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Q9UBG0

- MRC2_HUMAN

UniProt

Q9UBG0 - MRC2_HUMAN

Protein

C-type mannose receptor 2

Gene

MRC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 106 (01 Oct 2014)
      Sequence version 2 (11 Jan 2011)
      Previous versions | rss
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    Functioni

    May play a role as endocytotic lectin receptor displaying calcium-dependent lectin activity. Internalizes glycosylated ligands from the extracellular space for release in an endosomal compartment via clathrin-mediated endocytosis. May be involved in plasminogen activation system controlling the extracellular level of PLAUR/PLAU, and thus may regulate protease activity at the cell surface. May contribute to cellular uptake, remodeling and degradation of extracellular collagen matrices. May play a role during cancer progression as well as in other chronic tissue destructive diseases acting on collagen turnover. May participate in remodeling of extracellular matrix cooperating with the matrix metalloproteinases (MMPs).2 Publications

    GO - Molecular functioni

    1. carbohydrate binding Source: InterPro
    2. collagen binding Source: UniProt
    3. protein binding Source: UniProt

    GO - Biological processi

    1. collagen catabolic process Source: UniProt
    2. endocytosis Source: UniProtKB-KW
    3. osteoblast differentiation Source: UniProt

    Keywords - Molecular functioni

    Receptor

    Keywords - Biological processi

    Endocytosis

    Keywords - Ligandi

    Calcium, Lectin

    Enzyme and pathway databases

    ReactomeiREACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).

    Protein family/group databases

    MEROPSiI63.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    C-type mannose receptor 2
    Alternative name(s):
    C-type lectin domain family 13 member E
    Endocytic receptor 180
    Macrophage mannose receptor 2
    Urokinase-type plasminogen activator receptor-associated protein
    Short name:
    UPAR-associated protein
    Short name:
    Urokinase receptor-associated protein
    CD_antigen: CD280
    Gene namesi
    Name:MRC2
    Synonyms:CLEC13E, ENDO180, KIAA0709, UPARAP
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:16875. MRC2.

    Subcellular locationi

    GO - Cellular componenti

    1. integral component of membrane Source: UniProtKB-KW
    2. membrane Source: UniProt

    Keywords - Cellular componenti

    Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi472 – 4721N → D: Reduced sugar-binding activity. 1 Publication
    Mutagenesisi1452 – 14521Y → A: No alteration of distribution and trafficking. 1 Publication
    Mutagenesisi1464 – 14641E → A: Increased cell surface distribution. 1 Publication
    Mutagenesisi1468 – 14692LV → AA: Reduction of endocytotic activity; distribution almost restricted to the cell surface.

    Organism-specific databases

    PharmGKBiPA134988161.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 3030Sequence AnalysisAdd
    BLAST
    Chaini31 – 14791449C-type mannose receptor 2PRO_0000046078Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi54 ↔ 68By similarity
    Glycosylationi69 – 691N-linked (GlcNAc...) (complex)3 Publications
    Disulfide bondi93 ↔ 112By similarity
    Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi187 ↔ 213By similarity
    Disulfide bondi201 ↔ 228By similarity
    Disulfide bondi266 ↔ 359By similarity
    Disulfide bondi335 ↔ 351By similarity
    Glycosylationi364 – 3641N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi410 ↔ 504By similarity
    Disulfide bondi481 ↔ 496By similarity
    Glycosylationi588 – 5881N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi618 ↔ 635By similarity
    Disulfide bondi704 ↔ 808By similarity
    Disulfide bondi785 ↔ 800By similarity
    Disulfide bondi853 ↔ 950By similarity
    Disulfide bondi927 ↔ 942By similarity
    Glycosylationi954 – 9541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi1029 – 10291N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1078 ↔ 1098By similarity
    Cross-linki1142 – 1142Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO-1)
    Disulfide bondi1220 ↔ 1234By similarity
    Glycosylationi1350 – 13501N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi1369 ↔ 1384By similarity

    Post-translational modificationi

    N-glycosylated.3 Publications

    Keywords - PTMi

    Disulfide bond, Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ9UBG0.
    PaxDbiQ9UBG0.
    PRIDEiQ9UBG0.

    PTM databases

    PhosphoSiteiQ9UBG0.

    Expressioni

    Tissue specificityi

    Ubiquitous with low expression in brain, placenta, lung, kidney, pancreas, spleen, thymus and colon. Expressed in endothelial cells, fibroblasts and macrophages. Highly expressed in fetal lung and kidney.2 Publications

    Gene expression databases

    ArrayExpressiQ9UBG0.
    BgeeiQ9UBG0.
    CleanExiHS_MRC2.
    GenevestigatoriQ9UBG0.

    Organism-specific databases

    HPAiHPA041991.

    Interactioni

    Subunit structurei

    Interacts with C-terminal region of type I collagen/COL1A1 By similarity. Interacts directly with PLAUR/UPAR and PLAU/pro-UPA to form a tri-molecular complex. Interacts with collagen V.By similarity1 Publication

    Protein-protein interaction databases

    BioGridi115231. 3 interactions.
    IntActiQ9UBG0. 1 interaction.
    STRINGi9606.ENSP00000307513.

    Structurei

    3D structure databases

    ProteinModelPortaliQ9UBG0.
    SMRiQ9UBG0. Positions 161-361, 381-645, 681-811, 828-952, 972-1109, 1132-1235, 1260-1396.
    ModBaseiSearch...
    MobiDBiSearch...

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini31 – 14141384ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini1436 – 147944CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei1415 – 143521HelicalSequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini41 – 167127Ricin B-type lectinPROSITE-ProRule annotationAdd
    BLAST
    Domaini182 – 23049Fibronectin type-IIPROSITE-ProRule annotationAdd
    BLAST
    Domaini244 – 360117C-type lectin 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini389 – 505117C-type lectin 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini528 – 644117C-type lectin 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini678 – 809132C-type lectin 4PROSITE-ProRule annotationAdd
    BLAST
    Domaini832 – 951120C-type lectin 5PROSITE-ProRule annotationAdd
    BLAST
    Domaini979 – 1107129C-type lectin 6PROSITE-ProRule annotationAdd
    BLAST
    Domaini1132 – 1243112C-type lectin 7PROSITE-ProRule annotationAdd
    BLAST
    Domaini1273 – 1393121C-type lectin 8PROSITE-ProRule annotationAdd
    BLAST

    Domaini

    C-type lectin domains 3 to 8 are not required for calcium-dependent binding of mannose, fucose and N-acetylglucosamine. C-type lectin domain 2 is responsible for sugar-binding in a calcium-dependent manner.
    Fibronectin type-II domain mediates collagen-binding.
    Ricin B-type lectin domain contacts with the second C-type lectin domain.By similarity

    Sequence similaritiesi

    Contains 8 C-type lectin domains.PROSITE-ProRule annotation
    Contains 1 fibronectin type-II domain.PROSITE-ProRule annotation
    Contains 1 ricin B-type lectin domain.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG288621.
    HOGENOMiHOG000231191.
    HOVERGENiHBG053606.
    InParanoidiQ9UBG0.
    KOiK06560.
    OMAiMEMNEQQ.
    OrthoDBiEOG7FFMQR.
    PhylomeDBiQ9UBG0.
    TreeFamiTF316663.

    Family and domain databases

    Gene3Di2.10.10.10. 1 hit.
    3.10.100.10. 8 hits.
    InterProiIPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR000562. FN_type2_col-bd.
    IPR013806. Kringle-like.
    IPR000772. Ricin_B_lectin.
    [Graphical view]
    PfamiPF00040. fn2. 1 hit.
    PF00059. Lectin_C. 8 hits.
    [Graphical view]
    SMARTiSM00034. CLECT. 8 hits.
    SM00059. FN2. 1 hit.
    SM00458. RICIN. 1 hit.
    [Graphical view]
    SUPFAMiSSF50370. SSF50370. 1 hit.
    SSF56436. SSF56436. 8 hits.
    SSF57440. SSF57440. 1 hit.
    PROSITEiPS00615. C_TYPE_LECTIN_1. 3 hits.
    PS50041. C_TYPE_LECTIN_2. 8 hits.
    PS00023. FN2_1. 1 hit.
    PS51092. FN2_2. 1 hit.
    PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    Q9UBG0-1 [UniParc]FASTAAdd to Basket

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    MGPGRPAPAP WPRHLLRCVL LLGCLHLGRP GAPGDAALPE PNVFLIFSHG     50
    LQGCLEAQGG QVRVTPACNT SLPAQRWKWV SRNRLFNLGT MQCLGTGWPG 100
    TNTTASLGMY ECDREALNLR WHCRTLGDQL SLLLGARTSN ISKPGTLERG 150
    DQTRSGQWRI YGSEEDLCAL PYHEVYTIQG NSHGKPCTIP FKYDNQWFHG 200
    CTSTGREDGH LWCATTQDYG KDERWGFCPI KSNDCETFWD KDQLTDSCYQ 250
    FNFQSTLSWR EAWASCEQQG ADLLSITEIH EQTYINGLLT GYSSTLWIGL 300
    NDLDTSGGWQ WSDNSPLKYL NWESDQPDNP SEENCGVIRT ESSGGWQNRD 350
    CSIALPYVCK KKPNATAEPT PPDRWANVKV ECEPSWQPFQ GHCYRLQAEK 400
    RSWQESKKAC LRGGGDLVSI HSMAELEFIT KQIKQEVEEL WIGLNDLKLQ 450
    MNFEWSDGSL VSFTHWHPFE PNNFRDSLED CVTIWGPEGR WNDSPCNQSL 500
    PSICKKAGQL SQGAAEEDHG CRKGWTWHSP SCYWLGEDQV TYSEARRLCT 550
    DHGSQLVTIT NRFEQAFVSS LIYNWEGEYF WTALQDLNST GSFFWLSGDE 600
    VMYTHWNRDQ PGYSRGGCVA LATGSAMGLW EVKNCTSFRA RYICRQSLGT 650
    PVTPELPGPD PTPSLTGSCP QGWASDTKLR YCYKVFSSER LQDKKSWVQA 700
    QGACQELGAQ LLSLASYEEE HFVANMLNKI FGESEPEIHE QHWFWIGLNR 750
    RDPRGGQSWR WSDGVGFSYH NFDRSRHDDD DIRGCAVLDL ASLQWVAMQC 800
    DTQLDWICKI PRGTDVREPD DSPQGRREWL RFQEAEYKFF EHHSTWAQAQ 850
    RICTWFQAEL TSVHSQAELD FLSHNLQKFS RAQEQHWWIG LHTSESDGRF 900
    RWTDGSIINF ISWAPGKPRP VGKDKKCVYM TASREDWGDQ RCLTALPYIC 950
    KRSNVTKETQ PPDLPTTALG GCPSDWIQFL NKCFQVQGQE PQSRVKWSEA 1000
    QFSCEQQEAQ LVTITNPLEQ AFITASLPNV TFDLWIGLHA SQRDFQWVEQ 1050
    EPLMYANWAP GEPSGPSPAP SGNKPTSCAV VLHSPSAHFT GRWDDRSCTE 1100
    ETHGFICQKG TDPSLSPSPA ALPPAPGTEL SYLNGTFRLL QKPLRWHDAL 1150
    LLCESRNASL AYVPDPYTQA FLTQAARGLR TPLWIGLAGE EGSRRYSWVS 1200
    EEPLNYVGWQ DGEPQQPGGC TYVDVDGAWR TTSCDTKLQG AVCGVSSGPP 1250
    PPRRISYHGS CPQGLADSAW IPFREHCYSF HMELLLGHKE ARQRCQRAGG 1300
    AVLSILDEME NVFVWEHLQS YEGQSRGAWL GMNFNPKGGT LVWQDNTAVN 1350
    YSNWGPPGLG PSMLSHNSCY WIQSNSGLWR PGACTNITMG VVCKLPRAEQ 1400
    SSFSPSALPE NPAALVVVLM AVLLLLALLT AALILYRRRQ SIERGAFEGA 1450
    RYSRSSSSPT EATEKNILVS DMEMNEQQE 1479
    Length:1,479
    Mass (Da):166,674
    Last modified:January 11, 2011 - v2
    Checksum:iAAAA5286F91DF7E7
    GO

    Sequence cautioni

    The sequence BAA31684.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti43 – 431V → I.1 Publication
    Corresponds to variant rs2014055 [ dbSNP | Ensembl ].
    VAR_025304
    Natural varianti1156 – 11561R → H.5 Publications
    Corresponds to variant rs2429387 [ dbSNP | Ensembl ].
    VAR_025305

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF107292 mRNA. Translation: AAF14192.1.
    AF134838 mRNA. Translation: AAD30280.1.
    AB014609 mRNA. Translation: BAA31684.2. Different initiation.
    AC080038 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94341.1.
    CH471109 Genomic DNA. Translation: EAW94342.1.
    BC146647 mRNA. Translation: AAI46648.1.
    BC150212 mRNA. Translation: AAI50213.1.
    BC153884 mRNA. Translation: AAI53885.1.
    CCDSiCCDS11634.1.
    RefSeqiNP_006030.2. NM_006039.4.
    UniGeneiHs.7835.

    Genome annotation databases

    EnsembliENST00000303375; ENSP00000307513; ENSG00000011028.
    GeneIDi9902.
    KEGGihsa:9902.
    UCSCiuc002jad.4. human.

    Polymorphism databases

    DMDMi317373394.

    Keywords - Coding sequence diversityi

    Polymorphism

    Cross-referencesi

    Web resourcesi

    Functional Glycomics Gateway - Glycan Binding

    Endo180

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF107292 mRNA. Translation: AAF14192.1 .
    AF134838 mRNA. Translation: AAD30280.1 .
    AB014609 mRNA. Translation: BAA31684.2 . Different initiation.
    AC080038 Genomic DNA. No translation available.
    CH471109 Genomic DNA. Translation: EAW94341.1 .
    CH471109 Genomic DNA. Translation: EAW94342.1 .
    BC146647 mRNA. Translation: AAI46648.1 .
    BC150212 mRNA. Translation: AAI50213.1 .
    BC153884 mRNA. Translation: AAI53885.1 .
    CCDSi CCDS11634.1.
    RefSeqi NP_006030.2. NM_006039.4.
    UniGenei Hs.7835.

    3D structure databases

    ProteinModelPortali Q9UBG0.
    SMRi Q9UBG0. Positions 161-361, 381-645, 681-811, 828-952, 972-1109, 1132-1235, 1260-1396.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 115231. 3 interactions.
    IntActi Q9UBG0. 1 interaction.
    STRINGi 9606.ENSP00000307513.

    Protein family/group databases

    MEROPSi I63.001.

    PTM databases

    PhosphoSitei Q9UBG0.

    Polymorphism databases

    DMDMi 317373394.

    Proteomic databases

    MaxQBi Q9UBG0.
    PaxDbi Q9UBG0.
    PRIDEi Q9UBG0.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000303375 ; ENSP00000307513 ; ENSG00000011028 .
    GeneIDi 9902.
    KEGGi hsa:9902.
    UCSCi uc002jad.4. human.

    Organism-specific databases

    CTDi 9902.
    GeneCardsi GC17P060704.
    H-InvDB HIX0018596.
    HIX0027238.
    HGNCi HGNC:16875. MRC2.
    HPAi HPA041991.
    MIMi 612264. gene.
    neXtProti NX_Q9UBG0.
    PharmGKBi PA134988161.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG288621.
    HOGENOMi HOG000231191.
    HOVERGENi HBG053606.
    InParanoidi Q9UBG0.
    KOi K06560.
    OMAi MEMNEQQ.
    OrthoDBi EOG7FFMQR.
    PhylomeDBi Q9UBG0.
    TreeFami TF316663.

    Enzyme and pathway databases

    Reactomei REACT_111056. Cross-presentation of soluble exogenous antigens (endosomes).

    Miscellaneous databases

    ChiTaRSi MRC2. human.
    GenomeRNAii 9902.
    NextBioi 37337.
    PROi Q9UBG0.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UBG0.
    Bgeei Q9UBG0.
    CleanExi HS_MRC2.
    Genevestigatori Q9UBG0.

    Family and domain databases

    Gene3Di 2.10.10.10. 1 hit.
    3.10.100.10. 8 hits.
    InterProi IPR001304. C-type_lectin.
    IPR016186. C-type_lectin-like.
    IPR018378. C-type_lectin_CS.
    IPR016187. C-type_lectin_fold.
    IPR000562. FN_type2_col-bd.
    IPR013806. Kringle-like.
    IPR000772. Ricin_B_lectin.
    [Graphical view ]
    Pfami PF00040. fn2. 1 hit.
    PF00059. Lectin_C. 8 hits.
    [Graphical view ]
    SMARTi SM00034. CLECT. 8 hits.
    SM00059. FN2. 1 hit.
    SM00458. RICIN. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50370. SSF50370. 1 hit.
    SSF56436. SSF56436. 8 hits.
    SSF57440. SSF57440. 1 hit.
    PROSITEi PS00615. C_TYPE_LECTIN_1. 3 hits.
    PS50041. C_TYPE_LECTIN_2. 8 hits.
    PS00023. FN2_1. 1 hit.
    PS51092. FN2_2. 1 hit.
    PS50231. RICIN_B_LECTIN. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "A urokinase receptor-associated protein with specific collagen binding properties."
      Behrendt N., Jensen O.N., Engelholm L.H., Moertz E., Mann M., Danoe K.
      J. Biol. Chem. 275:1993-2002(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 350-360, IDENTIFICATION BY MASS SPECTROMETRY, SUBUNIT, VARIANT HIS-1156.
    2. "Endo180, an endocytic recycling glycoprotein related to the macrophage mannose receptor is expressed on fibroblasts, endothelial cells and macrophages and functions as a lectin receptor."
      Sheikh H., Yarwood H., Ashworth A., Isacke C.M.
      J. Cell Sci. 113:1021-1032(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, PHOSPHORYLATION, GLYCOSYLATION, TISSUE SPECIFICITY, VARIANTS ILE-43 AND HIS-1156.
    3. "Prediction of the coding sequences of unidentified human genes. X. The complete sequences of 100 new cDNA clones from brain which can code for large proteins in vitro."
      Ishikawa K., Nagase T., Suyama M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
      DNA Res. 5:169-176(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-1156.
      Tissue: Brain.
    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. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT HIS-1156.
    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], VARIANT HIS-1156.
    7. "Characterization of a novel member of the macrophage mannose receptor type C lectin family."
      Wu K., Yuan J., Lasky L.A.
      J. Biol. Chem. 271:21323-21330(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: TISSUE SPECIFICITY.
    8. "The C-type lectin receptor Endo180 displays internalization and recycling properties distinct from other members of the mannose receptor family."
      Howard M.J., Isacke C.M.
      J. Biol. Chem. 277:32320-32331(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: MUTAGENESIS OF TYR-1452; GLU-1464 AND 1468-LEU-VAL-1469.
    9. "Characterization of sugar binding by the mannose receptor family member, Endo180."
      East L., Rushton S., Taylor M.E., Isacke C.M.
      J. Biol. Chem. 277:50469-50475(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: DOMAIN, MUTAGENESIS OF ASN-472.
    10. "Identification and characterization of the endocytic transmembrane glycoprotein Endo180 as a novel collagen receptor."
      Wienke D., MacFadyen J.R., Isacke C.M.
      Mol. Biol. Cell 14:3592-3604(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DOMAIN.
    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-69.
      Tissue: Liver.
    12. Cited for: GLYCOSYLATION AT ASN-69.
    13. "In vivo identification of sumoylation sites by a signature tag and cysteine-targeted affinity purification."
      Blomster H.A., Imanishi S.Y., Siimes J., Kastu J., Morrice N.A., Eriksson J.E., Sistonen L.
      J. Biol. Chem. 285:19324-19329(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: SUMOYLATION AT LYS-1142.
      Tissue: Cervix carcinoma.

    Entry informationi

    Entry nameiMRC2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UBG0
    Secondary accession number(s): A6H8K4
    , D3DU08, Q7LGE7, Q9Y5P9
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 7, 2006
    Last sequence update: January 11, 2011
    Last modified: October 1, 2014
    This is version 106 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

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    2. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    3. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    4. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    5. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

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