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P30533

- AMRP_HUMAN

UniProt

P30533 - AMRP_HUMAN

Protein

Alpha-2-macroglobulin receptor-associated protein

Gene

LRPAP1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 143 (01 Oct 2014)
      Sequence version 1 (01 Apr 1993)
      Previous versions | rss
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    Functioni

    Interacts with LRP1/alpha-2-macroglobulin receptor and glycoprotein 330.

    GO - Molecular functioni

    1. asialoglycoprotein receptor activity Source: ProtInc
    2. heparin binding Source: ProtInc
    3. low-density lipoprotein particle receptor binding Source: MGI
    4. protein binding Source: IntAct
    5. receptor antagonist activity Source: BHF-UCL
    6. unfolded protein binding Source: ProtInc
    7. very-low-density lipoprotein particle receptor binding Source: BHF-UCL

    GO - Biological processi

    1. extracellular negative regulation of signal transduction Source: GOC
    2. negative regulation of beta-amyloid clearance Source: BHF-UCL
    3. negative regulation of protein binding Source: BHF-UCL
    4. negative regulation of very-low-density lipoprotein particle clearance Source: BHF-UCL
    5. protein folding Source: ProtInc
    6. receptor-mediated endocytosis Source: GOC
    7. vesicle-mediated transport Source: ProtInc

    Keywords - Ligandi

    Heparin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Alpha-2-macroglobulin receptor-associated protein
    Short name:
    Alpha-2-MRAP
    Alternative name(s):
    Low density lipoprotein receptor-related protein-associated protein 1
    Short name:
    RAP
    Gene namesi
    Name:LRPAP1
    Synonyms:A2MRAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 4

    Organism-specific databases

    HGNCiHGNC:6701. LRPAP1.

    Subcellular locationi

    Endoplasmic reticulum. Cytoplasm. Cell surface
    Note: Intracellular and associated with cell surface receptors. Found in the endoplasmic reticulum.

    GO - Cellular componenti

    1. cell surface Source: UniProtKB-SubCell
    2. endoplasmic reticulum Source: HPA
    3. extracellular region Source: GOC
    4. integral component of membrane Source: ProtInc
    5. plasma membrane Source: MGI
    6. rough endoplasmic reticulum lumen Source: Ensembl
    7. vesicle Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Endoplasmic reticulum

    Pathology & Biotechi

    Involvement in diseasei

    Myopia 23, autosomal recessive (MYP23) [MIM:615431]: A refractive error of the eye, in which parallel rays from a distant object come to focus in front of the retina, vision being better for near objects than for far.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    In complex with the alpha-2-MR or gp330, it may have some role in the pathogenesis of membrane glomerular nephritis.

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi283 – 2831H → A: Strongly reduced interaction with LRP1; when associated with A-291; A-293; A-302; A-307 and A-341. 1 Publication
    Mutagenesisi291 – 2911H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-293; A-302; A-307 and A-341. 1 Publication
    Mutagenesisi293 – 2931H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-302; A-307 and A-341. 1 Publication
    Mutagenesisi302 – 3021H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-307 and A-341. 1 Publication
    Mutagenesisi307 – 3071H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-302 and A-341. 1 Publication
    Mutagenesisi341 – 3411H → A: Strongly reduced interaction with LRP1; when associated with A-283; A-291; A-293; A-302 and A-307. 1 Publication

    Organism-specific databases

    MIMi615431. phenotype.
    Orphaneti98619. Rare isolated myopia.
    PharmGKBiPA30458.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3434Sequence AnalysisAdd
    BLAST
    Chaini35 – 357323Alpha-2-macroglobulin receptor-associated proteinPRO_0000020724Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Glycosylationi268 – 2681N-linked (GlcNAc...)2 Publications

    Post-translational modificationi

    N-glycosylated.2 Publications

    Keywords - PTMi

    Glycoprotein

    Proteomic databases

    MaxQBiP30533.
    PaxDbiP30533.
    PeptideAtlasiP30533.
    PRIDEiP30533.

    PTM databases

    PhosphoSiteiP30533.

    Expressioni

    Gene expression databases

    ArrayExpressiP30533.
    BgeeiP30533.
    CleanExiHS_LRPAP1.
    GenevestigatoriP30533.

    Organism-specific databases

    HPAiCAB025518.
    HPA008001.

    Interactioni

    Subunit structurei

    Present on cell surface forming a complex with the alpha-2-macroglobulin receptor heavy and light chains. Binds LRP1B; binding is followed by internalization and degradation.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    VLDLRP981554EBI-715927,EBI-9004309

    Protein-protein interaction databases

    BioGridi110221. 20 interactions.
    DIPiDIP-39355N.
    IntActiP30533. 13 interactions.
    MINTiMINT-1382467.
    STRINGi9606.ENSP00000296325.

    Structurei

    Secondary structure

    1
    357
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi53 – 564
    Helixi57 – 6812
    Helixi73 – 9927
    Helixi107 – 12216
    Beta strandi124 – 1263
    Beta strandi127 – 1304
    Helixi149 – 16113
    Helixi166 – 19530
    Beta strandi208 – 2103
    Beta strandi213 – 2164
    Helixi217 – 24327
    Beta strandi246 – 2494
    Helixi255 – 26511
    Helixi271 – 31141
    Turni314 – 3163
    Helixi317 – 35337

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1LRENMR-A51-131[»]
    1NRENMR-A51-131[»]
    1OP1NMR-A51-132[»]
    1OV2NMR-A35-133[»]
    2FCWX-ray1.26A249-357[»]
    2FTUNMR-A240-357[»]
    2FYLNMR-A51-131[»]
    2P01NMR-A35-357[»]
    2P03NMR-A35-357[»]
    ProteinModelPortaliP30533.
    SMRiP30533. Positions 35-357.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiP30533.

    Family & Domainsi

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni237 – 353117LDL receptor bindingSequence AnalysisAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili219 – 31092Sequence AnalysisAdd
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi354 – 3574Prevents secretion from ERPROSITE-ProRule annotation

    Sequence similaritiesi

    Belongs to the alpha-2-MRAP family.Curated

    Keywords - Domaini

    Coiled coil, Signal

    Phylogenomic databases

    eggNOGiNOG323629.
    HOGENOMiHOG000033926.
    HOVERGENiHBG000197.
    InParanoidiP30533.
    OMAiFRMAKLN.
    OrthoDBiEOG7P5T15.
    PhylomeDBiP30533.
    TreeFamiTF320678.

    Family and domain databases

    Gene3Di1.20.81.10. 1 hit.
    InterProiIPR010483. Alpha_2_MRAP_C.
    IPR009066. MG_RAP_rcpt_1.
    [Graphical view]
    PfamiPF06401. Alpha-2-MRAP_C. 1 hit.
    PF06400. Alpha-2-MRAP_N. 1 hit.
    [Graphical view]
    SUPFAMiSSF47045. SSF47045. 3 hits.
    PROSITEiPS00014. ER_TARGET. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P30533-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAPRRVRSFL RGLPALLLLL LFLGPWPAAS HGGKYSREKN QPKPSPKRES    50
    GEEFRMEKLN QLWEKAQRLH LPPVRLAELH ADLKIQERDE LAWKKLKLDG 100
    LDEDGEKEAR LIRNLNVILA KYGLDGKKDA RQVTSNSLSG TQEDGLDDPR 150
    LEKLWHKAKT SGKFSGEELD KLWREFLHHK EKVHEYNVLL ETLSRTEEIH 200
    ENVISPSDLS DIKGSVLHSR HTELKEKLRS INQGLDRLRR VSHQGYSTEA 250
    EFEEPRVIDL WDLAQSANLT DKELEAFREE LKHFEAKIEK HNHYQKQLEI 300
    AHEKLRHAES VGDGERVSRS REKHALLEGR TKELGYTVKK HLQDLSGRIS 350
    RARHNEL 357
    Length:357
    Mass (Da):41,466
    Last modified:April 1, 1993 - v1
    Checksum:iD56A7DA754125CFA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti100 – 1001G → D in BAD96247. 1 PublicationCurated
    Sequence conflicti183 – 1831V → A in BAD96224. 1 PublicationCurated
    Sequence conflicti339 – 3391K → M in BAD96247. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti114 – 1141N → S.
    Corresponds to variant rs2228158 [ dbSNP | Ensembl ].
    VAR_050660
    Natural varianti311 – 3111V → M.1 Publication
    Corresponds to variant rs1800493 [ dbSNP | Ensembl ].
    VAR_011821

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63959 mRNA. Translation: AAA51553.1.
    AF035767
    , AF035760, AF035761, AF035762, AF035763, AF035764, AF035765, AF035766 Genomic DNA. Translation: AAC67373.1.
    AK222504 mRNA. Translation: BAD96224.1.
    AK222527 mRNA. Translation: BAD96247.1.
    AL590235 Genomic DNA. Translation: CAM21451.1.
    CH471131 Genomic DNA. Translation: EAW82460.1.
    CH471131 Genomic DNA. Translation: EAW82461.1.
    BC105074 mRNA. Translation: AAI05075.1.
    BC112067 mRNA. Translation: AAI12068.1.
    U06976 Genomic DNA. Translation: AAA87889.1.
    CCDSiCCDS3371.1.
    PIRiA39875.
    RefSeqiNP_002328.1. NM_002337.3.
    UniGeneiHs.40966.

    Genome annotation databases

    EnsembliENST00000500728; ENSP00000421922; ENSG00000163956.
    GeneIDi4043.
    KEGGihsa:4043.
    UCSCiuc003ghh.4. human.

    Polymorphism databases

    DMDMi231539.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    M63959 mRNA. Translation: AAA51553.1 .
    AF035767
    , AF035760 , AF035761 , AF035762 , AF035763 , AF035764 , AF035765 , AF035766 Genomic DNA. Translation: AAC67373.1 .
    AK222504 mRNA. Translation: BAD96224.1 .
    AK222527 mRNA. Translation: BAD96247.1 .
    AL590235 Genomic DNA. Translation: CAM21451.1 .
    CH471131 Genomic DNA. Translation: EAW82460.1 .
    CH471131 Genomic DNA. Translation: EAW82461.1 .
    BC105074 mRNA. Translation: AAI05075.1 .
    BC112067 mRNA. Translation: AAI12068.1 .
    U06976 Genomic DNA. Translation: AAA87889.1 .
    CCDSi CCDS3371.1.
    PIRi A39875.
    RefSeqi NP_002328.1. NM_002337.3.
    UniGenei Hs.40966.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1LRE NMR - A 51-131 [» ]
    1NRE NMR - A 51-131 [» ]
    1OP1 NMR - A 51-132 [» ]
    1OV2 NMR - A 35-133 [» ]
    2FCW X-ray 1.26 A 249-357 [» ]
    2FTU NMR - A 240-357 [» ]
    2FYL NMR - A 51-131 [» ]
    2P01 NMR - A 35-357 [» ]
    2P03 NMR - A 35-357 [» ]
    ProteinModelPortali P30533.
    SMRi P30533. Positions 35-357.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 110221. 20 interactions.
    DIPi DIP-39355N.
    IntActi P30533. 13 interactions.
    MINTi MINT-1382467.
    STRINGi 9606.ENSP00000296325.

    PTM databases

    PhosphoSitei P30533.

    Polymorphism databases

    DMDMi 231539.

    Proteomic databases

    MaxQBi P30533.
    PaxDbi P30533.
    PeptideAtlasi P30533.
    PRIDEi P30533.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000500728 ; ENSP00000421922 ; ENSG00000163956 .
    GeneIDi 4043.
    KEGGi hsa:4043.
    UCSCi uc003ghh.4. human.

    Organism-specific databases

    CTDi 4043.
    GeneCardsi GC04M003508.
    HGNCi HGNC:6701. LRPAP1.
    HPAi CAB025518.
    HPA008001.
    MIMi 104225. gene.
    615431. phenotype.
    neXtProti NX_P30533.
    Orphaneti 98619. Rare isolated myopia.
    PharmGKBi PA30458.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG323629.
    HOGENOMi HOG000033926.
    HOVERGENi HBG000197.
    InParanoidi P30533.
    OMAi FRMAKLN.
    OrthoDBi EOG7P5T15.
    PhylomeDBi P30533.
    TreeFami TF320678.

    Miscellaneous databases

    ChiTaRSi LRPAP1. human.
    EvolutionaryTracei P30533.
    GeneWikii LDL-receptor-related_protein_associated_protein.
    GenomeRNAii 4043.
    NextBioi 15830.
    PROi P30533.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P30533.
    Bgeei P30533.
    CleanExi HS_LRPAP1.
    Genevestigatori P30533.

    Family and domain databases

    Gene3Di 1.20.81.10. 1 hit.
    InterProi IPR010483. Alpha_2_MRAP_C.
    IPR009066. MG_RAP_rcpt_1.
    [Graphical view ]
    Pfami PF06401. Alpha-2-MRAP_C. 1 hit.
    PF06400. Alpha-2-MRAP_N. 1 hit.
    [Graphical view ]
    SUPFAMi SSF47045. SSF47045. 3 hits.
    PROSITEi PS00014. ER_TARGET. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Primary structure of alpha 2-macroglobulin receptor-associated protein. Human homologue of a Heymann nephritis antigen."
      Strickland D.K., Ashcom J.D., Williams S., Battey F., Behre E., McTigue K., Battey J.F., Argraves W.S.
      J. Biol. Chem. 266:13364-13369(1991) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 183-195 AND 257-272.
      Tissue: Placenta.
    2. "Analysis of the human LRPAP1 gene coding for the lipoprotein receptor-associated protein: identification of 22 polymorphisms and one mutation."
      Van Leuven F., Thiry E., Stas L., Nelissen B.
      Genomics 52:145-151(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANT MET-311.
    3. Suzuki Y., Sugano S., Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.
      Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Adipose tissue.
    4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
      Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
      , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
      Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "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: Brain.
    7. "Cloning, characterization, and chromosomal localization to 4p16 of the human gene (LRPAP1) coding for the alpha 2-macroglobulin receptor-associated protein and structural comparison with the murine gene coding for the 44-kDa heparin-binding protein."
      Van Leuven F., Hilliker C., Serneels L., Umans L., Overbergh L., Strooper B., Fryns J.-P., Van den Berghe H.
      Genomics 25:492-500(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 204-250.
    8. "The 39-kDa receptor-associated protein interacts with two members of the low density lipoprotein receptor family, alpha 2-macroglobulin receptor and glycoprotein 330."
      Kounnas M.Z., Argraves W.S., Strickland D.K.
      J. Biol. Chem. 267:21162-21166(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION.
    9. "39 kDa receptor-associated protein is an ER resident protein and molecular chaperone for LDL receptor-related protein."
      Bu G., Geuze H.J., Strous G.J., Schwartz A.L.
      EMBO J. 14:2269-2280(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUBCELLULAR LOCATION, INTERACTION WITH LRP1.
    10. "The putative tumor suppressor LRP1B, a novel member of the low density lipoprotein (LDL) receptor family, exhibits both overlapping and distinct properties with the LDL receptor-related protein."
      Liu C.-X., Li Y., Obermoeller-McCormick L.M., Schwartz A.L., Bu G.
      J. Biol. Chem. 276:28889-28896(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH LRP1B.
    11. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
      Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
      J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-268.
      Tissue: Liver.
    12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    13. Cited for: INVOLVEMENT IN MYP23.
    14. "The solution structure of the N-terminal domain of alpha2-macroglobulin receptor-associated protein."
      Nielsen P.R., Ellgaard L., Etzerodt M., Thoegersen H.C., Poulsen F.M.
      Proc. Natl. Acad. Sci. U.S.A. 94:7521-7525(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 51-131.
    15. "1H, 13C and 15N resonance assignments of domain 1 of receptor associated protein."
      Wu Y., Migliorini M., Yu P., Strickland D.K., Wang Y.-X.
      J. Biomol. NMR 26:187-188(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 51-132.
    16. "Binding site structure of one LRP-RAP complex: implications for a common ligand-receptor binding motif."
      Jensen G.A., Andersen O.M.J.J., Bonvin A.M., Bjerrum-Bohr I., Etzerodt M., Thoegersen H.C., O'Shea C., Poulsen F.M., Kragelund B.B.
      J. Mol. Biol. 362:700-716(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 51-131 IN COMPLEX WITH LRP1.
    17. "Structure of an LDLR-RAP complex reveals a general mode for ligand recognition by lipoprotein receptors."
      Fisher C., Beglova N., Blacklow S.C.
      Mol. Cell 22:277-283(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.26 ANGSTROMS) OF 250-357 IN COMPLEX WITH LDLR.
    18. Cited for: STRUCTURE BY NMR OF 240-357, INTERACTION WITH LRP1, SUBCELLULAR LOCATION, GLYCOSYLATION, MUTAGENESIS OF HIS-283; HIS-291; HIS-293; HIS-302; HIS-307 AND HIS-341.

    Entry informationi

    Entry nameiAMRP_HUMAN
    AccessioniPrimary (citable) accession number: P30533
    Secondary accession number(s): D3DVR9
    , Q2M310, Q53HQ3, Q53HS6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: April 1, 1993
    Last sequence update: April 1, 1993
    Last modified: October 1, 2014
    This is version 143 of the entry and version 1 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, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 4
      Human chromosome 4: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3