LIME1_HUMAN
ID LIME1_HUMAN Reviewed; 295 AA.
AC Q9H400; E1P5K5; E1P5K6; Q5JWJ2; Q6XYB3; Q9NX69;
DT 20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 154.
DE RecName: Full=Lck-interacting transmembrane adapter 1;
DE Short=Lck-interacting membrane protein;
DE AltName: Full=Lck-interacting molecule;
GN Name=LIME1; Synonyms=LIME; ORFNames=LP8067;
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), TISSUE SPECIFICITY, SUBCELLULAR
RP LOCATION, INTERACTION WITH LCK AND CSK, PHOSPHORYLATION AT TYR-167; TYR-200
RP AND TYR-254, PALMITOYLATION AT CYS-28 AND CYS-31, MUTAGENESIS OF TYR-145;
RP TYR-167; TYR-200; TYR-235 AND TYR-254, AND FUNCTION.
RX PubMed=14610046; DOI=10.1084/jem.20031484;
RA Brdickova N., Brdicka T., Angelisova P., Horvath O., Spicka J., Hilgert I.,
RA Paces J., Simeoni L., Kliche S., Merten C., Schraven B., Horejsi V.;
RT "LIME: a new membrane raft-associated adaptor protein involved in CD4 and
RT CD8 coreceptor signaling.";
RL J. Exp. Med. 198:1453-1462(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH LCK,
RP PHOSPHORYLATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
RX PubMed=14610044; DOI=10.1084/jem.20030232;
RA Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.;
RT "LIME, a novel transmembrane adaptor protein, associates with p56lck and
RT mediates T cell activation.";
RL J. Exp. Med. 198:1463-1473(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Colon;
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 [8]
RP TISSUE SPECIFICITY.
RX PubMed=16160011; DOI=10.1182/blood-2005-06-2273;
RA Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T.,
RA Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L., Pozzobon M.,
RA Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T., Horejsi V.;
RT "Transmembrane adaptor molecules: a new category of lymphoid-cell
RT markers.";
RL Blood 107:213-221(2006).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
RP 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).
CC -!- FUNCTION: Involved in BCR (B-cell antigen receptor)-mediated signaling
CC in B-cells and TCR (T-cell antigen receptor)-mediated T-cell signaling
CC in T-cells. In absence of TCR signaling, may be involved in CD4-
CC mediated inhibition of T-cell activation. Couples activation of these
CC receptors and their associated kinases with distal intracellular events
CC such as calcium mobilization or MAPK activation through the recruitment
CC of PLCG2, GRB2, GRAP2, and other signaling molecules.
CC {ECO:0000269|PubMed:14610046}.
CC -!- SUBUNIT: When phosphorylated in response to BCR activation, interacts
CC with LYN, PIK3R1, PLCG2, and GRB2 (By similarity). When phosphorylated
CC in response to TCR stimulation and/or CD4 co-stimulation, interacts
CC with LCK, CSK, FYN, PTPN11/SHP2, GRB2, PIK3R1 and GRAP2. {ECO:0000250,
CC ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:14610046}.
CC -!- INTERACTION:
CC Q9H400; Q8TD06: AGR3; NbExp=3; IntAct=EBI-2830566, EBI-3925742;
CC Q9H400; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-2830566, EBI-11957045;
CC Q9H400; P29972: AQP1; NbExp=3; IntAct=EBI-2830566, EBI-745213;
CC Q9H400; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-2830566, EBI-2875816;
CC Q9H400; Q12982: BNIP2; NbExp=3; IntAct=EBI-2830566, EBI-752094;
CC Q9H400; Q9BXU9: CALN1; NbExp=3; IntAct=EBI-2830566, EBI-12187137;
CC Q9H400; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-2830566, EBI-752069;
CC Q9H400; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-2830566, EBI-6165897;
CC Q9H400; P50402: EMD; NbExp=3; IntAct=EBI-2830566, EBI-489887;
CC Q9H400; Q9BZ67: FRMD8; NbExp=3; IntAct=EBI-2830566, EBI-5773072;
CC Q9H400; Q05329: GAD2; NbExp=3; IntAct=EBI-2830566, EBI-9304251;
CC Q9H400; O14653: GOSR2; NbExp=3; IntAct=EBI-2830566, EBI-4401517;
CC Q9H400; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-2830566, EBI-2820517;
CC Q9H400; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-2830566, EBI-12033434;
CC Q9H400; Q9Y2E5: MAN2B2; NbExp=3; IntAct=EBI-2830566, EBI-12243024;
CC Q9H400; Q5EB52: MEST; NbExp=3; IntAct=EBI-2830566, EBI-1050204;
CC Q9H400; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-2830566, EBI-11988931;
CC Q9H400; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-2830566, EBI-11978907;
CC Q9H400; Q92982: NINJ1; NbExp=3; IntAct=EBI-2830566, EBI-2802124;
CC Q9H400; Q8N912: NRAC; NbExp=3; IntAct=EBI-2830566, EBI-12051377;
CC Q9H400; Q96AL5: PBX3; NbExp=3; IntAct=EBI-2830566, EBI-741171;
CC Q9H400; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-2830566, EBI-12257782;
CC Q9H400; Q9NVS9: PNPO; NbExp=3; IntAct=EBI-2830566, EBI-11030787;
CC Q9H400; P43378: PTPN9; NbExp=3; IntAct=EBI-2830566, EBI-742898;
CC Q9H400; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-2830566, EBI-10244780;
CC Q9H400; Q9BRL7: SEC22C; NbExp=3; IntAct=EBI-2830566, EBI-10297029;
CC Q9H400; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-2830566, EBI-10290130;
CC Q9H400; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-2830566, EBI-10244848;
CC Q9H400; Q13596: SNX1; NbExp=3; IntAct=EBI-2830566, EBI-2822329;
CC Q9H400; O43752: STX6; NbExp=3; IntAct=EBI-2830566, EBI-2695795;
CC Q9H400; O15400: STX7; NbExp=3; IntAct=EBI-2830566, EBI-3221827;
CC Q9H400; Q969Z0: TBRG4; NbExp=3; IntAct=EBI-2830566, EBI-702328;
CC Q9H400; P55061: TMBIM6; NbExp=3; IntAct=EBI-2830566, EBI-1045825;
CC Q9H400; Q96AN5: TMEM143; NbExp=3; IntAct=EBI-2830566, EBI-13342951;
CC Q9H400; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-2830566, EBI-12887458;
CC Q9H400; Q96NL1: TMEM74; NbExp=3; IntAct=EBI-2830566, EBI-10292091;
CC Q9H400; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2830566, EBI-2548832;
CC Q9H400; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-2830566, EBI-12111910;
CC Q9H400; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-2830566, EBI-765817;
CC Q9H400; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-2830566, EBI-4401271;
CC Q9H400; O00526: UPK2; NbExp=3; IntAct=EBI-2830566, EBI-10179682;
CC Q9H400; O95159: ZFPL1; NbExp=3; IntAct=EBI-2830566, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610044,
CC ECO:0000269|PubMed:14610046}; Single-pass type III membrane protein
CC {ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:14610046}.
CC Note=Present in lipid rafts. Recruited to the immunological synapse
CC upon conjugation of T-cell with antigen-presenting cell.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H400-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H400-2; Sequence=VSP_016642;
CC -!- TISSUE SPECIFICITY: Expressed in peripheral blood lymphocytes, lymphoid
CC tissues, and liver. Present in T-cells and plasma cells, and in various
CC hematopoietic cell lines (at protein level).
CC {ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:14610046,
CC ECO:0000269|PubMed:16160011}.
CC -!- PTM: Palmitoylation of Cys-28 and Cys-31 is required for raft
CC targeting. {ECO:0000269|PubMed:14610046}.
CC -!- PTM: Phosphorylated on tyrosines upon TCR activation and/or CD4
CC coreceptor stimulation, or upon BCR stimulation; which leads to the
CC recruitment of SH2-containing proteins. {ECO:0000269|PubMed:14610044,
CC ECO:0000269|PubMed:14610046}.
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DR EMBL; AY203957; AAP34480.1; -; mRNA.
DR EMBL; AK000413; BAA91148.1; -; mRNA.
DR EMBL; AL121845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471077; EAW75213.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75214.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75215.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75216.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75217.1; -; Genomic_DNA.
DR EMBL; CH471077; EAW75218.1; -; Genomic_DNA.
DR EMBL; BC017016; AAH17016.1; -; mRNA.
DR CCDS; CCDS13536.1; -. [Q9H400-1]
DR RefSeq; NP_001292583.1; NM_001305654.1.
DR RefSeq; NP_001292584.1; NM_001305655.1.
DR RefSeq; NP_060276.2; NM_017806.3. [Q9H400-1]
DR AlphaFoldDB; Q9H400; -.
DR BioGRID; 120264; 59.
DR IntAct; Q9H400; 46.
DR STRING; 9606.ENSP00000309521; -.
DR iPTMnet; Q9H400; -.
DR PhosphoSitePlus; Q9H400; -.
DR SwissPalm; Q9H400; -.
DR BioMuta; LIME1; -.
DR DMDM; 74752630; -.
DR EPD; Q9H400; -.
DR jPOST; Q9H400; -.
DR MassIVE; Q9H400; -.
DR MaxQB; Q9H400; -.
DR PaxDb; Q9H400; -.
DR PeptideAtlas; Q9H400; -.
DR PRIDE; Q9H400; -.
DR ProteomicsDB; 80775; -. [Q9H400-1]
DR ProteomicsDB; 80776; -. [Q9H400-2]
DR Antibodypedia; 4202; 358 antibodies from 29 providers.
DR CPTC; Q9H400; 1 antibody.
DR DNASU; 54923; -.
DR Ensembl; ENST00000309546.8; ENSP00000309521.3; ENSG00000203896.10. [Q9H400-1]
DR GeneID; 54923; -.
DR KEGG; hsa:54923; -.
DR MANE-Select; ENST00000309546.8; ENSP00000309521.3; NM_017806.4; NP_060276.2.
DR UCSC; uc002ygp.5; human. [Q9H400-1]
DR CTD; 54923; -.
DR DisGeNET; 54923; -.
DR GeneCards; LIME1; -.
DR HGNC; HGNC:26016; LIME1.
DR HPA; ENSG00000203896; Tissue enriched (liver).
DR MIM; 609809; gene.
DR neXtProt; NX_Q9H400; -.
DR OpenTargets; ENSG00000203896; -.
DR PharmGKB; PA142671551; -.
DR VEuPathDB; HostDB:ENSG00000203896; -.
DR eggNOG; ENOG502RGRF; Eukaryota.
DR GeneTree; ENSGT00510000050080; -.
DR InParanoid; Q9H400; -.
DR OMA; HQELPWA; -.
DR OrthoDB; 931070at2759; -.
DR PhylomeDB; Q9H400; -.
DR TreeFam; TF337416; -.
DR PathwayCommons; Q9H400; -.
DR SignaLink; Q9H400; -.
DR BioGRID-ORCS; 54923; 8 hits in 1013 CRISPR screens.
DR GeneWiki; LIME1; -.
DR GenomeRNAi; 54923; -.
DR Pharos; Q9H400; Tbio.
DR PRO; PR:Q9H400; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9H400; protein.
DR Bgee; ENSG00000203896; Expressed in granulocyte and 93 other tissues.
DR ExpressionAtlas; Q9H400; baseline and differential.
DR Genevisible; Q9H400; HS.
DR GO; GO:0019815; C:B cell receptor complex; IBA:GO_Central.
DR GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
DR GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
DR GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
DR GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0043405; P:regulation of MAP kinase activity; IBA:GO_Central.
DR GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IBA:GO_Central.
DR GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
DR GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0050852; P:T cell receptor signaling pathway; IEA:InterPro.
DR InterPro; IPR026072; Lime1.
DR PANTHER; PTHR47740; PTHR47740; 1.
DR Pfam; PF15332; LIME1; 1.
PE 1: Evidence at protein level;
KW Adaptive immunity; Alternative splicing; Cell membrane; Immunity;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Signal-anchor; Transmembrane; Transmembrane helix.
FT CHAIN 1..295
FT /note="Lck-interacting transmembrane adapter 1"
FT /id="PRO_0000083332"
FT TOPO_DOM 1..6
FT /note="Extracellular"
FT /evidence="ECO:0000255"
FT TRANSMEM 7..27
FT /note="Helical; Signal-anchor for type III membrane
FT protein"
FT /evidence="ECO:0000255"
FT TOPO_DOM 28..295
FT /note="Cytoplasmic"
FT /evidence="ECO:0000255"
FT REGION 145..148
FT /note="Interaction with GRB2"
FT /evidence="ECO:0000250"
FT REGION 167..170
FT /note="Interaction with CSK"
FT /evidence="ECO:0000269|PubMed:14610046"
FT REGION 170..192
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 200..203
FT /note="Interaction with CSK"
FT /evidence="ECO:0000269|PubMed:14610046"
FT REGION 204..223
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 235..238
FT /note="Interaction with LCK and PIK3R1"
FT /evidence="ECO:0000250"
FT REGION 254..257
FT /note="Interaction with LCK, PLCG2 and PIK3R1"
FT /evidence="ECO:0000250"
FT REGION 261..295
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 145
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQR5"
FT MOD_RES 167
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000305|PubMed:14610046"
FT MOD_RES 200
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:14610046"
FT MOD_RES 235
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9EQR5"
FT MOD_RES 254
FT /note="Phosphotyrosine; by LCK"
FT /evidence="ECO:0000305|PubMed:14610046"
FT MOD_RES 256
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT LIPID 28
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:14610046"
FT LIPID 31
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:14610046"
FT VAR_SEQ 1..95
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15498874"
FT /id="VSP_016642"
FT VARIANT 211
FT /note="P -> L (in dbSNP:rs1151625)"
FT /id="VAR_053918"
FT MUTAGEN 145
FT /note="Y->F: No change in binding to LCK, CSK or FYN."
FT /evidence="ECO:0000269|PubMed:14610046"
FT MUTAGEN 167
FT /note="Y->F: Abolishes binding to CSK."
FT /evidence="ECO:0000269|PubMed:14610046"
FT MUTAGEN 200
FT /note="Y->F: Reduces binding to CSK."
FT /evidence="ECO:0000269|PubMed:14610046"
FT MUTAGEN 235
FT /note="Y->F: No change in binding to LCK, CSK or FYN."
FT /evidence="ECO:0000269|PubMed:14610046"
FT MUTAGEN 254
FT /note="Y->F: Abolishes binding to LCK and reduces binding
FT to FYN."
FT /evidence="ECO:0000269|PubMed:14610046"
FT CONFLICT 246
FT /note="D -> G (in Ref. 4; BAA91148)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 295 AA; 31288 MW; D85ACE978F2DC99E CRC64;
MGLPVSWAPP ALWVLGCCAL LLSLWALCTA CRRPEDAVAP RKRARRQRAR LQGSATAAEA
SLLRRTHLCS LSKSDTRLHE LHRGPRSSRA LRPASMDLLR PHWLEVSRDI TGPQAAPSAF
PHQELPRALP AAAATAGCAG LEATYSNVGL AALPGVSLAA SPVVAEYARV QKRKGTHRSP
QEPQQGKTEV TPAAQVDVLY SRVCKPKRRD PGPTTDPLDP KGQGAILALA GDLAYQTLPL
RALDVDSGPL ENVYESIREL GDPAGRSSTC GAGTPPASSC PSLGRGWRPL PASLP
