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P29762 (RABP1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 122. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cellular retinoic acid-binding protein 1
Alternative name(s):
Cellular retinoic acid-binding protein I
Short name=CRABP-I
Gene names
Name:CRABP1
Synonyms:RBP5
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length137 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Cytosolic CRABPs may regulate the access of retinoic acid to the nuclear retinoic acid receptors.

Subcellular location

Cytoplasm Ref.5.

Domain

Forms a beta-barrel structure that accommodates hydrophobic ligands in its interior By similarity.

Sequence similarities

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

P279583EBI-725950,EBI-8753518From a different organism.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 137136Cellular retinoic acid-binding protein 1
PRO_0000067406

Regions

Region132 – 1343Retinoic acid binding By similarity
Motif21 – 3111Nuclear localization signal By similarity

Experimental info

Sequence conflict1121R → S in AAH22069. Ref.4
Sequence conflict1371E → D in CAG33298. Ref.3

Sequences

Sequence LengthMass (Da)Tools
P29762 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: A3DB048973E4E8C4

FASTA13715,566
        10         20         30         40         50         60 
MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ FYIKTSTTVR 

        70         80         90        100        110        120 
TTEINFKVGE GFEEETVDGR KCRSLATWEN ENKIHCTQTL LEGDGPKTYW TRELANDELI 

       130 
LTFGADDVVC TRIYVRE 

« Hide

References

« Hide 'large scale' references
[1]"The molecular cloning and expression of two CRABP cDNAs from human skin."
Eller M.S., Oleksiak M.F., McQuaid T.J., McAfee S.G., Gilchrest B.A.
Exp. Cell Res. 198:328-336(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]"Molecular cloning of two human cellular retinoic acid-binding proteins (CRABP). Retinoic acid-induced expression of CRABP-II but not CRABP-I in adult human skin in vivo and in skin fibroblasts in vitro."
Astroem A., Tavakkol A., Pettersson U., Cromie M., Elder J.T., Voorhees J.J.
J. Biol. Chem. 266:17662-17666(1991) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[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: Brain.
[5]"Direct channeling of retinoic acid between cellular retinoic acid-binding protein II and retinoic acid receptor sensitizes mammary carcinoma cells to retinoic acid-induced growth arrest."
Budhu A.S., Noy N.
Mol. Cell. Biol. 22:2632-2641(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
S74445 mRNA. Translation: AAB20773.1.
CR457017 mRNA. Translation: CAG33298.1.
BC022069 mRNA. Translation: AAH22069.1.
PIRRJHU1. JH0548.
RefSeqNP_004369.1. NM_004378.2.
UniGeneHs.346950.

3D structure databases

ProteinModelPortalP29762.
SMRP29762. Positions 2-137.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107772. 2 interactions.
IntActP29762. 3 interactions.
MINTMINT-5005962.
STRING9606.ENSP00000299529.

Chemistry

ChEMBLCHEMBL2079.
DrugBankDB00523. Alitretinoin.
DB00926. Etretinate.

PTM databases

PhosphoSiteP29762.

Polymorphism databases

DMDM266904.

Proteomic databases

PaxDbP29762.
PRIDEP29762.

Protocols and materials databases

DNASU1381.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000299529; ENSP00000299529; ENSG00000166426.
GeneID1381.
KEGGhsa:1381.
UCSCuc002bdp.2. human.

Organism-specific databases

CTD1381.
GeneCardsGC15P078632.
HGNCHGNC:2338. CRABP1.
HPAHPA017203.
MIM180230. gene.
neXtProtNX_P29762.
PharmGKBPA26858.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG258792.
HOGENOMHOG000004831.
HOVERGENHBG005633.
InParanoidP29762.
KOK17337.
OMAATWESEN.
OrthoDBEOG7NW6BZ.
PhylomeDBP29762.
TreeFamTF316894.

Gene expression databases

ArrayExpressP29762.
BgeeP29762.
CleanExHS_CRABP1.
HS_RBP5.
GenevestigatorP29762.

Family and domain databases

Gene3D2.40.128.20. 1 hit.
InterProIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSPR00178. FATTYACIDBP.
SUPFAMSSF50814. SSF50814. 1 hit.
PROSITEPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

GeneWikiCRABP1.
GenomeRNAi1381.
NextBio5611.
PROP29762.
SOURCESearch...

Entry information

Entry nameRABP1_HUMAN
AccessionPrimary (citable) accession number: P29762
Secondary accession number(s): Q6IAY7, Q8WTV5
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 122 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM