ID SLAP1_HUMAN Reviewed; 276 AA. AC Q13239; B7Z4J2; B7Z4L6; Q6FI01; Q9UMQ8; DT 23-APR-2003, integrated into UniProtKB/Swiss-Prot. DT 23-JAN-2007, sequence version 3. DT 24-JAN-2024, entry version 196. DE RecName: Full=Src-like-adapter; DE AltName: Full=Src-like-adapter protein 1; DE Short=SLAP-1; DE Short=hSLAP; GN Name=SLA; Synonyms=SLAP, SLAP1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1). RX PubMed=8825655; DOI=10.1006/geno.1995.1289; RA Angrist M., Wells D.E., Chakravarti A., Pandey A.; RT "Chromosomal localization of the mouse Src-like adapter protein (Slap) gene RT and its putative human homolog SLA."; RL Genomics 30:623-625(1995). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND INDUCTION BY ATRA. RC TISSUE=Histiocytic lymphoma; RX PubMed=9020066; DOI=10.1006/bbrc.1996.5887; RA Ohtsuki T., Hatake K., Ikeda M., Tomizuka H., Terui Y., Uwai M., Miura Y.; RT "Expression of Src-like adapter protein mRNA is induced by all-trans RT retinoic acid."; RL Biochem. Biophys. Res. Commun. 230:81-84(1997). RN [3] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND TISSUE SPECIFICITY. RC TISSUE=Fetal brain; RX PubMed=9660183; DOI=10.1046/j.1432-1327.1998.2540297.x; RA Meijerink P.H.S., Yanakiev P., Zorn I., Grierson A.J., Bikker H., Dye D., RA Kalaydjieva L., Baas F.; RT "The gene for the human Src-like adaptor protein (hSLAP) is located within RT the 64-kb intron of the thyroglobulin gene."; RL Eur. J. Biochem. 254:297-303(1998). RN [4] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND FUNCTION. RX PubMed=11696592; DOI=10.1084/jem.194.9.1263; RA Holland S.J., Liao X.C., Mendenhall M.K., Zhou X., Pardo J., Chu P., RA Spencer C., Fu A.C., Sheng N., Yu P., Pali E., Nagin A., Shen M., Yu S., RA Chan E., Wu X., Li C., Woisetschlager M., Aversa G., Kolbinger F., RA Bennett M.K., Molineaux S., Luo Y., Payan D.G., Mancebo H.S.Y., Wu J.; RT "Functional cloning of Src-like adapter protein-2 (SLAP-2), a novel RT inhibitor of antigen receptor signaling."; RL J. Exp. Med. 194:1263-1276(2001). RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4). RC TISSUE=Brain; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16421571; DOI=10.1038/nature04406; RA Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S., Garber M., RA Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A., Chang J.L., RA Cuomo C.A., Dewar K., FitzGerald M.G., Yang X., Allen N.R., Anderson S., RA Asakawa T., Blechschmidt K., Bloom T., Borowsky M.L., Butler J., Cook A., RA Corum B., DeArellano K., DeCaprio D., Dooley K.T., Dorris L. III, RA Engels R., Gloeckner G., Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., RA Jaffe D.B., Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P., RA Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H., RA Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C., O'Leary S.B., RA O'Neill K., Parker S.C.J., Polley A., Raymond C.K., Reichwald K., RA Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R., Smith C.L., RA Sneddon T.P., Talamas J.A., Tenzin P., Topham K., Venkataraman V., Wen G., RA Yamazaki S., Young S.K., Zeng Q., Zimmer A.R., Rosenthal A., Birren B.W., RA Platzer M., Shimizu N., Lander E.S.; RT "DNA sequence and analysis of human chromosome 8."; RL Nature 439:331-335(2006). RN [8] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [9] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). RC TISSUE=Bone marrow; 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 [10] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-72. RX PubMed=11179692; DOI=10.1016/s0378-1119(00)00516-3; RA Kratchmarova I., Sosinowski T., Weiss A., Witter K., Vincenz C., Pandey A.; RT "Characterization of promoter region and genomic structure of the murine RT and human genes encoding Src like adapter protein."; RL Gene 262:267-273(2001). RN [11] RP FUNCTION, HOMODIMERIZATION, PHOSPHORYLATION, INTERACTION WITH CBL; ZAP70; RP CD3Z; SYK AND LAT, AND MUTAGENESIS OF ARG-111; LEU-218; LEU-224; LEU-229 RP AND 237-LEU--LEU-239. RX PubMed=10449770; DOI=10.1073/pnas.96.17.9775; RA Tang J., Sawasdikosol S., Chang J.-H., Burakoff S.J.; RT "SLAP, a dimeric adapter protein, plays a functional role in T cell RT receptor signaling."; RL Proc. Natl. Acad. Sci. U.S.A. 96:9775-9780(1999). RN [12] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [13] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Leukemic T-cell; RX PubMed=19690332; DOI=10.1126/scisignal.2000007; RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., RA Rodionov V., Han D.K.; RT "Quantitative phosphoproteomic analysis of T cell receptor signaling RT reveals system-wide modulation of protein-protein interactions."; RL Sci. Signal. 2:RA46-RA46(2009). RN [14] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [15] RP STRUCTURE BY NMR OF 15-80. RG RIKEN structural genomics initiative (RSGI); RT "Solution structure of the SH3 domain of the human Src-like adapter protein RT (SLAP)."; RL Submitted (NOV-2005) to the PDB data bank. CC -!- FUNCTION: Adapter protein, which negatively regulates T-cell receptor CC (TCR) signaling. Inhibits T-cell antigen-receptor induced activation of CC nuclear factor of activated T-cells. Involved in the negative CC regulation of positive selection and mitosis of T-cells. May act by CC linking signaling proteins such as ZAP70 with CBL, leading to a CBL CC dependent degradation of signaling proteins. CC {ECO:0000269|PubMed:10449770, ECO:0000269|PubMed:11696592}. CC -!- SUBUNIT: Interacts with EPHA2, VAV1, LCP2 and PDGFRB (By similarity). CC Homodimer. Homodimerization and interaction with phosphorylated CBL CC occurs via its C-terminal domain. Interacts with phosphorylated CC proteins ZAP70, CD3Z, SYK and LAT via its SH2 domain. {ECO:0000250, CC ECO:0000269|PubMed:10449770}. CC -!- INTERACTION: CC Q13239; P00533: EGFR; NbExp=3; IntAct=EBI-726214, EBI-297353; CC Q13239; P09619: PDGFRB; NbExp=4; IntAct=EBI-726214, EBI-641237; CC Q13239-3; Q9NYB9-2: ABI2; NbExp=3; IntAct=EBI-17630587, EBI-11096309; CC Q13239-3; P51451: BLK; NbExp=3; IntAct=EBI-17630587, EBI-2105445; CC Q13239-3; A0A024R8L2: hCG_1987119; NbExp=3; IntAct=EBI-17630587, EBI-14103818; CC Q13239-3; Q13882: PTK6; NbExp=3; IntAct=EBI-17630587, EBI-1383632; CC Q13239-3; P47897: QARS1; NbExp=3; IntAct=EBI-17630587, EBI-347462; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Endosome {ECO:0000250}. CC Note=Colocalizes with endosomes. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=5; CC Name=1; CC IsoId=Q13239-1; Sequence=Displayed; CC Name=2; CC IsoId=Q13239-2; Sequence=VSP_055122; CC Name=3; CC IsoId=Q13239-3; Sequence=VSP_055123; CC Name=4; CC IsoId=Q13239-4; Sequence=VSP_055123, VSP_055125; CC Name=5; CC IsoId=Q13239-5; Sequence=VSP_055124; CC -!- TISSUE SPECIFICITY: Expressed in lung and fetal brain. Weakly expressed CC in heart, adult brain, placenta, liver, skeletal muscle, kidney and CC pancreas. {ECO:0000269|PubMed:9660183}. CC -!- INDUCTION: By all-trans retinoic acid (ATRA). Induction is indirect and CC is mediated through other proteins. {ECO:0000269|PubMed:9020066}. CC -!- DOMAIN: The C-terminal domain is essential for the homodimerization and CC the interaction with CBL. While the interaction with CBL is apparently CC mediated via the hydrophobic region of this domain, the highly charged CC region is apparently required for the homodimerization. CC -!- SEQUENCE CAUTION: CC Sequence=AAH07042.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC Sequence=BAG35478.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305}; CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; U30473; AAC50357.1; -; mRNA. DR EMBL; D89077; BAA13758.1; -; mRNA. DR EMBL; U44403; AAC27662.1; -; mRNA. DR EMBL; CR536537; CAG38774.1; -; mRNA. DR EMBL; AK297423; BAH12578.1; -; mRNA. DR EMBL; AK297519; BAH12602.1; -; mRNA. DR EMBL; AK312584; BAG35478.1; ALT_INIT; mRNA. DR EMBL; AF235100; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AF305872; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471060; EAW92159.1; -; Genomic_DNA. DR EMBL; BC007042; AAH07042.1; ALT_INIT; mRNA. DR EMBL; AJ238591; CAB53536.1; -; mRNA. DR CCDS; CCDS47922.1; -. [Q13239-3] DR CCDS; CCDS47923.1; -. [Q13239-5] DR CCDS; CCDS6370.1; -. [Q13239-1] DR CCDS; CCDS64977.1; -. [Q13239-2] DR CCDS; CCDS64978.1; -. [Q13239-4] DR RefSeq; NP_001039021.1; NM_001045556.2. [Q13239-1] DR RefSeq; NP_001039022.2; NM_001045557.2. [Q13239-3] DR RefSeq; NP_001269893.1; NM_001282964.1. [Q13239-4] DR RefSeq; NP_001269894.1; NM_001282965.1. [Q13239-2] DR RefSeq; NP_006739.2; NM_006748.3. [Q13239-5] DR RefSeq; XP_016869228.1; XM_017013739.1. DR PDB; 2CUD; NMR; -; A=15-80. DR PDBsum; 2CUD; -. DR AlphaFoldDB; Q13239; -. DR BMRB; Q13239; -. DR SMR; Q13239; -. DR BioGRID; 112394; 26. DR IntAct; Q13239; 38. DR MINT; Q13239; -. DR STRING; 9606.ENSP00000394049; -. DR iPTMnet; Q13239; -. DR PhosphoSitePlus; Q13239; -. DR BioMuta; SLA; -. DR DMDM; 30173237; -. DR MassIVE; Q13239; -. DR MaxQB; Q13239; -. DR PaxDb; 9606-ENSP00000394049; -. DR PeptideAtlas; Q13239; -. DR ProteomicsDB; 59242; -. [Q13239-1] DR ProteomicsDB; 6601; -. DR ProteomicsDB; 6612; -. DR Antibodypedia; 1995; 152 antibodies from 28 providers. DR DNASU; 6503; -. DR Ensembl; ENST00000338087.10; ENSP00000337548.5; ENSG00000155926.14. [Q13239-1] DR Ensembl; ENST00000395352.7; ENSP00000378759.3; ENSG00000155926.14. [Q13239-3] DR Ensembl; ENST00000427060.6; ENSP00000394049.2; ENSG00000155926.14. [Q13239-5] DR Ensembl; ENST00000517648.5; ENSP00000428559.1; ENSG00000155926.14. [Q13239-4] DR Ensembl; ENST00000524345.5; ENSP00000427928.1; ENSG00000155926.14. [Q13239-2] DR GeneID; 6503; -. DR KEGG; hsa:6503; -. DR MANE-Select; ENST00000338087.10; ENSP00000337548.5; NM_001045556.3; NP_001039021.1. DR UCSC; uc003ytz.4; human. [Q13239-1] DR AGR; HGNC:10902; -. DR CTD; 6503; -. DR DisGeNET; 6503; -. DR GeneCards; SLA; -. DR HGNC; HGNC:10902; SLA. DR HPA; ENSG00000155926; Group enriched (bone marrow, lymphoid tissue). DR MIM; 601099; gene. DR neXtProt; NX_Q13239; -. DR OpenTargets; ENSG00000155926; -. DR PharmGKB; PA35802; -. DR VEuPathDB; HostDB:ENSG00000155926; -. DR eggNOG; ENOG502QPWY; Eukaryota. DR GeneTree; ENSGT00940000159104; -. DR HOGENOM; CLU_084503_1_0_1; -. DR InParanoid; Q13239; -. DR OrthoDB; 5346049at2759; -. DR PhylomeDB; Q13239; -. DR PathwayCommons; Q13239; -. DR Reactome; R-HSA-9706369; Negative regulation of FLT3. DR SignaLink; Q13239; -. DR SIGNOR; Q13239; -. DR BioGRID-ORCS; 6503; 22 hits in 1155 CRISPR screens. DR ChiTaRS; SLA; human. DR EvolutionaryTrace; Q13239; -. DR GenomeRNAi; 6503; -. DR Pharos; Q13239; Tbio. DR PRO; PR:Q13239; -. DR Proteomes; UP000005640; Chromosome 8. DR RNAct; Q13239; Protein. DR Bgee; ENSG00000155926; Expressed in cortical plate and 179 other cell types or tissues. DR ExpressionAtlas; Q13239; baseline and differential. DR GO; GO:0008180; C:COP9 signalosome; IBA:GO_Central. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell. DR GO; GO:0005654; C:nucleoplasm; IBA:GO_Central. DR GO; GO:0005886; C:plasma membrane; IBA:GO_Central. DR GO; GO:0005154; F:epidermal growth factor receptor binding; IBA:GO_Central. DR GO; GO:0001784; F:phosphotyrosine residue binding; IBA:GO_Central. DR GO; GO:0043408; P:regulation of MAPK cascade; IBA:GO_Central. DR GO; GO:0007165; P:signal transduction; IBA:GO_Central. DR CDD; cd10344; SH2_SLAP; 1. DR CDD; cd12010; SH3_SLAP; 1. DR Gene3D; 3.30.505.10; SH2 domain; 1. DR Gene3D; 2.30.30.40; SH3 Domains; 1. DR InterPro; IPR043539; Grb2-like. DR InterPro; IPR000980; SH2. DR InterPro; IPR036860; SH2_dom_sf. DR InterPro; IPR036028; SH3-like_dom_sf. DR InterPro; IPR001452; SH3_domain. DR InterPro; IPR035052; SLAP_SH2. DR InterPro; IPR035596; SLAP_SH3. DR PANTHER; PTHR46037; PROTEIN ENHANCER OF SEVENLESS 2B; 1. DR PANTHER; PTHR46037:SF5; SRC-LIKE-ADAPTER; 1. DR Pfam; PF00017; SH2; 1. DR Pfam; PF00018; SH3_1; 1. DR PRINTS; PR00401; SH2DOMAIN. DR SMART; SM00252; SH2; 1. DR SMART; SM00326; SH3; 1. DR SUPFAM; SSF55550; SH2 domain; 1. DR SUPFAM; SSF50044; SH3-domain; 1. DR PROSITE; PS50001; SH2; 1. DR PROSITE; PS50002; SH3; 1. DR Genevisible; Q13239; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Cytoplasm; Endosome; Lipoprotein; KW Myristate; Phosphoprotein; Reference proteome; SH2 domain; SH3 domain. FT INIT_MET 1 FT /note="Removed" FT /evidence="ECO:0000250|UniProtKB:Q60898" FT CHAIN 2..276 FT /note="Src-like-adapter" FT /id="PRO_0000071946" FT DOMAIN 22..82 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 84..175 FT /note="SH2" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191" FT REGION 212..276 FT /note="SLA C-terminal" FT MOD_RES 253 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:P59622" FT MOD_RES 273 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q60898" FT LIPID 2 FT /note="N-myristoyl glycine" FT /evidence="ECO:0000250" FT VAR_SEQ 1..108 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055122" FT VAR_SEQ 1 FT /note="M -> MLHRLWASPAAPGKKKEM (in isoform 3 and isoform FT 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055123" FT VAR_SEQ 1 FT /note="M -> MLSKLGHSPLGGLRARLTFPVCLLYHRLWASPAAPGKKKEM (in FT isoform 5)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_055124" FT VAR_SEQ 118..161 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_055125" FT VARIANT 15 FT /note="P -> T (in dbSNP:rs4486183)" FT /id="VAR_061706" FT MUTAGEN 111 FT /note="R->K: Strongly reduces interaction with ZAP70, CD3Z, FT SYK and LAT." FT /evidence="ECO:0000269|PubMed:10449770" FT MUTAGEN 218 FT /note="L->S: Abolishes interaction with CBL. Does not FT affect dimerization; when associated with S-224 and S-229." FT /evidence="ECO:0000269|PubMed:10449770" FT MUTAGEN 224 FT /note="L->S: Abolishes interaction with CBL. Does not FT affect dimerization; when associated with S-218 and S-229." FT /evidence="ECO:0000269|PubMed:10449770" FT MUTAGEN 229 FT /note="L->S: Abolishes interaction with CBL. Does not FT affect dimerization; when associated with S-218 and S-224." FT /evidence="ECO:0000269|PubMed:10449770" FT MUTAGEN 237..239 FT /note="LSL->QSQ: Abolishes interaction with CBL. Slightly FT affects dimerization." FT /evidence="ECO:0000269|PubMed:10449770" FT CONFLICT 71 FT /note="Y -> D (in Ref. 10; CAB53536)" FT /evidence="ECO:0000305" FT STRAND 20..22 FT /evidence="ECO:0007829|PDB:2CUD" FT STRAND 26..31 FT /evidence="ECO:0007829|PDB:2CUD" FT TURN 36..38 FT /evidence="ECO:0007829|PDB:2CUD" FT STRAND 48..55 FT /evidence="ECO:0007829|PDB:2CUD" FT STRAND 58..63 FT /evidence="ECO:0007829|PDB:2CUD" FT TURN 64..66 FT /evidence="ECO:0007829|PDB:2CUD" FT STRAND 69..73 FT /evidence="ECO:0007829|PDB:2CUD" FT HELIX 74..76 FT /evidence="ECO:0007829|PDB:2CUD" FT STRAND 77..80 FT /evidence="ECO:0007829|PDB:2CUD" SQ SEQUENCE 276 AA; 31156 MW; B0FCC7D7B2ECA378 CRC64; MGNSMKSTPA PAERPLPNPE GLDSDFLAVL SDYPSPDISP PIFRRGEKLR VISDEGGWWK AISLSTGRES YIPGICVARV YHGWLFEGLG RDKAEELLQL PDTKVGSFMI RESETKKGFY SLSVRHRQVK HYRIFRLPNN WYYISPRLTF QCLEDLVNHY SEVADGLCCV LTTPCLTQST AAPAVRASSS PVTLRQKTVD WRRVSRLQED PEGTENPLGV DESLFSYGLR ESIASYLSLT SEDNTSFDRK KKSISLMYGG SKRKSSFFSS PPYFED //