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P50120

- RET2_HUMAN

UniProt

P50120 - RET2_HUMAN

Protein

Retinol-binding protein 2

Gene

RBP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 4 out of 5- Experimental evidence at protein leveli
  1. Functioni

    Intracellular transport of retinol.

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Binding sitei41 – 411Retinoic acid
    Binding sitei109 – 1091Retinoic acidBy similarity

    GO - Molecular functioni

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

    GO - Biological processi

    1. epidermis development Source: ProtInc
    2. phototransduction, visible light Source: Reactome
    3. retinoid metabolic process Source: Reactome
    4. vitamin A metabolic process Source: ProtInc

    Keywords - Biological processi

    Transport

    Keywords - Ligandi

    Retinol-binding, Vitamin A

    Enzyme and pathway databases

    BioCyciMetaCyc:ENSG00000114113-MONOMER.
    ReactomeiREACT_24968. Retinoid metabolism and transport.

    Protein family/group databases

    TCDBi8.A.33.1.3. the fatty acid binding protein (fabp) family.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Retinol-binding protein 2
    Alternative name(s):
    Cellular retinol-binding protein II
    Short name:
    CRBP-II
    Gene namesi
    Name:RBP2
    Synonyms:CRBP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 3

    Organism-specific databases

    HGNCiHGNC:9920. RBP2.

    Subcellular locationi

    GO - Cellular componenti

    1. cytosol Source: Reactome

    Keywords - Cellular componenti

    Cytoplasm

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34287.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11RemovedBy similarity
    Chaini2 – 134133Retinol-binding protein 2PRO_0000067395Add
    BLAST

    Proteomic databases

    MaxQBiP50120.
    PaxDbiP50120.
    PRIDEiP50120.

    PTM databases

    PhosphoSiteiP50120.

    Expressioni

    Tissue specificityi

    Higher expression in adult small intestine and to a much lesser extent in fetal kidney.1 Publication

    Gene expression databases

    ArrayExpressiP50120.
    BgeeiP50120.
    CleanExiHS_RBP2.
    GenevestigatoriP50120.

    Organism-specific databases

    HPAiHPA035866.

    Interactioni

    Protein-protein interaction databases

    BioGridi111882. 3 interactions.
    STRINGi9606.ENSP00000232217.

    Structurei

    Secondary structure

    1
    134
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi7 – 1610
    Helixi17 – 237
    Helixi28 – 347
    Beta strandi40 – 467
    Beta strandi49 – 557
    Beta strandi60 – 667
    Beta strandi71 – 744
    Turni76 – 794
    Beta strandi82 – 909
    Beta strandi93 – 10210
    Beta strandi106 – 1127
    Beta strandi115 – 1228
    Beta strandi125 – 13410

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2RCQX-ray1.20A2-134[»]
    2RCTX-ray1.20A2-134[»]
    4EDEX-ray1.40A/B2-134[»]
    4EEJX-ray1.50A/B2-134[»]
    4EFGX-ray1.58A/B2-134[»]
    4EXZX-ray1.61A/B2-134[»]
    4GKCX-ray1.30A/B2-134[»]
    ProteinModelPortaliP50120.
    SMRiP50120. Positions 2-134.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP50120.

    Family & Domainsi

    Domaini

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

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG284832.
    HOGENOMiHOG000004831.
    HOVERGENiHBG005633.
    InParanoidiP50120.
    KOiK14622.
    OMAiKKEGYKP.
    OrthoDBiEOG7NW6BZ.
    PhylomeDBiP50120.
    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.

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

    P50120-1 [UniParc]FASTAAdd to Basket

    « Hide

    MTRDQNGTWE MESNENFEGY MKALDIDFAT RKIAVRLTQT KVIDQDGDNF    50
    KTKTTSTFRN YDVDFTVGVE FDEYTKSLDN RHVKALVTWE GDVLVCVQKG 100
    EKENRGWKQW IEGDKLYLEL TCGDQVCRQV FKKK 134
    Length:134
    Mass (Da):15,707
    Last modified:January 23, 2007 - v3
    Checksum:iA4A7FB157B099A7D
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311R → P in AAC50162. (PubMed:7657783)Curated
    Sequence conflicti114 – 1141D → G in AAH69396. (PubMed:15489334)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13831 mRNA. Translation: AAC50162.1.
    AK291978 mRNA. Translation: BAF84667.1.
    CH471052 Genomic DNA. Translation: EAW79036.1.
    BC069296 mRNA. Translation: AAH69296.1.
    BC069361 mRNA. Translation: AAH69361.1.
    BC069396 mRNA. Translation: AAH69396.1.
    BC069424 mRNA. Translation: AAH69424.1.
    BC069447 mRNA. Translation: AAH69447.1.
    BC069513 mRNA. Translation: AAH69513.1.
    BC069522 mRNA. Translation: AAH69522.1.
    CCDSiCCDS3109.1.
    RefSeqiNP_004155.2. NM_004164.2.
    XP_005247750.1. XM_005247693.1.
    XP_006713785.1. XM_006713722.1.
    UniGeneiHs.655516.

    Genome annotation databases

    EnsembliENST00000232217; ENSP00000232217; ENSG00000114113.
    GeneIDi5948.
    KEGGihsa:5948.
    UCSCiuc003eth.3. human.

    Polymorphism databases

    DMDMi62297500.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    U13831 mRNA. Translation: AAC50162.1 .
    AK291978 mRNA. Translation: BAF84667.1 .
    CH471052 Genomic DNA. Translation: EAW79036.1 .
    BC069296 mRNA. Translation: AAH69296.1 .
    BC069361 mRNA. Translation: AAH69361.1 .
    BC069396 mRNA. Translation: AAH69396.1 .
    BC069424 mRNA. Translation: AAH69424.1 .
    BC069447 mRNA. Translation: AAH69447.1 .
    BC069513 mRNA. Translation: AAH69513.1 .
    BC069522 mRNA. Translation: AAH69522.1 .
    CCDSi CCDS3109.1.
    RefSeqi NP_004155.2. NM_004164.2.
    XP_005247750.1. XM_005247693.1.
    XP_006713785.1. XM_006713722.1.
    UniGenei Hs.655516.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2RCQ X-ray 1.20 A 2-134 [» ]
    2RCT X-ray 1.20 A 2-134 [» ]
    4EDE X-ray 1.40 A/B 2-134 [» ]
    4EEJ X-ray 1.50 A/B 2-134 [» ]
    4EFG X-ray 1.58 A/B 2-134 [» ]
    4EXZ X-ray 1.61 A/B 2-134 [» ]
    4GKC X-ray 1.30 A/B 2-134 [» ]
    ProteinModelPortali P50120.
    SMRi P50120. Positions 2-134.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 111882. 3 interactions.
    STRINGi 9606.ENSP00000232217.

    Chemistry

    BindingDBi P50120.
    DrugBanki DB00162. Vitamin A.

    Protein family/group databases

    TCDBi 8.A.33.1.3. the fatty acid binding protein (fabp) family.

    PTM databases

    PhosphoSitei P50120.

    Polymorphism databases

    DMDMi 62297500.

    Proteomic databases

    MaxQBi P50120.
    PaxDbi P50120.
    PRIDEi P50120.

    Protocols and materials databases

    DNASUi 5948.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000232217 ; ENSP00000232217 ; ENSG00000114113 .
    GeneIDi 5948.
    KEGGi hsa:5948.
    UCSCi uc003eth.3. human.

    Organism-specific databases

    CTDi 5948.
    GeneCardsi GC03M139171.
    HGNCi HGNC:9920. RBP2.
    HPAi HPA035866.
    MIMi 180280. gene.
    neXtProti NX_P50120.
    PharmGKBi PA34287.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG284832.
    HOGENOMi HOG000004831.
    HOVERGENi HBG005633.
    InParanoidi P50120.
    KOi K14622.
    OMAi KKEGYKP.
    OrthoDBi EOG7NW6BZ.
    PhylomeDBi P50120.
    TreeFami TF316894.

    Enzyme and pathway databases

    BioCyci MetaCyc:ENSG00000114113-MONOMER.
    Reactomei REACT_24968. Retinoid metabolism and transport.

    Miscellaneous databases

    EvolutionaryTracei P50120.
    GeneWikii RBP2.
    GenomeRNAii 5948.
    NextBioi 23174.
    PROi P50120.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P50120.
    Bgeei P50120.
    CleanExi HS_RBP2.
    Genevestigatori P50120.

    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. "Variation in the expression of cellular retinoid binding proteins in human endometrium throughout the menstrual cycle."
      Loughney A.D., Kumarendran M.K., Thomas E.J., Redfern C.P.F.
      Hum. Reprod. 10:1297-1304(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    2. "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: Small intestine.
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "Identification, retinoid binding and X-ray analysis of a human retinol-binding protein."
      Folli C., Calderone V., Ottonello S., Bolchi A., Zanotti G., Stoppini M., Berni R.
      Proc. Natl. Acad. Sci. U.S.A. 98:3710-3715(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    6. "Crystal structure of human cellular retinol-binding protein II to 1.2 A resolution."
      Tarter M., Capaldi S., Carrizo M.E., Ambrosi E., Perduca M., Monaco H.L.
      Proteins 70:1626-1630(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.2 ANGSTROMS) IN COMPLEX WITH RETINOL.

    Entry informationi

    Entry nameiRET2_HUMAN
    AccessioniPrimary (citable) accession number: P50120
    Secondary accession number(s): A8K7G3, Q6ISQ9, Q6ISS7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: January 23, 2007
    Last modified: October 1, 2014
    This is version 127 of the entry and version 3 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 3
      Human chromosome 3: 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