Did you know ? If you order before Friday 14h we deliver 90PCT of the the time next Tuesday, GENTAUR another in time delivery

Hepatitis A virus cellular receptor 2 (HAVcr-2) (T-cell immunoglobulin and mucin domain-containing protein 3) (TIMD-3) (T-cell immunoglobulin mucin receptor 3) (TIM-3) (T-cell membrane protein 3)

 HAVR2_HUMAN             Reviewed;         301 AA.
Q8TDQ0; B2RAY2; Q8WW60; Q96K94;
27-SEP-2005, integrated into UniProtKB/Swiss-Prot.
02-NOV-2010, sequence version 3.
25-OCT-2017, entry version 127.
RecName: Full=Hepatitis A virus cellular receptor 2;
Short=HAVcr-2;
AltName: Full=T-cell immunoglobulin and mucin domain-containing protein 3;
Short=TIMD-3;
AltName: Full=T-cell immunoglobulin mucin receptor 3;
Short=TIM-3;
AltName: Full=T-cell membrane protein 3;
Flags: Precursor;
Name=HAVCR2; Synonyms=TIM3, TIMD3;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, VARIANT LEU-140, AND
TISSUE SPECIFICITY.
PubMed=11823861; DOI=10.1038/415536a;
Monney L., Sabatos C.A., Gaglia J.L., Ryu A., Waldner H., Chernova T.,
Manning S., Greenfield E.A., Coyle A.J., Sobel R.A., Freeman G.J.,
Kuchroo V.K.;
"Th1-specific cell surface protein Tim-3 regulates macrophage
activation and severity of an autoimmune disease.";
Nature 415:536-541(2002).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-140.
Zhang W., Wan T., Li N., Cao X.;
"Novel human hepatitis A virus cellular receptor.";
Submitted (APR-2000) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANT LEU-140.
TISSUE=Hepatoma;
Kuehn E.W., Ichimura T., Bonventre J.V.;
"A homolog to human kidney injury molecule-1 is expressed in hepatoma
cells.";
Submitted (DEC-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-140.
TISSUE=Embryo, and Umbilical cord blood;
PubMed=14702039; DOI=10.1038/ng1285;
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).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15372022; DOI=10.1038/nature02919;
Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
"The DNA sequence and comparative analysis of human chromosome 5.";
Nature 431:268-274(2004).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA], AND VARIANT LEU-140.
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2), AND VARIANT
LEU-140.
TISSUE=Lung, and Pancreas;
PubMed=15489334; DOI=10.1101/gr.2596504;
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).
[8]
FUNCTION.
PubMed=14556005; DOI=10.1038/ni987;
Sanchez-Fueyo A., Tian J., Picarella D., Domenig C., Zheng X.X.,
Sabatos C.A., Manlongat N., Bender O., Kamradt T., Kuchroo V.K.,
Gutierrez-Ramos J.-C., Coyle A.J., Strom T.B.;
"Tim-3 inhibits T helper type 1-mediated auto- and alloimmune
responses and promotes immunological tolerance.";
Nat. Immunol. 4:1093-1101(2003).
[9]
FUNCTION AS A RECEPTOR FOR LGALS9.
PubMed=16286920; DOI=10.1038/ni1271;
Zhu C., Anderson A.C., Schubart A., Xiong H., Imitola J., Khoury S.J.,
Zheng X.X., Strom T.B., Kuchroo V.K.;
"The Tim-3 ligand galectin-9 negatively regulates T helper type 1
immunity.";
Nat. Immunol. 6:1245-1252(2005).
[10]
PHOSPHORYLATION AT TYR-265, AND TISSUE SPECIFICITY.
PubMed=17069754; DOI=10.1016/j.bbrc.2006.10.079;
van de Weyer P.S., Muehlfeit M., Klose C., Bonventre J.V., Walz G.,
Kuehn E.W.;
"A highly conserved tyrosine of Tim-3 is phosphorylated upon
stimulation by its ligand galectin-9.";
Biochem. Biophys. Res. Commun. 351:571-576(2006).
[11]
TISSUE SPECIFICITY.
PubMed=18006747; DOI=10.1126/science.1148536;
Anderson A.C., Anderson D.E., Bregoli L., Hastings W.D., Kassam N.,
Lei C., Chandwaskar R., Karman J., Su E.W., Hirashima M., Bruce J.N.,
Kane L.P., Kuchroo V.K., Hafler D.A.;
"Promotion of tissue inflammation by the immune receptor Tim-3
expressed on innate immune cells.";
Science 318:1141-1143(2007).
[12]
INVOLVEMENT IN T-CELL EXHAUSTION, AND TISSUE SPECIFICITY.
PubMed=19001139; DOI=10.1084/jem.20081398;
Jones R.B., Ndhlovu L.C., Barbour J.D., Sheth P.M., Jha A.R.,
Long B.R., Wong J.C., Satkunarajah M., Schweneker M., Chapman J.M.,
Gyenes G., Vali B., Hyrcza M.D., Yue F.Y., Kovacs C., Sassi A.,
Loutfy M., Halpenny R., Persad D., Spotts G., Hecht F.M., Chun T.W.,
McCune J.M., Kaul R., Rini J.M., Nixon D.F., Ostrowski M.A.;
"Tim-3 expression defines a novel population of dysfunctional T cells
with highly elevated frequencies in progressive HIV-1 infection.";
J. Exp. Med. 205:2763-2779(2008).
[13]
INVOLVEMENT IN T-CELL EXHAUSTION, AND TISSUE SPECIFICITY.
PubMed=19587053; DOI=10.1128/JVI.00639-09;
Golden-Mason L., Palmer B.E., Kassam N., Townshend-Bulson L.,
Livingston S., McMahon B.J., Castelblanco N., Kuchroo V., Gretch D.R.,
Rosen H.R.;
"Negative immune regulator Tim-3 is overexpressed on T cells in
hepatitis C virus infection and its blockade rescues dysfunctional
CD4+ and CD8+ T cells.";
J. Virol. 83:9122-9130(2009).
[14]
PHOSPHATIDYLSERINE-BINDING.
PubMed=20083673; DOI=10.4049/jimmunol.0903059;
DeKruyff R.H., Bu X., Ballesteros A., Santpiago C., Chim Y.L.,
Lee H.H., Karisola P., Pichavant M., Kaplan G.G., Umetsu D.T.,
Freeman G.J., Casasnovas J.M.;
"T cell/transmembrane, Ig, and mucin-3 allelic variants differentially
recognize phosphatidylserine and mediate phagocytosis of apoptotic
cells.";
J. Immunol. 184:1918-1930(2010).
[15]
GLYCOSYLATION AT THR-145, STRUCTURE OF CARBOHYDRATES, AND
IDENTIFICATION BY MASS SPECTROMETRY.
PubMed=22171320; DOI=10.1074/mcp.M111.013649;
Halim A., Nilsson J., Ruetschi U., Hesse C., Larson G.;
"Human urinary glycoproteomics; attachment site specific analysis of
N-and O-linked glycosylations by CID and ECD.";
Mol. Cell. Proteomics 0:0-0(2011).
[16]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22323453; DOI=10.1182/blood-2011-06-360321;
Gleason M.K., Lenvik T.R., McCullar V., Felices M., O'Brien M.S.,
Cooley S.A., Verneris M.R., Cichocki F., Holman C.J.,
Panoskaltsis-Mortari A., Niki T., Hirashima M., Blazar B.R.,
Miller J.S.;
"Tim-3 is an inducible human natural killer cell receptor that
enhances interferon gamma production in response to galectin-9.";
Blood 119:3064-3072(2012).
[17]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=22383801; DOI=10.1182/blood-2011-11-392951;
Ndhlovu L.C., Lopez-Verges S., Barbour J.D., Jones R.B., Jha A.R.,
Long B.R., Schoeffler E.C., Fujita T., Nixon D.F., Lanier L.L.;
"Tim-3 marks human natural killer cell maturation and suppresses cell-
mediated cytotoxicity.";
Blood 119:3734-3743(2012).
[18]
FUNCTION AS A RECEPTOR FOR LGALS9.
PubMed=23555261; DOI=10.1371/journal.ppat.1003253;
Leitner J., Rieger A., Pickl W.F., Zlabinger G.,
Grabmeier-Pfistershammer K., Steinberger P.;
"TIM-3 does not act as a receptor for galectin-9.";
PLoS Pathog. 9:E1003253-E1003253(2013).
[19]
FUNCTION, AND TISSUE SPECIFICITY.
PubMed=24838857; DOI=10.1002/eji.201344392;
Gautron A.S., Dominguez-Villar M., de Marcken M., Hafler D.A.;
"Enhanced suppressor function of TIM-3+ FoxP3+ regulatory T cells.";
Eur. J. Immunol. 44:2703-2711(2014).
[20]
REVIEW ON FUNCTION IN REGULATING T-CELL RESPONSES.
PubMed=24825777; DOI=10.1007/s12026-014-8524-1;
Gorman J.V., Colgan J.D.;
"Regulation of T cell responses by the receptor molecule Tim-3.";
Immunol. Res. 59:56-65(2014).
[21]
SUBCELLULAR LOCATION, INTERACTION WITH LGALS9 AND LCK, AND
PHOSPHORYLATION.
PubMed=24337741; DOI=10.4049/jimmunol.1302663;
Clayton K.L., Haaland M.S., Douglas-Vail M.B., Mujib S., Chew G.M.,
Ndhlovu L.C., Ostrowski M.A.;
"T cell Ig and mucin domain-containing protein 3 is recruited to the
immune synapse, disrupts stable synapse formation, and associates with
receptor phosphatases.";
J. Immunol. 192:782-791(2014).
[22]
FUNCTION, INTERACTION WITH VAV1; AKT; LCP2; ZAP70; SYK; PIK3R1; FYN;
SH3BP2 AND SH2D2A, AND MUTAGENESIS OF TYR-265 AND TYR-272.
PubMed=26492563; DOI=10.1371/journal.pone.0140694;
Tomkowicz B., Walsh E., Cotty A., Verona R., Sabins N., Kaplan F.,
Santulli-Marotto S., Chin C.N., Mooney J., Lingham R.B., Naso M.,
McCabe T.;
"TIM-3 Suppresses Anti-CD3/CD28-Induced TCR Activation and IL-2
Expression through the NFAT Signaling Pathway.";
PLoS ONE 10:E0140694-E0140694(2015).
-!- FUNCTION: Cell surface receptor implicated in modulating innate
and adaptive immune responses. Generally accepted to have an
inhibiting function. Reports on stimulating functions suggest that
the activity may be influenced by the cellular context and/or the
respective ligand (PubMed:24825777). Regulates macrophage
activation (PubMed:11823861). Inhibits T-helper type 1 lymphocyte
(Th1)-mediated auto- and alloimmune responses and promotes
immunological tolerance (PubMed:14556005). In CD8+ cells
attenuates TCR-induced signaling, specifically by blocking NF-
kappaB and NFAT promoter activities resulting in the loss of IL-2
secretion. The function may implicate its association with LCK
proposed to impair phosphorylation of TCR subunits, and/or LGALS9-
dependent recruitment of PTPRC to the immunological synapse
(PubMed:24337741, PubMed:26492563). In contrast, shown to activate
TCR-induced signaling in T-cells probably implicating ZAP70, LCP2,
LCK and FYN (By similarity). Expressed on Treg cells can inhibit
Th17 cell responses (PubMed:24838857). Receptor for LGALS9
(PubMed:16286920, PubMed:24337741). Binding to LGALS9 is believed
to result in suppression of T-cell responses; the resulting
apoptosis of antigen-specific cells may implicate HAVCR2
phosphorylation and disruption of its association with BAG6.
Binding to LGALS9 is proposed to be involved in innate immune
response to intracellular pathogens. Expressed on Th1 cells
interacts with LGALS9 expressed on Mycobacterium tuberculosis-
infected macrophages to stimulate antibactericidal activity
including IL-1 beta secretion and to restrict intracellular
bacterial growth (By similarity). However, the function as
receptor for LGALS9 has been challenged (PubMed:23555261). Also
reported to enhance CD8+ T-cell responses to an acute infection
such as by Listeria monocytogenes (By similarity). Receptor for
phosphatidylserine (PtSer); PtSer-binding is calcium-dependent.
May recognize PtSer on apoptotic cells leading to their
phagocytosis. Mediates the engulfment of apoptotic cells by
dendritic cells. Expressed on T-cells, promotes conjugation but
not engulfment of apoptotic cells. Expressed on dendritic cells
(DCs) positively regulates innate immune response and in synergy
with Toll-like receptors promotes secretion of TNF-alpha. In
tumor-imfiltrating DCs suppresses nucleic acid-mediated innate
immune repsonse by interaction with HMGB1 and interfering with
nucleic acid-sensing and trafficking of nucleid acids to endosomes
(By similarity). Expressed on natural killer (NK) cells acts as a
coreceptor to enhance IFN-gamma production in response to LGALS9
(PubMed:22323453). In contrast, shown to suppress NK cell-mediated
cytotoxicity (PubMed:22383801). Negatively regulates NK cell
function in LPS-induced endotoxic shock (By similarity).
{ECO:0000250|UniProtKB:Q8VIM0, ECO:0000269|PubMed:11823861,
ECO:0000269|PubMed:14556005, ECO:0000269|PubMed:16286920,
ECO:0000269|PubMed:22323453, ECO:0000269|PubMed:23555261,
ECO:0000269|PubMed:24838857, ECO:0000269|PubMed:26492563,
ECO:0000305|PubMed:24825777}.
-!- SUBUNIT: Interacts with HMGB1; impairs HMGB1 binding to B-DNA and
likely HMGB1-mediated innate immume response (By similarity).
Interacts with BAG6 (By similarity). Interacts (phosphorylated)
with PIK3R1 and PIK3R2. Interacts (not dependent on its
phosphorylation status) with FYN (By similarity). Interacts (in
basal state T-cells) with VAV1; AKT1/2, LCP2, ZAP70, SYK, PIK3R1,
FYN, SH3BP2 and SH2D2A. Interacts (in activated T-cells) with LCK
and PLCG (PubMed:26492563, PubMed:24337741).
{ECO:0000250|UniProtKB:Q8VIM0, ECO:0000269|PubMed:24337741,
ECO:0000269|PubMed:26492563}.
-!- INTERACTION:
P13688:CEACAM1; NbExp=4; IntAct=EBI-11472922, EBI-4314481;
-!- SUBCELLULAR LOCATION: Membrane {ECO:0000305}; Single-pass type I
membrane protein {ECO:0000305}. Cell junction
{ECO:0000269|PubMed:24337741}. Note=Localizes to the immunological
synapse between CD8+ T-cells and target cells.
{ECO:0000269|PubMed:24337741}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q8TDQ0-1; Sequence=Displayed;
Name=2;
IsoId=Q8TDQ0-2; Sequence=VSP_017287, VSP_017288;
-!- TISSUE SPECIFICITY: Expressed in T-helper type 1 (Th1)
lymphocytes. Expressed on regulatory T (Treg) cells after TCR
stimulation. Expressed in dendritic cells and natural killer (NK)
cells. Expressed in epithelial tissues. Expression is increased on
CD4+ and CD8+ T-cells in chronic hepatitis C virus (HCV)
infection. In progressive HIV-1 infection, expression is up-
regulated on HIV-1-specific CD8 T-cells.
{ECO:0000269|PubMed:11823861, ECO:0000269|PubMed:17069754,
ECO:0000269|PubMed:18006747, ECO:0000269|PubMed:19001139,
ECO:0000269|PubMed:19587053, ECO:0000269|PubMed:22323453,
ECO:0000269|PubMed:22383801, ECO:0000269|PubMed:24838857}.
-!- PTM: O-glycosylated with core 1 or possibly core 8 glycans.
{ECO:0000269|PubMed:22171320}.
-!- PTM: Phosphorylated on tyrosine residues; modestly increased after
TCR/CD28 stimulation. Can be phosphorylated in the cytoplasmatic
domain by FYN (By similarity). Phosphorylation at Tyr-265 is
increased by stimulation with ligand LGALS9.
{ECO:0000250|UniProtKB:Q8VIM0, ECO:0000269|PubMed:17069754,
ECO:0000269|PubMed:24337741}.
-!- DISEASE: Note=May be involved in T-cell exhaustion associated with
chronic viral infections such as with human immunodeficiency virus
(HIV) and hepatitic C virus (HCV). {ECO:0000269|PubMed:19001139,
ECO:0000269|PubMed:19587053}.
-!- SIMILARITY: Belongs to the immunoglobulin superfamily. TIM family.
{ECO:0000305}.
-!- CAUTION: Experimental results based on the injection of
HAVCR2/TIM-3 antibodies or use of HAVCR2/TIM-3-Fc fusion proteins
can reflect changes in the activity of several cell types and
pathways as HAVCR2/TIM-3 is expressed by multiple immune cell
types. {ECO:0000305|PubMed:24825777}.
-----------------------------------------------------------------------
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
Distributed under the Creative Commons Attribution-NoDerivs License
-----------------------------------------------------------------------
EMBL; AF251707; AAM19100.1; -; mRNA.
EMBL; AY069944; AAL55401.1; -; mRNA.
EMBL; AK027334; BAB55044.1; -; mRNA.
EMBL; AK314406; BAG37029.1; -; mRNA.
EMBL; AC011377; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471062; EAW61614.1; -; Genomic_DNA.
EMBL; BC020843; AAH20843.1; -; mRNA.
EMBL; BC063431; AAH63431.1; -; mRNA.
CCDS; CCDS4333.1; -. [Q8TDQ0-1]
RefSeq; NP_116171.3; NM_032782.4. [Q8TDQ0-1]
UniGene; Hs.710500; -.
PDB; 5DZL; X-ray; 3.40 A; A/B=22-126.
PDB; 5F71; X-ray; 2.40 A; A/B=22-130.
PDBsum; 5DZL; -.
PDBsum; 5F71; -.
ProteinModelPortal; Q8TDQ0; -.
SMR; Q8TDQ0; -.
BioGrid; 124313; 72.
DIP; DIP-61459N; -.
IntAct; Q8TDQ0; 13.
STRING; 9606.ENSP00000312002; -.
iPTMnet; Q8TDQ0; -.
PhosphoSitePlus; Q8TDQ0; -.
UniCarbKB; Q8TDQ0; -.
BioMuta; HAVCR2; -.
DMDM; 311033536; -.
PaxDb; Q8TDQ0; -.
PeptideAtlas; Q8TDQ0; -.
PRIDE; Q8TDQ0; -.
DNASU; 84868; -.
Ensembl; ENST00000307851; ENSP00000312002; ENSG00000135077. [Q8TDQ0-1]
GeneID; 84868; -.
KEGG; hsa:84868; -.
UCSC; uc003lwk.3; human. [Q8TDQ0-1]
CTD; 84868; -.
DisGeNET; 84868; -.
EuPathDB; HostDB:ENSG00000135077.8; -.
GeneCards; HAVCR2; -.
H-InvDB; HIX0005353; -.
HGNC; HGNC:18437; HAVCR2.
HPA; CAB026003; -.
HPA; HPA010505; -.
HPA; HPA047581; -.
MIM; 606652; gene.
neXtProt; NX_Q8TDQ0; -.
OpenTargets; ENSG00000135077; -.
PharmGKB; PA134883425; -.
eggNOG; ENOG410IJGA; Eukaryota.
eggNOG; ENOG410YSF7; LUCA.
GeneTree; ENSGT00440000039800; -.
HOVERGEN; HBG098563; -.
InParanoid; Q8TDQ0; -.
KO; K20414; -.
OMA; GCRFAMP; -.
OrthoDB; EOG091G0MO1; -.
PhylomeDB; Q8TDQ0; -.
TreeFam; TF336163; -.
Reactome; R-HSA-451927; Interleukin-2 family signaling.
GeneWiki; HAVCR2; -.
GenomeRNAi; 84868; -.
PRO; PR:Q8TDQ0; -.
Proteomes; UP000005640; Chromosome 5.
Bgee; ENSG00000135077; -.
CleanEx; HS_HAVCR2; -.
ExpressionAtlas; Q8TDQ0; baseline and differential.
Genevisible; Q8TDQ0; HS.
GO; GO:0030054; C:cell junction; IEA:UniProtKB-SubCell.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0001772; C:immunological synapse; IEA:Ensembl.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0071222; P:cellular response to lipopolysaccharide; IEA:Ensembl.
GO; GO:0050830; P:defense response to Gram-positive bacterium; IEA:Ensembl.
GO; GO:0006954; P:inflammatory response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002281; P:macrophage activation involved in immune response; IEA:Ensembl.
GO; GO:0060135; P:maternal process involved in female pregnancy; IDA:UniProtKB.
GO; GO:0002519; P:natural killer cell tolerance induction; IMP:UniProtKB.
GO; GO:1900425; P:negative regulation of defense response to bacterium; IEA:Ensembl.
GO; GO:0010629; P:negative regulation of gene expression; IMP:UniProtKB.
GO; GO:0071656; P:negative regulation of granulocyte colony-stimulating factor production; IDA:UniProtKB.
GO; GO:2000521; P:negative regulation of immunological synapse formation; IEA:Ensembl.
GO; GO:0032687; P:negative regulation of interferon-alpha production; IDA:UniProtKB.
GO; GO:0032689; P:negative regulation of interferon-gamma production; IDA:UniProtKB.
GO; GO:0032703; P:negative regulation of interleukin-2 production; IDA:UniProtKB.
GO; GO:0032712; P:negative regulation of interleukin-3 production; IDA:UniProtKB.
GO; GO:0032715; P:negative regulation of interleukin-6 production; IEA:Ensembl.
GO; GO:0030886; P:negative regulation of myeloid dendritic cell activation; IMP:UniProtKB.
GO; GO:0032815; P:negative regulation of natural killer cell activation; IEA:Ensembl.
GO; GO:0002859; P:negative regulation of natural killer cell mediated cytotoxicity directed against tumor cell target; IEA:Ensembl.
GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IMP:UniProtKB.
GO; GO:2001189; P:negative regulation of T cell activation via T cell receptor contact with antigen bound to MHC molecule on antigen presenting cell; IDA:UniProtKB.
GO; GO:0042130; P:negative regulation of T cell proliferation; IEA:Ensembl.
GO; GO:0002826; P:negative regulation of T-helper 1 type immune response; IEA:Ensembl.
GO; GO:0032720; P:negative regulation of tumor necrosis factor production; IMP:UniProtKB.
GO; GO:0032722; P:positive regulation of chemokine production; IEA:Ensembl.
GO; GO:1900426; P:positive regulation of defense response to bacterium; IEA:Ensembl.
GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IEA:Ensembl.
GO; GO:0032729; P:positive regulation of interferon-gamma production; IEA:Ensembl.
GO; GO:0032732; P:positive regulation of interleukin-1 production; IEA:Ensembl.
GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:UniProtKB.
GO; GO:0043032; P:positive regulation of macrophage activation; IEA:Ensembl.
GO; GO:1901224; P:positive regulation of NIK/NF-kappaB signaling; IEA:Ensembl.
GO; GO:0042102; P:positive regulation of T cell proliferation; IEA:Ensembl.
GO; GO:1904469; P:positive regulation of tumor necrosis factor secretion; IMP:UniProtKB.
GO; GO:0002652; P:regulation of tolerance induction dependent upon immune response; IEA:Ensembl.
GO; GO:0034138; P:toll-like receptor 3 signaling pathway; IEA:Ensembl.
GO; GO:0034154; P:toll-like receptor 7 signaling pathway; IEA:Ensembl.
GO; GO:0034162; P:toll-like receptor 9 signaling pathway; IEA:Ensembl.
Gene3D; 2.60.40.10; -; 1.
InterPro; IPR007110; Ig-like_dom.
InterPro; IPR036179; Ig-like_dom_sf.
InterPro; IPR013783; Ig-like_fold.
InterPro; IPR003599; Ig_sub.
InterPro; IPR013106; Ig_V-set.
Pfam; PF07686; V-set; 1.
SMART; SM00409; IG; 1.
SUPFAM; SSF48726; SSF48726; 1.
PROSITE; PS50835; IG_LIKE; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing; Cell junction;
Complete proteome; Disulfide bond; Glycoprotein; Immunity;
Immunoglobulin domain; Inflammatory response; Innate immunity;
Membrane; Metal-binding; Phosphoprotein; Polymorphism;
Reference proteome; Signal; Transmembrane; Transmembrane helix.
SIGNAL 1 21 {ECO:0000255}.
CHAIN 22 301 Hepatitis A virus cellular receptor 2.
/FTId=PRO_0000042101.
TOPO_DOM 22 202 Extracellular. {ECO:0000255}.
TRANSMEM 203 223 Helical. {ECO:0000255}.
TOPO_DOM 224 301 Cytoplasmic. {ECO:0000255}.
DOMAIN 22 124 Ig-like V-type.
METAL 116 116 Calcium; via carbonyl oxygen.
{ECO:0000250|UniProtKB:Q8VIM0}.
METAL 119 119 Calcium. {ECO:0000250|UniProtKB:Q8VIM0}.
BINDING 111 111 Phosphatidylserine.
{ECO:0000250|UniProtKB:Q8VIM0}.
BINDING 118 118 Phosphatidylserine; via amide nitrogen.
{ECO:0000250|UniProtKB:Q8VIM0}.
MOD_RES 265 265 Phosphotyrosine; by ITK.
{ECO:0000269|PubMed:17069754}.
CARBOHYD 145 145 O-linked (GalNAc...) threonine.
{ECO:0000269|PubMed:22171320}.
CARBOHYD 172 172 N-linked (GlcNAc...) asparagine.
{ECO:0000255}.
DISULFID 38 110 {ECO:0000250|UniProtKB:Q8VIM0,
ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 52 63 {ECO:0000250|UniProtKB:Q8VIM0,
ECO:0000255|PROSITE-ProRule:PRU00114}.
DISULFID 58 109 {ECO:0000250|UniProtKB:Q8VIM0,
ECO:0000255|PROSITE-ProRule:PRU00114}.
VAR_SEQ 132 142 AKVTPAPTRQR -> GEWTFACHLYE (in isoform
2). {ECO:0000303|PubMed:15489334}.
/FTId=VSP_017287.
VAR_SEQ 143 301 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_017288.
VARIANT 140 140 R -> L (in dbSNP:rs1036199).
{ECO:0000269|PubMed:11823861,
ECO:0000269|PubMed:14702039,
ECO:0000269|PubMed:15489334,
ECO:0000269|Ref.2, ECO:0000269|Ref.3,
ECO:0000269|Ref.6}.
/FTId=VAR_025342.
MUTAGEN 265 265 Y->A: Abolishes TCR-induced NFAT
activation; when associated with A-272.
{ECO:0000269|PubMed:26492563}.
MUTAGEN 265 265 Y->E: No effect on TCR-induced NFAT
activation (phosphomimetic mutation);
when associated with E-272.
{ECO:0000269|PubMed:26492563}.
MUTAGEN 272 272 Y->A: Abolishes TCR-induced NFAT
activation; when associated with A-265.
{ECO:0000269|PubMed:26492563}.
MUTAGEN 272 272 Y->E: No effect on TCR-induced NFAT
activation (phosphomimetic mutation);
when associated with E-265.
{ECO:0000269|PubMed:26492563}.
CONFLICT 101 101 T -> I (in Ref. 2; AAM19100).
{ECO:0000305}.
STRAND 26 29 {ECO:0000244|PDB:5F71}.
STRAND 34 36 {ECO:0000244|PDB:5F71}.
STRAND 44 46 {ECO:0000244|PDB:5F71}.
STRAND 51 57 {ECO:0000244|PDB:5F71}.
STRAND 60 62 {ECO:0000244|PDB:5F71}.
STRAND 64 69 {ECO:0000244|PDB:5F71}.
HELIX 77 79 {ECO:0000244|PDB:5F71}.
STRAND 80 83 {ECO:0000244|PDB:5F71}.
HELIX 88 90 {ECO:0000244|PDB:5F71}.
STRAND 95 97 {ECO:0000244|PDB:5F71}.
HELIX 102 104 {ECO:0000244|PDB:5F71}.
STRAND 106 112 {ECO:0000244|PDB:5F71}.
STRAND 121 130 {ECO:0000244|PDB:5F71}.
SEQUENCE 301 AA; 33394 MW; 519A5B0D512B6173 CRC64;
MFSHLPFDCV LLLLLLLLTR SSEVEYRAEV GQNAYLPCFY TPAAPGNLVP VCWGKGACPV
FECGNVVLRT DERDVNYWTS RYWLNGDFRK GDVSLTIENV TLADSGIYCC RIQIPGIMND
EKFNLKLVIK PAKVTPAPTR QRDFTAAFPR MLTTRGHGPA ETQTLGSLPD INLTQISTLA
NELRDSRLAN DLRDSGATIR IGIYIGAGIC AGLALALIFG ALIFKWYSHS KEKIQNLSLI
SLANLPPSGL ANAVAEGIRS EENIYTIEEN VYEVEEPNEY YCYVSSRQQP SQPLGCRFAM
P


Related products :

Catalog number Product name Quantity
EIAAB42457 Havcr2,HAVcr-2,Hepatitis A virus cellular receptor 2 homolog,Rat,Rattus norvegicus,T-cell immunoglobulin and mucin domain-containing protein 3,T-cell membrane protein 3,Tim3,TIM-3,Timd3,TIMD-3
18-783-75569 RABBIT ANTI TIM-1 - T-CELL IMMUNOGLOBULIN MUCIN-1; HAVcr-1; T-cell immunoglobulin and mucin domain-containing protein 1; TIMD-1; T-cell membrane protein 1; TIM-1; TIM Polyclonal 0.1 mg
E0785r ELISA kit Havcr1,HAVcr-1,Hepatitis A virus cellular receptor 1 homolog,Kidney injury molecule 1,Kim1,KIM-1,Rat,Rattus norvegicus,T cell immunoglobulin and mucin domain-containing protein 1,TIMD-1 96T
E0785r ELISA Havcr1,HAVcr-1,Hepatitis A virus cellular receptor 1 homolog,Kidney injury molecule 1,Kim1,KIM-1,Rat,Rattus norvegicus,T cell immunoglobulin and mucin domain-containing protein 1,TIMD-1 96T
U0785r CLIA Havcr1,HAVcr-1,Hepatitis A virus cellular receptor 1 homolog,Kidney injury molecule 1,Kim1,KIM-1,Rat,Rattus norvegicus,T cell immunoglobulin and mucin domain-containing protein 1,TIMD-1 96T
U0785h CLIA HAVCR1,HAVcr-1,Hepatitis A virus cellular receptor 1,Homo sapiens,Human,Kidney injury molecule 1,KIM1,KIM-1,T-cell immunoglobulin and mucin domain-containing protein 1,T-cell membrane protein 1,T 96T
E0785h ELISA HAVCR1,HAVcr-1,Hepatitis A virus cellular receptor 1,Homo sapiens,Human,Kidney injury molecule 1,KIM1,KIM-1,T-cell immunoglobulin and mucin domain-containing protein 1,T-cell membrane protein 1, 96T
E0785m ELISA Havcr1,HAVcr-1,Hepatitis A virus cellular receptor 1 homolog,Kidney injury molecule 1,Kim1,KIM-1,Mouse,Mus musculus,T cell immunoglobulin and mucin domain-containing protein 1,T cell membrane pr 96T
U0785m CLIA Havcr1,HAVcr-1,Hepatitis A virus cellular receptor 1 homolog,Kidney injury molecule 1,Kim1,KIM-1,Mouse,Mus musculus,T cell immunoglobulin and mucin domain-containing protein 1,T cell membrane pro 96T
E0785h ELISA kit HAVCR1,HAVcr-1,Hepatitis A virus cellular receptor 1,Homo sapiens,Human,Kidney injury molecule 1,KIM1,KIM-1,T-cell immunoglobulin and mucin domain-containing protein 1,T-cell membrane prote 96T
E0785m ELISA kit Havcr1,HAVcr-1,Hepatitis A virus cellular receptor 1 homolog,Kidney injury molecule 1,Kim1,KIM-1,Mouse,Mus musculus,T cell immunoglobulin and mucin domain-containing protein 1,T cell membra 96T
EIAAB42459 Mouse,Mus musculus,SMUCKLER,Spleen, mucin-containing, knockout of lymphotoxin protein,T-cell immunoglobulin and mucin domain-containing protein 4,T-cell membrane protein 4,Tim4,TIM-4,Timd4,TIMD-4
EIAAB42455 Mouse,Mus musculus,T-cell immunoglobulin and mucin domain-containing protein 2,T-cell membrane protein 2,Tim2,TIM-2,Timd2,TIMD-2
EIAAB42456 Rat,Rattus norvegicus,T-cell immunoglobulin and mucin domain-containing protein 2,T-cell membrane protein 2,Tim2,TIM-2,Timd2,TIMD-2
EIAAB42458 Homo sapiens,Human,T-cell immunoglobulin and mucin domain-containing protein 4,T-cell membrane protein 4,TIM4,TIM-4,TIMD4,TIMD-4
18-783-75570 RABBIT ANTI TIM-4 (C-TERMINAL) - T-CELL IMMUNOGLOBULIN MUCIN-4; TIMD-4; T-cell membrane protein 4; TIM-4 Polyclonal 0.1 mg
DS-PB-01961 Rabbit Anti-Kidney Injury Molecule 1 (KIM-1) _ T-cell Immunoglobulin and Mucin Protein 1 (TIM-1) _ Hepatitis A Virus Cellular Receptor 1 (HAVCR1) 100
DS-PB-02960 Rabbit Anti-Kidney Injury Molecule 1 (KIM-1) _ T-cell Immunoglobulin and Mucin Protein 1 (TIM-1) _ Hepatitis A Virus Cellular Receptor 1 (HAVCR1) 50
3809 (NT) T cell immunoglobulin and mucin domain containing protein 1 0.5 mg
3811 (IN) T cell immunoglobulin and mucin domain containing protein 1 0.5 mg
3813 (CT) T cell immunoglobulin and mucin domain containing protein 4 0.5 mg
3815 (IN) T cell immunoglobulin and mucin domain containing protein 4 0.5 mg
3815 (IN) T cell immunoglobulin and mucin domain containing protein 4 0.1 mg
3813 (CT) T cell immunoglobulin and mucin domain containing protein 4 0.1 mg
3811 (IN) T cell immunoglobulin and mucin domain containing protein 1 0.1 mg


 

GENTAUR Belgium BVBA BE0473327336
Voortstraat 49, 1910 Kampenhout BELGIUM
Tel 0032 16 58 90 45

Fax 0032 16 50 90 45
info@gentaur.com | Gentaur





GENTAUR Ltd.
Howard Frank Turnberry House
1404-1410 High Road
Whetstone London N20 9BH
Tel 020 3393 8531 Fax 020 8445 9411
uk@gentaur.com | Gentaur

 

 




GENTAUR France SARL
9, rue Lagrange, 75005 Paris
Tel 01 43 25 01 50

Fax 01 43 25 01 60
RCS Paris B 484 237 888

SIRET 48423788800017

BNP PARIBAS PARIS PL MAUBERT BIC BNPAFRPPPRG

france@gentaur.com | Gentaur

GENTAUR GmbH
Marienbongard 20
52062 Aachen Deutschland
Support Karolina Elandt
Tel: 0035929830070
Fax: (+49) 241 56 00 47 88

Logistic :0241 40 08 90 86
Bankleitzahl 39050000
IBAN lautet DE8839050000107569353
Handelsregister Aachen HR B 16058
Umsatzsteuer-Identifikationsnummer *** DE 815175831
Steuernummer 201/5961/3925
de@gentaur.com | Gentaur

GENTAUR U.S.A
Genprice Inc, Logistics
547, Yurok Circle
San Jose, CA 95123
CA 95123
Tel (408) 780-0908,
Fax (408) 780-0908,
sales@genprice.com

Genprice Inc, Invoices and accounting
6017 Snell Ave, Ste 357
San Jose, CA 95123




GENTAUR Nederland BV
NL850396268B01 KVK nummer 52327027
Kuiper 1
5521 DG Eersel Nederland
Tel:  0208-080893  Fax: 0497-517897
nl@gentaur.com | Gentaur
IBAN: NL04 RABO 0156 9854 62   SWIFT RABONL2U






GENTAUR Spain
tel:0911876558
spain@gentaur.com | Gentaur






ГЕНТАУЪР БЪЛГАРИЯ
ID # 201 358 931 /BULSTAT
София 1000, ул. "Граф Игнатиев" 53 вх. В, ет. 2
Tel 0035924682280 Fax 0035924808322
e-mail: Sofia@gentaur.com | Gentaur
IBAN: BG11FINV91501014771636
BIC: FINVBGSF

GENTAUR Poland Sp. z o.o.


ul. Grunwaldzka 88/A m.2
81-771 Sopot, Poland
TEL Gdansk 058 710 33 44 FAX  058 710 33 48              

poland@gentaur.com | Gentaur

Other countries

Österreich +43720880899

Canada Montreal +15149077481

Ceská republika Praha +420246019719

Danmark +4569918806

Finland Helsset +358942419041

Magyarország Budapest +3619980547

Ireland Dublin+35316526556

Luxembourg+35220880274

Norge Oslo+4721031366

Sverige Stockholm+46852503438

Schweiz Züri+41435006251

US New York+17185132983

GENTAUR Italy
SRL IVA IT03841300167
Piazza Giacomo Matteotti, 6
24122 Bergamo Tel 02 36 00 65 93
Fax 02 36 00 65 94
italia@gentaur.com | Gentaur