactions.
    MINTi MINT-239255.
    STRINGi 9606.ENSP00000273951.

    Chemistry

    BindingDBi P02774.
    ChEMBLi CHEMBL2259.
    DrugBanki DB01436. Alfacalcidol.
    DB00169. Cholecalciferol.

    PTM databases

    PhosphoSitei P02774.
    UniCarbKBi P02774.

    Polymorphism databases

    DMDMi 139641.

    2D gel databases

    DOSAC-COBS-2DPAGE P02774.
    REPRODUCTION-2DPAGE IPI00555812.
    P02774.
    SWISS-2DPAGE P02774.

    Proteomic databases

    MaxQBi P02774.
    PaxDbi P02774.
    PeptideAtlasi P02774.
    PRIDEi P02774.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000273951 ; ENSP00000273951 ; ENSG00000145321 .
    ENST00000504199 ; ENSP00000421725 ; ENSG00000145321 .
    GeneIDi 2638.
    KEGGi hsa:2638.

    Organism-specific databases

    CTDi 2638.
    GeneCardsi GC04M072596.
    HGNCi HGNC:4187. GC.
    HPAi CAB008596.
    HPA001526.
    HPA019855.
    MIMi 139200. gene+phenotype.
    neXtProti NX_P02774.
    PharmGKBi PA28601.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40465.
    HOGENOMi HOG000140946.
    HOVERGENi HBG009729.
    InParanoidi P02774.
    KOi K12258.
    OrthoDBi EOG7B05CR.
    PhylomeDBi P02774.
    TreeFami TF335561.

    Enzyme and pathway databases

    Reactomei REACT_13523. Vitamin D (calciferol) metabolism.

    Miscellaneous databases

    EvolutionaryTracei P02774.
    GeneWikii Vitamin_D-binding_protein.
    GenomeRNAii 2638.
    NextBioi 10400.
    PROi P02774.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P02774.
    Bgeei P02774.
    CleanExi HS_GC.
    Genevestigatori P02774.

    Family and domain databases

    InterProi IPR000264. ALB/AFP/VDB.
    IPR020858. Serum_albumin-like.
    IPR020857. Serum_albumin_CS.
    IPR014760. Serum_albumin_N.
    IPR000213. VitD-bd.
    IPR015247. VitD-bind_III.
    [Graphical view ]
    Pfami PF00273. Serum_albumin. 2 hits.
    PF09164. VitD-bind_III. 1 hit.
    [Graphical view ]
    PRINTSi PR00802. SERUMALBUMIN.
    PR00804. VITAMNDBNDNG.
    SMARTi SM00103. ALBUMIN. 2 hits.
    [Graphical view ]
    SUPFAMi SSF48552. SSF48552. 3 hits.
    PROSITEi PS00212. ALBUMIN_1. 1 hit.
    PS51438. ALBUMIN_2. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Serum vitamin D-binding protein is a third member of the albumin and alpha fetoprotein gene family."
      Cooke N.E., David E.V.
      J. Clin. Invest. 76:2420-2424(1985) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS GLU-432 AND THR-436.
    2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    3. "Sequence and organization of the human vitamin D-binding protein gene."
      Braun A., Kofler A., Morawietz S., Cleve H.
      Biochim. Biophys. Acta 1216:385-394(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-432 AND THR-436.
    4. "Complete structure of the human Gc gene: differences and similarities between members of the albumin gene family."
      Witke W.F., Gibbs P.E., Zielinski R., Yang F., Bowman B.H., Dugaiczyk A.
      Genomics 16:751-754(1993) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS GLU-432 AND THR-436.
    5. "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] (ISOFORMS 1 AND 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-47 (ISOFORM 2), VARIANTS GLU-432; THR-436 AND HIS-445.
      Tissue: Liver.
    6. 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] (ISOFORM 1), VARIANTS GLU-432 AND THR-436.
      Tissue: Kidney.
    7. "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], VARIANTS THR-436 AND HIS-445.
    8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANTS GLU-432 AND THR-436.
    9. "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), VARIANT THR-436.
      Tissue: Liver.
    10. "The vitamin D-binding protein gene contains conserved nucleotide sequences that respond to heavy metal, adipocyte and mitotic signals."
      Yang F., Naberhaus K.H., Adrian G.S., Gardella J.M., Brissenden J.E., Bowman B.H.
      Gene 54:285-290(1987) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-19.
    11. "Complete amino acid sequence of human vitamin D-binding protein (group-specific component): evidence of a three-fold internal homology as in serum albumin and alpha-fetoprotein."
      Schoentgen F., Metz-Boutigue M.-H., Jolles J., Constans J., Jolles P.
      Biochim. Biophys. Acta 871:189-198(1986) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-474.
    12. "Molecular basis for the three major forms of human serum vitamin D binding protein (group-specific component)."
      Svasti J., Kurosky A., Bennett A., Bowman B.H.
      Biochemistry 18:1611-1617(1979) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 17-31 AND 431-441.
    13. "Characterization of mutants of the vitamin-D-binding protein/group specific component: GC aborigine (1A1) from Australian aborigines and South African blacks, and 2A9 from south Germany."
      Kofler A., Braun A., Jenkins T., Serjeantson S.W., Cleve H.
      Vox Sang. 68:50-54(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 430-446, VARIANTS GC*1A1 THR-436 AND HIS-445, VARIANT GC*2A9 CYS-445.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. "Molecular analysis of the gene for the human vitamin-D-binding protein (group-specific component): allelic differences of the common genetic GC types."
      Braun A., Bichlmaier R., Cleve H.
      Hum. Genet. 89:401-406(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS GC*2; GC*1F AND GC*1S.
    16. "A structural basis for the unique binding features of the human vitamin D-binding protein."
      Verboven C., Rabijns A., De Maeyer M., Van Baelen H., Bouillon R., De Ranter C.
      Nat. Struct. Biol. 9:131-136(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.31 ANGSTROMS) OF 29-473.

    Entry informationi

    Entry nameiVTDB_HUMAN
    AccessioniPrimary (citable) accession number: P02774
    Secondary accession number(s): B4DPP2
    , D6RAK8, Q16309, Q16310, Q53F31, Q6GTG1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 21, 1986
    Last sequence update: July 21, 1986
    Last modified: October 1, 2014
    This is version 168 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. 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