SLAP1_HUMAN
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 03-AUG-2022, entry version 188.
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};
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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. [Q13239-2]
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; Q13239; -.
DR PeptideAtlas; Q13239; -.
DR PRIDE; Q13239; -.
DR ProteomicsDB; 59242; -. [Q13239-1]
DR ProteomicsDB; 6601; -.
DR ProteomicsDB; 6612; -.
DR Antibodypedia; 1995; 133 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 CTD; 6503; -.
DR DisGeNET; 6503; -.
DR GeneCards; SLA; -.
DR HGNC; HGNC:10902; SLA.
DR HPA; ENSG00000155926; Group enriched (bone marrow, lymphoid tissue).
DR MalaCards; SLA; -.
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; 1051480at2759; -.
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; 17 hits in 1075 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 177 other tissues.
DR ExpressionAtlas; Q13239; baseline and differential.
DR Genevisible; Q13239; HS.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0043197; C:dendritic spine; IBA:GO_Central.
DR GO; GO:0005768; C:endosome; IEA:UniProtKB-SubCell.
DR GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
DR GO; GO:0005925; C:focal adhesion; IBA:GO_Central.
DR GO; GO:0005102; F:signaling receptor binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
DR GO; GO:0045087; P:innate immune response; IBA:GO_Central.
DR GO; GO:0009966; P:regulation of signal transduction; IEA:InterPro.
DR GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
DR CDD; cd10344; SH2_SLAP; 1.
DR CDD; cd12010; SH3_SLAP; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR InterPro; IPR035055; SLAP.
DR InterPro; IPR035052; SLAP_SH2.
DR InterPro; IPR035596; SLAP_SH3.
DR PANTHER; PTHR24418:SF293; PTHR24418:SF293; 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; SSF50044; SSF50044; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
DR PROSITE; PS50002; SH3; 1.
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
