Skip Header

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

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-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

HGNCiHGNC:2338. CRABP1.

Subcellular locationi

  • Cytoplasm 1 Publication

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

DisGeNETi1381.
OpenTargetsiENSG00000166426.
PharmGKBiPA26858.

Chemistry databases

ChEMBLiCHEMBL2079.
DrugBankiDB00523. Alitretinoin.
DB00755. Tretinoin.

Polymorphism and mutation databases

BioMutaiCRABP1.
DMDMi266904.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Initiator methionineiRemovedBy similarity
ChainiPRO_00000674062 – 137Cellular retinoic acid-binding protein 1Add BLAST136

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

WithEntry#Exp.IntActNotes
P279583EBI-725950,EBI-8753518From a different organism.

Protein-protein interaction databases

BioGridi107772. 4 interactors.
IntActiP29762. 4 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.
OMAiESENKIH.
OrthoDBiEOG091G0QSV.
PhylomeDBiP29762.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031279. CRABP1.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF62. PTHR11955:SF62. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

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.

Cross-referencesi

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.

3D structure databases

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

Protein-protein interaction databases

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

Chemistry databases

ChEMBLiCHEMBL2079.
DrugBankiDB00523. Alitretinoin.
DB00755. Tretinoin.

PTM databases

iPTMnetiP29762.
PhosphoSitePlusiP29762.

Polymorphism and mutation databases

BioMutaiCRABP1.
DMDMi266904.

Proteomic databases

EPDiP29762.
MaxQBiP29762.
PaxDbiP29762.
PeptideAtlasiP29762.
PRIDEiP29762.

Protocols and materials databases

DNASUi1381.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi1381.
DisGeNETi1381.
GeneCardsiCRABP1.
HGNCiHGNC:2338. CRABP1.
HPAiHPA017203.
MIMi180230. gene.
neXtProtiNX_P29762.
OpenTargetsiENSG00000166426.
PharmGKBiPA26858.
GenAtlasiSearch...

Phylogenomic databases

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

Enzyme and pathway databases

ReactomeiR-HSA-5365859. RA biosynthesis pathway.

Miscellaneous databases

GeneWikiiCRABP1.
GenomeRNAii1381.
PROiP29762.
SOURCEiSearch...

Gene expression databases

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

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031279. CRABP1.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF62. PTHR11955:SF62. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRABP1_HUMAN
AccessioniPrimary (citable) accession number: P29762
Secondary accession number(s): Q6IAY7, Q8WTV5
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 1, 1993
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 144 of the entry and version 2 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

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

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 one 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.