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Protein

Retinol-binding protein 4

Gene

RBP4

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

Functioni

Delivers retinol from the liver stores to the peripheral tissues. In plasma, the RBP-retinol complex interacts with transthyretin, this prevents its loss by filtration through the kidney glomeruli.

GO - Molecular functioni

  1. retinal binding Source: UniProtKB-KW
  2. retinol binding Source: BHF-UCL
  3. retinol transporter activity Source: BHF-UCL

GO - Biological processi

  1. cardiac muscle tissue development Source: BHF-UCL
  2. detection of light stimulus involved in visual perception Source: Ensembl
  3. embryonic organ morphogenesis Source: BHF-UCL
  4. embryonic retina morphogenesis in camera-type eye Source: BHF-UCL
  5. embryonic skeletal system development Source: BHF-UCL
  6. eye development Source: BHF-UCL
  7. female genitalia morphogenesis Source: BHF-UCL
  8. gluconeogenesis Source: BHF-UCL
  9. glucose homeostasis Source: BHF-UCL
  10. heart development Source: BHF-UCL
  11. heart trabecula formation Source: BHF-UCL
  12. lung development Source: BHF-UCL
  13. maintenance of gastrointestinal epithelium Source: BHF-UCL
  14. male gonad development Source: Ensembl
  15. negative regulation of cardiac muscle cell proliferation Source: BHF-UCL
  16. phototransduction, visible light Source: Reactome
  17. positive regulation of immunoglobulin secretion Source: BHF-UCL
  18. positive regulation of insulin secretion Source: BHF-UCL
  19. response to ethanol Source: Ensembl
  20. response to insulin Source: Ensembl
  21. response to retinoic acid Source: BHF-UCL
  22. retinal metabolic process Source: Ensembl
  23. retinoid metabolic process Source: Reactome
  24. retinol metabolic process Source: BHF-UCL
  25. retinol transport Source: BHF-UCL
  26. spermatogenesis Source: Ensembl
  27. urinary bladder development Source: BHF-UCL
  28. uterus development Source: BHF-UCL
  29. vagina development Source: BHF-UCL
Complete GO annotation...

Keywords - Biological processi

Sensory transduction, Transport, Vision

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138207-MONOMER.
ReactomeiREACT_160130. Retinoid cycle disease events.
REACT_160156. The canonical retinoid cycle in rods (twilight vision).
REACT_24968. Retinoid metabolism and transport.

Names & Taxonomyi

Protein namesi
Recommended name:
Retinol-binding protein 4
Alternative name(s):
Plasma retinol-binding protein
Short name:
PRBP
Short name:
RBP
Cleaved into the following 4 chains:
Gene namesi
Name:RBP4
ORF Names:PRO2222
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 10

Organism-specific databases

HGNCiHGNC:9922. RBP4.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Reactome
  2. extracellular region Source: Reactome
  3. extracellular space Source: BHF-UCL
  4. extracellular vesicular exosome Source: UniProtKB
  5. protein complex Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Secreted

Pathology & Biotechi

Involvement in diseasei

Retinal dystrophy, iris coloboma, and comedogenic acne syndrome2 Publications

The disease is caused by mutations affecting the gene represented in this entry. Loss of functional RBP4 protein results in serum retinol deficiency. Lack of normal levels of retinol impairs the visual cycle leading to night blindness at early stages; prolonged deficiency may lead to retinal degeneration. Additionally, retinol deficiency may result in dry skin, increased susceptibility to infection and acne (PubMed:23189188).

Disease descriptionA disease characterized by retinal degeneration, ocular colobomas involving both the anterior and posterior segment, impaired night vision and loss of visual acuity. Additional characteristic features include developmental abnormalities and severe acne.

See also OMIM:615147
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591I → N in RDCCAS. 2 Publications
Corresponds to variant rs121918584 [ dbSNP | Ensembl ].
VAR_009276
Natural varianti93 – 931G → D in RDCCAS. 2 Publications
Corresponds to variant rs121918585 [ dbSNP | Ensembl ].
VAR_009277

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi615147. phenotype.
Orphaneti352718. Progressive retinal dystrophy due to retinol transport defect.
PharmGKBiPA34289.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 18183 PublicationsAdd
BLAST
Chaini19 – 201183Retinol-binding protein 4PRO_0000017961Add
BLAST
Chaini19 – 200182Plasma retinol-binding protein(1-182)PRO_0000017962Add
BLAST
Chaini19 – 199181Plasma retinol-binding protein(1-181)PRO_0000017963Add
BLAST
Chaini19 – 197179Plasma retinol-binding protein(1-179)PRO_0000017964Add
BLAST
Chaini19 – 194176Plasma retinol-binding protein(1-176)PRO_0000017965Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi22 ↔ 1781 Publication
Disulfide bondi88 ↔ 1921 Publication
Disulfide bondi138 ↔ 1471 Publication

Keywords - PTMi

Disulfide bond

Proteomic databases

MaxQBiP02753.
PaxDbiP02753.
PRIDEiP02753.

2D gel databases

SWISS-2DPAGEP02753.

PTM databases

PhosphoSiteiP02753.

Expressioni

Gene expression databases

BgeeiP02753.
CleanExiHS_RBP4.
ExpressionAtlasiP02753. baseline and differential.
GenevestigatoriP02753.

Organism-specific databases

HPAiCAB004555.
HPA001641.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
TTRO552452EBI-2116134,EBI-7038226From a different organism.

Protein-protein interaction databases

BioGridi111884. 4 interactions.
IntActiP02753. 4 interactions.
STRINGi9606.ENSP00000360519.

Structurei

Secondary structure

1
201
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi24 – 263Combined sources
Helixi35 – 384Combined sources
Beta strandi40 – 489Combined sources
Beta strandi51 – 533Combined sources
Beta strandi55 – 6511Combined sources
Beta strandi67 – 693Combined sources
Beta strandi71 – 8010Combined sources
Beta strandi82 – 843Combined sources
Beta strandi86 – 9712Combined sources
Beta strandi103 – 11210Combined sources
Beta strandi118 – 12710Combined sources
Beta strandi129 – 14113Combined sources
Beta strandi145 – 15814Combined sources
Helixi164 – 17613Combined sources
Turni180 – 1823Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BRPX-ray2.50A19-200[»]
1BRQX-ray2.50A19-200[»]
1JYDX-ray1.70A19-200[»]
1JYJX-ray2.00A19-200[»]
1QABX-ray3.20E/F22-201[»]
1RBPX-ray2.00A19-200[»]
1RLBX-ray3.10E/F19-192[»]
2WQ9X-ray1.65A19-192[»]
2WQAX-ray2.85E/F19-194[»]
2WR6X-ray1.80A19-192[»]
3BSZX-ray3.38E/F19-194[»]
3FMZX-ray2.90A/B19-201[»]
4O9SX-ray2.30A/B19-201[»]
4PSQX-ray2.40A/B19-201[»]
ProteinModelPortaliP02753.
SMRiP02753. Positions 19-192.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP02753.

Family & Domainsi

Sequence similaritiesi

Belongs to the calycin superfamily. Lipocalin family.Curated

Keywords - Domaini

Signal

Phylogenomic databases

eggNOGiNOG40507.
GeneTreeiENSGT00510000047107.
HOVERGENiHBG004493.
InParanoidiP02753.
KOiK18271.
OMAiTWYAVAK.
OrthoDBiEOG747PK3.
PhylomeDBiP02753.
TreeFamiTF331445.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]
PANTHERiPTHR11873. PTHR11873. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSiPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P02753-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MKWVWALLLL AALGSGRAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP
60 70 80 90 100
EGLFLQDNIV AEFSVDETGQ MSATAKGRVR LLNNWDVCAD MVGTFTDTED
110 120 130 140 150
PAKFKMKYWG VASFLQKGND DHWIVDTDYD TYAVQYSCRL LNLDGTCADS
160 170 180 190 200
YSFVFSRDPN GLPPEAQKIV RQRQEELCLA RQYRLIVHNG YCDGRSERNL

L
Length:201
Mass (Da):23,010
Last modified:March 29, 2005 - v3
Checksum:i660C6DD8CC9B811A
GO

Sequence cautioni

The sequence AAF69622.1 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti8 – 81L → F in AAH20633 (PubMed:15489334).Curated
Sequence conflicti13 – 175LGSGR → WAA (PubMed:6316270).Curated
Sequence conflicti13 – 175LGSGR → WAA (PubMed:2998779).Curated

Mass spectrometryi

Molecular mass is 21063.46±1.88 Da from positions 17 - 199. Determined by ESI. 1 Publication
Molecular mass is 20534 Da from positions 19 - 197. Determined by MALDI. 1 Publication
Molecular mass is 20162 Da from positions 19 - 194. Determined by MALDI. 1 Publication

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti59 – 591I → N in RDCCAS. 2 Publications
Corresponds to variant rs121918584 [ dbSNP | Ensembl ].
VAR_009276
Natural varianti93 – 931G → D in RDCCAS. 2 Publications
Corresponds to variant rs121918585 [ dbSNP | Ensembl ].
VAR_009277

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00129 mRNA. Translation: CAA24959.1.
AL356214 Genomic DNA. Translation: CAH72328.1.
CH471066 Genomic DNA. Translation: EAW50065.1.
CH471066 Genomic DNA. Translation: EAW50066.1.
CH471066 Genomic DNA. Translation: EAW50067.1.
BC020633 mRNA. Translation: AAH20633.1.
X02775 Genomic DNA. Translation: CAA26553.1.
X02824 Genomic DNA. Translation: CAB46489.1.
AF119868 mRNA. Translation: AAF69622.1. Different initiation.
AF025334 Genomic DNA. Translation: AAC02945.1.
AF025335 Genomic DNA. Translation: AAC02946.1.
CCDSiCCDS31249.1.
PIRiA93494. VAHU.
RefSeqiNP_006735.2. NM_006744.3.
UniGeneiHs.50223.

Genome annotation databases

EnsembliENST00000371464; ENSP00000360519; ENSG00000138207.
ENST00000371467; ENSP00000360522; ENSG00000138207.
GeneIDi5950.
KEGGihsa:5950.
UCSCiuc001kit.3. human.

Polymorphism databases

DMDMi62298174.

Cross-referencesi

Web resourcesi

Mutations of the RBP4 gene

Retina International's Scientific Newsletter

Wikipedia

Retinol-binding protein 4 entry

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X00129 mRNA. Translation: CAA24959.1.
AL356214 Genomic DNA. Translation: CAH72328.1.
CH471066 Genomic DNA. Translation: EAW50065.1.
CH471066 Genomic DNA. Translation: EAW50066.1.
CH471066 Genomic DNA. Translation: EAW50067.1.
BC020633 mRNA. Translation: AAH20633.1.
X02775 Genomic DNA. Translation: CAA26553.1.
X02824 Genomic DNA. Translation: CAB46489.1.
AF119868 mRNA. Translation: AAF69622.1. Different initiation.
AF025334 Genomic DNA. Translation: AAC02945.1.
AF025335 Genomic DNA. Translation: AAC02946.1.
CCDSiCCDS31249.1.
PIRiA93494. VAHU.
RefSeqiNP_006735.2. NM_006744.3.
UniGeneiHs.50223.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1BRPX-ray2.50A19-200[»]
1BRQX-ray2.50A19-200[»]
1JYDX-ray1.70A19-200[»]
1JYJX-ray2.00A19-200[»]
1QABX-ray3.20E/F22-201[»]
1RBPX-ray2.00A19-200[»]
1RLBX-ray3.10E/F19-192[»]
2WQ9X-ray1.65A19-192[»]
2WQAX-ray2.85E/F19-194[»]
2WR6X-ray1.80A19-192[»]
3BSZX-ray3.38E/F19-194[»]
3FMZX-ray2.90A/B19-201[»]
4O9SX-ray2.30A/B19-201[»]
4PSQX-ray2.40A/B19-201[»]
ProteinModelPortaliP02753.
SMRiP02753. Positions 19-192.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111884. 4 interactions.
IntActiP02753. 4 interactions.
STRINGi9606.ENSP00000360519.

Chemistry

BindingDBiP02753.
ChEMBLiCHEMBL3100.
DrugBankiDB00162. Vitamin A.

PTM databases

PhosphoSiteiP02753.

Polymorphism databases

DMDMi62298174.

2D gel databases

SWISS-2DPAGEP02753.

Proteomic databases

MaxQBiP02753.
PaxDbiP02753.
PRIDEiP02753.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371464; ENSP00000360519; ENSG00000138207.
ENST00000371467; ENSP00000360522; ENSG00000138207.
GeneIDi5950.
KEGGihsa:5950.
UCSCiuc001kit.3. human.

Organism-specific databases

CTDi5950.
GeneCardsiGC10M095341.
H-InvDBHIX0009047.
HGNCiHGNC:9922. RBP4.
HPAiCAB004555.
HPA001641.
MIMi180250. gene.
615147. phenotype.
neXtProtiNX_P02753.
Orphaneti352718. Progressive retinal dystrophy due to retinol transport defect.
PharmGKBiPA34289.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG40507.
GeneTreeiENSGT00510000047107.
HOVERGENiHBG004493.
InParanoidiP02753.
KOiK18271.
OMAiTWYAVAK.
OrthoDBiEOG747PK3.
PhylomeDBiP02753.
TreeFamiTF331445.

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000138207-MONOMER.
ReactomeiREACT_160130. Retinoid cycle disease events.
REACT_160156. The canonical retinoid cycle in rods (twilight vision).
REACT_24968. Retinoid metabolism and transport.

Miscellaneous databases

ChiTaRSiRBP4. human.
EvolutionaryTraceiP02753.
GeneWikiiRetinol_binding_protein_4.
GenomeRNAii5950.
NextBioi23182.
PROiP02753.
SOURCEiSearch...

Gene expression databases

BgeeiP02753.
CleanExiHS_RBP4.
ExpressionAtlasiP02753. baseline and differential.
GenevestigatoriP02753.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR002345. Lipocalin.
IPR022271. Lipocalin_ApoD.
IPR022272. Lipocalin_CS.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
IPR002449. Retinol-bd/Purpurin.
[Graphical view]
PANTHERiPTHR11873. PTHR11873. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PIRSFiPIRSF036893. Lipocalin_ApoD. 1 hit.
PIRSF500204. RBP_purpurin. 1 hit.
PRINTSiPR00179. LIPOCALIN.
PR01174. RETINOLBNDNG.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00213. LIPOCALIN. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and sequencing of a full length cDNA coding for human retinol-binding protein."
    Colantuoni V., Romano V., Bensi G., Santoro C., Costanzo F., Raugei G., Cortese R.
    Nucleic Acids Res. 11:7769-7776(1983) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "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: Liver.
  5. "Structure and cell-specific expression of a cloned human retinol binding protein gene: the 5'-flanking region contains hepatoma specific transcriptional signals."
    D'Onofrio C., Colantuoni V., Cortese R.
    EMBO J. 4:1981-1989(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-189.
  6. "The complete amino acid sequence of human serum retinol-binding protein."
    Rask L., Anundi H., Fohlman J., Peterson P.A.
    Ups. J. Med. Sci. 92:115-146(1987) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-201, DISULFIDE BONDS.
  7. "Structural and functional studies of vitamin A-binding proteins."
    Rask L., Anundi H., Boehme J., Eriksson U., Ronne H., Sege K., Peterson P.A.
    Ann. N. Y. Acad. Sci. 359:79-90(1981) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-201.
  8. "The primary structure of the human retinol-binding protein."
    Rask L., Anundi H., Peterson P.A.
    FEBS Lett. 104:55-58(1979) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 19-183.
  9. "Functional prediction of the coding sequences of 79 new genes deduced by analysis of cDNA clones from human fetal liver."
    Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 18-201.
    Tissue: Fetal liver.
  10. "Characterization of two post-translationally processed forms of human serum retinol-binding protein: altered ratios in chronic renal failure."
    Jaconi S., Rose K., Hughes G.J., Saurat J.-H., Siegenthaler G.
    J. Lipid Res. 36:1247-1253(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: PARTIAL PROTEIN SEQUENCE, MASS SPECTROMETRY.
  11. "Comparative phenotypic analyses of human plasma and urinary retinol binding protein using mass spectrometric immunoassay."
    Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., Nelson R.W.
    Biochem. Biophys. Res. Commun. 297:401-405(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: MASS SPECTROMETRY.
  12. "Comparative urine protein phenotyping using mass spectrometric immunoassay."
    Kiernan U.A., Tubbs K.A., Nedelkov D., Niederkofler E.E., McConnell E., Nelson R.W.
    J. Proteome Res. 2:191-197(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY.
  13. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Exome analysis identified a novel mutation in the RBP4 gene in a consanguineous pedigree with retinal dystrophy and developmental abnormalities."
    Cukras C., Gaasterland T., Lee P., Gudiseva H.V., Chavali V.R., Pullakhandam R., Maranhao B., Edsall L., Soares S., Reddy G.B., Sieving P.A., Ayyagari R.
    PLoS ONE 7:E50205-E50205(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RDCCAS.
  15. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  16. "The three-dimensional structure of retinol-binding protein."
    Newcomer M.E., Jones T.A., Aqvist J., Sundelin J., Eriksson U., Rask L., Peterson P.A.
    EMBO J. 3:1451-1454(1984) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.1 ANGSTROMS).
  17. "Crystallographic refinement of human serum retinol binding protein at 2-A resolution."
    Cowan S.W., Newcomer M.E., Jones T.A.
    Proteins 8:44-61(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
  18. "Three-dimensional structure and active site of three hydrophobic molecule-binding proteins with significant amino acid sequence similarity."
    Monaco H.L., Zanotti G.
    Biopolymers 32:457-465(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: COMPARISON OF X-RAY STRUCTURES.
  19. "The structure of human retinol-binding protein (RBP) with its carrier protein transthyretin reveals an interaction with the carboxy terminus of RBP."
    Naylor H.M., Newcomer M.E.
    Biochemistry 38:2647-2653(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (3.2 ANGSTROMS) OF COMPLEX WITH TTR.
  20. "Phenotype in retinol deficiency due to a hereditary defect in retinol binding protein synthesis."
    Seeliger M.W., Biesalski H.K., Wissinger B., Gollnick H., Gielen S., Frank J., Beck S.C., Zrenner E.
    Invest. Ophthalmol. Vis. Sci. 40:3-11(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: VARIANTS RDCCAS ASN-59 AND ASP-93.
  21. "Biochemical but not clinical vitamin A deficiency results from mutations in the gene for retinol binding protein."
    Biesalski H.K., Frank J., Beck S.C., Heinrich F., Illek B., Reifen R., Gollnick H., Seeliger M.W., Wissinger B., Zrenner E.
    Am. J. Clin. Nutr. 69:931-936(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: CHARACTERIZATION OF VARIANTS RDCCAS ASN-59 AND ASP-93.

Entry informationi

Entry nameiRET4_HUMAN
AccessioniPrimary (citable) accession number: P02753
Secondary accession number(s): D3DR38
, O43478, O43479, Q5VY24, Q8WWA3, Q9P178
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 21, 1986
Last sequence update: March 29, 2005
Last modified: March 4, 2015
This is version 181 of the entry and version 3 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 10
    Human chromosome 10: 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.