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Q9UHX3

- EMR2_HUMAN

UniProt

Q9UHX3 - EMR2_HUMAN

Protein

EGF-like module-containing mucin-like hormone receptor-like 2

Gene

EMR2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
    • BLAST
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    • History
      Entry version 140 (01 Oct 2014)
      Sequence version 2 (13 Jun 2006)
      Previous versions | rss
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    Functioni

    Cell surface receptor that binds to the chondroitin sulfate moiety of glycosaminoglycan chains and promotes cell attachment. Promotes granulocyte chemotaxis, degranulation and adhesion. In macrophages, promotes the release of inflammatory cytokines, including IL8 and TNF.3 Publications

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sitei517 – 5182Cleavage

    GO - Molecular functioni

    1. calcium ion binding Source: InterPro
    2. chondroitin sulfate binding Source: UniProtKB
    3. G-protein coupled receptor activity Source: GDB

    GO - Biological processi

    1. cell adhesion Source: UniProtKB
    2. cell migration Source: UniProtKB
    3. G-protein coupled receptor signaling pathway Source: GDB
    4. granulocyte chemotaxis Source: UniProtKB
    5. inflammatory response Source: UniProtKB-KW
    6. neuropeptide signaling pathway Source: InterPro

    Keywords - Molecular functioni

    G-protein coupled receptor, Receptor, Transducer

    Keywords - Biological processi

    Cell adhesion, Inflammatory response

    Keywords - Ligandi

    Calcium

    Enzyme and pathway databases

    ReactomeiREACT_18372. Class B/2 (Secretin family receptors).

    Protein family/group databases

    MEROPSiS63.001.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    EGF-like module-containing mucin-like hormone receptor-like 2
    Alternative name(s):
    EGF-like module receptor 2
    CD_antigen: CD312
    Gene namesi
    Name:EMR2
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:3337. EMR2.

    Subcellular locationi

    Cell membrane; Multi-pass membrane protein. Cell projectionruffle membrane; Multi-pass membrane protein
    Note: Localized at the leading edge of migrating cells.

    GO - Cellular componenti

    1. integral component of membrane Source: GDB
    2. leading edge membrane Source: UniProtKB
    3. plasma membrane Source: Reactome
    4. ruffle membrane Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cell membrane, Cell projection, Membrane

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi518 – 5181S → A: Abolishes cleavage. 1 Publication

    Organism-specific databases

    PharmGKBiPA27774.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Signal peptidei1 – 2323Sequence AnalysisAdd
    BLAST
    Chaini24 – 823800EGF-like module-containing mucin-like hormone receptor-like 2PRO_0000012875Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Disulfide bondi29 ↔ 391 PublicationPROSITE-ProRule annotation
    Disulfide bondi33 ↔ 451 PublicationPROSITE-ProRule annotation
    Glycosylationi41 – 411N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi47 ↔ 651 PublicationPROSITE-ProRule annotation
    Disulfide bondi71 ↔ 851 PublicationPROSITE-ProRule annotation
    Disulfide bondi79 ↔ 941 PublicationPROSITE-ProRule annotation
    Disulfide bondi96 ↔ 1171 PublicationPROSITE-ProRule annotation
    Glycosylationi111 – 1111N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi123 ↔ 1361 PublicationPROSITE-ProRule annotation
    Disulfide bondi130 ↔ 1451 PublicationPROSITE-ProRule annotation
    Disulfide bondi147 ↔ 161PROSITE-ProRule annotation
    Disulfide bondi167 ↔ 180PROSITE-ProRule annotation
    Disulfide bondi174 ↔ 189PROSITE-ProRule annotation
    Disulfide bondi191 ↔ 210PROSITE-ProRule annotation
    Glycosylationi206 – 2061N-linked (GlcNAc...)Sequence Analysis
    Disulfide bondi216 ↔ 229PROSITE-ProRule annotation
    Disulfide bondi223 ↔ 238PROSITE-ProRule annotation
    Disulfide bondi240 ↔ 259PROSITE-ProRule annotation
    Glycosylationi298 – 2981N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi347 – 3471N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi354 – 3541N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi456 – 4561N-linked (GlcNAc...)Sequence Analysis
    Glycosylationi460 – 4601N-linked (GlcNAc...)Sequence Analysis

    Post-translational modificationi

    Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane beta subunit.1 Publication

    Keywords - PTMi

    Autocatalytic cleavage, Disulfide bond, Glycoprotein

    Proteomic databases

    MaxQBiQ9UHX3.
    PaxDbiQ9UHX3.
    PRIDEiQ9UHX3.

    PTM databases

    PhosphoSiteiQ9UHX3.

    Miscellaneous databases

    PMAP-CutDBQ9UHX3.

    Expressioni

    Tissue specificityi

    Expression is restricted to myeloid cells. Highest expression was found in peripheral blood leukocytes, followed by spleen and lymph nodes, with intermediate to low levels in thymus, bone marrow, fetal liver, placenta, and lung, and no expression in heart, brain, skeletal muscle, kidney, or pancreas. Expression is also detected in monocyte/macrophage and Jurkat cell lines but not in other cell lines tested.2 Publications

    Gene expression databases

    ArrayExpressiQ9UHX3.
    BgeeiQ9UHX3.
    CleanExiHS_EMR2.
    GenevestigatoriQ9UHX3.

    Interactioni

    Subunit structurei

    Forms a heterodimer, consisting of a large extracellular region non-covalently linked to a seven-transmembrane moiety. Interacts with chondroitin sulfate; the interaction with chondroitin sulfate is calcium-dependent. Interacts with CD55.3 Publications

    Protein-protein interaction databases

    BioGridi119041. 2 interactions.
    STRINGi9606.ENSP00000319883.

    Structurei

    Secondary structure

    1
    823
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi37 – 437
    Beta strandi45 – 473
    Beta strandi54 – 585
    Helixi70 – 723
    Beta strandi74 – 763
    Beta strandi83 – 875
    Beta strandi92 – 965
    Beta strandi100 – 1023
    Beta strandi109 – 1113
    Helixi112 – 1143
    Turni215 – 2195
    Beta strandi227 – 2315
    Beta strandi236 – 2394
    Beta strandi242 – 2443
    Beta strandi248 – 2503
    Beta strandi252 – 2543

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2BO2X-ray2.60A/B25-260[»]
    2BOUX-ray1.90A25-260[»]
    2BOXX-ray2.50A25-260[»]
    ProteinModelPortaliQ9UHX3.
    SMRiQ9UHX3. Positions 28-260, 301-517.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UHX3.

    Topological domain

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Topological domaini24 – 540517ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini562 – 5698CytoplasmicSequence Analysis
    Topological domaini591 – 60515ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini627 – 64418CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini666 – 68318ExtracellularSequence AnalysisAdd
    BLAST
    Topological domaini705 – 73531CytoplasmicSequence AnalysisAdd
    BLAST
    Topological domaini757 – 7604ExtracellularSequence Analysis
    Topological domaini782 – 82342CytoplasmicSequence AnalysisAdd
    BLAST

    Transmembrane

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Transmembranei541 – 56121Helical; Name=1Sequence AnalysisAdd
    BLAST
    Transmembranei570 – 59021Helical; Name=2Sequence AnalysisAdd
    BLAST
    Transmembranei606 – 62621Helical; Name=3Sequence AnalysisAdd
    BLAST
    Transmembranei645 – 66521Helical; Name=4Sequence AnalysisAdd
    BLAST
    Transmembranei684 – 70421Helical; Name=5Sequence AnalysisAdd
    BLAST
    Transmembranei736 – 75621Helical; Name=6Sequence AnalysisAdd
    BLAST
    Transmembranei761 – 78121Helical; Name=7Sequence AnalysisAdd
    BLAST

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini25 – 6642EGF-like 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini67 – 11852EGF-like 2; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini119 – 16244EGF-like 3; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini163 – 21149EGF-like 4; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini212 – 26049EGF-like 5; calcium-bindingPROSITE-ProRule annotationAdd
    BLAST
    Domaini479 – 52951GPSPROSITE-ProRule annotationAdd
    BLAST

    Domaini

    The GPS domain is necessary, but not sufficient for receptor cleavage, which require the entire extracellular stalk.
    Binding to chondroitin sulfate is mediated by the fourth EGF domain.

    Sequence similaritiesi

    Contains 5 EGF-like domains.PROSITE-ProRule annotation
    Contains 1 GPS domain.PROSITE-ProRule annotation

    Keywords - Domaini

    EGF-like domain, Repeat, Signal, Transmembrane, Transmembrane helix

    Phylogenomic databases

    eggNOGiNOG320737.
    HOVERGENiHBG048917.
    InParanoidiQ9UHX3.
    KOiK08443.
    OrthoDBiEOG75J0MK.
    PhylomeDBiQ9UHX3.
    TreeFamiTF316380.

    Family and domain databases

    InterProiIPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR017981. GPCR_2-like.
    IPR003056. GPCR_2_CD97.
    IPR000832. GPCR_2_secretin-like.
    IPR017983. GPCR_2_secretin-like_CS.
    IPR000203. GPS.
    IPR009030. Growth_fac_rcpt_N_dom.
    [Graphical view]
    PfamiPF00002. 7tm_2. 1 hit.
    PF07645. EGF_CA. 4 hits.
    PF01825. GPS. 1 hit.
    [Graphical view]
    PRINTSiPR01278. CD97PROTEIN.
    PR00249. GPCRSECRETIN.
    SMARTiSM00179. EGF_CA. 4 hits.
    SM00303. GPS. 1 hit.
    [Graphical view]
    SUPFAMiSSF57184. SSF57184. 1 hit.
    PROSITEiPS00010. ASX_HYDROXYL. 4 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 4 hits.
    PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    PS50221. GPS. 1 hit.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

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

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Note: A number of isoforms are probably produced. A soluble form due to a frameshift which introduced a stop codon immediately before the first TM domain is also detected.

    Isoform 1 (identifier: Q9UHX3-1) [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

    MGGRVFLVFL AFCVWLTLPG AETQDSRGCA RWCPQDSSCV NATACRCNPG    50
    FSSFSEIITT PMETCDDINE CATLSKVSCG KFSDCWNTEG SYDCVCSPGY 100
    EPVSGAKTFK NESENTCQDV DECQQNPRLC KSYGTCVNTL GSYTCQCLPG 150
    FKLKPEDPKL CTDVNECTSG QNPCHSSTHC LNNVGSYQCR CRPGWQPIPG 200
    SPNGPNNTVC EDVDECSSGQ HQCDSSTVCF NTVGSYSCRC RPGWKPRHGI 250
    PNNQKDTVCE DMTFSTWTPP PGVHSQTLSR FFDKVQDLGR DYKPGLANNT 300
    IQSILQALDE LLEAPGDLET LPRLQQHCVA SHLLDGLEDV LRGLSKNLSN 350
    GLLNFSYPAG TELSLEVQKQ VDRSVTLRQN QAVMQLDWNQ AQKSGDPGPS 400
    VVGLVSIPGM GKLLAEAPLV LEPEKQMLLH ETHQGLLQDG SPILLSDVIS 450
    AFLSNNDTQN LSSPVTFTFS HRSVIPRQKV LCVFWEHGQN GCGHWATTGC 500
    STIGTRDTST ICRCTHLSSF AVLMAHYDVQ EEDPVLTVIT YMGLSVSLLC 550
    LLLAALTFLL CKAIQNTSTS LHLQLSLCLF LAHLLFLVAI DQTGHKVLCS 600
    IIAGTLHYLY LATLTWMLLE ALYLFLTARN LTVVNYSSIN RFMKKLMFPV 650
    GYGVPAVTVA ISAASRPHLY GTPSRCWLQP EKGFIWGFLG PVCAIFSVNL 700
    VLFLVTLWIL KNRLSSLNSE VSTLRNTRML AFKATAQLFI LGCTWCLGIL 750
    QVGPAARVMA YLFTIINSLQ GVFIFLVYCL LSQQVREQYG KWSKGIRKLK 800
    TESEMHTLSS SAKADTSKPS TVN 823
    Length:823
    Mass (Da):90,472
    Last modified:June 13, 2006 - v2
    Checksum:i4D38C30A07B46FF4
    GO
    Isoform 2 (identifier: Q9UHX3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         397-407: Missing.

    Show »
    Length:812
    Mass (Da):89,466
    Checksum:i9A98853A77E71FFD
    GO
    Isoform 3 (identifier: Q9UHX3-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         163-211: Missing.

    Show »
    Length:774
    Mass (Da):85,230
    Checksum:i9687785185F52A7F
    GO
    Isoform 4 (identifier: Q9UHX3-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         119-211: Missing.

    Show »
    Length:730
    Mass (Da):80,351
    Checksum:iA7509F01725F3A18
    GO
    Isoform 5 (identifier: Q9UHX3-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         119-260: Missing.

    Show »
    Length:681
    Mass (Da):74,936
    Checksum:iADE8AC326340F0CB
    GO
    Isoform 6 (identifier: Q9UHX3-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         473-530: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:765
    Mass (Da):84,079
    Checksum:iD427C949296B61F8
    GO

    Sequence cautioni

    The sequence BAC06146.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti531 – 5311Missing in AAC05172. (PubMed:15057824)Curated
    Sequence conflicti823 – 8231N → R in BAC06146. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti314 – 3141A → V.
    Corresponds to variant rs35612307 [ dbSNP | Ensembl ].
    VAR_061229
    Natural varianti605 – 6051T → I.
    Corresponds to variant rs4410209 [ dbSNP | Ensembl ].
    VAR_026719
    Natural varianti614 – 6141L → F.3 Publications
    Corresponds to variant rs2524383 [ dbSNP | Ensembl ].
    VAR_026720
    Natural varianti665 – 6651S → F.
    Corresponds to variant rs3752187 [ dbSNP | Ensembl ].
    VAR_026721
    Natural varianti720 – 7201E → D.
    Corresponds to variant rs57865820 [ dbSNP | Ensembl ].
    VAR_061230

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei119 – 260142Missing in isoform 5. CuratedVSP_041364Add
    BLAST
    Alternative sequencei119 – 21193Missing in isoform 4. CuratedVSP_041365Add
    BLAST
    Alternative sequencei163 – 21149Missing in isoform 3. CuratedVSP_041366Add
    BLAST
    Alternative sequencei397 – 40711Missing in isoform 2. CuratedVSP_041367Add
    BLAST
    Alternative sequencei473 – 53058Missing in isoform 6. 1 PublicationVSP_047535Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF114491 mRNA. Translation: AAF21974.1.
    AB065931 Genomic DNA. Translation: BAC06146.1. Sequence problems.
    AK298700 mRNA. Translation: BAG60858.1.
    AC004262 Genomic DNA. Translation: AAC05172.1.
    AC005327 Genomic DNA. No translation available.
    AC090427 Genomic DNA. No translation available.
    CCDSiCCDS32935.1. [Q9UHX3-1]
    CCDS59361.1. [Q9UHX3-6]
    RefSeqiNP_001257981.1. NM_001271052.1. [Q9UHX3-6]
    NP_038475.2. NM_013447.3. [Q9UHX3-1]
    UniGeneiHs.531619.

    Genome annotation databases

    EnsembliENST00000315576; ENSP00000319883; ENSG00000127507. [Q9UHX3-1]
    ENST00000392965; ENSP00000376692; ENSG00000127507. [Q9UHX3-6]
    ENST00000594076; ENSP00000472735; ENSG00000127507. [Q9UHX3-4]
    ENST00000594294; ENSP00000470725; ENSG00000127507. [Q9UHX3-3]
    ENST00000595839; ENSP00000469277; ENSG00000127507. [Q9UHX3-5]
    ENST00000596991; ENSP00000472280; ENSG00000127507. [Q9UHX3-2]
    GeneIDi30817.
    KEGGihsa:30817.
    UCSCiuc002mzp.2. human. [Q9UHX3-1]
    uc031rjs.1. human. [Q9UHX3-2]

    Polymorphism databases

    DMDMi108935835.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF114491 mRNA. Translation: AAF21974.1 .
    AB065931 Genomic DNA. Translation: BAC06146.1 . Sequence problems.
    AK298700 mRNA. Translation: BAG60858.1 .
    AC004262 Genomic DNA. Translation: AAC05172.1 .
    AC005327 Genomic DNA. No translation available.
    AC090427 Genomic DNA. No translation available.
    CCDSi CCDS32935.1. [Q9UHX3-1 ]
    CCDS59361.1. [Q9UHX3-6 ]
    RefSeqi NP_001257981.1. NM_001271052.1. [Q9UHX3-6 ]
    NP_038475.2. NM_013447.3. [Q9UHX3-1 ]
    UniGenei Hs.531619.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2BO2 X-ray 2.60 A/B 25-260 [» ]
    2BOU X-ray 1.90 A 25-260 [» ]
    2BOX X-ray 2.50 A 25-260 [» ]
    ProteinModelPortali Q9UHX3.
    SMRi Q9UHX3. Positions 28-260, 301-517.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 119041. 2 interactions.
    STRINGi 9606.ENSP00000319883.

    Protein family/group databases

    MEROPSi S63.001.
    GPCRDBi Search...

    PTM databases

    PhosphoSitei Q9UHX3.

    Polymorphism databases

    DMDMi 108935835.

    Proteomic databases

    MaxQBi Q9UHX3.
    PaxDbi Q9UHX3.
    PRIDEi Q9UHX3.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000315576 ; ENSP00000319883 ; ENSG00000127507 . [Q9UHX3-1 ]
    ENST00000392965 ; ENSP00000376692 ; ENSG00000127507 . [Q9UHX3-6 ]
    ENST00000594076 ; ENSP00000472735 ; ENSG00000127507 . [Q9UHX3-4 ]
    ENST00000594294 ; ENSP00000470725 ; ENSG00000127507 . [Q9UHX3-3 ]
    ENST00000595839 ; ENSP00000469277 ; ENSG00000127507 . [Q9UHX3-5 ]
    ENST00000596991 ; ENSP00000472280 ; ENSG00000127507 . [Q9UHX3-2 ]
    GeneIDi 30817.
    KEGGi hsa:30817.
    UCSCi uc002mzp.2. human. [Q9UHX3-1 ]
    uc031rjs.1. human. [Q9UHX3-2 ]

    Organism-specific databases

    CTDi 30817.
    GeneCardsi GC19M014844.
    H-InvDB HIX0174383.
    HGNCi HGNC:3337. EMR2.
    MIMi 606100. gene.
    neXtProti NX_Q9UHX3.
    PharmGKBi PA27774.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG320737.
    HOVERGENi HBG048917.
    InParanoidi Q9UHX3.
    KOi K08443.
    OrthoDBi EOG75J0MK.
    PhylomeDBi Q9UHX3.
    TreeFami TF316380.

    Enzyme and pathway databases

    Reactomei REACT_18372. Class B/2 (Secretin family receptors).

    Miscellaneous databases

    EvolutionaryTracei Q9UHX3.
    GeneWikii EMR2.
    GenomeRNAii 30817.
    NextBioi 35474078.
    PMAP-CutDB Q9UHX3.
    PROi Q9UHX3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHX3.
    Bgeei Q9UHX3.
    CleanExi HS_EMR2.
    Genevestigatori Q9UHX3.

    Family and domain databases

    InterProi IPR000742. EG-like_dom.
    IPR001881. EGF-like_Ca-bd_dom.
    IPR000152. EGF-type_Asp/Asn_hydroxyl_site.
    IPR018097. EGF_Ca-bd_CS.
    IPR017981. GPCR_2-like.
    IPR003056. GPCR_2_CD97.
    IPR000832. GPCR_2_secretin-like.
    IPR017983. GPCR_2_secretin-like_CS.
    IPR000203. GPS.
    IPR009030. Growth_fac_rcpt_N_dom.
    [Graphical view ]
    Pfami PF00002. 7tm_2. 1 hit.
    PF07645. EGF_CA. 4 hits.
    PF01825. GPS. 1 hit.
    [Graphical view ]
    PRINTSi PR01278. CD97PROTEIN.
    PR00249. GPCRSECRETIN.
    SMARTi SM00179. EGF_CA. 4 hits.
    SM00303. GPS. 1 hit.
    [Graphical view ]
    SUPFAMi SSF57184. SSF57184. 1 hit.
    PROSITEi PS00010. ASX_HYDROXYL. 4 hits.
    PS50026. EGF_3. 4 hits.
    PS01187. EGF_CA. 4 hits.
    PS00650. G_PROTEIN_RECEP_F2_2. 1 hit.
    PS50261. G_PROTEIN_RECEP_F2_4. 1 hit.
    PS50221. GPS. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Human EMR2, a novel EGF-TM7 molecule on chromosome 19p13.1, is closely related to CD97."
      Lin H.-H., Stacey M., Hamann J., Gordon S., McKnight A.J.
      Genomics 67:188-200(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, ALTERNATIVE SPLICING (ISOFORMS 2; 3; 4 AND 5), VARIANT PHE-614.
    2. "Genome-wide discovery and analysis of human seven transmembrane helix receptor genes."
      Suwa M., Sato T., Okouchi I., Arita M., Futami K., Matsumoto S., Tsutsumi S., Aburatani H., Asai K., Akiyama Y.
      Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    3. "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] (ISOFORM 6), VARIANT PHE-614.
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], VARIANT PHE-614.
    5. "Proteolytic cleavage of the EMR2 receptor requires both the extracellular stalk and the GPS motif."
      Chang G.-W., Stacey M., Kwakkenbos M.J., Hamann J., Gordon S., Lin H.-H.
      FEBS Lett. 547:145-150(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PROTEIN SEQUENCE OF 518-527, PROTEOLYTIC PROCESSING, MUTAGENESIS OF SER-518.
    6. "The human EGF-TM7 family member EMR2 is a heterodimeric receptor expressed on myeloid cells."
      Kwakkenbos M.J., Chang G.-W., Lin H.-H., Pouwels W., de Jong E.C., van Lier R.A.W., Gordon S., Hamann J.
      J. Leukoc. Biol. 71:854-862(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: CHARACTERIZATION, TISSUE SPECIFICITY.
    7. "The epidermal growth factor-like domains of the human EMR2 receptor mediate cell attachment through chondroitin sulfate glycosaminoglycans."
      Stacey M., Chang G.-W., Davies J.Q., Kwakkenbos M.J., Sanderson R.D., Hamann J., Gordon S., Lin H.-H.
      Blood 102:2916-2924(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH CHONDROITIN SULFATE.
    8. "Autocatalytic cleavage of the EMR2 receptor occurs at a conserved G protein-coupled receptor proteolytic site motif."
      Lin H.H., Chang G.W., Davies J.Q., Stacey M., Harris J., Gordon S.
      J. Biol. Chem. 279:31823-31832(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: AUTOPROTEOLYTIC CLEAVAGE, SUBUNIT.
    9. Cited for: FUNCTION, SUBCELLULAR LOCATION.
    10. "Activation of myeloid cell-specific adhesion class G protein-coupled receptor EMR2 via ligation-induced translocation and interaction of receptor subunits in lipid raft microdomains."
      Huang Y.S., Chiang N.Y., Hu C.H., Hsiao C.C., Cheng K.F., Tsai W.P., Yona S., Stacey M., Gordon S., Chang G.W., Lin H.H.
      Mol. Cell. Biol. 32:1408-1420(2012) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, SUBCELLULAR LOCATION.
    11. "Structural and functional characterization of a novel T cell receptor co-regulatory protein complex, CD97-CD55."
      Abbott R.J., Spendlove I., Roversi P., Fitzgibbon H., Knott V., Teriete P., McDonnell J.M., Handford P.A., Lea S.M.
      J. Biol. Chem. 282:22023-22032(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 25-260, INTERACTION WITH CD55, CALCIUM-BINDING, DISULFIDE BONDS.

    Entry informationi

    Entry nameiEMR2_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHX3
    Secondary accession number(s): B4DQ96
    , E7ESD7, E9PBR1, E9PEL6, E9PFQ5, E9PG91, Q8NG96, Q9Y4B1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 1, 2004
    Last sequence update: June 13, 2006
    Last modified: October 1, 2014
    This is version 140 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, Direct protein sequencing, Reference proteome

    Documents

    1. 7-transmembrane G-linked receptors
      List of 7-transmembrane G-linked receptor entries
    2. Human cell differentiation molecules
      CD nomenclature of surface proteins of human leucocytes and list of entries
    3. Human chromosome 19
      Human chromosome 19: entries, gene names and cross-references to MIM
    4. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    5. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    6. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    7. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    8. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3