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P29373

- RABP2_HUMAN

UniProt

P29373 - RABP2_HUMAN

Protein

Cellular retinoic acid-binding protein 2

Gene

CRABP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
  1. 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

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Retinol-binding, Vitamin A

    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. endoplasmic reticulum Source: UniProtKB-SubCell
    3. extracellular vesicular exosome Source: UniProt
    4. nucleus Source: HPA

    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

    ArrayExpressiP29373.
    BgeeiP29373.
    CleanExiHS_CRABP2.
    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. 6 interactions.
    STRINGi9606.ENSP00000357204.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    HOGENOMiHOG000004831.
    HOVERGENiHBG005633.
    InParanoidiP29373.
    KOiK17289.
    OMAiGELVLTM.
    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

    MPNFSGNWKI IRSENFEELL KVLGVNVMLR KIAVAAASKP AVEIKQEGDT    50
    FYIKTSTTVR TTEINFKVGE EFEEQTVDGR PCKSLVKWES ENKMVCEQKL 100
    LKGEGPKTSW TRELTNDGEL ILTMTADDVV CTRVYVRE 138
    Length:138
    Mass (Da):15,693
    Last modified:January 23, 2007 - v2
    Checksum:i982833700775B377
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.
    GeneIDi1382.
    KEGGihsa:1382.
    UCSCiuc001fpr.3. human.

    Polymorphism databases

    DMDMi132401.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1152.1.
    PIRi A45057. RJHU2.
    RefSeqi NP_001186652.1. NM_001199723.1.
    NP_001869.1. NM_001878.3.
    XP_006711232.1. XM_006711169.1.
    UniGenei Hs.405662.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1BLR NMR - A 2-138 [» ]
    1BM5 NMR - A 2-138 [» ]
    1CBQ X-ray 2.20 A 2-138 [» ]
    1CBS X-ray 1.80 A 2-138 [» ]
    1XCA X-ray 2.30 A/B 2-138 [» ]
    2CBS X-ray 2.10 A 2-138 [» ]
    2FR3 X-ray 1.48 A 2-138 [» ]
    2FRS X-ray 1.51 A/B 2-138 [» ]
    2FS6 X-ray 1.35 A/B 2-138 [» ]
    2FS7 X-ray 1.55 A/B 2-138 [» ]
    2G78 X-ray 1.70 A 2-138 [» ]
    2G79 X-ray 1.69 A 2-138 [» ]
    2G7B X-ray 1.18 A 2-138 [» ]
    3CBS X-ray 2.00 A 2-138 [» ]
    3CR6 X-ray 1.22 A 2-138 [» ]
    3CWK X-ray 1.60 A 2-138 [» ]
    3D95 X-ray 1.20 A/B 2-138 [» ]
    3D96 X-ray 1.71 A/B 2-138 [» ]
    3D97 X-ray 1.50 A/B 2-138 [» ]
    3F8A X-ray 1.95 A 2-138 [» ]
    3F9D X-ray 2.00 A/B 2-138 [» ]
    3FA6 X-ray 1.54 A/B 2-138 [» ]
    3FA7 X-ray 1.90 A/B 2-138 [» ]
    3FA8 X-ray 1.78 A/B 2-138 [» ]
    3FA9 X-ray 1.94 A/B 2-138 [» ]
    3FEK X-ray 1.51 A/B 2-138 [» ]
    3FEL X-ray 1.85 A/B 2-138 [» ]
    3FEN X-ray 1.56 A/B 2-138 [» ]
    3FEP X-ray 2.60 A 2-138 [» ]
    3I17 X-ray 1.68 A/B 2-138 [» ]
    4I9R X-ray 2.60 A 2-138 [» ]
    4I9S X-ray 2.58 A 2-138 [» ]
    4M6S X-ray 2.47 A 2-138 [» ]
    4M7M X-ray 2.57 A 2-138 [» ]
    ProteinModelPortali P29373.
    SMRi P29373. Positions 2-138.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 107773. 6 interactions.
    STRINGi 9606.ENSP00000357204.

    Chemistry

    ChEMBLi CHEMBL2221342.
    DrugBanki DB00523. Alitretinoin.

    PTM databases

    PhosphoSitei P29373.

    Polymorphism databases

    DMDMi 132401.

    2D gel databases

    DOSAC-COBS-2DPAGE P29373.

    Proteomic databases

    MaxQBi P29373.
    PaxDbi P29373.
    PeptideAtlasi P29373.
    PRIDEi P29373.

    Protocols and materials databases

    DNASUi 1382.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000368221 ; ENSP00000357204 ; ENSG00000143320 .
    ENST00000368222 ; ENSP00000357205 ; ENSG00000143320 .
    GeneIDi 1382.
    KEGGi hsa:1382.
    UCSCi uc001fpr.3. human.

    Organism-specific databases

    CTDi 1382.
    GeneCardsi GC01M156669.
    HGNCi HGNC:2339. CRABP2.
    HPAi HPA004135.
    MIMi 180231. gene.
    neXtProti NX_P29373.
    PharmGKBi PA26859.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG300013.
    HOGENOMi HOG000004831.
    HOVERGENi HBG005633.
    InParanoidi P29373.
    KOi K17289.
    OMAi GELVLTM.
    OrthoDBi EOG7NW6BZ.
    PhylomeDBi P29373.
    TreeFami TF316894.

    Miscellaneous databases

    EvolutionaryTracei P29373.
    GeneWikii CRABP2.
    GenomeRNAii 1382.
    NextBioi 5615.
    PROi P29373.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P29373.
    Bgeei P29373.
    CleanExi HS_CRABP2.
    Genevestigatori P29373.

    Family and domain databases

    Gene3Di 2.40.128.20. 1 hit.
    InterProi IPR012674. Calycin.
    IPR011038. Calycin-like.
    IPR000463. Fatty_acid-bd.
    IPR000566. Lipocln_cytosolic_FA-bd_dom.
    [Graphical view ]
    Pfami PF00061. Lipocalin. 1 hit.
    [Graphical view ]
    PRINTSi PR00178. FATTYACIDBP.
    SUPFAMi SSF50814. SSF50814. 1 hit.
    PROSITEi PS00214. FABP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 145 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