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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

  1. retinal binding Source: UniProtKB-KW
  2. retinoic acid binding Source: Ensembl
  3. retinoid binding Source: ProtInc
  4. retinol binding Source: UniProtKB-KW
  5. transporter activity Source: InterPro

GO - Biological processi

  1. embryonic forelimb morphogenesis Source: Ensembl
  2. epidermis development Source: ProtInc
  3. regulation of transcription, DNA-templated Source: ProtInc
  4. retinoic acid metabolic process Source: Ensembl
  5. signal transduction Source: ProtInc
  6. transmembrane transport Source: Reactome
Complete GO annotation...

Keywords - Biological processi

Transport

Keywords - Ligandi

Retinol-binding, Vitamin A

Enzyme and pathway databases

ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.

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
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:2339. CRABP2.

Subcellular locationi

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

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. endoplasmic reticulum Source: UniProtKB-SubCell
  4. extracellular vesicular exosome Source: UniProtKB
  5. nucleoplasm Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Endoplasmic reticulum, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi21 – 211K → A: Loss of ligand-induced nuclear import; when associated with A-30 and A-31. 1 Publication
Mutagenesisi30 – 301R → A: Loss of ligand-induced nuclear import; when associated with A-21 and A-31. 1 Publication
Mutagenesisi31 – 311K → A: Loss of ligand-induced nuclear import; when associated with A-21 and A-30. 1 Publication

Organism-specific databases

PharmGKBiPA26859.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 138138Cellular retinoic acid-binding protein 2PRO_0000067415Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki102 – 102Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO)

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

MaxQBiP29373.
PaxDbiP29373.
PeptideAtlasiP29373.
PRIDEiP29373.

2D gel databases

DOSAC-COBS-2DPAGEP29373.

PTM databases

PhosphoSiteiP29373.

Expressioni

Inductioni

By retinoic acid.

Gene expression databases

BgeeiP29373.
CleanExiHS_CRABP2.
ExpressionAtlasiP29373. baseline and differential.
GenevestigatoriP29373.

Organism-specific databases

HPAiHPA004135.

Interactioni

Subunit structurei

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

Protein-protein interaction databases

BioGridi107773. 9 interactions.
STRINGi9606.ENSP00000357204.

Structurei

Secondary structure

1
138
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 149Combined sources
Helixi16 – 227Combined sources
Helixi27 – 3711Combined sources
Beta strandi41 – 477Combined sources
Beta strandi50 – 578Combined sources
Beta strandi60 – 678Combined sources
Beta strandi72 – 754Combined sources
Beta strandi77 – 793Combined sources
Beta strandi81 – 9010Combined sources
Beta strandi93 – 10311Combined sources
Beta strandi108 – 1147Combined sources
Beta strandi116 – 1183Combined sources
Beta strandi120 – 1267Combined sources
Beta strandi129 – 1379Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP29373.
SMRiP29373. Positions 2-138.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP29373.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni133 – 1353Retinoic acid binding

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi21 – 3111Nuclear localization signalAdd
BLAST

Domaini

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

Sequence similaritiesi

Phylogenomic databases

eggNOGiNOG300013.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP29373.
KOiK17289.
OMAiWEMKSSE.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP29373.
TreeFamiTF316894.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
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_006711232.1. XM_006711169.1.
UniGeneiHs.405662.

Genome annotation databases

EnsembliENST00000368221; ENSP00000357204; ENSG00000143320.
ENST00000368222; ENSP00000357205; ENSG00000143320.
ENST00000621784; ENSP00000482841; ENSG00000143320.
GeneIDi1382.
KEGGihsa:1382.
UCSCiuc001fpr.3. human.

Polymorphism databases

DMDMi132401.

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_006711232.1. XM_006711169.1.
UniGeneiHs.405662.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
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[»]
ProteinModelPortaliP29373.
SMRiP29373. Positions 2-138.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi107773. 9 interactions.
STRINGi9606.ENSP00000357204.

Chemistry

ChEMBLiCHEMBL2221342.
DrugBankiDB00523. Alitretinoin.
DB00755. Tretinoin.

PTM databases

PhosphoSiteiP29373.

Polymorphism databases

DMDMi132401.

2D gel databases

DOSAC-COBS-2DPAGEP29373.

Proteomic databases

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.3. human.

Organism-specific databases

CTDi1382.
GeneCardsiGC01M156669.
HGNCiHGNC:2339. CRABP2.
HPAiHPA004135.
MIMi180231. gene.
neXtProtiNX_P29373.
PharmGKBiPA26859.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG300013.
GeneTreeiENSGT00760000118898.
HOGENOMiHOG000004831.
HOVERGENiHBG005633.
InParanoidiP29373.
KOiK17289.
OMAiWEMKSSE.
OrthoDBiEOG7NW6BZ.
PhylomeDBiP29373.
TreeFamiTF316894.

Enzyme and pathway databases

ReactomeiREACT_11082. Import of palmitoyl-CoA into the mitochondrial matrix.
REACT_12528. Regulation of pyruvate dehydrogenase (PDH) complex.

Miscellaneous databases

EvolutionaryTraceiP29373.
GeneWikiiCRABP2.
GenomeRNAii1382.
NextBioi5615.
PROiP29373.
SOURCEiSearch...

Gene expression databases

BgeeiP29373.
CleanExiHS_CRABP2.
ExpressionAtlasiP29373. baseline and differential.
GenevestigatoriP29373.

Family and domain databases

Gene3Di2.40.128.20. 1 hit.
InterProiIPR012674. Calycin.
IPR011038. Calycin-like.
IPR000463. Fatty_acid-bd.
IPR000566. Lipocln_cytosolic_FA-bd_dom.
[Graphical view]
PfamiPF00061. Lipocalin. 1 hit.
[Graphical view]
PRINTSiPR00178. FATTYACIDBP.
SUPFAMiSSF50814. SSF50814. 1 hit.
PROSITEiPS00214. FABP. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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.
    , 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. 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. 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.

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: March 4, 2015
This is version 150 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

External Data

Dasty 3

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 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.