P02774 (VTDB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Vitamin D-binding protein
Short name=DBP
Short name=VDB

Alternative name(s):
Gc-globulin
Group-specific component

Gene names

Name:

GC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	474 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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.
Subcellular location	Secreted.
Polymorphism	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.
Sequence similarities	Belongs to the ALB/AFP/VDB family. Contains 3 albumin domains.
Sequence caution	The sequence BAG60654.1 differs from that shown. Reason: Erroneous translation. Wrong choice of CDS.

Ontologies

Keywords
Biological process	Transport
Cellular component	Secreted
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Repeat Signal
Ligand	Actin-binding Vitamin D
PTM	Disulfide bond Glycoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	vitamin D metabolic process Traceable author statement. Source: Reactome vitamin transport Traceable author statement PubMed 1696927. Source: ProtInc
Cellular_component	cytosol Traceable author statement. Source: Reactome extracellular region Non-traceable author statement PubMed 14718574. Source: UniProtKB extracellular space Inferred from electronic annotation. Source: InterPro lysosomal lumen Traceable author statement. Source: Reactome
Molecular_function	vitamin D binding Traceable author statement PubMed 1696927. Source: ProtInc vitamin transporter activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P02774-1)

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.

Isoform 2 (identifier: P02774-2)

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.

Isoform 3 (identifier: P02774-3)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Signal peptide

1 – 16

16

Ref.11 Ref.12

Chain

17 – 474

458

Vitamin D-binding protein

PRO_0000001102

Regions

Domain

17 – 208

192

Albumin 1

Domain

209 – 394

186

Albumin 2

Domain

395 – 474

80

Albumin 3

Amino acid modifications

Glycosylation

288

1

N-linked (GlcNAc...) Potential

Disulfide bond

29 ↔ 75

Disulfide bond

74 ↔ 83

By similarity

Disulfide bond

96 ↔ 112

Disulfide bond

111 ↔ 122

Disulfide bond

145 ↔ 190

Disulfide bond

189 ↔ 198

Disulfide bond

220 ↔ 266

Disulfide bond

265 ↔ 273

Disulfide bond

286 ↔ 300

Disulfide bond

299 ↔ 311

Disulfide bond

335 ↔ 376

Disulfide bond

375 ↔ 384

Disulfide bond

407 ↔ 453

Disulfide bond

452 ↔ 462

Natural variations

Alternative sequence

1 – 122

122

Missing in isoform 2.

VSP_038427

Alternative sequence

1

1

M → MLWSWSEERGGAARLSGRKM in isoform 3.

VSP_044523

Natural variant

432

1

D → E in allele GC*1S. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.8
Corresponds to variant rs7041 [ dbSNP | Ensembl ].

VAR_000548

Natural variant

436

1

K → T in allele GC*1F, allele GC*1A1 and allele GC*1S. Ref.1 Ref.3 Ref.4 Ref.5 Ref.6 Ref.7 Ref.8 Ref.9 Ref.13
Corresponds to variant rs4588 [ dbSNP | Ensembl ].

VAR_000549

Natural variant

445

1

R → C in allele GC*2A9. Ref.13

VAR_014120

Natural variant

445

1

R → H in allele GC*1A1. Ref.5 Ref.7 Ref.13
Corresponds to variant rs9016 [ dbSNP | Ensembl ].

VAR_014121

Experimental info

Sequence conflict

168

1

G → E in AAA52173. Ref.1

Sequence conflict

183

1

L → P in AK309595. Ref.5

Sequence conflict

327

1

E → R in AAA52173. Ref.1

Secondary structure

1

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474

Helix Strand Turn

Details...

Helix

23 – 35

13

Helix

37 – 51

15

Helix

57 – 74

18

Beta strand

76 – 79

4

Helix

83 – 94

12

Beta strand

97 – 99

3

Helix

108 – 111

4

Helix

116 – 125

10

Helix

141 – 150

10

Helix

152 – 166

15

Helix

172 – 190

19

Beta strand

192 – 194

3

Helix

195 – 226

32

Helix

228 – 242

15

Helix

248 – 265

18

Helix

273 – 289

17

Turn

290 – 292

3

Helix

294 – 299

6

Beta strand

302 – 304

3

Helix

305 – 314

10

Helix

331 – 335

5

Beta strand

336 – 338

3

Helix

340 – 351

12

Helix

358 – 373

16

Turn

374 – 377

4

Helix

381 – 406

26

Turn

407 – 412

6

Helix

415 – 429

15

Helix

435 – 452

18

Helix

459 – 470

12

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 21, 1986. Version 1. Checksum: 6AD8F163B551F1E4	FASTA	474	52,964
	10 20 30 40 50 60 MKRVLVLLLA VAFGHALERG RDYEKNKVCK EFSHLGKEDF TSLSLVLYSR KFPSGTFEQV 70 80 90 100 110 120 SQLVKEVVSL TEACCAEGAD PDCYDTRTSA LSAKSCESNS PFPVHPGTAE CCTKEGLERK 130 140 150 160 170 180 LCMAALKHQP QEFPTYVEPT NDEICEAFRK DPKEYANQFM WEYSTNYGQA PLSLLVSYTK 190 200 210 220 230 240 SYLSMVGSCC TSASPTVCFL KERLQLKHLS LLTTLSNRVC SQYAAYGEKK SRLSNLIKLA 250 260 270 280 290 300 QKVPTADLED VLPLAEDITN ILSKCCESAS EDCMAKELPE HTVKLCDNLS TKNSKFEDCC 310 320 330 340 350 360 QEKTAMDVFV CTYFMPAAQL PELPDVELPT NKDVCDPGNT KVMDKYTFEL SRRTHLPEVF 370 380 390 400 410 420 LSKVLEPTLK SLGECCDVED STTCFNAKGP LLKKELSSFI DKGQELCADY SENTFTEYKK 430 440 450 460 470 KLAERLKAKL PDATPKELAK LVNKRSDFAS NCCSINSPPL YCDSEIDAEL KNIL
	Isoform 2 [UniParc]. Checksum: 13170DD8F989B341	FASTA	352	39,542
	10 20 30 40 50 60 MAALKHQPQE FPTYVEPTND EICEAFRKDP KEYANQFMWE YSTNYGQAPL SLLVSYTKSY 70 80 90 100 110 120 LSMVGSCCTS ASPTVCFLKE RLQLKHLSLL TTLSNRVCSQ YAAYGEKKSR LSNLIKLAQK 130 140 150 160 170 180 VPTADLEDVL PLAEDITNIL SKCCESASED CMAKELPEHT VKLCDNLSTK NSKFEDCCQE 190 200 210 220 230 240 KTAMDVFVCT YFMPAAQLPE LPDVELPTNK DVCDPGNTKV MDKYTFELSR RTHLPEVFLS 250 260 270 280 290 300 KVLEPTLKSL GECCDVEDST TCFNAKGPLL KKELSSFIDK GQELCADYSE NTFTEYKKKL 310 320 330 340 350 AERLKAKLPD ATPKELAKLV NKRSDFASNC CSINSPPLYC DSEIDAELKN IL
	Isoform 3 [UniParc]. Checksum: C4738F41F3B76713	FASTA	493	55,123
	10 20 30 40 50 60 MLWSWSEERG GAARLSGRKM KRVLVLLLAV AFGHALERGR DYEKNKVCKE FSHLGKEDFT 70 80 90 100 110 120 SLSLVLYSRK FPSGTFEQVS QLVKEVVSLT EACCAEGADP DCYDTRTSAL SAKSCESNSP 130 140 150 160 170 180 FPVHPGTAEC CTKEGLERKL CMAALKHQPQ EFPTYVEPTN DEICEAFRKD PKEYANQFMW 190 200 210 220 230 240 EYSTNYGQAP LSLLVSYTKS YLSMVGSCCT SASPTVCFLK ERLQLKHLSL LTTLSNRVCS 250 260 270 280 290 300 QYAAYGEKKS RLSNLIKLAQ KVPTADLEDV LPLAEDITNI LSKCCESASE DCMAKELPEH 310 320 330 340 350 360 TVKLCDNLST KNSKFEDCCQ EKTAMDVFVC TYFMPAAQLP ELPDVELPTN KDVCDPGNTK 370 380 390 400 410 420 VMDKYTFELS RRTHLPEVFL SKVLEPTLKS LGECCDVEDS TTCFNAKGPL LKKELSSFID 430 440 450 460 470 480 KGQELCADYS ENTFTEYKKK LAERLKAKLP DATPKELAKL VNKRSDFASN CCSINSPPLY 490 CDSEIDAELK NIL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	"Human group-specific component (Gc) is a member of the albumin family." Yang F., Brune J.L., Naylor S.L., Cupples R.L., Naberhaus K.H., Bowman B.H. Proc. Natl. Acad. Sci. U.S.A. 82:7994-7998(1985) [PubMed] [Europe PMC] [Abstract] 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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00555812.
IPI00968027.

PIR

VYHUD. A94076.

RefSeq

NP_000574.2. NM_000583.3.
NP_001191235.1. NM_001204306.1.
NP_001191236.1. NM_001204307.1.

UniGene

Hs.418497.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P02774.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-17038N.

IntAct

P02774. 6 interactions.

MINT

MINT-239255.

STRING

9606.ENSP00000273951.

PTM databases

GlycoSuiteDB

P02774.

PhosphoSite

P02774.

Polymorphism databases

DMDM

139641.

2D gel databases

DOSAC-COBS-2DPAGE

P02774.

REPRODUCTION-2DPAGE

IPI00555812.
P02774.

SWISS-2DPAGE

P02774.

Proteomic databases

PaxDb

P02774.

PeptideAtlas

P02774.

PRIDE

P02774.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000273951; ENSP00000273951; ENSG00000145321.
ENST00000504199; ENSP00000421725; ENSG00000145321.

GeneID

2638.

KEGG

hsa:2638.

Organism-specific databases

CTD

2638.

GeneCards

GC04M072596.

HGNC

HGNC:4187. GC.

HPA

CAB008596.
HPA001526.
HPA019855.

MIM

139200. gene+phenotype.

neXtProt

NX_P02774.

PharmGKB

PA28601.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG40465.

HOGENOM

HOG000140946.

HOVERGEN

HBG009729.

InParanoid

P02774.

KO

K12258.

OrthoDB

EOG4MKNG5.

Enzyme and pathway databases

Reactome

REACT_111217. Metabolism.
REACT_15493. Steroid hormones.

Gene expression databases

ArrayExpress

P02774.

Bgee

P02774.

CleanEx

HS_GC.

Genevestigator

P02774.

GermOnline

ENSG00000145321. Homo sapiens.

Family and domain databases

InterPro

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]

Pfam

PF00273. Serum_albumin. 2 hits.
PF09164. VitD-bind_III. 1 hit.
[Graphical view]

PRINTS

PR00802. SERUMALBUMIN.
PR00804. VITAMNDBNDNG.

SMART

SM00103. ALBUMIN. 2 hits.
[Graphical view]

SUPFAM

SSF48552. Serum_albumin. 3 hits.

PROSITE

PS00212. ALBUMIN_1. 1 hit.
PS51438. ALBUMIN_2. 2 hits.
[Graphical view]

ProtoNet

Search...

Other

BindingDB

P02774.

ChEMBL

CHEMBL2259.

DrugBank

DB00169. Cholecalciferol.

EvolutionaryTrace

P02774.

GenomeRNAi

2638.

NextBio

10400.

SOURCE

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Entry information

Entry name

VTDB_HUMAN

Accession

Primary (citable) accession number: P02774
Secondary accession number(s): B4DPP2 , D6RAK8, Q16309, Q16310, Q53F31, Q6GTG1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 21, 1986
Last sequence update:	July 21, 1986
Last modified:	May 1, 2013
This is version 154 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.