Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q9UHX3 (EMR2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 138. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (8) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
EGF-like module-containing mucin-like hormone receptor-like 2
Alternative name(s):
EGF-like module receptor 2
CD_antigen=CD312
Gene names
Name:EMR2
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length823 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.7 Ref.9 Ref.10

Subunit structure

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. Ref.7 Ref.8 Ref.11

Subcellular location

Cell membrane; Multi-pass membrane protein. Cell projectionruffle membrane; Multi-pass membrane protein. Note: Localized at the leading edge of migrating cells. Ref.9 Ref.10

Tissue specificity

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. Ref.1 Ref.6

Domain

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.

Post-translational modification

Autoproteolytically cleaved into 2 subunits, an extracellular alpha subunit and a seven-transmembrane beta subunit. Ref.5 Ref.8

Sequence similarities

Belongs to the G-protein coupled receptor 2 family. LN-TM7 subfamily.

Contains 5 EGF-like domains.

Contains 1 GPS domain.

Sequence caution

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

Ontologies

Keywords
   Biological processCell adhesion
Inflammatory response
   Cellular componentCell membrane
Cell projection
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainEGF-like domain
Repeat
Signal
Transmembrane
Transmembrane helix
   LigandCalcium
   Molecular functionG-protein coupled receptor
Receptor
Transducer
   PTMAutocatalytic cleavage
Disulfide bond
Glycoprotein
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processG-protein coupled receptor signaling pathway

Traceable author statement PubMed 15203201. Source: GDB

cell adhesion

Inferred from mutant phenotype Ref.7. Source: UniProtKB

cell migration

Inferred from mutant phenotype Ref.9. Source: UniProtKB

granulocyte chemotaxis

Inferred from mutant phenotype Ref.9. Source: UniProtKB

inflammatory response

Inferred from electronic annotation. Source: UniProtKB-KW

neuropeptide signaling pathway

Inferred from electronic annotation. Source: InterPro

   Cellular_componentintegral component of membrane

Traceable author statement PubMed 15203201. Source: GDB

leading edge membrane

Inferred from direct assay Ref.9. Source: UniProtKB

plasma membrane

Traceable author statement. Source: Reactome

ruffle membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

   Molecular_functionG-protein coupled receptor activity

Traceable author statement PubMed 15203201. Source: GDB

calcium ion binding

Inferred from electronic annotation. Source: InterPro

chondroitin sulfate binding

Inferred from mutant phenotype Ref.7. Source: UniProtKB

Complete GO annotation...

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]

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)

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.
Isoform 2 (identifier: Q9UHX3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     397-407: Missing.
Isoform 3 (identifier: Q9UHX3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     163-211: Missing.
Isoform 4 (identifier: Q9UHX3-4)

The sequence of this isoform differs from the canonical sequence as follows:
     119-211: Missing.
Isoform 5 (identifier: Q9UHX3-5)

The sequence of this isoform differs from the canonical sequence as follows:
     119-260: Missing.
Isoform 6 (identifier: Q9UHX3-6)

The sequence of this isoform differs from the canonical sequence as follows:
     473-530: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Signal peptide1 – 2323 Potential
Chain24 – 823800EGF-like module-containing mucin-like hormone receptor-like 2
PRO_0000012875

Regions

Topological domain24 – 540517Extracellular Potential
Transmembrane541 – 56121Helical; Name=1; Potential
Topological domain562 – 5698Cytoplasmic Potential
Transmembrane570 – 59021Helical; Name=2; Potential
Topological domain591 – 60515Extracellular Potential
Transmembrane606 – 62621Helical; Name=3; Potential
Topological domain627 – 64418Cytoplasmic Potential
Transmembrane645 – 66521Helical; Name=4; Potential
Topological domain666 – 68318Extracellular Potential
Transmembrane684 – 70421Helical; Name=5; Potential
Topological domain705 – 73531Cytoplasmic Potential
Transmembrane736 – 75621Helical; Name=6; Potential
Topological domain757 – 7604Extracellular Potential
Transmembrane761 – 78121Helical; Name=7; Potential
Topological domain782 – 82342Cytoplasmic Potential
Domain25 – 6642EGF-like 1
Domain67 – 11852EGF-like 2; calcium-binding
Domain119 – 16244EGF-like 3; calcium-binding
Domain163 – 21149EGF-like 4; calcium-binding Potential
Domain212 – 26049EGF-like 5; calcium-binding Potential
Domain479 – 52951GPS

Sites

Site517 – 5182Cleavage

Amino acid modifications

Glycosylation411N-linked (GlcNAc...) Potential
Glycosylation1111N-linked (GlcNAc...) Potential
Glycosylation2061N-linked (GlcNAc...) Potential
Glycosylation2981N-linked (GlcNAc...) Potential
Glycosylation3471N-linked (GlcNAc...) Potential
Glycosylation3541N-linked (GlcNAc...) Potential
Glycosylation4561N-linked (GlcNAc...) Potential
Glycosylation4601N-linked (GlcNAc...) Potential
Disulfide bond29 ↔ 39 Ref.11
Disulfide bond33 ↔ 45 Ref.11
Disulfide bond47 ↔ 65 Ref.11
Disulfide bond71 ↔ 85 Ref.11
Disulfide bond79 ↔ 94 Ref.11
Disulfide bond96 ↔ 117 Ref.11
Disulfide bond123 ↔ 136 Ref.11
Disulfide bond130 ↔ 145 Ref.11
Disulfide bond147 ↔ 161 By similarity
Disulfide bond167 ↔ 180 By similarity
Disulfide bond174 ↔ 189 By similarity
Disulfide bond191 ↔ 210 By similarity
Disulfide bond216 ↔ 229 By similarity
Disulfide bond223 ↔ 238 By similarity
Disulfide bond240 ↔ 259 By similarity

Natural variations

Alternative sequence119 – 260142Missing in isoform 5.
VSP_041364
Alternative sequence119 – 21193Missing in isoform 4.
VSP_041365
Alternative sequence163 – 21149Missing in isoform 3.
VSP_041366
Alternative sequence397 – 40711Missing in isoform 2.
VSP_041367
Alternative sequence473 – 53058Missing in isoform 6.
VSP_047535
Natural variant3141A → V.
Corresponds to variant rs35612307 [ dbSNP | Ensembl ].
VAR_061229
Natural variant6051T → I.
Corresponds to variant rs4410209 [ dbSNP | Ensembl ].
VAR_026719
Natural variant6141L → F. Ref.1 Ref.3 Ref.4
Corresponds to variant rs2524383 [ dbSNP | Ensembl ].
VAR_026720
Natural variant6651S → F.
Corresponds to variant rs3752187 [ dbSNP | Ensembl ].
VAR_026721
Natural variant7201E → D.
Corresponds to variant rs57865820 [ dbSNP | Ensembl ].
VAR_061230

Experimental info

Mutagenesis5181S → A: Abolishes cleavage. Ref.5
Sequence conflict5311Missing in AAC05172. Ref.4
Sequence conflict8231N → R in BAC06146. Ref.2

Secondary structure

................................ 823
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified June 13, 2006. Version 2.
Checksum: 4D38C30A07B46FF4

FASTA82390,472
        10         20         30         40         50         60 
MGGRVFLVFL AFCVWLTLPG AETQDSRGCA RWCPQDSSCV NATACRCNPG FSSFSEIITT 

        70         80         90        100        110        120 
PMETCDDINE CATLSKVSCG KFSDCWNTEG SYDCVCSPGY EPVSGAKTFK NESENTCQDV 

       130        140        150        160        170        180 
DECQQNPRLC KSYGTCVNTL GSYTCQCLPG FKLKPEDPKL CTDVNECTSG QNPCHSSTHC 

       190        200        210        220        230        240 
LNNVGSYQCR CRPGWQPIPG SPNGPNNTVC EDVDECSSGQ HQCDSSTVCF NTVGSYSCRC 

       250        260        270        280        290        300 
RPGWKPRHGI PNNQKDTVCE DMTFSTWTPP PGVHSQTLSR FFDKVQDLGR DYKPGLANNT 

       310        320        330        340        350        360 
IQSILQALDE LLEAPGDLET LPRLQQHCVA SHLLDGLEDV LRGLSKNLSN GLLNFSYPAG 

       370        380        390        400        410        420 
TELSLEVQKQ VDRSVTLRQN QAVMQLDWNQ AQKSGDPGPS VVGLVSIPGM GKLLAEAPLV 

       430        440        450        460        470        480 
LEPEKQMLLH ETHQGLLQDG SPILLSDVIS AFLSNNDTQN LSSPVTFTFS HRSVIPRQKV 

       490        500        510        520        530        540 
LCVFWEHGQN GCGHWATTGC STIGTRDTST ICRCTHLSSF AVLMAHYDVQ EEDPVLTVIT 

       550        560        570        580        590        600 
YMGLSVSLLC LLLAALTFLL CKAIQNTSTS LHLQLSLCLF LAHLLFLVAI DQTGHKVLCS 

       610        620        630        640        650        660 
IIAGTLHYLY LATLTWMLLE ALYLFLTARN LTVVNYSSIN RFMKKLMFPV GYGVPAVTVA 

       670        680        690        700        710        720 
ISAASRPHLY GTPSRCWLQP EKGFIWGFLG PVCAIFSVNL VLFLVTLWIL KNRLSSLNSE 

       730        740        750        760        770        780 
VSTLRNTRML AFKATAQLFI LGCTWCLGIL QVGPAARVMA YLFTIINSLQ GVFIFLVYCL 

       790        800        810        820 
LSQQVREQYG KWSKGIRKLK TESEMHTLSS SAKADTSKPS TVN 

« Hide

Isoform 2 [UniParc].

Checksum: 9A98853A77E71FFD
Show »

FASTA81289,466
Isoform 3 [UniParc].

Checksum: 9687785185F52A7F
Show »

FASTA77485,230
Isoform 4 [UniParc].

Checksum: A7509F01725F3A18
Show »

FASTA73080,351
Isoform 5 [UniParc].

Checksum: ADE8AC326340F0CB
Show »

FASTA68174,936
Isoform 6 [UniParc].

Checksum: D427C949296B61F8
Show »

FASTA76584,079

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]"Ligation of the adhesion-GPCR EMR2 regulates human neutrophil function."
Yona S., Lin H.H., Dri P., Davies J.Q., Hayhoe R.P., Lewis S.M., Heinsbroek S.E., Brown K.A., Perretti M., Hamann J., Treacher D.F., Gordon S., Stacey M.
FASEB J. 22:741-751(2008) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS32935.1. [Q9UHX3-1]
CCDS59361.1. [Q9UHX3-6]
RefSeqNP_001257981.1. NM_001271052.1. [Q9UHX3-6]
NP_038475.2. NM_013447.3. [Q9UHX3-1]
UniGeneHs.531619.

3D structure databases

PDBe
RCSB-PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2BO2X-ray2.60A/B25-260[»]
2BOUX-ray1.90A25-260[»]
2BOXX-ray2.50A25-260[»]
ProteinModelPortalQ9UHX3.
SMRQ9UHX3. Positions 28-260, 301-517.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid119041. 2 interactions.
STRING9606.ENSP00000319883.

Protein family/group databases

MEROPSS63.001.
GPCRDBSearch...

PTM databases

PhosphoSiteQ9UHX3.

Polymorphism databases

DMDM108935835.

Proteomic databases

MaxQBQ9UHX3.
PaxDbQ9UHX3.
PRIDEQ9UHX3.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000315576; ENSP00000319883; ENSG00000127507. [Q9UHX3-1]
ENST00000346057; ENSP00000263380; ENSG00000127507. [Q9UHX3-3]
ENST00000353005; ENSP00000319838; ENSG00000127507. [Q9UHX3-5]
ENST00000353876; ENSP00000319454; ENSG00000127507. [Q9UHX3-4]
ENST00000392965; ENSP00000376692; ENSG00000127507. [Q9UHX3-6]
ENST00000392967; ENSP00000376694; ENSG00000127507. [Q9UHX3-2]
ENST00000594076; ENSP00000472735; ENSG00000127507. [Q9UHX3-4]
ENST00000594294; ENSP00000470725; ENSG00000127507. [Q9UHX3-3]
ENST00000595839; ENSP00000469277; ENSG00000127507. [Q9UHX3-5]
ENST00000596991; ENSP00000472280; ENSG00000127507. [Q9UHX3-2]
GeneID30817.
KEGGhsa:30817.
UCSCuc002mzp.2. human. [Q9UHX3-1]
uc031rjs.1. human. [Q9UHX3-2]

Organism-specific databases

CTD30817.
GeneCardsGC19M014844.
H-InvDBHIX0174383.
HGNCHGNC:3337. EMR2.
MIM606100. gene.
neXtProtNX_Q9UHX3.
PharmGKBPA27774.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG320737.
HOVERGENHBG048917.
InParanoidQ9UHX3.
KOK08443.
OrthoDBEOG75J0MK.
PhylomeDBQ9UHX3.
TreeFamTF316380.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.

Gene expression databases

ArrayExpressQ9UHX3.
BgeeQ9UHX3.
CleanExHS_EMR2.
GenevestigatorQ9UHX3.

Family and domain databases

InterProIPR000742. 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]
PfamPF00002. 7tm_2. 1 hit.
PF07645. EGF_CA. 4 hits.
PF01825. GPS. 1 hit.
[Graphical view]
PRINTSPR01278. CD97PROTEIN.
PR00249. GPCRSECRETIN.
SMARTSM00179. EGF_CA. 4 hits.
SM00303. GPS. 1 hit.
[Graphical view]
SUPFAMSSF57184. SSF57184. 1 hit.
PROSITEPS00010. 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]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UHX3.
GeneWikiEMR2.
GenomeRNAi30817.
NextBio35474078.
PMAP-CutDBQ9UHX3.
PROQ9UHX3.
SOURCESearch...

Entry information

Entry nameEMR2_HUMAN
AccessionPrimary (citable) accession number: Q9UHX3
Secondary accession number(s): B4DQ96 expand/collapse secondary AC list , E7ESD7, E9PBR1, E9PEL6, E9PFQ5, E9PG91, Q8NG96, Q9Y4B1
Entry history
Integrated into UniProtKB/Swiss-Prot: March 1, 2004
Last sequence update: June 13, 2006
Last modified: July 9, 2014
This is version 138 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM

Human cell differentiation molecules

CD nomenclature of surface proteins of human leucocytes and list of entries

7-transmembrane G-linked receptors

List of 7-transmembrane G-linked receptor entries