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Q9UHX3

- EMR2_HUMAN

UniProt

Q9UHX3 - EMR2_HUMAN

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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

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
Complete GO annotation...

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.2 Publications

Topology

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Topological domaini24 – 540517Extracellular Reviewed predictionAdd
BLAST
Transmembranei541 – 56121Helical; Name=1; Reviewed predictionAdd
BLAST
Topological domaini562 – 5698Cytoplasmic Reviewed prediction
Transmembranei570 – 59021Helical; Name=2; Reviewed predictionAdd
BLAST
Topological domaini591 – 60515Extracellular Reviewed predictionAdd
BLAST
Transmembranei606 – 62621Helical; Name=3; Reviewed predictionAdd
BLAST
Topological domaini627 – 64418Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei645 – 66521Helical; Name=4; Reviewed predictionAdd
BLAST
Topological domaini666 – 68318Extracellular Reviewed predictionAdd
BLAST
Transmembranei684 – 70421Helical; Name=5; Reviewed predictionAdd
BLAST
Topological domaini705 – 73531Cytoplasmic Reviewed predictionAdd
BLAST
Transmembranei736 – 75621Helical; Name=6; Reviewed predictionAdd
BLAST
Topological domaini757 – 7604Extracellular Reviewed prediction
Transmembranei761 – 78121Helical; Name=7; Reviewed predictionAdd
BLAST
Topological domaini782 – 82342Cytoplasmic Reviewed predictionAdd
BLAST

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
Complete GO annotation...

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 – 2323 Reviewed predictionAdd
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 Publication
Disulfide bondi33 ↔ 451 Publication
Glycosylationi41 – 411N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi47 ↔ 651 Publication
Disulfide bondi71 ↔ 851 Publication
Disulfide bondi79 ↔ 941 Publication
Disulfide bondi96 ↔ 1171 Publication
Glycosylationi111 – 1111N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi123 ↔ 1361 Publication
Disulfide bondi130 ↔ 1451 Publication
Disulfide bondi147 ↔ 161 By similarity
Disulfide bondi167 ↔ 180 By similarity
Disulfide bondi174 ↔ 189 By similarity
Disulfide bondi191 ↔ 210 By similarity
Glycosylationi206 – 2061N-linked (GlcNAc...) Reviewed prediction
Disulfide bondi216 ↔ 229 By similarity
Disulfide bondi223 ↔ 238 By similarity
Disulfide bondi240 ↔ 259 By similarity
Glycosylationi298 – 2981N-linked (GlcNAc...) Reviewed prediction
Glycosylationi347 – 3471N-linked (GlcNAc...) Reviewed prediction
Glycosylationi354 – 3541N-linked (GlcNAc...) Reviewed prediction
Glycosylationi456 – 4561N-linked (GlcNAc...) Reviewed prediction
Glycosylationi460 – 4601N-linked (GlcNAc...) Reviewed prediction

Post-translational modificationi

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

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.

Miscellaneous databases

EvolutionaryTraceiQ9UHX3.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini25 – 6642EGF-like 1Add
BLAST
Domaini67 – 11852EGF-like 2; calcium-bindingAdd
BLAST
Domaini119 – 16244EGF-like 3; calcium-bindingAdd
BLAST
Domaini163 – 21149EGF-like 4; calcium-binding Reviewed predictionAdd
BLAST
Domaini212 – 26049EGF-like 5; calcium-binding Reviewed predictionAdd
BLAST
Domaini479 – 52951GPSAdd
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.
Contains 1 GPS domain.

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.

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. VSP_041364Add
BLAST
Alternative sequencei119 – 21193Missing in isoform 4. VSP_041365Add
BLAST
Alternative sequencei163 – 21149Missing in isoform 3. VSP_041366Add
BLAST
Alternative sequencei397 – 40711Missing in isoform 2. VSP_041367Add
BLAST
Alternative sequencei473 – 53058Missing in isoform 6. VSP_047535Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti531 – 5311Missing in AAC05172. 1 Publication
Sequence conflicti823 – 8231N → R in BAC06146. 1 Publication

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]
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]
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 ]
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 ]
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

« Hide 'large scale' publications
  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: September 3, 2014
This is version 139 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

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