CD22_MOUSE
ID CD22_MOUSE Reviewed; 868 AA.
AC P35329; Q3UP36; Q9JHL2; Q9JJX9; Q9JJY0; Q9JJY1; Q9R056; Q9R094; Q9WU51;
DT 01-FEB-1994, integrated into UniProtKB/Swiss-Prot.
DT 23-FEB-2022, sequence version 2.
DT 03-AUG-2022, entry version 188.
DE RecName: Full=B-cell receptor CD22 {ECO:0000305};
DE AltName: Full=B-lymphocyte cell adhesion molecule;
DE Short=BL-CAM;
DE AltName: Full=Sialic acid-binding Ig-like lectin 2;
DE Short=Siglec-2;
DE AltName: Full=T-cell surface antigen Leu-14;
DE AltName: CD_antigen=CD22;
DE Flags: Precursor;
GN Name=Cd22 {ECO:0000303|PubMed:10501843, ECO:0000312|MGI:MGI:88322};
GN Synonyms=Lyb-8, Siglec2;
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], AND VARIANTS ALA-15; GLN-19; LYS-76;
RP 83-ALA--THR-86 DELINS LYS-ALA-GLU-PRO; 88-LYS--GLU-93 DEL; 96-LEU-SER-97
RP DELINS PRO-PRO; ARG-100; SER-108; GLU-179; GLN-185 AND LYS-192; VAL-196;
RP PRO-198; GLU-242; MET-793; ALA-796.
RC STRAIN=DBA/2J; TISSUE=Liver;
RX PubMed=8100843;
RA Law C.-L., Torres R.M., Sundberg H.A., Parkhouse R.M., Brannan C.I.,
RA Copeland N.G., Jenkins N.A., Clark E.A.;
RT "Organization of the murine Cd22 locus. Mapping to chromosome 7 and
RT characterization of two alleles.";
RL J. Immunol. 151:175-187(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANTS LYS-76; 118-PRO--ARG-120 DELINS
RP LEU-ILE-HIS; GLU-179; GLN-185; LYS-192; VAL-196; PRO-198; GLU-242; HIS-250;
RP GLN-279; ILE-386; HIS-393; LEU-409; ARG-425; GLY-429; SER-488; LYS-554;
RP ARG-626; ALA-796 AND THR-814.
RC STRAIN=BXSB, C57BL/6J, and MRL/MpJ;
RX PubMed=10501843; DOI=10.1007/s002510050584;
RA Lajaunias F., Ibnou-Zekri N., Fossati Jimack L., Chicheportiche Y.,
RA Parkhouse R.M., Mary C., Reininger L., Brighouse G., Izui S.;
RT "Polymorphisms in the Cd22 gene of inbred mouse strains.";
RL Immunogenetics 49:991-995(1999).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J; TISSUE=Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [5]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-184 (ISOFORMS 1; 2 AND 3), AND VARIANTS
RP ALA-15; GLN-19; LYS-76; 83-ALA--THR-86 DELINS LYS-ALA-GLU-PRO;
RP 83-ALA-THR-84 DELINS LYS-ALA; 85-LYS--PRO-90 DEL; 88-LYS--GLU-93 DEL;
RP 92-SER-GLU-93 DELINS PRO-GLY; 96-LEU-SER-97 DELINS PRO-PRO; ARG-100;
RP SER-108 AND GLU-179.
RC STRAIN=NZW/LacJ; TISSUE=Spleen;
RX PubMed=10975807; DOI=10.4049/jimmunol.165.6.2987;
RA Mary C., Laporte C., Parzy D., Santiago M.L., Stefani F., Lajaunias F.,
RA Parkhouse M.E., O'Keefe T.L., Neuberger M.S., Izui S., Reininger L.;
RT "Dysregulated expression of the Cd22 gene as a result of a short
RT interspersed nucleotide element insertion in Cd22alpha lupus-prone mice.";
RL J. Immunol. 165:2987-2996(2000).
RN [6]
RP SIALIC ACID-BINDING.
RX PubMed=7533044; DOI=10.1016/s0960-9822(00)00220-7;
RA Kelm S., Pelz A., Schauer R., Filbin M.T., Tang S., de Bellard M.E.,
RA Schnaar R.L., Mahoney J.A., Hartnell A., Bradfield P., Crocker P.R.;
RT "Sialoadhesin, myelin-associated glycoprotein and CD22 define a new family
RT of sialic acid-dependent adhesion molecules of the immunoglobulin
RT superfamily.";
RL Curr. Biol. 4:965-972(1994).
RN [7]
RP PHOSPHORYLATION BY LYN.
RX PubMed=9601638; DOI=10.1016/s0960-9822(98)70223-4;
RA Chan V.W., Lowell C.A., DeFranco A.L.;
RT "Defective negative regulation of antigen receptor signaling in Lyn-
RT deficient B lymphocytes.";
RL Curr. Biol. 8:545-553(1998).
RN [8]
RP INTERACTION WITH GRB2; SYK; PIK3R1/PIK3R2 AND PLCG1, PHOSPHORYLATION AT
RP TYR-783; TYR-828; TYR-843 AND TYR-863, AND MUTAGENESIS OF TYR-828.
RX PubMed=10373493; DOI=10.1074/jbc.274.26.18769;
RA Yohannan J., Wienands J., Coggeshall K.M., Justement L.B.;
RT "Analysis of tyrosine phosphorylation-dependent interactions between
RT stimulatory effector proteins and the B cell co-receptor CD22.";
RL J. Biol. Chem. 274:18769-18776(1999).
RN [9]
RP INTERACTION WITH GRB2; SHC1 AND INPP5D, AND PHOSPHORYLATION BY LYN.
RX PubMed=10748054; DOI=10.1074/jbc.m001892200;
RA Poe J.C., Fujimoto M., Jansen P.J., Miller A.S., Tedder T.F.;
RT "CD22 forms a quaternary complex with SHIP, Grb2, and Shc. A pathway for
RT regulation of B lymphocyte antigen receptor-induced calcium flux.";
RL J. Biol. Chem. 275:17420-17427(2000).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-746; SER-747 AND SER-750, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Spleen;
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: Mediates B-cell B-cell interactions. May be involved in the
CC localization of B-cells in lymphoid tissues. Binds sialylated
CC glycoproteins; one of which is CD45. Preferentially binds to alpha-2,6-
CC linked sialic acid. The sialic acid recognition site can be masked by
CC cis interactions with sialic acids on the same cell surface. Upon
CC ligand induced tyrosine phosphorylation in the immune response seems to
CC be involved in regulation of B-cell antigen receptor signaling. Plays a
CC role in positive regulation through interaction with Src family
CC tyrosine kinases and may also act as an inhibitory receptor by
CC recruiting cytoplasmic phosphatases via their SH2 domains that block
CC signal transduction through dephosphorylation of signaling molecules.
CC -!- SUBUNIT: Interacts with LYN, SYK, PIK3R1/PIK3R2, PLCG1, SHC1, INPP5D
CC and GRB2 upon phosphorylation. May form a complex with INPP5D/SHIP,
CC GRB2 and SHC1. Interacts with PTPN6/SHP-1 upon phosphorylation (By
CC similarity). {ECO:0000250}.
CC -!- INTERACTION:
CC P35329; Q60631: Grb2; NbExp=4; IntAct=EBI-300059, EBI-1688;
CC P35329; P29351: Ptpn6; NbExp=5; IntAct=EBI-300059, EBI-2620699;
CC -!- SUBCELLULAR LOCATION: Cell membrane; Single-pass type I membrane
CC protein.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=CD22-beta;
CC IsoId=P35329-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P35329-2; Sequence=VSP_002532;
CC Name=3;
CC IsoId=P35329-3; Sequence=VSP_002533;
CC -!- TISSUE SPECIFICITY: B-lymphocytes.
CC -!- DOMAIN: Contains 3 copies of a cytoplasmic motif that is referred to as
CC the immunoreceptor tyrosine-based inhibitor motif (ITIM). This motif is
CC involved in modulation of cellular responses. The phosphorylated ITIM
CC motif can bind the SH2 domain of several SH2-containing phosphatases.
CC -!- PTM: Phosphorylated on tyrosine residues by LYN. {ECO:0000305}.
CC -!- PTM: Phosphorylation of Tyr-783 and Tyr-843 are involved in binding to
CC SYK. Phosphorylation of Tyr-828 is involved in binding to GRB2.
CC Phosphorylation of Tyr-863 is involved in binding to SYK, PLCG2 and
CC PIK3R1/PIK3R2. {ECO:0000269|PubMed:10373493}.
CC -!- SIMILARITY: Belongs to the immunoglobulin superfamily. SIGLEC (sialic
CC acid binding Ig-like lectin) family. {ECO:0000305}.
CC -!- WEB RESOURCE: Name=Functional Glycomics Gateway - Glycan Binding;
CC Note=Siglec-2;
CC URL="http://www.functionalglycomics.org/glycomics/GBPServlet?&operationType=view&cbpId=cbp_mou_Itlect_194";
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DR EMBL; L16928; AAA02562.1; -; mRNA.
DR EMBL; AF115401; AAD30392.1; -; mRNA.
DR EMBL; AF115400; AAD30391.1; -; mRNA.
DR EMBL; AF102134; AAF02417.1; -; mRNA.
DR EMBL; AK143835; BAE25561.1; -; mRNA.
DR EMBL; AC165340; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AJ250676; CAB85609.1; -; mRNA.
DR EMBL; AJ250677; CAB85610.1; -; mRNA.
DR EMBL; AJ250678; CAB85611.1; -; mRNA.
DR EMBL; AJ250679; CAB85612.1; -; mRNA.
DR EMBL; AJ250680; CAB85613.1; -; mRNA.
DR EMBL; AJ250682; CAB85615.1; -; mRNA.
DR EMBL; AJ250683; CAB85616.1; -; mRNA.
DR CCDS; CCDS21114.1; -. [P35329-1]
DR PIR; A46512; A46512.
DR PIR; I49583; I49583.
DR RefSeq; NP_001036782.1; NM_001043317.2.
DR RefSeq; NP_033975.3; NM_009845.3.
DR RefSeq; XP_006539556.1; XM_006539493.1.
DR RefSeq; XP_006539557.1; XM_006539494.2.
DR AlphaFoldDB; P35329; -.
DR SMR; P35329; -.
DR BioGRID; 198581; 8.
DR CORUM; P35329; -.
DR IntAct; P35329; 13.
DR MINT; P35329; -.
DR STRING; 10090.ENSMUSP00000019248; -.
DR BindingDB; P35329; -.
DR ChEMBL; CHEMBL1075279; -.
DR GlyGen; P35329; 11 sites.
DR iPTMnet; P35329; -.
DR PhosphoSitePlus; P35329; -.
DR jPOST; P35329; -.
DR MaxQB; P35329; -.
DR PaxDb; P35329; -.
DR PRIDE; P35329; -.
DR ProteomicsDB; 283740; -. [P35329-1]
DR ProteomicsDB; 283741; -. [P35329-2]
DR ProteomicsDB; 283742; -. [P35329-3]
DR ProteomicsDB; 328745; -.
DR Antibodypedia; 3714; 2402 antibodies from 56 providers.
DR DNASU; 12483; -.
DR Ensembl; ENSMUST00000019248; ENSMUSP00000019248; ENSMUSG00000030577. [P35329-1]
DR Ensembl; ENSMUST00000108125; ENSMUSP00000103760; ENSMUSG00000030577. [P35329-1]
DR Ensembl; ENSMUST00000186154; ENSMUSP00000139685; ENSMUSG00000030577. [P35329-1]
DR Ensembl; ENSMUST00000189718; ENSMUSP00000140521; ENSMUSG00000030577. [P35329-1]
DR Ensembl; ENSMUST00000190617; ENSMUSP00000139871; ENSMUSG00000030577. [P35329-1]
DR GeneID; 12483; -.
DR KEGG; mmu:12483; -.
DR UCSC; uc009ggr.2; mouse.
DR CTD; 933; -.
DR MGI; MGI:88322; Cd22.
DR VEuPathDB; HostDB:ENSMUSG00000030577; -.
DR eggNOG; KOG4475; Eukaryota.
DR GeneTree; ENSGT01050000244990; -.
DR HOGENOM; CLU_017949_0_0_1; -.
DR InParanoid; P35329; -.
DR OMA; GCYICNA; -.
DR OrthoDB; 54136at2759; -.
DR PhylomeDB; P35329; -.
DR TreeFam; TF334827; -.
DR Reactome; R-MMU-198933; Immunoregulatory interactions between a Lymphoid and a non-Lymphoid cell.
DR Reactome; R-MMU-5690714; CD22 mediated BCR regulation.
DR Reactome; R-MMU-983695; Antigen activates B Cell Receptor (BCR) leading to generation of second messengers.
DR BioGRID-ORCS; 12483; 4 hits in 75 CRISPR screens.
DR PRO; PR:P35329; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; P35329; protein.
DR Bgee; ENSMUSG00000030577; Expressed in peripheral lymph node and 52 other tissues.
DR GO; GO:0009986; C:cell surface; IDA:ARUK-UCL.
DR GO; GO:0005769; C:early endosome; ISO:MGI.
DR GO; GO:0009897; C:external side of plasma membrane; IDA:MGI.
DR GO; GO:0005887; C:integral component of plasma membrane; IPI:MGI.
DR GO; GO:0032809; C:neuronal cell body membrane; IDA:ARUK-UCL.
DR GO; GO:0055037; C:recycling endosome; ISO:MGI.
DR GO; GO:0030246; F:carbohydrate binding; IEA:UniProtKB-KW.
DR GO; GO:0042609; F:CD4 receptor binding; IPI:ARUK-UCL.
DR GO; GO:0015026; F:coreceptor activity; TAS:MGI.
DR GO; GO:0019903; F:protein phosphatase binding; IPI:ARUK-UCL.
DR GO; GO:0033691; F:sialic acid binding; IPI:ARUK-UCL.
DR GO; GO:0042113; P:B cell activation; ISO:MGI.
DR GO; GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
DR GO; GO:0007166; P:cell surface receptor signaling pathway; TAS:MGI.
DR GO; GO:0050859; P:negative regulation of B cell receptor signaling pathway; ISO:MGI.
DR GO; GO:0050849; P:negative regulation of calcium-mediated signaling; IGI:ARUK-UCL.
DR GO; GO:0002638; P:negative regulation of immunoglobulin production; IGI:ARUK-UCL.
DR GO; GO:0030888; P:regulation of B cell proliferation; IGI:ARUK-UCL.
DR GO; GO:0030100; P:regulation of endocytosis; ISO:MGI.
DR GO; GO:0050776; P:regulation of immune response; IGI:ARUK-UCL.
DR Gene3D; 2.60.40.10; -; 6.
DR InterPro; IPR013162; CD80_C2-set.
DR InterPro; IPR007110; Ig-like_dom.
DR InterPro; IPR036179; Ig-like_dom_sf.
DR InterPro; IPR013783; Ig-like_fold.
DR InterPro; IPR003599; Ig_sub.
DR InterPro; IPR003598; Ig_sub2.
DR Pfam; PF08205; C2-set_2; 1.
DR Pfam; PF13895; Ig_2; 1.
DR SMART; SM00409; IG; 7.
DR SMART; SM00408; IGc2; 5.
DR SUPFAM; SSF48726; SSF48726; 7.
DR PROSITE; PS50835; IG_LIKE; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell adhesion; Cell membrane; Disulfide bond;
KW Glycoprotein; Immunoglobulin domain; Lectin; Membrane; Phosphoprotein;
KW Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT SIGNAL 1..21
FT /evidence="ECO:0000255"
FT CHAIN 22..868
FT /note="B-cell receptor CD22"
FT /id="PRO_0000014874"
FT TOPO_DOM 22..708
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 709..727
FT /note="Helical"
FT /evidence="ECO:0000255"
FT TOPO_DOM 728..868
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT DOMAIN 22..148
FT /note="Ig-like V-type"
FT DOMAIN 153..250
FT /note="Ig-like C2-type 1"
FT DOMAIN 257..347
FT /note="Ig-like C2-type 2"
FT DOMAIN 352..435
FT /note="Ig-like C2-type 3"
FT DOMAIN 440..521
FT /note="Ig-like C2-type 4"
FT DOMAIN 526..603
FT /note="Ig-like C2-type 5"
FT DOMAIN 614..697
FT /note="Ig-like C2-type 6"
FT REGION 738..772
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 790..812
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 781..786
FT /note="ITIM motif 1"
FT MOTIF 841..846
FT /note="ITIM motif 2"
FT MOTIF 861..866
FT /note="ITIM motif 3"
FT COMPBIAS 738..754
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 794..812
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 130
FT /ligand="N-acetylneuraminate"
FT /ligand_id="ChEBI:CHEBI:35418"
FT /evidence="ECO:0000250"
FT MOD_RES 746
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 747
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 783
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:10373493"
FT MOD_RES 828
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:10373493"
FT MOD_RES 843
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:10373493"
FT MOD_RES 863
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:10373493"
FT CARBOHYD 111
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 122
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 145
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 174
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 271
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 281
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 384
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 414
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 466
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 567
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT CARBOHYD 595
FT /note="N-linked (GlcNAc...) asparagine"
FT /evidence="ECO:0000255"
FT DISULFID 41..177
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 46..112
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 171..235
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 278..330
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 374..417
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 463..505
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 550..592
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT DISULFID 637..680
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00114"
FT VAR_SEQ 54..121
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:10975807"
FT /id="VSP_002532"
FT VAR_SEQ 106..139
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:10975807"
FT /id="VSP_002533"
FT VARIANT 15
FT /note="V -> A (in strain: DBA/2J and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 19
FT /note="R -> Q (in strain: DBA/2J and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 76
FT /note="T -> K (in strain: DBA/2J, BXSB and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10501843,
FT ECO:0000269|PubMed:10975807, ECO:0000269|PubMed:8100843"
FT VARIANT 83..86
FT /note="ATKT -> KAEP (in strain: DBA/2J and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 83..84
FT /note="AT -> KA (in strain: NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807"
FT VARIANT 85..90
FT /note="Missing (in strain: NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807"
FT VARIANT 88..93
FT /note="Missing (in strain: DBA/2J and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 92..93
FT /note="SE -> PG (in strain: NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807"
FT VARIANT 96..97
FT /note="LS -> PP (in strain: DBA/2J and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 100
FT /note="G -> R (in strain: DBA/2J and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 108
FT /note="R -> S (in strain: DBA/2J and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10975807,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 118..120
FT /note="PIR -> LIH (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 179
FT /note="G -> E (in strain: DBA/2J, BXSB and NZW/LacJ)"
FT /evidence="ECO:0000269|PubMed:10501843,
FT ECO:0000269|PubMed:10975807, ECO:0000269|PubMed:8100843"
FT VARIANT 185
FT /note="K -> Q (in strain: DBA/2J and BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 192
FT /note="E -> K (in strain: DBA/2J and BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 196
FT /note="I -> V (in strain: DBA/2J and BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 198
FT /note="S -> P (in strain: DBA/2J and BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 242
FT /note="K -> E (in strain: DBA/2J and BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 250
FT /note="R -> H (in strain: MRL/MpJ)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 279
FT /note="R -> Q (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 386
FT /note="T -> I (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 393
FT /note="P -> H (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 409
FT /note="P -> L (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 425
FT /note="H -> R (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 429
FT /note="D -> G (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 488
FT /note="P -> S (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 554
FT /note="E -> K (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 626
FT /note="H -> R (in strain: BXSB)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT VARIANT 793
FT /note="T -> M (in strain: DBA/2J)"
FT /evidence="ECO:0000269|PubMed:8100843"
FT VARIANT 796
FT /note="T -> A (in strain: DBA/2J; BXSB and MRL/MpJ)"
FT /evidence="ECO:0000269|PubMed:10501843,
FT ECO:0000269|PubMed:8100843"
FT VARIANT 814
FT /note="S -> T (in strain: BXSB and MRL/MpJ)"
FT /evidence="ECO:0000269|PubMed:10501843"
FT MUTAGEN 828
FT /note="Y->F: Abolishes binding to GRB2."
FT /evidence="ECO:0000269|PubMed:10373493"
SQ SEQUENCE 868 AA; 97181 MW; 763991EE28747E7F CRC64;
MRVHYLWLLL ILGHVASARY SSANDWTVDH PQTLFAWEGA CIRIPCKYKT PLPKARLDNI
LLFQNYEFDK ATKKFTGTVL YNATKTEKDP ESELYLSKQG RVTFLGNRID NCTLKIHPIR
ANDSGNLGLR MTAGTERWME PIHLNVSEKP FQPYIQMPSE IRESQSVTLT CGLNFSCFGY
DILLKWFLED SEITSITSSV TSITSSVTSS IKNVYTESKL TFQPKWTDHG KSVKCQVQHS
SKVLSERTVR LDVKYTPKLE IKVNPTEVEK NNSVTMTCRV NSSNPKLRTV AVSWFKDGRP
LEDQELEQEQ QMSKLILHSV TKDMRGKYRC QASNDIGPGE SEEVELTVHY APEPSRVHIY
PSPAEEGQSV ELICESLASP SATNYTWYHN RKPIPGDTQE KLRIPKVSPW HAGNYSCLAE
NRLGHGKIDQ EAKLDVHYAP KAVTTVIQSF TPILEGDSVT LVCRYNSSNP DVTSYRWNPQ
GSGSVLKPGV LRIQKVTWDS MPVSCAACNH KCSWALPVIL NVHYAPRDVK VLKVSPASEI
RAGQRVLLQC DFAESNPAEV RFFWKKNGSL VQEGRYLSFG SVSPEDSGNY NCMVNNSIGE
TLSQAWNLQV LYAPRRLRVS ISPGDHVMEG KKATLSCESD ANPPISQYTW FDSSGQDLHS
SGQKLRLEPL EVQHTGSYRC KGTNGIGTGE SPPSTLTVYY SPETIGKRVA LGLGFCLTIC
ILAIWGMKIQ KKWKQNRSQQ GLQENSSGQS FFVRNKKARR TPLSEGPQSQ GCYNPAMDDT
VSYAILRFPE SDTHNTGDAG TPATQAPPPN NSDSVTYSVI QKRPMGDYEN VNPSCPEDES
IHYSELVQFG AGKRPQAKED VDYVTLKH
