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P29373 (RABP2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 141. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Cellular retinoic acid-binding protein 2
Alternative name(s):
Cellular retinoic acid-binding protein II
Short name=CRABP-II
Gene names
Name:CRABP2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length138 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Transports retinoic acid to the nucleus. Regulates the access of retinoic acid to the nuclear retinoic acid receptors.

Subunit structure

Interacts with RXR and RARA By similarity. Interacts with importin alpha. Ref.11

Subcellular location

Cytoplasm. Endoplasmic reticulum. Nucleus. Note: Upon ligand binding, a conformation change exposes a nuclear localization motif and the protein is transported into the nucleus. Ref.11 Ref.12

Induction

By retinoic acid.

Domain

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

Post-translational modification

Sumoylated in response to retinoic acid binding, sumoylation is critical for dissociation from ER and subsequent nuclear translocation. Ref.14

Sequence similarities

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 138138Cellular retinoic acid-binding protein 2
PRO_0000067415

Regions

Region133 – 1353Retinoic acid binding
Motif21 – 3111Nuclear localization signal

Amino acid modifications

Cross-link102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO) Ref.14

Experimental info

Mutagenesis211K → A: Loss of ligand-induced nuclear import; when associated with A-30 and A-31. Ref.12
Mutagenesis301R → A: Loss of ligand-induced nuclear import; when associated with A-21 and A-31. Ref.12
Mutagenesis311K → A: Loss of ligand-induced nuclear import; when associated with A-21 and A-30. Ref.12

Secondary structure

............................. 138
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P29373 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 982833700775B377

FASTA13815,693
        10         20         30         40         50         60 
MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT FYIKTSTTVR 

        70         80         90        100        110        120 
TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL LKGEGPKTSW TRELTNDGEL 

       130 
ILTMTADDVV CTRVYVRE 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"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].
[3]"Structure of the human cellular retinoic acid-binding protein II gene. Early transcriptional regulation by retinoic acid."
Aastroem A., Pettersson U., Voorhees J.J.
J. Biol. Chem. 267:25251-25255(1992) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
Tissue: Placenta.
[4]"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 (MAY-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[5]"Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
Submitted (OCT-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[6]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Brain.
[7]"Full-length transcriptome analysis of human retina-derived cell lines ARPE-19 and Y79 using the vector-capping method."
Oshikawa M., Tsutsui C., Ikegami T., Fuchida Y., Matsubara M., Toyama S., Usami R., Ohtoko K., Kato S.
Invest. Ophthalmol. Vis. Sci. 52:6662-6670(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[8]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[10]"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: Colon.
[11]"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, INTERACTION WITH NUCLEAR RETINOIC ACID RECEPTORS.
[12]"A ligand-activated nuclear localization signal in cellular retinoic acid binding protein-II."
Sessler R.J., Noy N.
Mol. Cell 18:343-353(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION, MUTAGENESIS OF LYS-21; ARG-30 AND LYS-31.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"Nuclear translocation of cellular retinoic acid-binding protein II is regulated by retinoic acid-controlled SUMOylation."
Majumdar A., Petrescu A.D., Xiong Y., Noy N.
J. Biol. Chem. 286:42749-42757(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: SUMOYLATION AT LYS-102.
[15]"Crystal structures of cellular retinoic acid binding proteins I and II in complex with all-trans-retinoic acid and a synthetic retinoid."
Kleywegt G.J., Bergfors T., Senn H., le Motte P., Gsell B., Shudo K., Jones T.A.
Structure 2:1241-1258(1994) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
[16]"Crystal structure of apo-cellular retinoic acid-binding protein type II (R111M) suggests a mechanism of ligand entry."
Chen X., Tordova M., Gilliland G.L., Wang L., Li Y., Yan H., Ji X.
J. Mol. Biol. 278:641-653(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
[17]"Structures of cellular retinoic acid binding proteins I and II in complex with synthetic retinoids."
Chaudhuri B.N., Kleywegt G.J., Broutin-L'Hermite I., Bergfors T., Senn H., Le Motte P., Partouche O., Jones T.A.
Acta Crystallogr. D 55:1850-1857(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.1 ANGSTROMS).
[18]"NMR solution structure of type II human cellular retinoic acid binding protein: implications for ligand binding."
Wang L., Li Y., Abildgaard F., Markley J.L., Yan H.
Biochemistry 37:12727-12736(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[19]"NMR study suggests a major role for Arg111 in maintaining the structure and dynamical properties of type II human cellular retinoic acid binding protein."
Wang L., Yan H.
Biochemistry 37:13021-13032(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: STRUCTURE BY NMR.
[20]"The structure of apo-wild-type cellular retinoic acid binding protein II at 1.4 A and its relationship to ligand binding and nuclear translocation."
Vaezeslami S., Mathes E., Vasileiou C., Borhan B., Geiger J.H.
J. Mol. Biol. 363:687-701(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.35 ANGSTROMS).
[21]"Protein design: reengineering cellular retinoic acid binding protein II into a rhodopsin protein mimic."
Vasileiou C., Vaezeslami S., Crist R.M., Rabago-Smith M., Geiger J.H., Borhan B.
J. Am. Chem. Soc. 129:6140-6148(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.18 ANGSTROMS) IN COMPLEX WITH RETINOIC ACID.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRRJHU2. A45057.
RefSeqNP_001186652.1. NM_001199723.1.
NP_001869.1. NM_001878.3.
UniGeneHs.405662.

3D structure databases

PDBe
RCSB PDB
PDBj
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[»]
ProteinModelPortalP29373.
SMRP29373. Positions 2-138.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid107773. 6 interactions.
STRING9606.ENSP00000357204.

Chemistry

ChEMBLCHEMBL2221342.
DrugBankDB00523. Alitretinoin.

PTM databases

PhosphoSiteP29373.

Polymorphism databases

DMDM132401.

2D gel databases

DOSAC-COBS-2DPAGEP29373.

Proteomic databases

PaxDbP29373.
PeptideAtlasP29373.
PRIDEP29373.

Protocols and materials databases

DNASU1382.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000368221; ENSP00000357204; ENSG00000143320.
ENST00000368222; ENSP00000357205; ENSG00000143320.
GeneID1382.
KEGGhsa:1382.
UCSCuc001fpr.3. human.

Organism-specific databases

CTD1382.
GeneCardsGC01M156669.
HGNCHGNC:2339. CRABP2.
HPAHPA004135.
MIM180231. gene.
neXtProtNX_P29373.
PharmGKBPA26859.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG300013.
HOGENOMHOG000004831.
HOVERGENHBG005633.
InParanoidP29373.
KOK17289.
OMANMMLRKI.
OrthoDBEOG7NW6BZ.
PhylomeDBP29373.
TreeFamTF316894.

Gene expression databases

ArrayExpressP29373.
BgeeP29373.
CleanExHS_CRABP2.
GenevestigatorP29373.

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

EvolutionaryTraceP29373.
GeneWikiCRABP2.
GenomeRNAi1382.
NextBio5615.
PROP29373.
SOURCESearch...

Entry information

Entry nameRABP2_HUMAN
AccessionPrimary (citable) accession number: P29373
Secondary accession number(s): B2R4Z8 expand/collapse secondary AC list , D3DVC5, F1T098, Q6ICN6
Entry history
Integrated into UniProtKB/Swiss-Prot: December 1, 1992
Last sequence update: January 23, 2007
Last modified: March 19, 2014
This is version 141 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

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

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM