Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P02774

- VTDB_HUMAN

UniProt

P02774 - VTDB_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

Vitamin D-binding protein

Gene

GC

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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
Complete GO annotation...

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: UniProtKB
  6. lysosomal lumen Source: Reactome
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Organism-specific databases

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

BgeeiP02774.
CleanExiHS_GC.
ExpressionAtlasiP02774. baseline and differential.
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 – 3513Combined sources
Helixi37 – 5115Combined sources
Helixi57 – 7418Combined sources
Beta strandi76 – 794Combined sources
Helixi83 – 9412Combined sources
Beta strandi97 – 993Combined sources
Helixi108 – 1114Combined sources
Helixi116 – 12510Combined sources
Helixi141 – 15010Combined sources
Helixi152 – 16615Combined sources
Helixi172 – 19019Combined sources
Beta strandi192 – 1943Combined sources
Helixi195 – 22632Combined sources
Helixi228 – 24215Combined sources
Helixi248 – 26518Combined sources
Helixi273 – 28917Combined sources
Turni290 – 2923Combined sources
Helixi294 – 2996Combined sources
Beta strandi302 – 3043Combined sources
Helixi305 – 31410Combined sources
Helixi331 – 3355Combined sources
Beta strandi336 – 3383Combined sources
Helixi340 – 35112Combined sources
Helixi358 – 37316Combined sources
Turni374 – 3774Combined sources
Helixi381 – 40626Combined sources
Turni407 – 4126Combined sources
Helixi415 – 42915Combined sources
Helixi435 – 45218Combined sources
Helixi459 – 47012Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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

        10         20         30         40         50
MKRVLVLLLA VAFGHALERG RDYEKNKVCK EFSHLGKEDF TSLSLVLYSR
60 70 80 90 100
KFPSGTFEQV SQLVKEVVSL TEACCAEGAD PDCYDTRTSA LSAKSCESNS
110 120 130 140 150
PFPVHPGTAE CCTKEGLERK LCMAALKHQP QEFPTYVEPT NDEICEAFRK
160 170 180 190 200
DPKEYANQFM WEYSTNYGQA PLSLLVSYTK SYLSMVGSCC TSASPTVCFL
210 220 230 240 250
KERLQLKHLS LLTTLSNRVC SQYAAYGEKK SRLSNLIKLA QKVPTADLED
260 270 280 290 300
VLPLAEDITN ILSKCCESAS EDCMAKELPE HTVKLCDNLS TKNSKFEDCC
310 320 330 340 350
QEKTAMDVFV CTYFMPAAQL PELPDVELPT NKDVCDPGNT KVMDKYTFEL
360 370 380 390 400
SRRTHLPEVF LSKVLEPTLK SLGECCDVED STTCFNAKGP LLKKELSSFI
410 420 430 440 450
DKGQELCADY SENTFTEYKK KLAERLKAKL PDATPKELAK LVNKRSDFAS
460 470
NCCSINSPPL YCDSEIDAEL KNIL
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:
EMBLi
GenBanki
DDBJi
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:
EMBLi
GenBanki
DDBJi
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:
PDBei
RCSB PDBi
PDBji
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.
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

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

Gene expression databases

Bgeei P02774.
CleanExi HS_GC.
ExpressionAtlasi P02774. baseline and differential.
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

« Hide 'large scale' publications
  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: November 26, 2014
This is version 170 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