SCIMP_HUMAN
ID SCIMP_HUMAN Reviewed; 145 AA.
AC Q6UWF3; A6XGL4; B4DLK1; Q96MD0;
DT 10-JUL-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 124.
DE RecName: Full=SLP adapter and CSK-interacting membrane protein;
DE AltName: Full=SLP65/SLP76, Csk-interacting membrane protein;
GN Name=SCIMP; Synonyms=C17orf87; ORFNames=UNQ5783/PRO16090;
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 [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=12975309; DOI=10.1101/gr.1293003;
RA Clark H.F., Gurney A.L., Abaya E., Baker K., Baldwin D.T., Brush J.,
RA Chen J., Chow B., Chui C., Crowley C., Currell B., Deuel B., Dowd P.,
RA Eaton D., Foster J.S., Grimaldi C., Gu Q., Hass P.E., Heldens S., Huang A.,
RA Kim H.S., Klimowski L., Jin Y., Johnson S., Lee J., Lewis L., Liao D.,
RA Mark M.R., Robbie E., Sanchez C., Schoenfeld J., Seshagiri S., Simmons L.,
RA Singh J., Smith V., Stinson J., Vagts A., Vandlen R.L., Watanabe C.,
RA Wieand D., Woods K., Xie M.-H., Yansura D.G., Yi S., Yu G., Yuan J.,
RA Zhang M., Zhang Z., Goddard A.D., Wood W.I., Godowski P.J., Gray A.M.;
RT "The secreted protein discovery initiative (SPDI), a large-scale effort to
RT identify novel human secreted and transmembrane proteins: a bioinformatics
RT assessment.";
RL Genome Res. 13:2265-2270(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Spleen, and Umbilical cord blood;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RA Yu Z., Zheng Z., Tang T., Fu Y.;
RT "A computer system platform used to predict novel genes.";
RL Submitted (JUN-2006) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain;
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 [7]
RP FUNCTION, INTERACTION WITH BLNK; CD37; CD53; CD81; CSK AND LYN,
RP PALMITOYLATION AT CYS-40 AND CYS-42, PHOSPHORYLATION AT TYR-69; TYR-107 AND
RP TYR-131, MUTAGENESIS OF TYR-69; 81-PRO--PRO-86; TYR-107 AND TYR-131,
RP SUBCELLULAR LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=21930792; DOI=10.1128/mcb.05817-11;
RA Draber P., Vonkova I., Stepanek O., Hrdinka M., Kucova M., Skopcova T.,
RA Otahal P., Angelisova P., Horejsi V., Yeung M., Weiss A., Brdicka T.;
RT "SCIMP, a transmembrane adapter protein involved in major
RT histocompatibility complex class II signaling.";
RL Mol. Cell. Biol. 31:4550-4562(2011).
CC -!- FUNCTION: Lipid tetraspanin-associated transmembrane adapter/mediator
CC that acts as a scaffold for Src-family kinases and other signaling
CC proteins in immune cells (PubMed:21930792). It is involved in major
CC histocompatibility complex class II (MHC-II) signaling transduction in
CC B cells, where it is required in generating the calcium response and
CC enhancing ERK activity upon MHC-II stimulation (PubMed:21930792). In
CC dendritic cells, it is involved in sustaining CLEC7A/DECTIN1 signaling
CC after CLEC7A activation by fungal beta-glucans (By similarity). It also
CC acts as an agonist-inducible signaling adapter for TLR1, TLR2, TLR3,
CC TLR4, and TLR7 by selectively enabling the expression of pro-
CC inflammatory cytokines IL6 and IL12B in macrophages and acting as a
CC scaffold for phosphorylation of Toll-like receptors by Src-family
CC kinases (By similarity). {ECO:0000250|UniProtKB:Q3UU41,
CC ECO:0000269|PubMed:21930792}.
CC -!- SUBUNIT: Interacts with CD37, CD53 and CD81 (PubMed:21930792).
CC Interacts (via proline-rich region) with LYN (via SH3 domain)
CC (PubMed:21930792). Interacts with CSK (via SH2 domain); this
CC interaction is dependent on phosphorylation of Tyr-107
CC (PubMed:21930792). Interacts with BLNK (via SH2 domain); this
CC interaction is dependent on phosphorylation of Tyr-131
CC (PubMed:21930792). Interacts with GRB2 (via SH2 domain); this
CC interaction may be dependent on phosphorylation of Tyr-69 (By
CC similarity). Interacts with TLR4; this interaction occurs upon
CC lipopolysaccharide activation of TLR4 and is enhanced by
CC phosphorylation of Tyr-107 by LYN (By similarity). This interaction
CC facilitates the phosphorylation of TLR4 by LYN which elicits a
CC selective cytokine response in macrophages (By similarity).
CC {ECO:0000250|UniProtKB:Q3UU41, ECO:0000269|PubMed:21930792}.
CC -!- INTERACTION:
CC Q6UWF3; Q6ZN84: CCDC81; NbExp=5; IntAct=EBI-2872510, EBI-14404745;
CC Q6UWF3; P41240: CSK; NbExp=3; IntAct=EBI-2872510, EBI-1380630;
CC Q6UWF3; P07948: LYN; NbExp=3; IntAct=EBI-2872510, EBI-79452;
CC Q6UWF3; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-2872510, EBI-16439278;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000305}; Single-pass membrane
CC protein {ECO:0000255}. Cell membrane {ECO:0000269|PubMed:21930792};
CC Lipid-anchor {ECO:0000269|PubMed:21930792}. Cytoplasmic vesicle,
CC phagosome {ECO:0000250|UniProtKB:Q3UU41}. Cell projection, ruffle
CC {ECO:0000250|UniProtKB:Q3UU41}. Cell projection, filopodium
CC {ECO:0000250|UniProtKB:Q3UU41}. Note=Together with MHC-II, associates
CC with lipid-enriched microdomains called tetraspanin-enriched
CC microdomains (TEMs) (PubMed:21930792). Rapidly translocates into
CC immunological synapse (IS) at cell-cell contacts between antigen-
CC presenting cells (APCs) and T-cells (PubMed:21930792). Colocalized with
CC tetraspanins CD37, CD53, and CD81 at the uropod (PubMed:21930792).
CC Present at regions of cell-cell contacts but also at the leading edge
CC of migrating cells (PubMed:21930792). Localizes to phagosomes in
CC dendritic cells after exposure to particulate beta-glucan (By
CC similarity). {ECO:0000250|UniProtKB:Q3UU41,
CC ECO:0000269|PubMed:21930792}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q6UWF3-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6UWF3-2; Sequence=VSP_026853, VSP_026854, VSP_026855;
CC Name=3;
CC IsoId=Q6UWF3-3; Sequence=VSP_026853;
CC -!- TISSUE SPECIFICITY: Expressed in antigen-presenting cells, like
CC peripheral blood leukocytes and monocyte-derived dendritic cells (MDDC)
CC (at protein level) (PubMed:21930792). Highly expressed in lymph nodes
CC and spleen. Expressed in antigen-presenting cells (PubMed:21930792).
CC Faintly expressed in the majority of nonimmune system tissues
CC (PubMed:21930792). {ECO:0000269|PubMed:21930792}.
CC -!- PTM: Phosphorylated by the Src-family protein tyrosine kinases LYN and
CC SRC (PubMed:21930792). Phosphorylation occurs on tyrosine residues upon
CC MHC-II stimulation (PubMed:21930792). Phosphorylation also occurs on
CC tyrosine residues after activation of CLEC7A/DECTIN1 by particulate
CC beta-glucan (By similarity). Lipopolysaccharide (LPS) induces
CC phosphorylation of Tyr-69, Tyr-107 and Tyr-131 differentially to allow
CC temporal recruitment of effector proteins GRB2, CSK and BLNK (By
CC similarity). Phosphorylation of Tyr-69 is immediately induced by LPS
CC stimulation and allows GRB2 to bind (By similarity). Tyr-107 is
CC phosphorylated 5 minutes after LPS stimulation, which then allows CSK
CC to bind, followed by phosphorylation of Tyr-131 10 minutes after LPS
CC induction, which allows BLNK to bind (By similarity). Phosphorylation
CC at Tyr-107 by LYN occurs after activation of TLR4 by
CC lipopolysaccharide; phosphorylation enhances binding to TLR4 (By
CC similarity). {ECO:0000250|UniProtKB:Q3UU41,
CC ECO:0000269|PubMed:21930792}.
CC -!- PTM: Palmitoylated. {ECO:0000269|PubMed:21930792}.
CC -!- CAUTION: It is uncertain whether Met-1 or Met-12 is the initiator.
CC {ECO:0000305}.
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DR EMBL; AY358809; AAQ89169.1; -; mRNA.
DR EMBL; AK057142; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK297035; BAG59563.1; -; mRNA.
DR EMBL; DQ778084; ABI63348.1; -; mRNA.
DR EMBL; AC087500; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471108; EAW90349.1; -; Genomic_DNA.
DR EMBL; CH471108; EAW90350.1; -; Genomic_DNA.
DR EMBL; BC127925; AAI27926.1; -; mRNA.
DR EMBL; BC130554; AAI30555.1; -; mRNA.
DR EMBL; BC130556; AAI30557.1; -; mRNA.
DR EMBL; BC144395; AAI44396.1; -; mRNA.
DR CCDS; CCDS42242.1; -. [Q6UWF3-1]
DR CCDS; CCDS62044.1; -. [Q6UWF3-3]
DR CCDS; CCDS82046.1; -. [Q6UWF3-2]
DR RefSeq; NP_001258771.1; NM_001271842.1. [Q6UWF3-3]
DR RefSeq; NP_001306119.1; NM_001319190.1. [Q6UWF3-2]
DR RefSeq; NP_996986.1; NM_207103.3. [Q6UWF3-1]
DR AlphaFoldDB; Q6UWF3; -.
DR SMR; Q6UWF3; -.
DR BioGRID; 132643; 5.
DR IntAct; Q6UWF3; 10.
DR STRING; 9606.ENSP00000461269; -.
DR iPTMnet; Q6UWF3; -.
DR PhosphoSitePlus; Q6UWF3; -.
DR SwissPalm; Q6UWF3; -.
DR BioMuta; SCIMP; -.
DR DMDM; 74738081; -.
DR MassIVE; Q6UWF3; -.
DR PaxDb; Q6UWF3; -.
DR PeptideAtlas; Q6UWF3; -.
DR PRIDE; Q6UWF3; -.
DR ProteomicsDB; 67470; -. [Q6UWF3-1]
DR ProteomicsDB; 67471; -. [Q6UWF3-2]
DR Antibodypedia; 1618; 96 antibodies from 17 providers.
DR DNASU; 388325; -.
DR Ensembl; ENST00000399600.8; ENSP00000382509.4; ENSG00000161929.15. [Q6UWF3-3]
DR Ensembl; ENST00000571800.5; ENSP00000459605.1; ENSG00000161929.15. [Q6UWF3-2]
DR Ensembl; ENST00000574081.6; ENSP00000461269.1; ENSG00000161929.15. [Q6UWF3-1]
DR GeneID; 388325; -.
DR KEGG; hsa:388325; -.
DR MANE-Select; ENST00000574081.6; ENSP00000461269.1; NM_207103.3; NP_996986.1.
DR UCSC; uc002gbh.4; human. [Q6UWF3-1]
DR CTD; 388325; -.
DR DisGeNET; 388325; -.
DR GeneCards; SCIMP; -.
DR HGNC; HGNC:33504; SCIMP.
DR HPA; ENSG00000161929; Tissue enhanced (lymphoid).
DR MIM; 614406; gene.
DR neXtProt; NX_Q6UWF3; -.
DR OpenTargets; ENSG00000161929; -.
DR PharmGKB; PA162378517; -.
DR VEuPathDB; HostDB:ENSG00000161929; -.
DR eggNOG; ENOG502T3K5; Eukaryota.
DR GeneTree; ENSGT00390000007003; -.
DR HOGENOM; CLU_1781827_0_0_1; -.
DR InParanoid; Q6UWF3; -.
DR OMA; NTEKHHF; -.
DR OrthoDB; 1442988at2759; -.
DR PhylomeDB; Q6UWF3; -.
DR TreeFam; TF340362; -.
DR PathwayCommons; Q6UWF3; -.
DR SignaLink; Q6UWF3; -.
DR BioGRID-ORCS; 388325; 9 hits in 1066 CRISPR screens.
DR ChiTaRS; SCIMP; human.
DR GenomeRNAi; 388325; -.
DR Pharos; Q6UWF3; Tbio.
DR PRO; PR:Q6UWF3; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q6UWF3; protein.
DR Bgee; ENSG00000161929; Expressed in monocyte and 106 other tissues.
DR ExpressionAtlas; Q6UWF3; baseline and differential.
DR GO; GO:0030175; C:filopodium; IEA:UniProtKB-SubCell.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0031256; C:leading edge membrane; IDA:UniProtKB.
DR GO; GO:0016020; C:membrane; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; ISS:UniProtKB.
DR GO; GO:0043235; C:receptor complex; ISS:UniProtKB.
DR GO; GO:0001726; C:ruffle; IEA:UniProtKB-SubCell.
DR GO; GO:0097197; C:tetraspanin-enriched microdomain; IDA:UniProtKB.
DR GO; GO:0031259; C:uropod membrane; IDA:UniProtKB.
DR GO; GO:0060090; F:molecular adaptor activity; ISS:UniProtKB.
DR GO; GO:0071226; P:cellular response to molecule of fungal origin; ISS:UniProtKB.
DR GO; GO:0002720; P:positive regulation of cytokine production involved in immune response; ISS:UniProtKB.
DR GO; GO:0002732; P:positive regulation of dendritic cell cytokine production; ISS:UniProtKB.
DR GO; GO:0070374; P:positive regulation of ERK1 and ERK2 cascade; IDA:UniProtKB.
DR GO; GO:0032735; P:positive regulation of interleukin-12 production; ISS:UniProtKB.
DR GO; GO:0032755; P:positive regulation of interleukin-6 production; ISS:UniProtKB.
DR GO; GO:0031666; P:positive regulation of lipopolysaccharide-mediated signaling pathway; ISS:UniProtKB.
DR GO; GO:0032874; P:positive regulation of stress-activated MAPK cascade; ISS:UniProtKB.
DR GO; GO:0034138; P:toll-like receptor 3 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034142; P:toll-like receptor 4 signaling pathway; ISS:UniProtKB.
DR GO; GO:0034154; P:toll-like receptor 7 signaling pathway; ISS:UniProtKB.
DR GO; GO:0038123; P:toll-like receptor TLR1:TLR2 signaling pathway; ISS:UniProtKB.
DR InterPro; IPR028181; SCIMP.
DR PANTHER; PTHR12044:SF11; PTHR12044:SF11; 1.
DR Pfam; PF15050; SCIMP; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell membrane; Cell projection; Cytoplasmic vesicle;
KW Lipoprotein; Membrane; Palmitate; Phosphoprotein; Reference proteome;
KW Transmembrane; Transmembrane helix.
FT CHAIN 1..145
FT /note="SLP adapter and CSK-interacting membrane protein"
FT /id="PRO_0000295237"
FT TRANSMEM 19..39
FT /note="Helical"
FT /evidence="ECO:0000255"
FT REGION 74..107
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 81..86
FT /note="Proline-rich region necessary for constitutive
FT interaction with LYN"
FT /evidence="ECO:0000269|PubMed:21930792"
FT REGION 104..145
FT /note="Interaction with TLR4"
FT /evidence="ECO:0000250|UniProtKB:Q3UU41"
FT COMPBIAS 90..107
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 69
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21930792"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UU41"
FT MOD_RES 107
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21930792"
FT MOD_RES 131
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000269|PubMed:21930792"
FT LIPID 40
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:21930792"
FT LIPID 42
FT /note="S-palmitoyl cysteine"
FT /evidence="ECO:0000305|PubMed:21930792"
FT VAR_SEQ 43..49
FT /note="Missing (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.3"
FT /id="VSP_026853"
FT VAR_SEQ 95..130
FT /note="SPQEAPSQPPATYSLVNKVKNKKTVSIPSYIEPEDD -> YGVLLCHPGWSA
FT MARSRLTASSASRVHAILLPQPPE (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026854"
FT VAR_SEQ 131..145
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_026855"
FT MUTAGEN 69
FT /note="Y->F: Inhibits interaction with GRB2."
FT /evidence="ECO:0000269|PubMed:21930792"
FT MUTAGEN 81..86
FT /note="Missing: Inhibits interaction with LYN."
FT /evidence="ECO:0000269|PubMed:21930792"
FT MUTAGEN 107
FT /note="Y->F: Inhibits interaction with CSK. Stimulates
FT activation of several downstream signaling pathways."
FT /evidence="ECO:0000269|PubMed:21930792"
FT MUTAGEN 131
FT /note="Y->F: Inhibits interaction with BLNK. Inhibits
FT activation of several downstream signaling pathways."
FT /evidence="ECO:0000269|PubMed:21930792"
SQ SEQUENCE 145 AA; 16618 MW; 8093F1087A7428EF CRC64;
MDTFTVQDST AMSWWRNNFW IILAVAIIVV SVGLGLILYC VCKWQLRRGK KWEIAKPLKH
KQVDEEKMYE NVLNESPVQL PPLPPRNWPS LEDSSPQEAP SQPPATYSLV NKVKNKKTVS
IPSYIEPEDD YDDVEIPANT EKASF
