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Protein

Cellular retinoic acid-binding protein 2

Gene

CRABP2

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

Functioni

Transports retinoic acid to the nucleus. Regulates 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

  • embryonic forelimb morphogenesis Source: Ensembl
  • epidermis development Source: ProtInc
  • positive regulation of collateral sprouting Source: Ensembl
  • regulation of retinoic acid receptor signaling pathway Source: InterPro
  • regulation of transcription, DNA-templated Source: ProtInc
  • retinoic acid metabolic process Source: Ensembl
  • signal transduction Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiR-HSA-5362517. Signaling by Retinoic Acid.
SIGNORiP29373.

Names & Taxonomyi

Protein namesi
Recommended name:
Cellular retinoic acid-binding protein 2
Alternative name(s):
Cellular retinoic acid-binding protein II
Short name:
CRABP-II
Gene namesi
Name:CRABP2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:2339. CRABP2.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: HPA
  • cytosol Source: Reactome
  • endoplasmic reticulum Source: UniProtKB-SubCell
  • extracellular exosome Source: UniProtKB
  • nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi21K → A: Loss of ligand-induced nuclear import; when associated with A-30 and A-31. 1 Publication1
Mutagenesisi30R → A: Loss of ligand-induced nuclear import; when associated with A-21 and A-31. 1 Publication1
Mutagenesisi31K → A: Loss of ligand-induced nuclear import; when associated with A-21 and A-30. 1 Publication1

Organism-specific databases

DisGeNETi1382.
OpenTargetsiENSG00000143320.
PharmGKBiPA26859.

Chemistry databases

ChEMBLiCHEMBL2221342.
DrugBankiDB00523. Alitretinoin.
DB00755. Tretinoin.

Polymorphism and mutation databases

BioMutaiCRABP2.
DMDMi132401.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000674151 – 138Cellular retinoic acid-binding protein 2Add BLAST138

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Cross-linki102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)1 Publication

Post-translational modificationi

Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation.1 Publication

Keywords - PTMi

Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiP29373.
MaxQBiP29373.
PaxDbiP29373.
PeptideAtlasiP29373.
PRIDEiP29373.

2D gel databases

DOSAC-COBS-2DPAGEP29373.

PTM databases

iPTMnetiP29373.
PhosphoSitePlusiP29373.

Expressioni

Inductioni

By retinoic acid.

Gene expression databases

BgeeiENSG00000143320.
CleanExiHS_CRABP2.
ExpressionAtlasiP29373. baseline and differential.
GenevisibleiP29373. HS.

Organism-specific databases

HPAiHPA004135.

Interactioni

Subunit structurei

Interacts with RXR and RARA (By similarity). Interacts with importin alpha.By similarity2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CCDC155Q8N6L05EBI-10204806,EBI-749265

Protein-protein interaction databases

BioGridi107773. 11 interactors.
IntActiP29373. 3 interactors.
STRINGi9606.ENSP00000357204.

Structurei

Secondary structure

1138
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi6 – 14Combined sources9
Helixi16 – 22Combined sources7
Helixi27 – 37Combined sources11
Beta strandi41 – 47Combined sources7
Beta strandi50 – 57Combined sources8
Beta strandi60 – 67Combined sources8
Beta strandi72 – 75Combined sources4
Beta strandi77 – 79Combined sources3
Beta strandi81 – 90Combined sources10
Beta strandi93 – 103Combined sources11
Beta strandi108 – 114Combined sources7
Beta strandi116 – 118Combined sources3
Beta strandi120 – 126Combined sources7
Beta strandi129 – 137Combined sources9

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BLRNMR-A2-138[»]
1BM5NMR-A2-138[»]
1CBQX-ray2.20A2-138[»]
1CBSX-ray1.80A2-138[»]
1XCAX-ray2.30A/B2-138[»]
2CBSX-ray2.10A2-138[»]
2FR3X-ray1.48A2-138[»]
2FRSX-ray1.51A/B2-138[»]
2FS6X-ray1.35A/B2-138[»]
2FS7X-ray1.55A/B2-138[»]
2G78X-ray1.70A2-138[»]
2G79X-ray1.69A2-138[»]
2G7BX-ray1.18A2-138[»]
3CBSX-ray2.00A2-138[»]
3CR6X-ray1.22A2-138[»]
3CWKX-ray1.60A2-138[»]
3D95X-ray1.20A/B2-138[»]
3D96X-ray1.71A/B2-138[»]
3D97X-ray1.50A/B2-138[»]
3F8AX-ray1.95A2-138[»]
3F9DX-ray2.00A/B2-138[»]
3FA6X-ray1.54A/B2-138[»]
3FA7X-ray1.90A/B2-138[»]
3FA8X-ray1.78A/B2-138[»]
3FA9X-ray1.94A/B2-138[»]
3FEKX-ray1.51A/B2-138[»]
3FELX-ray1.85A/B2-138[»]
3FENX-ray1.56A/B2-138[»]
3FEPX-ray2.60A2-138[»]
3I17X-ray1.68A/B2-138[»]
4I9RX-ray2.60A2-138[»]
4I9SX-ray2.58A2-138[»]
4M6SX-ray2.47A2-138[»]
4M7MX-ray2.57A2-138[»]
4QGVX-ray1.73A/B2-138[»]
4QGWX-ray1.77A/B2-138[»]
4QGXX-ray1.47A/B2-138[»]
4YBPX-ray1.83A2-138[»]
4YBUX-ray1.92A2-138[»]
4YCEX-ray1.95A2-138[»]
4YCHX-ray1.96A2-138[»]
4YDAX-ray1.95A2-138[»]
4YDBX-ray2.03A2-138[»]
4YFPX-ray1.95A2-138[»]
4YFQX-ray1.62A2-138[»]
4YFRX-ray1.95A2-138[»]
4YGGX-ray1.90A2-138[»]
4YGHX-ray2.10A2-138[»]
4YGZX-ray2.06A2-138[»]
4YH0X-ray2.14A2-138[»]
4YKMX-ray1.58A/B2-138[»]
4YKOX-ray1.57A/B2-138[»]
5HZQX-ray1.75A/B1-138[»]
ProteinModelPortaliP29373.
SMRiP29373.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29373.

Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni133 – 135Retinoic acid binding3

Motif

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

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP29373.
KOiK17289.
OMAiGELVLTM.
OrthoDBiEOG091G0QSV.
PhylomeDBiP29373.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031281. CRABP2.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF60. PTHR11955:SF60. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P29373-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT
60 70 80 90 100
FYIKTSTTVR TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL
110 120 130
LKGEGPKTSW TRELTNDGEL ILTMTADDVV CTRVYVRE
Length:138
Mass (Da):15,693
Last modified:January 23, 2007 - v2
Checksum:i982833700775B377
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68867 mRNA. Translation: AAA52068.1.
M97815, M97814 Genomic DNA. Translation: AAA58430.1.
CR450357 mRNA. Translation: CAG29353.1.
BT019827 mRNA. Translation: AAV38630.1.
AK312007 mRNA. Translation: BAG34945.1.
AB593017 mRNA. Translation: BAJ83972.1.
AL590666 Genomic DNA. Translation: CAI16339.1.
CH471121 Genomic DNA. Translation: EAW52921.1.
CH471121 Genomic DNA. Translation: EAW52922.1.
BC001109 mRNA. Translation: AAH01109.1.
CCDSiCCDS1152.1.
PIRiA45057. RJHU2.
RefSeqiNP_001186652.1. NM_001199723.1.
NP_001869.1. NM_001878.3.
XP_016855832.1. XM_017000343.1.
UniGeneiHs.405662.

Genome annotation databases

EnsembliENST00000368221; ENSP00000357204; ENSG00000143320.
ENST00000368222; ENSP00000357205; ENSG00000143320.
ENST00000621784; ENSP00000482841; ENSG00000143320.
GeneIDi1382.
KEGGihsa:1382.
UCSCiuc001fpr.4. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M68867 mRNA. Translation: AAA52068.1.
M97815, M97814 Genomic DNA. Translation: AAA58430.1.
CR450357 mRNA. Translation: CAG29353.1.
BT019827 mRNA. Translation: AAV38630.1.
AK312007 mRNA. Translation: BAG34945.1.
AB593017 mRNA. Translation: BAJ83972.1.
AL590666 Genomic DNA. Translation: CAI16339.1.
CH471121 Genomic DNA. Translation: EAW52921.1.
CH471121 Genomic DNA. Translation: EAW52922.1.
BC001109 mRNA. Translation: AAH01109.1.
CCDSiCCDS1152.1.
PIRiA45057. RJHU2.
RefSeqiNP_001186652.1. NM_001199723.1.
NP_001869.1. NM_001878.3.
XP_016855832.1. XM_017000343.1.
UniGeneiHs.405662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1BLRNMR-A2-138[»]
1BM5NMR-A2-138[»]
1CBQX-ray2.20A2-138[»]
1CBSX-ray1.80A2-138[»]
1XCAX-ray2.30A/B2-138[»]
2CBSX-ray2.10A2-138[»]
2FR3X-ray1.48A2-138[»]
2FRSX-ray1.51A/B2-138[»]
2FS6X-ray1.35A/B2-138[»]
2FS7X-ray1.55A/B2-138[»]
2G78X-ray1.70A2-138[»]
2G79X-ray1.69A2-138[»]
2G7BX-ray1.18A2-138[»]
3CBSX-ray2.00A2-138[»]
3CR6X-ray1.22A2-138[»]
3CWKX-ray1.60A2-138[»]
3D95X-ray1.20A/B2-138[»]
3D96X-ray1.71A/B2-138[»]
3D97X-ray1.50A/B2-138[»]
3F8AX-ray1.95A2-138[»]
3F9DX-ray2.00A/B2-138[»]
3FA6X-ray1.54A/B2-138[»]
3FA7X-ray1.90A/B2-138[»]
3FA8X-ray1.78A/B2-138[»]
3FA9X-ray1.94A/B2-138[»]
3FEKX-ray1.51A/B2-138[»]
3FELX-ray1.85A/B2-138[»]
3FENX-ray1.56A/B2-138[»]
3FEPX-ray2.60A2-138[»]
3I17X-ray1.68A/B2-138[»]
4I9RX-ray2.60A2-138[»]
4I9SX-ray2.58A2-138[»]
4M6SX-ray2.47A2-138[»]
4M7MX-ray2.57A2-138[»]
4QGVX-ray1.73A/B2-138[»]
4QGWX-ray1.77A/B2-138[»]
4QGXX-ray1.47A/B2-138[»]
4YBPX-ray1.83A2-138[»]
4YBUX-ray1.92A2-138[»]
4YCEX-ray1.95A2-138[»]
4YCHX-ray1.96A2-138[»]
4YDAX-ray1.95A2-138[»]
4YDBX-ray2.03A2-138[»]
4YFPX-ray1.95A2-138[»]
4YFQX-ray1.62A2-138[»]
4YFRX-ray1.95A2-138[»]
4YGGX-ray1.90A2-138[»]
4YGHX-ray2.10A2-138[»]
4YGZX-ray2.06A2-138[»]
4YH0X-ray2.14A2-138[»]
4YKMX-ray1.58A/B2-138[»]
4YKOX-ray1.57A/B2-138[»]
5HZQX-ray1.75A/B1-138[»]
ProteinModelPortaliP29373.
SMRiP29373.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107773. 11 interactors.
IntActiP29373. 3 interactors.
STRINGi9606.ENSP00000357204.

Chemistry databases

ChEMBLiCHEMBL2221342.
DrugBankiDB00523. Alitretinoin.
DB00755. Tretinoin.

PTM databases

iPTMnetiP29373.
PhosphoSitePlusiP29373.

Polymorphism and mutation databases

BioMutaiCRABP2.
DMDMi132401.

2D gel databases

DOSAC-COBS-2DPAGEP29373.

Proteomic databases

EPDiP29373.
MaxQBiP29373.
PaxDbiP29373.
PeptideAtlasiP29373.
PRIDEiP29373.

Protocols and materials databases

DNASUi1382.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000368221; ENSP00000357204; ENSG00000143320.
ENST00000368222; ENSP00000357205; ENSG00000143320.
ENST00000621784; ENSP00000482841; ENSG00000143320.
GeneIDi1382.
KEGGihsa:1382.
UCSCiuc001fpr.4. human.

Organism-specific databases

CTDi1382.
DisGeNETi1382.
GeneCardsiCRABP2.
HGNCiHGNC:2339. CRABP2.
HPAiHPA004135.
MIMi180231. gene.
neXtProtiNX_P29373.
OpenTargetsiENSG00000143320.
PharmGKBiPA26859.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG4015. Eukaryota.
ENOG4111US8. LUCA.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP29373.
KOiK17289.
OMAiGELVLTM.
OrthoDBiEOG091G0QSV.
PhylomeDBiP29373.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiR-HSA-5362517. Signaling by Retinoic Acid.
SIGNORiP29373.

Miscellaneous databases

EvolutionaryTraceiP29373.
GeneWikiiCRABP2.
GenomeRNAii1382.
PROiP29373.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000143320.
CleanExiHS_CRABP2.
ExpressionAtlasiP29373. baseline and differential.
GenevisibleiP29373. HS.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR031281. CRABP2.
IPR000463. Fatty_acid-bd.
IPR031259. iLBP.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PANTHERiPTHR11955. PTHR11955. 1 hit.
PTHR11955:SF60. PTHR11955:SF60. 1 hit.
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRABP2_HUMAN
AccessioniPrimary (citable) accession number: P29373
Secondary accession number(s): B2R4Z8
, D3DVC5, F1T098, Q6ICN6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: November 30, 2016
This is version 168 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: 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. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.