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SH2 domain-containing protein 1B (EWS/FLI1-activated transcript 2) (EAT-2)

 SH21B_HUMAN             Reviewed;         132 AA.
O14796; B2RBN6; Q5T0L1; Q8NI18; Q969K9;
27-APR-2001, integrated into UniProtKB/Swiss-Prot.
19-SEP-2002, sequence version 2.
12-SEP-2018, entry version 150.
RecName: Full=SH2 domain-containing protein 1B;
AltName: Full=EWS/FLI1-activated transcript 2;
Short=EAT-2;
Name=SH2D1B; Synonyms=EAT2;
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), AND CHARACTERIZATION.
PubMed=11689425; DOI=10.1093/emboj/20.21.5840;
Morra M., Lu J., Poy F., Martin M., Sayos J., Calpe S., Gullo C.,
Howie D., Rietdijk S., Thompson A., Coyle A.J., Denny C., Yaffe M.B.,
Engel P., Eck M.J., Terhorst C.;
"Structural basis for the interaction of the free SH2 domain EAT-2
with SLAM receptors in hematopoietic cells.";
EMBO J. 20:5840-5852(2001).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Leukocyte;
Colonna M.;
Submitted (JUL-2001) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH CD84, AND
VARIANT LYS-122.
PubMed=12115647;
DOI=10.1002/1521-4141(200206)32:6<1640::AID-IMMU1640>3.0.CO;2-S;
Tangye S.G., van de Weerdt B.C.M., Avery D.T., Hodgkin P.D.;
"CD84 is up-regulated on a major population of human memory B cells
and recruits the SH2 domain containing proteins SAP and EAT-2.";
Eur. J. Immunol. 32:1640-1649(2002).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Spleen;
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=16710414; DOI=10.1038/nature04727;
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
Beck S., Rogers J., Bentley D.R.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Leukocyte, and Lung;
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]
NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-45.
PubMed=9000139;
Thompson A.D., Braun B.S., Arvand A., Stewart S.D., May W.A., Chen E.,
Korenberg J., Denny C.;
"EAT-2 is a novel SH2 domain containing protein that is up regulated
by Ewing's sarcoma EWS/FLI1 fusion gene.";
Oncogene 13:2649-2658(1996).
[9]
REVIEW.
PubMed=21219180; DOI=10.1146/annurev-immunol-030409-101302;
Cannons J.L., Tangye S.G., Schwartzberg P.L.;
"SLAM family receptors and SAP adaptors in immunity.";
Annu. Rev. Immunol. 29:665-705(2011).
[10]
FUNCTION, MUTAGENESIS OF TYR-127, INTERACTION WITH PLCG1, AND
PHOSPHORYLATION AT TYR-127.
PubMed=24687958; DOI=10.1084/jem.20132038;
Perez-Quintero L.A., Roncagalli R., Guo H., Latour S., Davidson D.,
Veillette A.;
"EAT-2, a SAP-like adaptor, controls NK cell activation through
phospholipase Cgamma, Ca++, and Erk, leading to granule
polarization.";
J. Exp. Med. 211:727-742(2014).
-!- FUNCTION: Cytoplasmic adapter regulating receptors of the
signaling lymphocytic activation molecule (SLAM) family such as
CD84, SLAMF1, LY9 and CD244 (PubMed:11689425). In SLAM signaling
seems to cooperate with SH2D1A/SAP. Plays a role in regulation of
effector functions of natural killer (NK) cells by controlling
signal transduction through CD244/2B4 without effecting its
tyrosine phosphorylation; downstream signaling involves PLCG1 and
ERK activation (PubMed:24687958). Activation of SLAMF7-mediated NK
cell function does not effect receptor tyrosine phosphorylation
but distal signaling (By similarity). In the context of NK cell-
mediated cytotoxicity does not enhance conjugate formation with
target cells but stimulates polarization of the microtubule-
organizing center and cytotoxic granules toward the NK cell
synapse (PubMed:24687958). Negatively regulates CD40-induced
cytokine production in dendritic cells downstream of SLAM family
receptors probably by inducing activation of the PI3K pathway to
inhibit p38 MAPK and JNK activation (By similarity).
{ECO:0000250|UniProtKB:O35324, ECO:0000269|PubMed:11689425,
ECO:0000269|PubMed:24687958, ECO:0000305|PubMed:21219180}.
-!- SUBUNIT: Binds to the phosphorylated receptors CD84, SLAMF1, LY9
and CD244. Does not bind to non-phosphorylated SLAMF1
(PubMed:11689425). Interacts with SLAMF7 (via ITSM phosphorylated
on 'Tyr-304'). Interacts with Src kinases HCK, LYN, FYN, FGR and
LCK (via kinase domains) (By similarity). Interacts
(phosphorylated at Tyr-127) with PLCG1.
{ECO:0000250|UniProtKB:O35324, ECO:0000269|PubMed:11689425,
ECO:0000269|PubMed:24687958}.
-!- INTERACTION:
Q53HF2:-; NbExp=3; IntAct=EBI-3923013, EBI-877761;
P10275:AR; NbExp=3; IntAct=EBI-3923013, EBI-608057;
Q9BZW8:CD244; NbExp=7; IntAct=EBI-3923013, EBI-1580565;
Q9UIB8:CD84; NbExp=3; IntAct=EBI-3923013, EBI-6691679;
Q13480:GAB1; NbExp=8; IntAct=EBI-3923013, EBI-517684;
P10721:KIT; NbExp=8; IntAct=EBI-3923013, EBI-1379503;
P08581:MET; NbExp=6; IntAct=EBI-3923013, EBI-1039152;
Q8TAK6:OLIG1; NbExp=2; IntAct=EBI-3923013, EBI-3867416;
P19174:PLCG1; NbExp=2; IntAct=EBI-3923013, EBI-79387;
P16885:PLCG2; NbExp=2; IntAct=EBI-3923013, EBI-617403;
Q96DU3:SLAMF6; NbExp=4; IntAct=EBI-3923013, EBI-14058448;
Q9BYV2:TRIM54; NbExp=5; IntAct=EBI-3923013, EBI-2130429;
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=O14796-1; Sequence=Displayed;
Name=2;
IsoId=O14796-2; Sequence=VSP_010341;
-----------------------------------------------------------------------
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EMBL; AF256653; AAL26000.1; -; mRNA.
EMBL; AF403479; AAL27357.1; -; mRNA.
EMBL; AF484964; AAM28522.1; -; mRNA.
EMBL; AK097162; BAC04968.1; -; mRNA.
EMBL; AK314743; BAG37283.1; -; mRNA.
EMBL; AL512785; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471067; EAW90703.1; -; Genomic_DNA.
EMBL; BC022407; AAH22407.1; -; mRNA.
EMBL; BC066595; AAH66595.1; -; mRNA.
EMBL; AF020264; AAB70927.1; -; Genomic_DNA.
CCDS; CCDS30928.1; -. [O14796-1]
RefSeq; NP_444512.2; NM_053282.4. [O14796-1]
UniGene; Hs.350581; -.
PDB; 5KAZ; X-ray; 1.70 A; A=1-104.
PDBsum; 5KAZ; -.
ProteinModelPortal; O14796; -.
SMR; O14796; -.
BioGrid; 125563; 14.
IntAct; O14796; 31.
MINT; O14796; -.
STRING; 9606.ENSP00000356906; -.
iPTMnet; O14796; -.
PhosphoSitePlus; O14796; -.
BioMuta; SH2D1B; -.
PaxDb; O14796; -.
PeptideAtlas; O14796; -.
PRIDE; O14796; -.
ProteomicsDB; 48245; -.
ProteomicsDB; 48246; -. [O14796-2]
DNASU; 117157; -.
Ensembl; ENST00000367929; ENSP00000356906; ENSG00000198574. [O14796-1]
GeneID; 117157; -.
KEGG; hsa:117157; -.
UCSC; uc001gbz.2; human. [O14796-1]
CTD; 117157; -.
DisGeNET; 117157; -.
EuPathDB; HostDB:ENSG00000198574.5; -.
GeneCards; SH2D1B; -.
HGNC; HGNC:30416; SH2D1B.
HPA; HPA054791; -.
MIM; 608510; gene.
neXtProt; NX_O14796; -.
OpenTargets; ENSG00000198574; -.
PharmGKB; PA142670926; -.
eggNOG; KOG0565; Eukaryota.
eggNOG; COG5411; LUCA.
GeneTree; ENSGT00510000046904; -.
HOGENOM; HOG000231700; -.
HOVERGEN; HBG003702; -.
InParanoid; O14796; -.
KO; K07989; -.
OMA; PYYHGPL; -.
OrthoDB; EOG091G0ULG; -.
PhylomeDB; O14796; -.
TreeFam; TF343096; -.
Reactome; R-HSA-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
SignaLink; O14796; -.
GeneWiki; SH2D1B; -.
GenomeRNAi; 117157; -.
PRO; PR:O14796; -.
Proteomes; UP000005640; Chromosome 1.
Bgee; ENSG00000198574; Expressed in 97 organ(s), highest expression level in leukocyte.
CleanEx; HS_SH2D1B; -.
Genevisible; O14796; HS.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0005622; C:intracellular; IDA:UniProtKB.
GO; GO:0030674; F:protein binding, bridging; TAS:UniProtKB.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0045087; P:innate immune response; IEA:UniProtKB-KW.
GO; GO:0002366; P:leukocyte activation involved in immune response; ISS:UniProtKB.
GO; GO:0045089; P:positive regulation of innate immune response; ISS:UniProtKB.
GO; GO:0002717; P:positive regulation of natural killer cell mediated immunity; ISS:UniProtKB.
GO; GO:0050776; P:regulation of immune response; TAS:Reactome.
CDD; cd10342; SH2_SAP1; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR035049; EAT2_SH2.
InterPro; IPR000980; SH2.
InterPro; IPR036860; SH2_dom_sf.
PANTHER; PTHR45419; PTHR45419; 1.
Pfam; PF00017; SH2; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00252; SH2; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
1: Evidence at protein level;
3D-structure; Adaptive immunity; Alternative splicing;
Complete proteome; Immunity; Innate immunity; Phosphoprotein;
Polymorphism; Reference proteome; SH2 domain.
CHAIN 1 132 SH2 domain-containing protein 1B.
/FTId=PRO_0000097724.
DOMAIN 5 101 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
MOD_RES 127 127 Phosphotyrosine.
{ECO:0000305|PubMed:24687958}.
VAR_SEQ 67 121 Missing (in isoform 2).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010341.
VARIANT 36 36 I -> T (in dbSNP:rs35688243).
/FTId=VAR_051347.
VARIANT 122 122 N -> K (in dbSNP:rs34001279).
{ECO:0000269|PubMed:12115647}.
/FTId=VAR_051348.
MUTAGEN 127 127 Y->F: No stimulation of granule
polarization during NK-mediated
cytoxicity, abolishes activation of
CD244/2B4-mediated cytotoxicity,
abolishes augmentation of CD244/2B4-
triggered PLCG1 phosphorylation and ERK
activation.
{ECO:0000269|PubMed:24687958}.
HELIX 12 20 {ECO:0000244|PDB:5KAZ}.
STRAND 27 32 {ECO:0000244|PDB:5KAZ}.
STRAND 34 36 {ECO:0000244|PDB:5KAZ}.
STRAND 40 46 {ECO:0000244|PDB:5KAZ}.
STRAND 49 57 {ECO:0000244|PDB:5KAZ}.
STRAND 63 65 {ECO:0000244|PDB:5KAZ}.
STRAND 74 78 {ECO:0000244|PDB:5KAZ}.
HELIX 79 87 {ECO:0000244|PDB:5KAZ}.
STRAND 88 95 {ECO:0000244|PDB:5KAZ}.
SEQUENCE 132 AA; 15297 MW; BC9FEA398B6B27DE CRC64;
MDLPYYHGRL TKQDCETLLL KEGVDGNFLL RDSESIPGVL CLCVSFKNIV YTYRIFREKH
GYYRIQTAEG SPKQVFPSLK ELISKFEKPN QGMVVHLLKP IKRTSPSLRW RGLKLELETF
VNSNSDYVDV LP


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