Skip Header

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

UniProtKB - P09455 (RET1_HUMAN)

Protein

Retinol-binding protein 1

Gene

RBP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

Cytoplasmic retinol-binding protein (PubMed:22665496, PubMed:26900151, PubMed:28057518). Accepts retinol from the transport protein STRA6, and thereby contributes to retinol uptake, storage and retinoid homeostasis (PubMed:15632377, PubMed:22665496).4 Publications

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Function’ section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei41RetinolCombined sources1 Publication1
Binding sitei63RetinolCombined sources1 Publication1
Binding sitei109RetinolCombined sources2 Publications1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

  • all-trans-retinol binding Source: UniProtKB
  • retinal binding Source: UniProtKB-KW
  • retinoid binding Source: ProtInc
View the complete GO annotation on QuickGO ...

GO - Biological processi

  • lipid homeostasis Source: UniProtKB
  • retinoic acid biosynthetic process Source: InterPro
  • retinoid metabolic process Source: Reactome
  • vitamin A metabolic process Source: UniProtKB
View the complete GO annotation on QuickGO ...

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Biological processTransport
LigandRetinol-binding, Vitamin A

Enzyme and pathway databases

BioCyc Collection of Pathway/Genome Databases

More...BioCyci		MetaCyc:ENSG00000114115-MONOMER

Reactome - a knowledgebase of biological pathways and processes

More...Reactomei		R-HSA-2453864 Retinoid cycle disease events
R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-975634 Retinoid metabolism and transport

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Retinol-binding protein 1
Alternative name(s):
Cellular retinol-binding protein
Short name:
CRBP
Cellular retinol-binding protein I
Short name:
CRBP-I
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:RBP1
Synonyms:CRBP1
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiHomo sapiens (Human)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri9606 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000005640 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 3

Organism-specific databases

Eukaryotic Pathogen Database Resources

More...EuPathDBi		HostDB:ENSG00000114115.9

Human Gene Nomenclature Database

More...HGNCi		HGNC:9919 RBP1

Online Mendelian Inheritance in Man (OMIM)

More...MIMi		180260 gene

neXtProt; the human protein knowledge platform

More...neXtProti		NX_P09455

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Lipid droplet

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/manual/pathology_and_biotech_section">'Pathology and Biotech'</a> section describes the effect of the experimental mutation of one or more amino acid(s) on the biological properties of the protein.<p><a href='/help/mutagen' target='_top'>More...</a></p>Mutagenesisi22R → A: No effect on retinol binding. Abolishes interaction with STA6 and the ability to enhance STA6-mediated vitamin A uptake. 1 Publication1
Mutagenesisi30L → A: Decreases cellular retinol uptake and impairs retinol storage. 1 Publication1
Mutagenesisi31R → A: No effect on retinol binding. Abolishes interaction with STA6 and the ability to enhance STA6-mediated vitamin A uptake. 1 Publication1
Mutagenesisi32K → A: No effect on retinol binding. Abolishes interaction with STA6 and the ability to enhance STA6-mediated vitamin A uptake. 1 Publication1
Mutagenesisi41K → L: Strongly decreased affinity for retinol. Further decrease in affinity for retinol; when associated with L-109. 1 Publication1
Mutagenesisi59R → E: Decreases cellular retinol uptake and impairs retinol storage. 1 Publication1
Mutagenesisi109Q → L: Strongly decreased affinity for retinol. Further decrease in for retinol; when associated with L-41. 1 Publication1

Organism-specific databases

DisGeNET

More...DisGeNETi		5947

Open Targets

More...OpenTargetsi		ENSG00000114115

The Pharmacogenetics and Pharmacogenomics Knowledge Base

More...PharmGKBi		PA34286

Chemistry databases

Drug and drug target database

More...DrugBanki		DB00459 Acitretin
DB00162 Vitamin A

Polymorphism and mutation databases

BioMuta curated single-nucleotide variation and disease association database

More...BioMutai		RBP1

Domain mapping of disease mutations (DMDM)

More...DMDMi		132387

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00000673921 – 135Retinol-binding protein 1Add BLAST135

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 2 (identifier: P09455-2)
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei9Omega-N-methylarginineCombined sourcesCurated1
Isoform 3 (identifier: P09455-3)
Modified residuei9Omega-N-methylarginineCombined sources1

Keywords - PTMi

Methylation

Proteomic databases

Encyclopedia of Proteome Dynamics

More...EPDi		P09455

jPOST - Japan Proteome Standard Repository/Database

More...jPOSTi		P09455

MaxQB - The MaxQuant DataBase

More...MaxQBi		P09455

PaxDb, a database of protein abundance averages across all three domains of life

More...PaxDbi		P09455

PeptideAtlas

More...PeptideAtlasi		P09455

PRoteomics IDEntifications database

More...PRIDEi		P09455

ProteomicsDB human proteome resource

More...ProteomicsDBi		52219

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...iPTMneti		P09455

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...PhosphoSitePlusi		P09455

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in nearly all the tissues with higher expression in adult ovary, pancreas, pituitary gland and adrenal gland, and fetal liver.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...Bgeei		ENSG00000114115 Expressed in 211 organ(s), highest expression level in pigmented layer of retina

CleanEx database of gene expression profiles

More...CleanExi		HS_RBP1

ExpressionAtlas, Differential and Baseline Expression

More...ExpressionAtlasi		P09455 baseline and differential

Genevisible search portal to normalized and curated expression data from Genevestigator

More...Genevisiblei		P09455 HS

Organism-specific databases

Human Protein Atlas

More...HPAi		CAB018603
CAB019276
HPA007338

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts (only as retinol-free apoprotein) with STRA6.1 Publication

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...BioGridi		111881, 13 interactors

Protein interaction database and analysis system

More...IntActi		P09455, 8 interactors

STRING: functional protein association networks

More...STRINGi		9606.ENSP00000232219

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

Secondary structure

1135
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details

3D structure databases

Select the link destinations:

Protein Data Bank Europe

More...PDBei

Protein Data Bank RCSB

More...RCSB PDBi

Protein Data Bank Japan

More...PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5H8TX-ray1.21A2-135[»]
5H9AX-ray1.38A2-135[»]
5HA1X-ray1.35A2-135[»]
5HBSX-ray0.89A2-135[»]
5LJBX-ray1.26A1-135[»]
5LJCX-ray1.43A1-135[»]
5LJDX-ray1.61A1-135[»]
5LJEX-ray1.40A1-135[»]
5LJGX-ray1.15A1-135[»]
5LJHX-ray1.52A1-135[»]
5LJKX-ray1.70A1-135[»]

Protein Model Portal of the PSI-Nature Structural Biology Knowledgebase

More...ProteinModelPortali		P09455

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...SMRi		P09455

Database of comparative protein structure models

More...ModBasei		Search...

MobiDB: a database of protein disorder and mobility annotations

More...MobiDBi		Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni22 – 32Important for interaction with STRA61 PublicationAdd BLAST11

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>Domaini

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior.2 Publications

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Belongs to the calycin superfamily. Fatty-acid binding protein (FABP) family.Curated

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...eggNOGi		KOG4015 Eukaryota
ENOG4111US8 LUCA

Ensembl GeneTree

More...GeneTreei		ENSGT00940000159675

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

More...HOGENOMi		HOG000004831

The HOVERGEN Database of Homologous Vertebrate Genes

More...HOVERGENi		HBG005633

InParanoid: Eukaryotic Ortholog Groups

More...InParanoidi		P09455

Database of Orthologous Groups

More...OrthoDBi		1377380at2759

Database for complete collections of gene phylogenies

More...PhylomeDBi		P09455

TreeFam database of animal gene trees

More...TreeFami		TF316894

Family and domain databases

Gene3D Structural and Functional Annotation of Protein Families

More...Gene3Di		2.40.128.20, 1 hit

Integrated resource of protein families, domains and functional sites

More...InterProi		View protein in InterPro
IPR012674 Calycin
IPR031264 CRBP1
IPR000463 Fatty_acid-bd
IPR031259 ILBP
IPR000566 Lipocln_cytosolic_FA-bd_dom

The PANTHER Classification System

More...PANTHERi		PTHR11955 PTHR11955, 1 hit
PTHR11955:SF56 PTHR11955:SF56, 1 hit

Pfam protein domain database

More...Pfami		View protein in Pfam
PF00061 Lipocalin, 1 hit

Protein Motif fingerprint database; a protein domain database

More...PRINTSi		PR00178 FATTYACIDBP

Superfamily database of structural and functional annotation

More...SUPFAMi		SSF50814 SSF50814, 1 hit

PROSITE; a protein domain and family database

More...PROSITEi		View protein in PROSITE
PS00214 FABP, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>.<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequences (3+)i

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

This entry describes 3 <p>This subsection of the ‘Sequence’ section lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.<p><a href='/help/alternative_products' target='_top'>More...</a></p> isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 3 described isoforms and 3 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: P09455-1) [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
MPVDFTGYWK MLVNENFEEY LRALDVNVAL RKIANLLKPD KEIVQDGDHM 
        60         70         80         90        100
IIRTLSTFRN YIMDFQVGKE FEEDLTGIDD RKCMTTVSWD GDKLQCVQKG 
       110        120        130 
EKEGRGWTQW IEGDELHLEM RVEGVVCKQV FKKVQ
Length:135
Mass (Da):15,850
Last modified:January 23, 2007 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iFA47545761AFA3A2
GO
Isoform 2 (identifier: P09455-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPPAGFVRAGNPAVAAPQSPLSPEGAHFRAAHHPRSTGSRCPGSLQPSRPLVANWLQSLPEM
     85-135: TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ → SETGFSS

Note: No experimental confirmation available.Combined sourcesCurated
Show »
Length:153
Mass (Da):17,104
Checksum:i6142D55498572358
GO
Isoform 3 (identifier: P09455-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MDPPAGFVRAGNPAVAAPQSPLSPEGAHFRAAHHPRSTGSRCPGSLQPSRPLVANWLQSLPEM
     85-135: TTVSWDGDKLQCVQKGEKEGRGWTQWIEGDELHLEMRVEGVVCKQVFKKVQ → AGVQSRDLSSL

Note: No experimental confirmation available.Combined sources
Show »
Length:157
Mass (Da):17,523
Checksum:i454E1DC7BE53793A
GO

<p>In eukaryotic reference proteomes, unreviewed entries that are likely to belong to the same gene are computationally mapped, based on gene identifiers from Ensembl, EnsemblGenomes and model organism databases.<p><a href='/help/gene_centric_isoform_mapping' target='_top'>More...</a></p>Computationally mapped potential isoform sequencesi

There are 3 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A0A0MQT0A0A0A0MQT0_HUMAN
Retinol binding protein 1, cellular
RBP1 hCG_16055
197Annotation score:

Annotation score:2 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
H0YAK8H0YAK8_HUMAN
Retinol-binding protein 1
RBP1
98Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
A0A0A0MTB9A0A0A0MTB9_HUMAN
Retinol-binding protein 1
RBP1
91Annotation score:

Annotation score:1 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Isoform 2 (identifier: P09455-2)
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti18P → L in BAH13536 (PubMed:14702039).Combined sourcesCurated1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.<p><a href='/help/var_seq' target='_top'>More...</a></p>Alternative sequenceiVSP_0462011M → MDPPAGFVRAGNPAVAAPQS PLSPEGAHFRAAHHPRSTGS RCPGSLQPSRPLVANWLQSL PEM in isoform 2 and isoform 3. 1 Publication1
Alternative sequenceiVSP_04620285 – 135TTVSW…FKKVQ → SETGFSS in isoform 2. 1 PublicationAdd BLAST51
Alternative sequenceiVSP_04620385 – 135TTVSW…FKKVQ → AGVQSRDLSSL in isoform 3. 1 PublicationAdd BLAST51

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...EMBLi

GenBank nucleotide sequence database

More...GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...DDBJi
Links Updated
M11433 mRNA Translation: AAA60257.1
X07437, X07438 Genomic DNA Translation: CAA30318.1
AK290315 mRNA Translation: BAF83004.1
AK301684 mRNA Translation: BAH13536.1
AK309492 Genomic DNA No translation available.
CR541979 mRNA Translation: CAG46776.1
CR542005 mRNA Translation: CAG46802.1
AC046134 Genomic DNA No translation available.
BC121052 mRNA Translation: AAI21053.1
M36809 mRNA Translation: AAA35714.1

The Consensus CDS (CCDS) project

More...CCDSi		CCDS46925.1 [P09455-2]
CCDS46926.1 [P09455-3]

Protein sequence database of the Protein Information Resource

More...PIRi		S00399 RJHUO

NCBI Reference Sequences

More...RefSeqi		NP_001124464.1, NM_001130992.1 [P09455-3]
NP_001124465.1, NM_001130993.1 [P09455-2]
NP_002890.2, NM_002899.3

UniGene gene-oriented nucleotide sequence clusters

More...UniGenei		Hs.529571
Hs.708528
Hs.721405

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...Ensembli		ENST00000492918; ENSP00000429166; ENSG00000114115 [P09455-3]
ENST00000617459; ENSP00000477621; ENSG00000114115 [P09455-2]
ENST00000619087; ENSP00000482165; ENSG00000114115 [P09455-1]

Database of genes from NCBI RefSeq genomes

More...GeneIDi		5947

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...KEGGi		hsa:5947

UCSC genome browser

More...UCSCi		uc011bmx.2 human [P09455-1]

Keywords - Coding sequence diversityi

Alternative splicing

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11433 mRNA Translation: AAA60257.1
X07437, X07438 Genomic DNA Translation: CAA30318.1
AK290315 mRNA Translation: BAF83004.1
AK301684 mRNA Translation: BAH13536.1
AK309492 Genomic DNA No translation available.
CR541979 mRNA Translation: CAG46776.1
CR542005 mRNA Translation: CAG46802.1
AC046134 Genomic DNA No translation available.
BC121052 mRNA Translation: AAI21053.1
M36809 mRNA Translation: AAA35714.1
CCDSiCCDS46925.1 [P09455-2]
CCDS46926.1 [P09455-3]
PIRiS00399 RJHUO
RefSeqiNP_001124464.1, NM_001130992.1 [P09455-3]
NP_001124465.1, NM_001130993.1 [P09455-2]
NP_002890.2, NM_002899.3
UniGeneiHs.529571
Hs.708528
Hs.721405

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
5H8TX-ray1.21A2-135[»]
5H9AX-ray1.38A2-135[»]
5HA1X-ray1.35A2-135[»]
5HBSX-ray0.89A2-135[»]
5LJBX-ray1.26A1-135[»]
5LJCX-ray1.43A1-135[»]
5LJDX-ray1.61A1-135[»]
5LJEX-ray1.40A1-135[»]
5LJGX-ray1.15A1-135[»]
5LJHX-ray1.52A1-135[»]
5LJKX-ray1.70A1-135[»]
ProteinModelPortaliP09455
SMRiP09455
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi111881, 13 interactors
IntActiP09455, 8 interactors
STRINGi9606.ENSP00000232219

Chemistry databases

DrugBankiDB00459 Acitretin
DB00162 Vitamin A

PTM databases

iPTMnetiP09455
PhosphoSitePlusiP09455

Polymorphism and mutation databases

BioMutaiRBP1
DMDMi132387

Proteomic databases

EPDiP09455
jPOSTiP09455
MaxQBiP09455
PaxDbiP09455
PeptideAtlasiP09455
PRIDEiP09455
ProteomicsDBi52219

Protocols and materials databases

The DNASU plasmid repository

More...DNASUi		5947
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000492918; ENSP00000429166; ENSG00000114115 [P09455-3]
ENST00000617459; ENSP00000477621; ENSG00000114115 [P09455-2]
ENST00000619087; ENSP00000482165; ENSG00000114115 [P09455-1]
GeneIDi5947
KEGGihsa:5947
UCSCiuc011bmx.2 human [P09455-1]

Organism-specific databases

Comparative Toxicogenomics Database

More...CTDi		5947
DisGeNETi5947
EuPathDBiHostDB:ENSG00000114115.9

GeneCards: human genes, protein and diseases

More...GeneCardsi		RBP1

H-Invitational Database, human transcriptome db

More...H-InvDBi		HIX0030850
HGNCiHGNC:9919 RBP1
HPAiCAB018603
CAB019276
HPA007338
MIMi180260 gene
neXtProtiNX_P09455
OpenTargetsiENSG00000114115
PharmGKBiPA34286

GenAtlas: human gene database

More...GenAtlasi		Search...

Phylogenomic databases

eggNOGiKOG4015 Eukaryota
ENOG4111US8 LUCA
GeneTreeiENSGT00940000159675
HOGENOMiHOG000004831
HOVERGENiHBG005633
InParanoidiP09455
OrthoDBi1377380at2759
PhylomeDBiP09455
TreeFamiTF316894

Enzyme and pathway databases

BioCyciMetaCyc:ENSG00000114115-MONOMER
ReactomeiR-HSA-2453864 Retinoid cycle disease events
R-HSA-2453902 The canonical retinoid cycle in rods (twilight vision)
R-HSA-975634 Retinoid metabolism and transport

Miscellaneous databases

The Gene Wiki collection of pages on human genes and proteins

More...GeneWikii		RBP1

Database of phenotypes from RNA interference screens in Drosophila and Homo sapiens

More...GenomeRNAii		5947

Protein Ontology

More...PROi		PR:P09455

The Stanford Online Universal Resource for Clones and ESTs

More...SOURCEi		Search...

Gene expression databases

BgeeiENSG00000114115 Expressed in 211 organ(s), highest expression level in pigmented layer of retina
CleanExiHS_RBP1
ExpressionAtlasiP09455 baseline and differential
GenevisibleiP09455 HS

Family and domain databases

Gene3Di2.40.128.20, 1 hit
InterProiView protein in InterPro
IPR012674 Calycin
IPR031264 CRBP1
IPR000463 Fatty_acid-bd
IPR031259 ILBP
IPR000566 Lipocln_cytosolic_FA-bd_dom
PANTHERiPTHR11955 PTHR11955, 1 hit
PTHR11955:SF56 PTHR11955:SF56, 1 hit
PfamiView protein in Pfam
PF00061 Lipocalin, 1 hit
PRINTSiPR00178 FATTYACIDBP
SUPFAMiSSF50814 SSF50814, 1 hit
PROSITEiView protein in PROSITE
PS00214 FABP, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...ProtoNeti		Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiRET1_HUMAN
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: P09455
Secondary accession number(s): A8K2Q0
, B7Z7A0, E7EWV0, F2Z2F2, Q6FGX8
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: January 16, 2019
This is version 174 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>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.

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. Human chromosome 3
    Human chromosome 3: entries, gene names and cross-references to MIM
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again