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Lck-interacting transmembrane adapter 1 (Lck-interacting membrane protein) (Lck-interacting molecule)

 LIME1_HUMAN             Reviewed;         295 AA.
Q9H400; E1P5K5; E1P5K6; Q5JWJ2; Q6XYB3; Q9NX69;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-MAR-2001, sequence version 1.
17-JUN-2020, entry version 144.
RecName: Full=Lck-interacting transmembrane adapter 1;
Short=Lck-interacting membrane protein;
AltName: Full=Lck-interacting molecule;
Name=LIME1; Synonyms=LIME; ORFNames=LP8067;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), TISSUE SPECIFICITY, SUBCELLULAR
LOCATION, INTERACTION WITH LCK AND CSK, PHOSPHORYLATION AT TYR-167; TYR-200
AND TYR-254, PALMITOYLATION AT CYS-28 AND CYS-31, MUTAGENESIS OF TYR-145;
TYR-167; TYR-200; TYR-235 AND TYR-254, AND FUNCTION.
PubMed=14610046; DOI=10.1084/jem.20031484;
Brdickova N., Brdicka T., Angelisova P., Horvath O., Spicka J., Hilgert I.,
Paces J., Simeoni L., Kliche S., Merten C., Schraven B., Horejsi V.;
"LIME: a new membrane raft-associated adaptor protein involved in CD4 and
CD8 coreceptor signaling.";
J. Exp. Med. 198:1453-1462(2003).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH LCK,
PHOSPHORYLATION, TISSUE SPECIFICITY, AND SUBCELLULAR LOCATION.
PubMed=14610044; DOI=10.1084/jem.20030232;
Hur E.M., Son M., Lee O.-H., Choi Y.B., Park C., Lee H., Yun Y.;
"LIME, a novel transmembrane adaptor protein, associates with p56lck and
mediates T cell activation.";
J. Exp. Med. 198:1463-1473(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
PubMed=15498874; DOI=10.1073/pnas.0404089101;
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
"Large-scale cDNA transfection screening for genes related to cancer
development and progression.";
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=11780052; DOI=10.1038/414865a;
Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
"The DNA sequence and comparative analysis of human chromosome 20.";
Nature 414:865-871(2001).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project:
the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[8]
TISSUE SPECIFICITY.
PubMed=16160011; DOI=10.1182/blood-2005-06-2273;
Tedoldi S., Paterson J.C., Hansmann M.-L., Natkunam Y., Rudiger T.,
Angelisova P., Du M.Q., Roberton H., Roncador G., Sanchez L., Pozzobon M.,
Masir N., Barry R., Pileri S., Mason D.Y., Marafioti T., Horejsi V.;
"Transmembrane adaptor molecules: a new category of lymphoid-cell
markers.";
Blood 107:213-221(2006).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-256, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- FUNCTION: Involved in BCR (B-cell antigen receptor)-mediated signaling
in B-cells and TCR (T-cell antigen receptor)-mediated T-cell signaling
in T-cells. In absence of TCR signaling, may be involved in CD4-
mediated inhibition of T-cell activation. Couples activation of these
receptors and their associated kinases with distal intracellular events
such as calcium mobilization or MAPK activation through the recruitment
of PLCG2, GRB2, GRAP2, and other signaling molecules.
{ECO:0000269|PubMed:14610046}.
-!- SUBUNIT: When phosphorylated in response to BCR activation, interacts
with LYN, PIK3R1, PLCG2, and GRB2 (By similarity). When phosphorylated
in response to TCR stimulation and/or CD4 co-stimulation, interacts
with LCK, CSK, FYN, PTPN11/SHP2, GRB2, PIK3R1 and GRAP2. {ECO:0000250,
ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:14610046}.
-!- INTERACTION:
Q9H400; Q8TD06: AGR3; NbExp=3; IntAct=EBI-2830566, EBI-3925742;
Q9H400; Q9NVV5-2: AIG1; NbExp=3; IntAct=EBI-2830566, EBI-11957045;
Q9H400; P29972: AQP1; NbExp=3; IntAct=EBI-2830566, EBI-745213;
Q9H400; Q9NP61: ARFGAP3; NbExp=3; IntAct=EBI-2830566, EBI-2875816;
Q9H400; Q12982: BNIP2; NbExp=3; IntAct=EBI-2830566, EBI-752094;
Q9H400; Q9BXU9: CALN1; NbExp=3; IntAct=EBI-2830566, EBI-12187137;
Q9H400; Q9H5X1: CIAO2A; NbExp=3; IntAct=EBI-2830566, EBI-752069;
Q9H400; Q9NWW5: CLN6; NbExp=3; IntAct=EBI-2830566, EBI-6165897;
Q9H400; P50402: EMD; NbExp=3; IntAct=EBI-2830566, EBI-489887;
Q9H400; Q9BZ67: FRMD8; NbExp=3; IntAct=EBI-2830566, EBI-5773072;
Q9H400; Q05329: GAD2; NbExp=3; IntAct=EBI-2830566, EBI-9304251;
Q9H400; O14653: GOSR2; NbExp=3; IntAct=EBI-2830566, EBI-4401517;
Q9H400; Q8TAF8: LHFPL5; NbExp=3; IntAct=EBI-2830566, EBI-2820517;
Q9H400; Q9UBY5: LPAR3; NbExp=3; IntAct=EBI-2830566, EBI-12033434;
Q9H400; Q9Y2E5: MAN2B2; NbExp=3; IntAct=EBI-2830566, EBI-12243024;
Q9H400; Q5EB52: MEST; NbExp=3; IntAct=EBI-2830566, EBI-1050204;
Q9H400; Q96C03-3: MIEF2; NbExp=3; IntAct=EBI-2830566, EBI-11988931;
Q9H400; Q9ULP0-2: NDRG4; NbExp=3; IntAct=EBI-2830566, EBI-11978907;
Q9H400; Q92982: NINJ1; NbExp=3; IntAct=EBI-2830566, EBI-2802124;
Q9H400; Q8N912: NRAC; NbExp=3; IntAct=EBI-2830566, EBI-12051377;
Q9H400; Q96AL5: PBX3; NbExp=3; IntAct=EBI-2830566, EBI-741171;
Q9H400; Q99640-2: PKMYT1; NbExp=3; IntAct=EBI-2830566, EBI-12257782;
Q9H400; Q9NVS9: PNPO; NbExp=3; IntAct=EBI-2830566, EBI-11030787;
Q9H400; P43378: PTPN9; NbExp=3; IntAct=EBI-2830566, EBI-742898;
Q9H400; Q5QGT7: RTP2; NbExp=3; IntAct=EBI-2830566, EBI-10244780;
Q9H400; Q9BRL7: SEC22C; NbExp=3; IntAct=EBI-2830566, EBI-10297029;
Q9H400; Q96JW4: SLC41A2; NbExp=3; IntAct=EBI-2830566, EBI-10290130;
Q9H400; Q5SQN1: SNAP47; NbExp=3; IntAct=EBI-2830566, EBI-10244848;
Q9H400; Q13596: SNX1; NbExp=3; IntAct=EBI-2830566, EBI-2822329;
Q9H400; O43752: STX6; NbExp=3; IntAct=EBI-2830566, EBI-2695795;
Q9H400; O15400: STX7; NbExp=3; IntAct=EBI-2830566, EBI-3221827;
Q9H400; Q969Z0: TBRG4; NbExp=3; IntAct=EBI-2830566, EBI-702328;
Q9H400; P55061: TMBIM6; NbExp=3; IntAct=EBI-2830566, EBI-1045825;
Q9H400; Q96AN5: TMEM143; NbExp=3; IntAct=EBI-2830566, EBI-13342951;
Q9H400; Q9BU79: TMEM243; NbExp=3; IntAct=EBI-2830566, EBI-12887458;
Q9H400; Q96NL1: TMEM74; NbExp=3; IntAct=EBI-2830566, EBI-10292091;
Q9H400; Q8N661: TMEM86B; NbExp=3; IntAct=EBI-2830566, EBI-2548832;
Q9H400; Q5BJF2: TMEM97; NbExp=3; IntAct=EBI-2830566, EBI-12111910;
Q9H400; Q9Y228: TRAF3IP3; NbExp=3; IntAct=EBI-2830566, EBI-765817;
Q9H400; Q9H1C4: UNC93B1; NbExp=3; IntAct=EBI-2830566, EBI-4401271;
Q9H400; O00526: UPK2; NbExp=3; IntAct=EBI-2830566, EBI-10179682;
Q9H400; O95159: ZFPL1; NbExp=3; IntAct=EBI-2830566, EBI-718439;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:14610044,
ECO:0000269|PubMed:14610046}; Single-pass type III membrane protein
{ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:14610046}.
Note=Present in lipid rafts. Recruited to the immunological synapse
upon conjugation of T-cell with antigen-presenting cell.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=Q9H400-1; Sequence=Displayed;
Name=2;
IsoId=Q9H400-2; Sequence=VSP_016642;
-!- TISSUE SPECIFICITY: Expressed in peripheral blood lymphocytes, lymphoid
tissues, and liver. Present in T-cells and plasma cells, and in various
hematopoietic cell lines (at protein level).
{ECO:0000269|PubMed:14610044, ECO:0000269|PubMed:14610046,
ECO:0000269|PubMed:16160011}.
-!- PTM: Palmitoylation of Cys-28 and Cys-31 is required for raft
targeting. {ECO:0000269|PubMed:14610046}.
-!- PTM: Phosphorylated on tyrosines upon TCR activation and/or CD4
coreceptor stimulation, or upon BCR stimulation; which leads to the
recruitment of SH2-containing proteins. {ECO:0000269|PubMed:14610044,
ECO:0000269|PubMed:14610046}.
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EMBL; AY203957; AAP34480.1; -; mRNA.
EMBL; AK000413; BAA91148.1; -; mRNA.
EMBL; AL121845; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471077; EAW75213.1; -; Genomic_DNA.
EMBL; CH471077; EAW75214.1; -; Genomic_DNA.
EMBL; CH471077; EAW75215.1; -; Genomic_DNA.
EMBL; CH471077; EAW75216.1; -; Genomic_DNA.
EMBL; CH471077; EAW75217.1; -; Genomic_DNA.
EMBL; CH471077; EAW75218.1; -; Genomic_DNA.
EMBL; BC017016; AAH17016.1; -; mRNA.
CCDS; CCDS13536.1; -. [Q9H400-1]
RefSeq; NP_001292583.1; NM_001305654.1.
RefSeq; NP_001292584.1; NM_001305655.1.
RefSeq; NP_060276.2; NM_017806.3. [Q9H400-1]
BioGRID; 120264; 4.
IntAct; Q9H400; 46.
STRING; 9606.ENSP00000309521; -.
iPTMnet; Q9H400; -.
PhosphoSitePlus; Q9H400; -.
SwissPalm; Q9H400; -.
BioMuta; LIME1; -.
DMDM; 74752630; -.
EPD; Q9H400; -.
jPOST; Q9H400; -.
MassIVE; Q9H400; -.
MaxQB; Q9H400; -.
PaxDb; Q9H400; -.
PeptideAtlas; Q9H400; -.
PRIDE; Q9H400; -.
ProteomicsDB; 80775; -. [Q9H400-1]
ProteomicsDB; 80776; -. [Q9H400-2]
Antibodypedia; 4202; 342 antibodies.
Ensembl; ENST00000309546; ENSP00000309521; ENSG00000203896. [Q9H400-1]
GeneID; 54923; -.
KEGG; hsa:54923; -.
UCSC; uc002ygp.5; human. [Q9H400-1]
CTD; 54923; -.
EuPathDB; HostDB:ENSG00000203896.9; -.
GeneCards; LIME1; -.
HGNC; HGNC:26016; LIME1.
HPA; ENSG00000203896; Group enriched (blood, liver, lymphoid tissue).
MIM; 609809; gene.
neXtProt; NX_Q9H400; -.
OpenTargets; ENSG00000203896; -.
PharmGKB; PA142671551; -.
eggNOG; ENOG410J9JT; Eukaryota.
eggNOG; ENOG41114H9; LUCA.
GeneTree; ENSGT00510000050080; -.
InParanoid; Q9H400; -.
OMA; HQELPWA; -.
OrthoDB; 931070at2759; -.
PhylomeDB; Q9H400; -.
TreeFam; TF337416; -.
BioGRID-ORCS; 54923; 0 hits in 784 CRISPR screens.
GeneWiki; LIME1; -.
GenomeRNAi; 54923; -.
Pharos; Q9H400; Tdark.
PRO; PR:Q9H400; -.
Proteomes; UP000005640; Chromosome 20.
RNAct; Q9H400; protein.
Bgee; ENSG00000203896; Expressed in liver and 86 other tissues.
ExpressionAtlas; Q9H400; baseline and differential.
Genevisible; Q9H400; HS.
GO; GO:0019815; C:B cell receptor complex; IBA:GO_Central.
GO; GO:0005615; C:extracellular space; HDA:UniProtKB.
GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
GO; GO:0019901; F:protein kinase binding; IBA:GO_Central.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0050853; P:B cell receptor signaling pathway; IBA:GO_Central.
GO; GO:0043122; P:regulation of I-kappaB kinase/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0043405; P:regulation of MAP kinase activity; IBA:GO_Central.
GO; GO:1901222; P:regulation of NIK/NF-kappaB signaling; IBA:GO_Central.
GO; GO:0014066; P:regulation of phosphatidylinositol 3-kinase signaling; IBA:GO_Central.
GO; GO:0051279; P:regulation of release of sequestered calcium ion into cytosol; IBA:GO_Central.
GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
GO; GO:0050852; P:T cell receptor signaling pathway; IEA:InterPro.
InterPro; IPR026072; Lime1.
PANTHER; PTHR47740; PTHR47740; 1.
Pfam; PF15332; LIME1; 1.
1: Evidence at protein level;
Adaptive immunity; Alternative splicing; Cell membrane; Immunity;
Lipoprotein; Membrane; Palmitate; Phosphoprotein; Polymorphism;
Reference proteome; Signal-anchor; Transmembrane; Transmembrane helix.
CHAIN 1..295
/note="Lck-interacting transmembrane adapter 1"
/id="PRO_0000083332"
TOPO_DOM 1..6
/note="Extracellular"
/evidence="ECO:0000255"
TRANSMEM 7..27
/note="Helical; Signal-anchor for type III membrane
protein"
/evidence="ECO:0000255"
TOPO_DOM 28..295
/note="Cytoplasmic"
/evidence="ECO:0000255"
REGION 145..148
/note="Interaction with GRB2"
/evidence="ECO:0000250"
REGION 167..170
/note="Interaction with CSK"
/evidence="ECO:0000269|PubMed:14610046"
REGION 200..203
/note="Interaction with CSK"
/evidence="ECO:0000269|PubMed:14610046"
REGION 235..238
/note="Interaction with LCK and PIK3R1"
/evidence="ECO:0000250"
REGION 254..257
/note="Interaction with LCK, PLCG2 and PIK3R1"
/evidence="ECO:0000250"
MOD_RES 145
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:Q9EQR5"
MOD_RES 167
/note="Phosphotyrosine"
/evidence="ECO:0000305|PubMed:14610046"
MOD_RES 200
/note="Phosphotyrosine"
/evidence="ECO:0000269|PubMed:14610046"
MOD_RES 235
/note="Phosphotyrosine"
/evidence="ECO:0000250|UniProtKB:Q9EQR5"
MOD_RES 254
/note="Phosphotyrosine; by LCK"
/evidence="ECO:0000305|PubMed:14610046"
MOD_RES 256
/note="Phosphoserine"
/evidence="ECO:0000244|PubMed:24275569"
LIPID 28
/note="S-palmitoyl cysteine"
/evidence="ECO:0000305|PubMed:14610046"
LIPID 31
/note="S-palmitoyl cysteine"
/evidence="ECO:0000305|PubMed:14610046"
VAR_SEQ 1..95
/note="Missing (in isoform 2)"
/evidence="ECO:0000303|PubMed:15498874"
/id="VSP_016642"
VARIANT 211
/note="P -> L (in dbSNP:rs1151625)"
/id="VAR_053918"
MUTAGEN 145
/note="Y->F: No change in binding to LCK, CSK or FYN."
/evidence="ECO:0000269|PubMed:14610046"
MUTAGEN 167
/note="Y->F: Abolishes binding to CSK."
/evidence="ECO:0000269|PubMed:14610046"
MUTAGEN 200
/note="Y->F: Reduces binding to CSK."
/evidence="ECO:0000269|PubMed:14610046"
MUTAGEN 235
/note="Y->F: No change in binding to LCK, CSK or FYN."
/evidence="ECO:0000269|PubMed:14610046"
MUTAGEN 254
/note="Y->F: Abolishes binding to LCK and reduces binding
to FYN."
/evidence="ECO:0000269|PubMed:14610046"
CONFLICT 246
/note="D -> G (in Ref. 4; BAA91148)"
/evidence="ECO:0000305"
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


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Related Genes :
[LIME1 LIME LP8067] Lck-interacting transmembrane adapter 1 (Lck-interacting membrane protein) (Lck-interacting molecule)
[Lime1 Lime] Lck-interacting transmembrane adapter 1 (Lck-interacting molecule)
[TRAT1 TCRIM HSPC062] T-cell receptor-associated transmembrane adapter 1 (T-cell receptor-interacting molecule) (TRIM) (pp29/30)
[SIT1 SIT] Signaling threshold-regulating transmembrane adapter 1 (SHP2-interacting transmembrane adapter protein) (Suppression-inducing transmembrane adapter 1) (gp30/40)
[SQSTM1 ORCA OSIL] Sequestosome-1 (EBI3-associated protein of 60 kDa) (EBIAP) (p60) (Phosphotyrosine-independent ligand for the Lck SH2 domain of 62 kDa) (Ubiquitin-binding protein p62)
[LYN JTK8] Tyrosine-protein kinase Lyn (EC 2.7.10.2) (Lck/Yes-related novel protein tyrosine kinase) (V-yes-1 Yamaguchi sarcoma viral related oncogene homolog) (p53Lyn) (p56Lyn)
[LCK] Tyrosine-protein kinase Lck (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (Protein YT16) (Proto-oncogene Lck) (T cell-specific protein-tyrosine kinase) (p56-LCK)
[Lck Lsk-t] Proto-oncogene tyrosine-protein kinase LCK (EC 2.7.10.2) (Leukocyte C-terminal Src kinase) (LSK) (Lymphocyte cell-specific protein-tyrosine kinase) (p56-LCK)
[LCK] Tyrosine-protein kinase Lck (EC 2.7.10.2) (Lymphocyte cell-specific protein-tyrosine kinase) (Proto-oncogene Lck) (p56-LCK)
[Lck] Proto-oncogene tyrosine-protein kinase LCK (EC 2.7.10.2) (Lymphocyte cell-specific protein-tyrosine kinase) (p56-LCK)
[LCK] Proto-oncogene tyrosine-protein kinase LCK (EC 2.7.10.2) (Lymphocyte cell-specific protein-tyrosine kinase) (p56-LCK)
[Sqstm1 Zip] Sequestosome-1 (Protein kinase C-zeta-interacting protein) (PKC-zeta-interacting protein) (Ubiquitin-binding protein p62)
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[SCIMP C17orf87 UNQ5783/PRO16090] SLP adapter and CSK-interacting membrane protein (SLP65/SLP76, Csk-interacting membrane protein)
[LAMTOR2 MAPBPIP ROBLD3 HSPC003] Ragulator complex protein LAMTOR2 (Endosomal adaptor protein p14) (Late endosomal/lysosomal Mp1-interacting protein) (Late endosomal/lysosomal adaptor and MAPK and MTOR activator 2) (Mitogen-activated protein-binding protein-interacting protein) (MAPBP-interacting protein) (Roadblock domain-containing protein 3)
[PIAS2 PIASX] E3 SUMO-protein ligase PIAS2 (EC 2.3.2.-) (Androgen receptor-interacting protein 3) (ARIP3) (DAB2-interacting protein) (DIP) (E3 SUMO-protein transferase PIAS2) (Msx-interacting zinc finger protein) (Miz1) (PIAS-NY protein) (Protein inhibitor of activated STAT x) (Protein inhibitor of activated STAT2)
[psbA WH49_00001] Photosystem II protein D1 (PSII D1 protein) (EC 1.10.3.9) (Photosystem II Q(B) protein)
[MICAL1 MICAL NICAL] [F-actin]-monooxygenase MICAL1 (EC 1.14.13.225) (Molecule interacting with CasL protein 1) (MICAL-1) (NEDD9-interacting protein with calponin homology and LIM domains)
[Mical1 Mical Nical] [F-actin]-monooxygenase MICAL1 (EC 1.14.13.225) (Molecule interacting with CasL protein 1) (MICAL-1) (mMical1) (NEDD9-interacting protein with calponin homology and LIM domains)
[APPL1 APPL DIP13A KIAA1428] DCC-interacting protein 13-alpha (Dip13-alpha) (Adapter protein containing PH domain, PTB domain and leucine zipper motif 1)
[MAGI2 ACVRINP1 AIP1 KIAA0705] Membrane-associated guanylate kinase, WW and PDZ domain-containing protein 2 (Atrophin-1-interacting protein 1) (AIP-1) (Atrophin-1-interacting protein A) (Membrane-associated guanylate kinase inverted 2) (MAGI-2)
[UBQLN4 C1orf6 CIP75 UBIN] Ubiquilin-4 (Ataxin-1 interacting ubiquitin-like protein) (A1Up) (Ataxin-1 ubiquitin-like-interacting protein A1U) (Connexin43-interacting protein of 75 kDa) (CIP75)
[NAV3 KIAA0938 POMFIL1 STEERIN3] Neuron navigator 3 (Pore membrane and/or filament-interacting-like protein 1) (Steerin-3) (Unc-53 homolog 3) (unc53H3)
[RIPK1 RIP RIP1] Receptor-interacting serine/threonine-protein kinase 1 (EC 2.7.11.1) (Cell death protein RIP) (Receptor-interacting protein 1) (RIP-1)
[NAV1 KIAA1151 KIAA1213 POMFIL3 STEERIN1] Neuron navigator 1 (Pore membrane and/or filament-interacting-like protein 3) (Steerin-1) (Unc-53 homolog 1) (unc53H1)
[Mapk8ip1 Ib1 Jip1 Mapk8ip Prkm8ip] C-Jun-amino-terminal kinase-interacting protein 1 (JIP-1) (JNK-interacting protein 1) (Islet-brain-1) (IB-1) (JNK MAP kinase scaffold protein 1) (Mitogen-activated protein kinase 8-interacting protein 1)
[NAV2 HELAD1 KIAA1419 POMFIL2 RAINB1 STEERIN2] Neuron navigator 2 (EC 3.6.4.12) (Helicase APC down-regulated 1) (Pore membrane and/or filament-interacting-like protein 2) (Retinoic acid inducible in neuroblastoma 1) (Steerin-2) (Unc-53 homolog 2) (unc53H2)

Bibliography :
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