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UniProtKB/Swiss-Prot entry Q9H6X2


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name ANTR1_HUMAN
Primary accession number Q9H6X2
Secondary accession numbers Q96P02 Q9NVP3
Integrated into Swiss-Prot on November 2, 2001
Sequence was last modified on November 2, 2001 (Sequence version 2)
Annotations were last modified on    June 16, 2009 (Entry version 89)
Name and origin of the protein
Protein name Anthrax toxin receptor 1 [Precursor]
Synonym Tumor endothelial marker 8
Gene name
Name: ANTXR1
Synonyms: ATR, TEM8
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1126/science.289.5482.1197; PubMed=10947988 [NCBI, ExPASy, EBI, Israel, Japan]
St Croix B., Rago C., Velculescu V.E., Traverso G., Romans K.E., Montgomery E., Lal A., Riggins G.J., Lengauer C., Vogelstein B., Kinzler K.W.;
"Genes expressed in human tumor endothelium.";
Science 289:1197-1202(2000).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND INTERACTION WITH ANTHRAX TOXIN.
DOI=10.1038/n35101999; PubMed=11700562 [NCBI, ExPASy, EBI, Israel, Japan]
Bradley K.A., Mogridge J., Mourez M., Collier R.J., Young J.A.T.;
"Identification of the cellular receptor for anthrax toxin.";
Nature 414:225-229(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 184-564 (ISOFORM 1), AND NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
TISSUE=Kidney;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
INTERACTION WITH ANTHRAX TOXIN.
TISSUE=Placenta;
DOI=10.1073/pnas.0431098100; PubMed=12700348 [NCBI, ExPASy, EBI, Israel, Japan]
Scobie H.M., Rainey G.J.A., Bradley K.A., Young J.A.T.;
"Human capillary morphogenesis protein 2 functions as an anthrax toxin receptor.";
Proc. Natl. Acad. Sci. U.S.A. 100:5170-5174(2003).
[6]
SPLICE ISOFORM(S) THAT ARE POTENTIAL NMD TARGET(S).
DOI=10.1186/gb-2004-5-2-r8; PubMed=14759258 [NCBI, ExPASy, EBI, Israel, Japan]
Hillman R.T., Green R.E., Brenner S.E.;
"An unappreciated role for RNA surveillance.";
Genome Biol. 5:RESEARCH008.1-RESEARCH008.16(2004).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-362, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-425, AND MASS SPECTROMETRY.
DOI=10.1016/j.cell.2007.11.025; PubMed=18083107 [NCBI, ExPASy, EBI, Israel, Japan]
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J., Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X., Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.";
Cell 131:1190-1203(2007).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF279145; AAK52094.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF421380; AAL26496.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK025429; BAB15128.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001463; BAA91707.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC012074; AAH12074.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
IPI IPI00030431; -.
IPI00071177; -.
IPI00219619; -.
IPI00871735; -.
RefSeq NP_060623.2; -.
NP_115584.1; -.
NP_444262.1; -.
UniGene Hs.165859
3D structure databases
ModBase Q9H6X2.
Protein-protein interaction databases
IntAct Q9H6X2; 2.
PTM databases
PhosphoSite Q9H6X2; -.
Enzyme and pathway databases
Pathway_Interaction_DB anthraxpathway; Cellular roles of Anthrax toxin.
Organism-specific databases
GeneCards GC02P069152; -.
H-InvDB HIX0002125; -.
HGNC HGNC:21014; ANTXR1.
GenAtlas ANTXR1.
MIM 606410; gene. [NCBI / EBI]
PharmGKB PA134956382; -.
Gene expression databases
ArrayExpress Q9H6X2; -.
Bgee Q9H6X2; -.
CleanEx HS_ANTXR1; -.
HS_ATR; -.
GermOnline ENSG00000169604; Homo sapiens.
Ontologies
GO
GO:0016021; Cellular component: integral to membrane (inferred from electronic annotation from UniProtKB-KW).
GO:0046872; Molecular function: metal ion binding (inferred from electronic annotation from UniProtKB-KW).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004872; Molecular function: receptor activity (inferred from electronic annotation from UniProtKB-KW).
QuickGo view.
Family and domain databases
InterPro IPR017360; Anthrax_toxin_rcpt_2.
IPR008399; Anthrax_toxin_rcpt_C.
IPR008400; Anthrax_toxin_rcpt_extracel.
IPR002035; VWF_A.
Graphical view of domain structure.
Pfam PF05586; Ant_C; 1.
PF05587; Anth_Ig; 1.
PF00092; VWA; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF038023; Anthrax_toxin_receptor_2; 1.
SMART SM00327; VWA; 1.
SMART graphical view of domain structure.
PROSITE PS50234; VWFA; 1.
PROSITE graphical view of domain structure (profiles).
Proteomic databases
PRIDE Q9H6X2; -.
Genome annotation databases
Ensembl ENSG00000169604; Homo sapiens. [Contig view]
GeneID 84168; -.
Phylogenomic databases
HOGENOM Q9H6X2; -.
HOVERGEN Q9H6X2; -.
OMA Q9H6X2; QGGRRED.
Other
NextBio 73524; -.
SOURCE ANTXR1; Homo sapiens.
ProtoNet Q9H6X2.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Alternative splicing; Glycoprotein; Membrane; Metal-binding; Phosphoprotein; Polymorphism; Receptor; Signal; Transmembrane.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
SIGNAL   1    32  32     Potential. 
CHAIN   33   564  532     Anthrax toxin receptor 1. PRO_0000002692
TOPO_DOM   33   321  289     Extracellular (Potential). 
TRANSMEM   322   342  21     Potential. 
TOPO_DOM   343   564  222     Cytoplasmic (Potential). 
DOMAIN   44   215  172     VWFA. 
COMPBIAS   360   368  9     Asp/Glu-rich (highly acidic). 
COMPBIAS   506   564  59     Pro-rich. 
METAL   52    52        Divalent metal cation (By similarity). 
METAL   54    54        Divalent metal cation (By similarity). 
METAL   118   118        Divalent metal cation (By similarity). 
MOD_RES   362   362        Phosphoserine. 
MOD_RES   425   425        Phosphotyrosine. 
CARBOHYD   166   166        N-linked (GlcNAc...) (Potential). 
CARBOHYD   184   184        N-linked (GlcNAc...) (Potential). 
CARBOHYD   262   262        N-linked (GlcNAc...) (Potential). 
VAR_SEQ   268   297        NEKPFSVEDTYLLCPAPILKEVGMKAALQV -> SKSLQSPWVSSTSGFKEGNSHPCLPARPHT (in isoform 3). VSP_000446
VAR_SEQ   298   564        Missing (in isoform 3). VSP_000447
VAR_SEQ   319   333        DGSILAIALLILFLL -> LHKIASGPTTAACME (in isoform 4). VSP_000448
VAR_SEQ   334   564        Missing (in isoform 4). VSP_000449
VAR_SEQ   365   368        EDDD -> NKIK (in isoform 2). VSP_000444
VAR_SEQ   369   564        Missing (in isoform 2). VSP_000445
VARIANT   7     7  1     R -> K (in dbSNP:rs28365986 [NCBI]). VAR_053015 
Sequence information
Length: 564 AA [This is the length of the unprocessed precursor] Molecular weight: 62789 Da [This is the MW of the unprocessed precursor] CRC64: B118A00AD5DF2233 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MATAERRALG IGFQWLSLAT LVLICAGQGG RREDGGPACY GGFDLYFILD KSGSVLHHWN 

        70         80         90        100        110        120 
EIYYFVEQLA HKFISPQLRM SFIVFSTRGT TLMKLTEDRE QIRQGLEELQ KVLPGGDTYM 

       130        140        150        160        170        180 
HEGFERASEQ IYYENRQGYR TASVIIALTD GELHEDLFFY SEREANRSRD LGAIVYCVGV 

       190        200        210        220        230        240 
KDFNETQLAR IADSKDHVFP VNDGFQALQG IIHSILKKSC IEILAAEPST ICAGESFQVV 

       250        260        270        280        290        300 
VRGNGFRHAR NVDRVLCSFK INDSVTLNEK PFSVEDTYLL CPAPILKEVG MKAALQVSMN 

       310        320        330        340        350        360 
DGLSFISSSV IITTTHCSDG SILAIALLIL FLLLALALLW WFWPLCCTVI IKEVPPPPAE 

       370        380        390        400        410        420 
ESEEEDDDGL PKKKWPTVDA SYYGGRGVGG IKRMEVRWGE KGSTEEGAKL EKAKNARVKM 

       430        440        450        460        470        480 
PEQEYEFPEP RNLNNNMRRP SSPRKWYSPI KGKLDALWVL LRKGYDRVSV MRPQPGDTGR 

       490        500        510        520        530        540 
CINFTRVKNN QPAKYPLNNA YHTSSPPPAP IYTPPPPAPH CPPPPPSAPT PPIPSPPSTL 

       550        560 
PPPPQAPPPN RAPPPSRPPP RPSV 

Q9H6X2 in FASTA format

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