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Protein

Cellular retinoic acid-binding protein 1

Gene

CRABP1

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

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

GO - Molecular functioni

  • retinal binding Source: UniProtKB-KW
  • retinoic acid binding Source: Ensembl
  • retinoid binding Source: ProtInc
  • retinol binding Source: UniProtKB-KW
  • transporter activity Source: InterPro

GO - Biological processi

  • multicellular organism development Source: ProtInc
  • retinoic acid catabolic process Source: InterPro
  • signal transduction Source: ProtInc

Keywordsi

Biological processTransport
LigandRetinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiR-HSA-5365859. RA biosynthesis pathway.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular retinoic acid-binding protein 1
Alternative name(s):
Cellular retinoic acid-binding protein I
Short name:
CRABP-I
Gene namesi
Name:CRABP1
Synonyms:RBP5
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

EuPathDBiHostDB:ENSG00000166426.7.
HGNCiHGNC:2338. CRABP1.

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

Pathology & Biotechi

Organism-specific databases

DisGeNETi1381.
OpenTargetsiENSG00000166426.
PharmGKBiPA26858.

Chemistry databases

ChEMBLiCHEMBL2079.
DrugBankiDB00523. Alitretinoin.
DB00926. Etretinate.
DB00755. Tretinoin.

Polymorphism and mutation databases

BioMutaiCRABP1.
DMDMi266904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000674061 – 137Cellular retinoic acid-binding protein 1Add BLAST137

Proteomic databases

EPDiP29762.
MaxQBiP29762.
PaxDbiP29762.
PeptideAtlasiP29762.
PRIDEiP29762.

PTM databases

iPTMnetiP29762.
PhosphoSitePlusiP29762.

Expressioni

Gene expression databases

BgeeiENSG00000166426.
CleanExiHS_CRABP1.
HS_RBP5.
ExpressionAtlasiP29762. baseline and differential.
GenevisibleiP29762. HS.

Organism-specific databases

HPAiHPA017203.

Interactioni

Binary interactionsi

Show more details

Protein-protein interaction databases

BioGridi107772. 4 interactors.
IntActiP29762. 5 interactors.
MINTiMINT-5005962.
STRINGi9606.ENSP00000299529.

Structurei

3D structure databases

ProteinModelPortaliP29762.
SMRiP29762.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni132 – 134Retinoic acid bindingBy similarity3

Motif

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Motifi21 – 31Nuclear localization signalBy similarityAdd BLAST11

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP29762.
KOiK17337.
OMAiTWESENK.
OrthoDBiEOG091G0QSV.
PhylomeDBiP29762.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiView protein in InterPro
IPR012674. Calycin.
IPR031279. CRABP1.
IPR000463. Fatty_acid-bd.
IPR031259. ILBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF122. PTHR11955:SF122. 1 hit.
PfamiView protein in Pfam
PF00061. Lipocalin. 1 hit.
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiView protein in PROSITE
PS00214. FABP. 1 hit.

Sequencei

Sequence statusi: Complete.

P29762-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNFAGTWKM RSSENFDELL KALGVNAMLR KVAVAAASKP HVEIRQDGDQ
60 70 80 90 100
FYIKTSTTVR TTEINFKVGE GFEEETVDGR KCRSLATWEN ENKIHCTQTL
110 120 130
LEGDGPKTYW TRELANDELI LTFGADDVVC TRIYVRE
Length:137
Mass (Da):15,566
Last modified:January 23, 2007 - v2
Checksum:iA3DB048973E4E8C4
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti112R → S in AAH22069 (PubMed:15489334).Curated1
Sequence conflicti137E → D in CAG33298 (Ref. 3) Curated1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
S74445 mRNA. Translation: AAB20773.1.
CR457017 mRNA. Translation: CAG33298.1.
BC022069 mRNA. Translation: AAH22069.1.
CCDSiCCDS10301.1.
PIRiJH0548. RJHU1.
RefSeqiNP_004369.1. NM_004378.2.
UniGeneiHs.346950.

Genome annotation databases

EnsembliENST00000299529; ENSP00000299529; ENSG00000166426.
GeneIDi1381.
KEGGihsa:1381.
UCSCiuc002bdp.2. human.

Similar proteinsi

Entry informationi

Entry nameiRABP1_HUMAN
AccessioniPrimary (citable) accession number: P29762
Secondary accession number(s): Q6IAY7, Q8WTV5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: September 27, 2017
This is version 151 of the entry and version 2 of the sequence. See 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 15
    Human chromosome 15: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families