SH2B3_MOUSE
ID SH2B3_MOUSE Reviewed; 548 AA.
AC O09039;
DT 27-APR-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 2.
DT 03-AUG-2022, entry version 161.
DE RecName: Full=SH2B adapter protein 3;
DE AltName: Full=Lymphocyte adapter protein;
DE AltName: Full=Lymphocyte-specific adapter protein Lnk;
DE AltName: Full=Signal transduction protein Lnk;
GN Name=Sh2b3; Synonyms=Lnk;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC STRAIN=129/Sv;
RX PubMed=11114373; DOI=10.1016/s1074-7613(00)00060-1;
RA Takaki S., Sauer K., Iritani B.M., Chien S., Ebihara Y., Tsuji K.,
RA Takatsu K., Perlmutter R.M.;
RT "Control of B cell production by the adaptor protein lnk. Definition Of a
RT conserved family of signal-modulating proteins.";
RL Immunity 13:599-609(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=FVB/N; TISSUE=Mammary gland;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-13 AND SER-302, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, Lung, Spleen, and Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Links T-cell receptor activation signal to phospholipase C-
CC gamma-1, GRB2 and phosphatidylinositol 3-kinase. {ECO:0000250}.
CC -!- PTM: Tyrosine phosphorylated. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the SH2B adapter family. {ECO:0000305}.
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DR EMBL; U89992; AAB58580.2; -; mRNA.
DR EMBL; U89993; AAB58581.1; -; Genomic_DNA.
DR EMBL; BC006759; AAH06759.1; -; mRNA.
DR CCDS; CCDS19641.1; -.
DR RefSeq; NP_001293055.1; NM_001306126.1.
DR RefSeq; NP_001293056.1; NM_001306127.1.
DR RefSeq; NP_032533.1; NM_008507.4.
DR RefSeq; XP_006530233.1; XM_006530170.3.
DR RefSeq; XP_006530234.1; XM_006530171.3.
DR RefSeq; XP_006530235.1; XM_006530172.1.
DR RefSeq; XP_006530236.1; XM_006530173.3.
DR PDB; 7R8W; X-ray; 1.90 A; A=325-437.
DR PDB; 7R8X; X-ray; 2.30 A; A=328-438.
DR PDBsum; 7R8W; -.
DR PDBsum; 7R8X; -.
DR AlphaFoldDB; O09039; -.
DR SMR; O09039; -.
DR BioGRID; 201186; 5.
DR STRING; 10090.ENSMUSP00000113926; -.
DR iPTMnet; O09039; -.
DR PhosphoSitePlus; O09039; -.
DR jPOST; O09039; -.
DR MaxQB; O09039; -.
DR PaxDb; O09039; -.
DR PRIDE; O09039; -.
DR ProteomicsDB; 261210; -.
DR Antibodypedia; 1179; 270 antibodies from 36 providers.
DR DNASU; 16923; -.
DR Ensembl; ENSMUST00000040308; ENSMUSP00000041611; ENSMUSG00000042594.
DR Ensembl; ENSMUST00000086310; ENSMUSP00000083490; ENSMUSG00000042594.
DR Ensembl; ENSMUST00000122426; ENSMUSP00000113926; ENSMUSG00000042594.
DR GeneID; 16923; -.
DR KEGG; mmu:16923; -.
DR UCSC; uc008zkg.1; mouse.
DR CTD; 10019; -.
DR MGI; MGI:893598; Sh2b3.
DR VEuPathDB; HostDB:ENSMUSG00000042594; -.
DR eggNOG; ENOG502QS89; Eukaryota.
DR GeneTree; ENSGT00950000183191; -.
DR InParanoid; O09039; -.
DR OMA; HADVTHF; -.
DR OrthoDB; 556279at2759; -.
DR PhylomeDB; O09039; -.
DR TreeFam; TF323184; -.
DR Reactome; R-MMU-1433559; Regulation of KIT signaling.
DR Reactome; R-MMU-9706369; Negative regulation of FLT3.
DR Reactome; R-MMU-983231; Factors involved in megakaryocyte development and platelet production.
DR BioGRID-ORCS; 16923; 2 hits in 76 CRISPR screens.
DR ChiTaRS; Sh2b3; mouse.
DR PRO; PR:O09039; -.
DR Proteomes; UP000000589; Chromosome 5.
DR RNAct; O09039; protein.
DR Bgee; ENSMUSG00000042594; Expressed in granulocyte and 210 other tissues.
DR ExpressionAtlas; O09039; baseline and differential.
DR Genevisible; O09039; MM.
DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central.
DR GO; GO:0042301; F:phosphate ion binding; ISO:MGI.
DR GO; GO:1990782; F:protein tyrosine kinase binding; IPI:BHF-UCL.
DR GO; GO:0044877; F:protein-containing complex binding; ISO:MGI.
DR GO; GO:0030159; F:signaling receptor complex adaptor activity; IPI:BHF-UCL.
DR GO; GO:0005173; F:stem cell factor receptor binding; IDA:BHF-UCL.
DR GO; GO:0005068; F:transmembrane receptor protein tyrosine kinase adaptor activity; IBA:GO_Central.
DR GO; GO:1990869; P:cellular response to chemokine; IMP:ARUK-UCL.
DR GO; GO:0036016; P:cellular response to interleukin-3; IDA:ARUK-UCL.
DR GO; GO:0035162; P:embryonic hemopoiesis; IDA:MGI.
DR GO; GO:0048821; P:erythrocyte development; ISO:MGI.
DR GO; GO:0060218; P:hematopoietic stem cell differentiation; IMP:MGI.
DR GO; GO:0030097; P:hemopoiesis; IMP:MGI.
DR GO; GO:0035556; P:intracellular signal transduction; IDA:MGI.
DR GO; GO:0035855; P:megakaryocyte development; IMP:ARUK-UCL.
DR GO; GO:0035702; P:monocyte homeostasis; IGI:BHF-UCL.
DR GO; GO:0008285; P:negative regulation of cell population proliferation; IMP:ARUK-UCL.
DR GO; GO:0070100; P:negative regulation of chemokine-mediated signaling pathway; IMP:ARUK-UCL.
DR GO; GO:1900235; P:negative regulation of Kit signaling pathway; IMP:BHF-UCL.
DR GO; GO:0043407; P:negative regulation of MAP kinase activity; IMP:ARUK-UCL.
DR GO; GO:0090331; P:negative regulation of platelet aggregation; IGI:BHF-UCL.
DR GO; GO:0051898; P:negative regulation of protein kinase B signaling; IDA:ARUK-UCL.
DR GO; GO:0046426; P:negative regulation of receptor signaling pathway via JAK-STAT; ISO:MGI.
DR GO; GO:0060761; P:negative regulation of response to cytokine stimulus; ISO:MGI.
DR GO; GO:1903671; P:negative regulation of sprouting angiogenesis; ISO:MGI.
DR GO; GO:0042532; P:negative regulation of tyrosine phosphorylation of STAT protein; IMP:ARUK-UCL.
DR GO; GO:0001780; P:neutrophil homeostasis; IGI:BHF-UCL.
DR GO; GO:0045589; P:regulation of regulatory T cell differentiation; ISO:MGI.
DR GO; GO:0038163; P:thrombopoietin-mediated signaling pathway; IMP:ARUK-UCL.
DR CDD; cd10412; SH2_SH2B3; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR015012; Phe_ZIP.
DR InterPro; IPR036290; Phe_ZIP_sf.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR030523; SH2B.
DR InterPro; IPR030522; SH2B3.
DR InterPro; IPR035059; SH2B3_SH2.
DR PANTHER; PTHR10872; PTHR10872; 1.
DR PANTHER; PTHR10872:SF1; PTHR10872:SF1; 1.
DR Pfam; PF08916; Phe_ZIP; 1.
DR Pfam; PF00017; SH2; 1.
DR PRINTS; PR00401; SH2DOMAIN.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF109805; SSF109805; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome; SH2 domain.
FT CHAIN 1..548
FT /note="SH2B adapter protein 3"
FT /id="PRO_0000084455"
FT DOMAIN 168..279
FT /note="PH"
FT DOMAIN 336..434
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT REGION 1..25
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 78..108
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 128..160
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 290..313
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 13
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 102
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ2"
FT MOD_RES 129
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9UQQ2"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT HELIX 327..331
FT /evidence="ECO:0007829|PDB:7R8W"
FT HELIX 343..351
FT /evidence="ECO:0007829|PDB:7R8W"
FT HELIX 354..357
FT /evidence="ECO:0007829|PDB:7R8W"
FT STRAND 361..365
FT /evidence="ECO:0007829|PDB:7R8W"
FT STRAND 367..369
FT /evidence="ECO:0007829|PDB:7R8W"
FT STRAND 373..379
FT /evidence="ECO:0007829|PDB:7R8W"
FT STRAND 382..390
FT /evidence="ECO:0007829|PDB:7R8W"
FT STRAND 396..398
FT /evidence="ECO:0007829|PDB:7R8W"
FT STRAND 401..405
FT /evidence="ECO:0007829|PDB:7R8W"
FT HELIX 406..415
FT /evidence="ECO:0007829|PDB:7R8W"
FT TURN 421..425
FT /evidence="ECO:0007829|PDB:7R8W"
SQ SEQUENCE 548 AA; 60487 MW; D21DCE46185962B8 CRC64;
MNEPTVQPSR TSSAPASPAS PRGWSDFCEQ HAAAAARELA RQYWLFARAH PQPPRADLVS
LQFAELFQRH FCREVRESLA GPPGHDYRAT APPRPALPKA RSSEDLGPRP ACALQHLRRG
LRQLFRRRSA GELPGATSDT NDIDTTAASR PGPARKLLPW GLREPPTEAL KEVVLRYSLA
DEAAMDSGAR WQRGRLVLRS PGPGHSHFLQ LFDPPKSSKP KLQEACSSIR EVRPCTRLEM
PDNLYTFVLK VQDQTDIIFE VGDEQQLNSW LAELRASTGL GLEHPDTELP LSLAAEPGPA
RSPRGSTDSL DQGASPGVLL DPACQKTDHF LSCYPWFHGP ISRVRAAQLV QLQGPDAHGV
FLVRQSESRR GEYVLTFNLQ GRAKHLRLVL TERGQCRVQH LHFPSVVDML RHFQRSPIPL
ECGAACDVRL SGYVVVLSQA PGSSNTVLFP FSLPHWDSEL GHPHLSSVGC PPSHGAEALP
GQVTPPEQIF HLVPSPEELA NSLRQLELES VSSARDSDYD MDSSSRGHLR AIDNQYTPLS
QLCREADV
