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Src-like-adapter 2 (Modulator of antigen receptor signaling) (MARS) (Src-like adapter protein 2) (SLAP-2)

 SLAP2_HUMAN             Reviewed;         261 AA.
Q9H6Q3; A8K648; E1P5U1; E1P5U2; Q5TH27; Q5TH28; Q8WY18; Q96QI4;
Q9H135;
23-APR-2003, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
30-AUG-2017, entry version 146.
RecName: Full=Src-like-adapter 2;
AltName: Full=Modulator of antigen receptor signaling;
Short=MARS;
AltName: Full=Src-like adapter protein 2;
Short=SLAP-2;
Name=SLA2; Synonyms=C20orf156, SLAP2;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE (ISOFORM 1), CHARACTERIZATION, FUNCTION,
MYRISTOYLATION AT GLY-2, INTERACTION WITH CBL, AND MUTAGENESIS OF
GLY-2.
PubMed=11696592; DOI=10.1084/jem.194.9.1263;
Holland S.J., Liao X.C., Mendenhall M.K., Zhou X., Pardo J., Chu P.,
Spencer C., Fu A.C., Sheng N., Yu P., Pali E., Nagin A., Shen M.,
Yu S., Chan E., Wu X., Li C., Woisetschlager M., Aversa G.,
Kolbinger F., Bennett M.K., Molineaux S., Luo Y., Payan D.G.,
Mancebo H.S.Y., Wu J.;
"Functional cloning of Src-like adapter protein-2 (SLAP-2), a novel
inhibitor of antigen receptor signaling.";
J. Exp. Med. 194:1263-1276(2001).
[2]
NUCLEOTIDE SEQUENCE (ISOFORMS 1; 2; 3 AND 4), AND ALTERNATIVE
INITIATION.
TISSUE=Thymus;
PubMed=12527895; DOI=10.1038/sj.onc.1206114;
Loreto M.P., McGlade C.J.;
"Cloning and characterization of human Src-like adaptor protein 2 and
a novel splice isoform, SLAP-2-v.";
Oncogene 22:266-273(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Hepatoma;
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).
[4]
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).
[5]
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.
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Prostate;
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).
[7]
CHARACTERIZATION.
PubMed=11891219; DOI=10.1074/jbc.M110318200;
Pandey A., Ibarrola N., Kratchmarova I., Fernandez M.M.,
Constantinescu S.N., Ohara O., Sawasdikosol S., Lodish H.F., Mann M.;
"A novel Src homology 2 domain-containing molecule, Src-like adapter
protein-2 (SLAP-2), which negatively regulates T cell receptor
signaling.";
J. Biol. Chem. 277:19131-19138(2002).
-!- FUNCTION: Adapter protein, which negatively regulates T-cell
receptor (TCR) signaling. Inhibits T-cell antigen-receptor induced
activation of nuclear factor of activated T-cells. May act by
linking signaling proteins such as ZAP70 with CBL, leading to a
CBL dependent degradation of signaling proteins.
{ECO:0000269|PubMed:11696592}.
-!- SUBUNIT: Interacts (via SH2 domain) with ZAP70 (phosphorylated)
and CD3Z (phosphorylated). Interacts (via SH2 domain) with CSF1R
(phosphorylated) (By similarity). Interacts (via its C-terminal
domain) with CBL (phosphorylated). {ECO:0000250,
ECO:0000269|PubMed:11696592}.
-!- INTERACTION:
P04626:ERBB2; NbExp=2; IntAct=EBI-1222854, EBI-641062;
Q13480:GAB1; NbExp=4; IntAct=EBI-1222854, EBI-517684;
P10721:KIT; NbExp=2; IntAct=EBI-1222854, EBI-1379503;
P08581:MET; NbExp=4; IntAct=EBI-1222854, EBI-1039152;
-!- SUBCELLULAR LOCATION: Cytoplasm.
-!- SUBCELLULAR LOCATION: Isoform 1: Cell membrane. Cytoplasmic
vesicle. Note=Localized to the plasma membrane and intracellular
vesicles, including late endosomal vesicles.
-!- SUBCELLULAR LOCATION: Isoform 2: Cytoplasm {ECO:0000305}. Note=May
be cytoplasmic and is not localized to membranes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing, Alternative initiation; Named isoforms=4;
Name=1; Synonyms=p28;
IsoId=Q9H6Q3-1; Sequence=Displayed;
Name=2; Synonyms=p23, SLAP-2-v, MARS-v;
IsoId=Q9H6Q3-2; Sequence=VSP_007240, VSP_007241;
Name=3; Synonyms=p25;
IsoId=Q9H6Q3-3; Sequence=VSP_018794;
Note=Produced by alternative initiation at Met-28 of isoform 1.;
Name=4; Synonyms=p20;
IsoId=Q9H6Q3-4; Sequence=VSP_018794, VSP_007240, VSP_007241;
Note=Produced by alternative initiation at Met-28 of isoform 2.;
-!- TISSUE SPECIFICITY: Predominantly expressed in immune system, with
highest levels in peripheral blood leukocytes. Expressed in
spleen, thymus and lymph nodes. Expressed in T-cells as well as in
monocytes, and at low level in B-cells. Also detected in placenta,
prostate, skin, retina and colon.
-!- DOMAIN: The loss of the C-terminal domain partially abolishes the
inhibitory function, but can be partially compensated by higher
level of protein expression.
-!- PTM: Phosphorylated by CSF1R. {ECO:0000250}.
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EMBL; AF326353; AAL29204.1; -; mRNA.
EMBL; AF290985; AAL38197.1; -; mRNA.
EMBL; AF290986; AAL38198.1; -; mRNA.
EMBL; AK025645; BAB15201.1; -; mRNA.
EMBL; AK291513; BAF84202.1; -; mRNA.
EMBL; AL031662; CAI21397.1; -; Genomic_DNA.
EMBL; AL050318; CAI21397.1; JOINED; Genomic_DNA.
EMBL; AL031662; CAI21398.1; -; Genomic_DNA.
EMBL; AL050318; CAI21398.1; JOINED; Genomic_DNA.
EMBL; AL050318; CAI23504.1; -; Genomic_DNA.
EMBL; AL031662; CAI23504.1; JOINED; Genomic_DNA.
EMBL; AL050318; CAI23505.1; -; Genomic_DNA.
EMBL; AL031662; CAI23505.1; JOINED; Genomic_DNA.
EMBL; CH471077; EAW76116.1; -; Genomic_DNA.
EMBL; CH471077; EAW76117.1; -; Genomic_DNA.
EMBL; CH471077; EAW76118.1; -; Genomic_DNA.
EMBL; CH471077; EAW76119.1; -; Genomic_DNA.
EMBL; BC042041; AAH42041.1; -; mRNA.
CCDS; CCDS13282.1; -. [Q9H6Q3-1]
CCDS; CCDS13283.1; -. [Q9H6Q3-2]
RefSeq; NP_115590.1; NM_032214.3. [Q9H6Q3-1]
RefSeq; NP_778252.1; NM_175077.2. [Q9H6Q3-2]
UniGene; Hs.713578; -.
PDB; 4M4Z; X-ray; 2.10 A; A=29-193.
PDBsum; 4M4Z; -.
ProteinModelPortal; Q9H6Q3; -.
SMR; Q9H6Q3; -.
BioGrid; 123928; 14.
ELM; Q9H6Q3; -.
IntAct; Q9H6Q3; 8.
MINT; MINT-1493503; -.
STRING; 9606.ENSP00000262866; -.
iPTMnet; Q9H6Q3; -.
PhosphoSitePlus; Q9H6Q3; -.
BioMuta; SLA2; -.
DMDM; 30173374; -.
MaxQB; Q9H6Q3; -.
PaxDb; Q9H6Q3; -.
PeptideAtlas; Q9H6Q3; -.
PRIDE; Q9H6Q3; -.
Ensembl; ENST00000262866; ENSP00000262866; ENSG00000101082. [Q9H6Q3-1]
Ensembl; ENST00000360672; ENSP00000353890; ENSG00000101082. [Q9H6Q3-2]
GeneID; 84174; -.
KEGG; hsa:84174; -.
UCSC; uc002xfu.4; human. [Q9H6Q3-1]
CTD; 84174; -.
GeneCards; SLA2; -.
HGNC; HGNC:17329; SLA2.
HPA; HPA053746; -.
HPA; HPA058217; -.
MIM; 606577; gene.
neXtProt; NX_Q9H6Q3; -.
OpenTargets; ENSG00000101082; -.
PharmGKB; PA38231; -.
eggNOG; ENOG410IKI6; Eukaryota.
eggNOG; ENOG4111GMN; LUCA.
GeneTree; ENSGT00390000001681; -.
HOVERGEN; HBG054908; -.
InParanoid; Q9H6Q3; -.
OMA; WLYEGLS; -.
OrthoDB; EOG091G0GB0; -.
PhylomeDB; Q9H6Q3; -.
TreeFam; TF354288; -.
SignaLink; Q9H6Q3; -.
GeneWiki; SLA2; -.
GenomeRNAi; 84174; -.
PRO; PR:Q9H6Q3; -.
Proteomes; UP000005640; Chromosome 20.
Bgee; ENSG00000101082; -.
CleanEx; HS_SLA2; -.
Genevisible; Q9H6Q3; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0010008; C:endosome membrane; NAS:UniProtKB.
GO; GO:0031234; C:extrinsic component of cytoplasmic side of plasma membrane; IBA:GO_Central.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0043231; C:intracellular membrane-bounded organelle; IDA:HPA.
GO; GO:0005770; C:late endosome; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; TAS:UniProtKB.
GO; GO:0004715; F:non-membrane spanning protein tyrosine kinase activity; IBA:GO_Central.
GO; GO:0047485; F:protein N-terminus binding; IPI:UniProtKB.
GO; GO:0005102; F:receptor binding; IBA:GO_Central.
GO; GO:0005070; F:SH3/SH2 adaptor activity; IDA:UniProtKB.
GO; GO:0050851; P:antigen receptor-mediated signaling pathway; TAS:UniProtKB.
GO; GO:0019724; P:B cell mediated immunity; TAS:UniProtKB.
GO; GO:0030154; P:cell differentiation; IBA:GO_Central.
GO; GO:0016477; P:cell migration; IBA:GO_Central.
GO; GO:0045087; P:innate immune response; IBA:GO_Central.
GO; GO:0030522; P:intracellular receptor signaling pathway; TAS:UniProtKB.
GO; GO:0050869; P:negative regulation of B cell activation; TAS:UniProtKB.
GO; GO:0050849; P:negative regulation of calcium-mediated signaling; IDA:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; IDA:UniProtKB.
GO; GO:0038083; P:peptidyl-tyrosine autophosphorylation; IBA:GO_Central.
GO; GO:0042127; P:regulation of cell proliferation; IBA:GO_Central.
GO; GO:0050776; P:regulation of immune response; NAS:UniProtKB.
GO; GO:0042110; P:T cell activation; TAS:UniProtKB.
GO; GO:0007169; P:transmembrane receptor protein tyrosine kinase signaling pathway; IBA:GO_Central.
CDD; cd10344; SH2_SLAP; 1.
Gene3D; 3.30.505.10; -; 1.
InterPro; IPR000980; SH2.
InterPro; IPR001452; SH3_domain.
InterPro; IPR035054; SLAP2.
InterPro; IPR035052; SLAP_SH2.
PANTHER; PTHR24418:SF326; PTHR24418:SF326; 1.
Pfam; PF00017; SH2; 1.
Pfam; PF00018; SH3_1; 1.
PRINTS; PR00401; SH2DOMAIN.
SMART; SM00252; SH2; 1.
SMART; SM00326; SH3; 1.
SUPFAM; SSF50044; SSF50044; 1.
SUPFAM; SSF55550; SSF55550; 1.
PROSITE; PS50001; SH2; 1.
PROSITE; PS50002; SH3; 1.
1: Evidence at protein level;
3D-structure; Alternative initiation; Alternative splicing;
Cell membrane; Complete proteome; Cytoplasm; Cytoplasmic vesicle;
Lipoprotein; Membrane; Myristate; Phosphoprotein; Polymorphism;
Reference proteome; SH2 domain; SH3 domain.
INIT_MET 1 1 Removed.
CHAIN 2 261 Src-like-adapter 2.
/FTId=PRO_0000022351.
DOMAIN 32 92 SH3. {ECO:0000255|PROSITE-
ProRule:PRU00192}.
DOMAIN 94 191 SH2. {ECO:0000255|PROSITE-
ProRule:PRU00191}.
REGION 195 261 SLA C-terminal.
LIPID 2 2 N-myristoyl glycine.
{ECO:0000269|PubMed:11696592}.
VAR_SEQ 1 27 Missing (in isoform 3 and isoform 4).
{ECO:0000305}.
/FTId=VSP_018794.
VAR_SEQ 179 210 LADDICCLLKEPCVLQRAGPLPGKDIPLPVTV -> GWPAP
WQGYTPTCDCAEDTTQLERAGQLPPVF (in isoform 2
and isoform 4). {ECO:0000305}.
/FTId=VSP_007240.
VAR_SEQ 211 261 Missing (in isoform 2 and isoform 4).
{ECO:0000305}.
/FTId=VSP_007241.
VARIANT 210 210 V -> M (in dbSNP:rs34834764).
/FTId=VAR_051361.
MUTAGEN 2 2 G->A: Abolishes localization to
membranes. {ECO:0000269|PubMed:11696592}.
STRAND 37 39 {ECO:0000244|PDB:4M4Z}.
STRAND 58 65 {ECO:0000244|PDB:4M4Z}.
STRAND 68 73 {ECO:0000244|PDB:4M4Z}.
TURN 74 76 {ECO:0000244|PDB:4M4Z}.
STRAND 79 83 {ECO:0000244|PDB:4M4Z}.
HELIX 84 86 {ECO:0000244|PDB:4M4Z}.
STRAND 87 91 {ECO:0000244|PDB:4M4Z}.
TURN 92 94 {ECO:0000244|PDB:4M4Z}.
STRAND 95 98 {ECO:0000244|PDB:4M4Z}.
HELIX 101 108 {ECO:0000244|PDB:4M4Z}.
STRAND 118 122 {ECO:0000244|PDB:4M4Z}.
STRAND 124 128 {ECO:0000244|PDB:4M4Z}.
STRAND 130 135 {ECO:0000244|PDB:4M4Z}.
STRAND 145 152 {ECO:0000244|PDB:4M4Z}.
STRAND 158 161 {ECO:0000244|PDB:4M4Z}.
STRAND 164 168 {ECO:0000244|PDB:4M4Z}.
HELIX 169 176 {ECO:0000244|PDB:4M4Z}.
SEQUENCE 261 AA; 28585 MW; 858AF03451672B3D CRC64;
MGSLPSRRKS LPSPSLSSSV QGQGPVTMEA ERSKATAVAL GSFPAGGPAE LSLRLGEPLT
IVSEDGDWWT VLSEVSGREY NIPSVHVAKV SHGWLYEGLS REKAEELLLL PGNPGGAFLI
RESQTRRGSY SLSVRLSRPA SWDRIRHYRI HCLDNGWLYI SPRLTFPSLQ ALVDHYSELA
DDICCLLKEP CVLQRAGPLP GKDIPLPVTV QRTPLNWKEL DSSLLFSEAA TGEESLLSEG
LRESLSFYIS LNDEAVSLDD A


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EIAAB38197 Homo sapiens,Human,LNK,Lymphocyte adapter protein,Lymphocyte-specific adapter protein Lnk,SH2B adapter protein 3,SH2B3,Signal transduction protein Lnk
EIAAB38194 Adapter protein with pleckstrin homology and Src homology 2 domains,Aps,Mouse,Mus musculus,SH2 and PH domain-containing adapter protein APS,SH2B adapter protein 2,Sh2b2
EIAAB38193 Adapter protein with pleckstrin homology and Src homology 2 domains,Aps,Rat,Rattus norvegicus,SH2 and PH domain-containing adapter protein APS,SH2B adapter protein 2,Sh2b2
EIAAB38196 Lnk,Lymphocyte adapter protein,Lymphocyte-specific adapter protein Lnk,Mouse,Mus musculus,SH2B adapter protein 3,Sh2b3,Signal transduction protein Lnk
EIAAB38198 Lnk,Lymphocyte adapter protein,Lymphocyte-specific adapter protein Lnk,Rat,Rattus norvegicus,SH2B adapter protein 3,Sh2b3,Signal transduction protein Lnk


 

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