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P02753

- RET4_HUMAN

UniProt

P02753 - RET4_HUMAN

Protein

Retinol-binding protein 4

Gene

RBP4

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 176 (01 Oct 2014)
      Sequence version 3 (29 Mar 2005)
      Previous versions | rss
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    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. protein binding Source: UniProtKB
    2. retinal binding Source: UniProtKB-KW
    3. retinol binding Source: BHF-UCL
    4. 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

    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: UniProt
    5. protein complex Source: Ensembl

    Keywords - Cellular componenti

    Secreted

    Pathology & Biotechi

    Involvement in diseasei

    Retinal dystrophy, iris coloboma, and comedogenic acne syndrome (RDCCAS) [MIM:615147]: A 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.2 Publications
    Note: 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).1 Publication
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti59 – 591I → N in RDCCAS. 1 Publication
    Corresponds to variant rs121918584 [ dbSNP | Ensembl ].
    VAR_009276
    Natural varianti93 – 931G → D in RDCCAS. 1 Publication
    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.
    GenevestigatoriP02753.

    Organism-specific databases

    HPAiCAB004555.
    HPA001641.

    Interactioni

    Binary interactionsi

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

    Protein-protein interaction databases

    BioGridi111884. 6 interactions.
    IntActiP02753. 4 interactions.
    STRINGi9606.ENSP00000360519.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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[»]
    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.
    HOVERGENiHBG004493.
    InParanoidiP02753.
    KOiK18271.
    OMAiRYSGTWY.
    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

    MKWVWALLLL AALGSGRAER DCRVSSFRVK ENFDKARFSG TWYAMAKKDP    50
    EGLFLQDNIV AEFSVDETGQ MSATAKGRVR LLNNWDVCAD MVGTFTDTED 100
    PAKFKMKYWG VASFLQKGND DHWIVDTDYD TYAVQYSCRL LNLDGTCADS 150
    YSFVFSRDPN GLPPEAQKIV RQRQEELCLA RQYRLIVHNG YCDGRSERNL 200
    L 201
    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.

    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. 1 Publication
    Corresponds to variant rs121918584 [ dbSNP | Ensembl ].
    VAR_009276
    Natural varianti93 – 931G → D in RDCCAS. 1 Publication
    Corresponds to variant rs121918585 [ dbSNP | Ensembl ].
    VAR_009277

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS31249.1.
    PIRi A93494. VAHU.
    RefSeqi NP_006735.2. NM_006744.3.
    UniGenei Hs.50223.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BRP X-ray 2.50 A 19-200 [» ]
    1BRQ X-ray 2.50 A 19-200 [» ]
    1JYD X-ray 1.70 A 19-200 [» ]
    1JYJ X-ray 2.00 A 19-200 [» ]
    1QAB X-ray 3.20 E/F 22-201 [» ]
    1RBP X-ray 2.00 A 19-200 [» ]
    1RLB X-ray 3.10 E/F 19-192 [» ]
    2WQ9 X-ray 1.65 A 19-192 [» ]
    2WQA X-ray 2.85 E/F 19-194 [» ]
    2WR6 X-ray 1.80 A 19-192 [» ]
    3BSZ X-ray 3.38 E/F 19-194 [» ]
    3FMZ X-ray 2.90 A/B 19-201 [» ]
    ProteinModelPortali P02753.
    SMRi P02753. Positions 19-192.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111884. 6 interactions.
    IntActi P02753. 4 interactions.
    STRINGi 9606.ENSP00000360519.

    Chemistry

    BindingDBi P02753.
    ChEMBLi CHEMBL3100.
    DrugBanki DB00162. Vitamin A.

    PTM databases

    PhosphoSitei P02753.

    Polymorphism databases

    DMDMi 62298174.

    2D gel databases

    SWISS-2DPAGE P02753.

    Proteomic databases

    MaxQBi P02753.
    PaxDbi P02753.
    PRIDEi P02753.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000371464 ; ENSP00000360519 ; ENSG00000138207 .
    ENST00000371467 ; ENSP00000360522 ; ENSG00000138207 .
    GeneIDi 5950.
    KEGGi hsa:5950.
    UCSCi uc001kit.3. human.

    Organism-specific databases

    CTDi 5950.
    GeneCardsi GC10M095341.
    H-InvDB HIX0009047.
    HGNCi HGNC:9922. RBP4.
    HPAi CAB004555.
    HPA001641.
    MIMi 180250. gene.
    615147. phenotype.
    neXtProti NX_P02753.
    Orphaneti 352718. Progressive retinal dystrophy due to retinol transport defect.
    PharmGKBi PA34289.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG40507.
    HOVERGENi HBG004493.
    InParanoidi P02753.
    KOi K18271.
    OMAi RYSGTWY.
    OrthoDBi EOG747PK3.
    PhylomeDBi P02753.
    TreeFami TF331445.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000138207-MONOMER.
    Reactomei REACT_160130. Retinoid cycle disease events.
    REACT_160156. The canonical retinoid cycle in rods (twilight vision).
    REACT_24968. Retinoid metabolism and transport.

    Miscellaneous databases

    ChiTaRSi RBP4. human.
    EvolutionaryTracei P02753.
    GeneWikii Retinol_binding_protein_4.
    GenomeRNAii 5950.
    NextBioi 23182.
    PROi P02753.
    SOURCEi Search...

    Gene expression databases

    Bgeei P02753.
    CleanExi HS_RBP4.
    Genevestigatori P02753.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR002345. Lipocalin.
    IPR022271. Lipocalin_ApoD.
    IPR022272. Lipocalin_CS.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    IPR002449. Retinol-bd/Purpurin.
    [Graphical view ]
    PANTHERi PTHR11873. PTHR11873. 1 hit.
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PIRSFi PIRSF036893. Lipocalin_ApoD. 1 hit.
    PIRSF500204. RBP_purpurin. 1 hit.
    PRINTSi PR00179. LIPOCALIN.
    PR01174. RETINOLBNDNG.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00213. LIPOCALIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. "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).
    16. "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).
    17. "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.
    18. "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.
    19. "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.
    20. "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: October 1, 2014
    This is version 176 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