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O60895

- RAMP2_HUMAN

UniProt

O60895 - RAMP2_HUMAN

Protein

Receptor activity-modifying protein 2

Gene

RAMP2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 128 (01 Oct 2014)
      Sequence version 2 (10 Jan 2003)
      Previous versions | rss
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    Functioni

    Transports the calcitonin gene-related peptide type 1 receptor (CALCRL) to the plasma membrane. Acts as a receptor for adrenomedullin (AM) together with CALCRL.2 Publications

    GO - Molecular functioni

    1. coreceptor activity Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein transporter activity Source: InterPro

    GO - Biological processi

    1. adherens junction assembly Source: UniProtKB
    2. angiogenesis Source: UniProtKB
    3. basement membrane assembly Source: UniProtKB
    4. calcium ion transport Source: UniProtKB
    5. cAMP biosynthetic process Source: UniProtKB
    6. cellular response to hormone stimulus Source: Ensembl
    7. cellular response to vascular endothelial growth factor stimulus Source: UniProtKB
    8. female pregnancy Source: Ensembl
    9. G-protein coupled receptor signaling pathway Source: Ensembl
    10. heart development Source: UniProtKB
    11. intracellular protein transport Source: InterPro
    12. negative regulation of endothelial cell apoptotic process Source: UniProtKB
    13. negative regulation of vascular permeability Source: UniProtKB
    14. positive regulation of angiogenesis Source: UniProtKB
    15. positive regulation of cAMP biosynthetic process Source: UniProtKB
    16. positive regulation of gene expression Source: UniProtKB
    17. positive regulation of vasculogenesis Source: Ensembl
    18. protein localization to plasma membrane Source: UniProtKB
    19. protein transport Source: UniProtKB
    20. receptor internalization Source: UniProtKB
    21. regulation of blood pressure Source: UniProtKB
    22. regulation of G-protein coupled receptor protein signaling pathway Source: InterPro
    23. response to estradiol Source: Ensembl
    24. response to hypoxia Source: Ensembl
    25. response to progesterone Source: Ensembl
    26. sprouting angiogenesis Source: UniProtKB
    27. tight junction assembly Source: UniProtKB
    28. vascular smooth muscle cell development Source: UniProtKB
    29. vasculogenesis Source: UniProtKB

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Transport

    Enzyme and pathway databases

    ReactomeiREACT_18290. Calcitonin-like ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Receptor activity-modifying protein 2
    Alternative name(s):
    Calcitonin-receptor-like receptor activity-modifying protein 2
    Short name:
    CRLR activity-modifying protein 2
    Gene namesi
    Name:RAMP2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:9844. RAMP2.

    Subcellular locationi

    GO - Cellular componenti

    1. cell surface Source: UniProtKB
    2. coated pit Source: ProtInc
    3. cytoplasm Source: UniProtKB
    4. integral component of membrane Source: InterPro
    5. integral component of plasma membrane Source: ProtInc
    6. lysosome Source: ProtInc
    7. plasma membrane Source: Reactome
    8. receptor complex Source: UniProtKB

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA34203.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 4242Sequence AnalysisAdd
    BLAST
    Chaini43 – 175133Receptor activity-modifying protein 2PRO_0000030172Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi68 ↔ 99
    Disulfide bondi84 ↔ 131
    Glycosylationi130 – 1301N-linked (GlcNAc...)Sequence Analysis

    Keywords - PTMi

    Disulfide bond, Glycoprotein

    Proteomic databases

    PaxDbiO60895.
    PRIDEiO60895.

    PTM databases

    PhosphoSiteiO60895.

    Expressioni

    Tissue specificityi

    Strongly expressed in lung, breast, immune system and fetal tissues.1 Publication

    Gene expression databases

    ArrayExpressiO60895.
    BgeeiO60895.
    CleanExiHS_RAMP2.
    GenevestigatoriO60895.

    Interactioni

    Subunit structurei

    Heterodimer of CALCRL and RAMP2.By similarity

    Protein-protein interaction databases

    BioGridi115557. 1 interaction.
    STRINGi9606.ENSP00000253796.

    Structurei

    Secondary structure

    1
    175
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi61 – 7616
    Helixi77 – 826
    Helixi86 – 10621
    Helixi114 – 12613
    Turni127 – 1304

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2XVTX-ray2.05A/B/C/D/E/F48-139[»]
    3AQEX-ray2.00A/B/C/D/E/F56-139[»]
    3AQFX-ray2.60A56-139[»]
    ProteinModelPortaliO60895.
    SMRiO60895. Positions 60-135.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini43 – 145103ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini167 – 1759CytoplasmicSequence Analysis

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei146 – 16621HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Sequence similaritiesi

    Belongs to the RAMP family.Curated

    Keywords - Domaini

    Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG42995.
    HOGENOMiHOG000230963.
    HOVERGENiHBG067366.
    InParanoidiO60895.
    KOiK08448.
    PhylomeDBiO60895.
    TreeFamiTF333286.

    Family and domain databases

    InterProiIPR006985. RAMP.
    [Graphical view]
    PANTHERiPTHR14076. PTHR14076. 1 hit.
    PfamiPF04901. RAMP. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

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

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O60895-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MASLRVERAG GPRLPRTRVG RPAALRLLLL LGAVLNPHEA LAQPLPTTGT    50
    PGSEGGTVKN YETAVQFCWN HYKDQMDPIE KDWCDWAMIS RPYSTLRDCL 100
    EHFAELFDLG FPNPLAERII FETHQIHFAN CSLVQPTFSD PPEDVLLAMI 150
    IAPICLIPFL ITLVVWRSKD SEAQA 175
    Length:175
    Mass (Da):19,608
    Last modified:January 10, 2003 - v2
    Checksum:iAF69A9A461EFFCA3
    GO
    Isoform 2 (identifier: O60895-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         54-54: E → EASVPT

    Show »
    Length:180
    Mass (Da):20,063
    Checksum:i17FEBC82A10A0E2F
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti13 – 131R → C in ABS28868. 1 PublicationCurated
    Sequence conflicti25 – 251L → V in CAA04473. (PubMed:9620797)Curated

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei54 – 541E → EASVPT in isoform 2. 1 PublicationVSP_055838

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001015 mRNA. Translation: CAA04473.1.
    EF687002 mRNA. Translation: ABS28868.1.
    AY265458 mRNA. Translation: AAP23299.1.
    AC100793 Genomic DNA. No translation available.
    BC027975 mRNA. Translation: AAH27975.1.
    CCDSiCCDS11437.1.
    RefSeqiNP_005845.2. NM_005854.2.
    UniGeneiHs.514193.

    Genome annotation databases

    EnsembliENST00000253796; ENSP00000253796; ENSG00000131477. [O60895-1]
    ENST00000587142; ENSP00000466455; ENSG00000131477. [O60895-2]
    GeneIDi10266.
    KEGGihsa:10266.
    UCSCiuc002ibg.3. human.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AJ001015 mRNA. Translation: CAA04473.1 .
    EF687002 mRNA. Translation: ABS28868.1 .
    AY265458 mRNA. Translation: AAP23299.1 .
    AC100793 Genomic DNA. No translation available.
    BC027975 mRNA. Translation: AAH27975.1 .
    CCDSi CCDS11437.1.
    RefSeqi NP_005845.2. NM_005854.2.
    UniGenei Hs.514193.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2XVT X-ray 2.05 A/B/C/D/E/F 48-139 [» ]
    3AQE X-ray 2.00 A/B/C/D/E/F 56-139 [» ]
    3AQF X-ray 2.60 A 56-139 [» ]
    ProteinModelPortali O60895.
    SMRi O60895. Positions 60-135.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115557. 1 interaction.
    STRINGi 9606.ENSP00000253796.

    Chemistry

    ChEMBLi CHEMBL2364173.
    DrugBanki DB01278. Pramlintide.

    PTM databases

    PhosphoSitei O60895.

    Proteomic databases

    PaxDbi O60895.
    PRIDEi O60895.

    Protocols and materials databases

    DNASUi 10266.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000253796 ; ENSP00000253796 ; ENSG00000131477 . [O60895-1 ]
    ENST00000587142 ; ENSP00000466455 ; ENSG00000131477 . [O60895-2 ]
    GeneIDi 10266.
    KEGGi hsa:10266.
    UCSCi uc002ibg.3. human.

    Organism-specific databases

    CTDi 10266.
    GeneCardsi GC17P040913.
    HGNCi HGNC:9844. RAMP2.
    MIMi 605154. gene.
    neXtProti NX_O60895.
    PharmGKBi PA34203.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG42995.
    HOGENOMi HOG000230963.
    HOVERGENi HBG067366.
    InParanoidi O60895.
    KOi K08448.
    PhylomeDBi O60895.
    TreeFami TF333286.

    Enzyme and pathway databases

    Reactomei REACT_18290. Calcitonin-like ligand receptors.
    REACT_19327. G alpha (s) signalling events.

    Miscellaneous databases

    GeneWikii RAMP2.
    GenomeRNAii 10266.
    NextBioi 38894.
    PROi O60895.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O60895.
    Bgeei O60895.
    CleanExi HS_RAMP2.
    Genevestigatori O60895.

    Family and domain databases

    InterProi IPR006985. RAMP.
    [Graphical view ]
    PANTHERi PTHR14076. PTHR14076. 1 hit.
    Pfami PF04901. RAMP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "RAMPs regulate the transport and ligand specificity of the calcitonin-receptor-like receptor."
      McLatchie L.M., Fraser N.J., Main M.J., Wise A., Brown J., Thompson N., Solari R., Lee M.G., Foord S.M.
      Nature 393:333-339(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, TISSUE SPECIFICITY.
      Tissue: Neuroblastoma.
    2. "Characterization of adrenomedullin receptors and identification of a receptor activity modifying protein 2 (RAMP2) variant in SV40LT-SMC cells."
      Rorabaugh B.R., Witt K.M., Smith D.D., Abel P.W., Scofield M.A.
      Submitted (JUN-2007) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    3. "cDNA clones of human proteins involved in signal transduction sequenced by the Guthrie cDNA resource center (www.cdna.org)."
      Kopatz S.A., Aronstam R.S., Sharma S.V.
      Submitted (MAR-2003) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Heart.
    4. "DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
      Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L.
      , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
      Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 1).
      Tissue: Pancreas.
    6. "Structure of the extracellular domain of human RAMP2."
      Structural genomics consortium (SGC)
      Submitted (DEC-2010) to the PDB data bank
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 48-139, DISULFIDE BONDS.
    7. "Structural basis for extracellular interactions between calcitonin receptor-like receptor and receptor activity-modifying protein 2 for adrenomedullin-specific binding."
      Kusano S., Kukimoto-Niino M., Hino N., Ohsawa N., Okuda K., Sakamoto K., Shirouzu M., Shindo T., Yokoyama S.
      Protein Sci. 21:199-210(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 52-139 IN COMPLEX WITH CALCRL, FUNCTION, DISULFIDE BONDS.

    Entry informationi

    Entry nameiRAMP2_HUMAN
    AccessioniPrimary (citable) accession number: O60895
    Secondary accession number(s): A7L9S6, K7EMD3, Q8N1F2
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: December 1, 2000
    Last sequence update: January 10, 2003
    Last modified: October 1, 2014
    This is version 128 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 17
      Human chromosome 17: 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