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Signaling threshold-regulating transmembrane adapter 1 (SHP2-interacting transmembrane adapter protein) (Suppression-inducing transmembrane adapter 1) (gp30/40)

 SIT1_HUMAN              Reviewed;         196 AA.
Q9Y3P8; B2RBP9;
20-DEC-2005, integrated into UniProtKB/Swiss-Prot.
01-NOV-1999, sequence version 1.
12-SEP-2018, entry version 120.
RecName: Full=Signaling threshold-regulating transmembrane adapter 1;
AltName: Full=SHP2-interacting transmembrane adapter protein;
AltName: Full=Suppression-inducing transmembrane adapter 1;
AltName: Full=gp30/40;
Flags: Precursor;
Name=SIT1; Synonyms=SIT;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 148-158,
IDENTIFICATION BY MASS SPECTROMETRY, DIMERIZATION, GLYCOSYLATION AT
ASN-26, PHOSPHORYLATION AT TYR-148, MUTAGENESIS OF ASN-26 AND TYR-148,
TISSUE SPECIFICITY, SUBCELLULAR LOCATION, INTERACTION WITH PTPN11, AND
FUNCTION.
PubMed=10209036; DOI=10.1084/jem.189.8.1181;
Marie-Cardine A., Kirchgessner H., Bruyns E., Shevchenko A., Mann M.,
Autschbach F., Ratnofsky S., Meuer S., Schraven B.;
"SHP2-interacting transmembrane adaptor protein (SIT), a novel
disulfide-linked dimer regulating human T-cell activation.";
J. Exp. Med. 189:1181-1194(1999).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=11491537; DOI=10.1007/s002510100328;
Huebener C., Mincheva A., Lichter P., Schraven B., Bruyns E.;
"Complete sequence, genomic organization, and chromosomal localization
of the human gene encoding the SHP2-interacting transmembrane adaptor
protein (SIT).";
Immunogenetics 53:337-341(2001).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Thymus;
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=15164053; DOI=10.1038/nature02465;
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
Rogers J., Dunham I.;
"DNA sequence and analysis of human chromosome 9.";
Nature 429:369-374(2004).
[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].
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]
MUTAGENESIS OF TYR-90; TYR-127; TYR-148; TYR-169 AND TYR-188,
PHOSPHORYLATION AT TYR-90; TYR-127; TYR-148; TYR-169 AND TYR-188, AND
INTERACTION WITH PTPN11; GRB2 AND CSK.
PubMed=11433379;
DOI=10.1002/1521-4141(200106)31:6<1825::AID-IMMU1825>3.0.CO;2-V;
Pfrepper K.-I., Marie-Cardine A., Simeoni L., Kuramitsu Y., Leo A.,
Spicka J., Hilgert I., Scherer J., Schraven B.;
"Structural and functional dissection of the cytoplasmic domain of the
transmembrane adaptor protein SIT (SHP2-interacting transmembrane
adaptor protein).";
Eur. J. Immunol. 31:1825-1836(2001).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-80; TYR-90; THR-144;
SER-182 AND TYR-188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[9]
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).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-102; THR-144; TYR-148;
SER-182 AND TYR-188, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
-!- FUNCTION: Negatively regulates TCR (T-cell antigen receptor)-
mediated signaling in T-cells. Involved in positive selection of
T-cells. {ECO:0000269|PubMed:10209036}.
-!- SUBUNIT: Homodimer; disulfide-linked. When phosphorylated,
interacts with PTPN11/SHP2, GRB2 and CSK.
{ECO:0000269|PubMed:10209036, ECO:0000269|PubMed:11433379}.
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:10209036};
Single-pass type I membrane protein {ECO:0000269|PubMed:10209036}.
-!- TISSUE SPECIFICITY: Specifically expressed in T- and B-cells.
Present in plasma cells but not in germinal center B-cells (at
protein level). Expressed in T- and B-cell lymphoma.
{ECO:0000269|PubMed:10209036, ECO:0000269|PubMed:16160011}.
-!- PTM: Phosphorylated on tyrosines by LCK, FYN or ZAP70 upon TCR
activation; which leads to the recruitment of PTPN11, GRB2 and
CSK. {ECO:0000269|PubMed:10209036, ECO:0000269|PubMed:11433379}.
-!- CAUTION: In contrast to its orthologs it harbors a signal
sequence. {ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AJ010059; CAB41504.1; -; mRNA.
EMBL; AJ271888; CAC81313.1; -; Genomic_DNA.
EMBL; AK314758; BAG37296.1; -; mRNA.
EMBL; AL357874; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; CH471071; EAW58370.1; -; Genomic_DNA.
EMBL; BC102029; AAI02030.1; -; mRNA.
EMBL; BC104491; AAI04492.1; -; mRNA.
EMBL; BC107484; AAI07485.1; -; mRNA.
CCDS; CCDS6582.1; -.
RefSeq; NP_055265.1; NM_014450.2.
UniGene; Hs.88012; -.
ProteinModelPortal; Q9Y3P8; -.
SMR; Q9Y3P8; -.
BioGrid; 118088; 5.
IntAct; Q9Y3P8; 10.
MINT; Q9Y3P8; -.
STRING; 9606.ENSP00000259608; -.
iPTMnet; Q9Y3P8; -.
PhosphoSitePlus; Q9Y3P8; -.
BioMuta; SIT1; -.
DMDM; 74753488; -.
EPD; Q9Y3P8; -.
MaxQB; Q9Y3P8; -.
PaxDb; Q9Y3P8; -.
PeptideAtlas; Q9Y3P8; -.
PRIDE; Q9Y3P8; -.
ProteomicsDB; 86053; -.
Ensembl; ENST00000259608; ENSP00000259608; ENSG00000137078.
GeneID; 27240; -.
KEGG; hsa:27240; -.
UCSC; uc003zxe.3; human.
CTD; 27240; -.
DisGeNET; 27240; -.
EuPathDB; HostDB:ENSG00000137078.8; -.
GeneCards; SIT1; -.
HGNC; HGNC:17710; SIT1.
HPA; HPA018506; -.
MIM; 604964; gene.
neXtProt; NX_Q9Y3P8; -.
OpenTargets; ENSG00000137078; -.
PharmGKB; PA142670914; -.
eggNOG; ENOG410IYYR; Eukaryota.
eggNOG; ENOG4111C3Q; LUCA.
GeneTree; ENSGT00390000016476; -.
HOGENOM; HOG000231524; -.
HOVERGEN; HBG080311; -.
InParanoid; Q9Y3P8; -.
PhylomeDB; Q9Y3P8; -.
TreeFam; TF337816; -.
SignaLink; Q9Y3P8; -.
ChiTaRS; SIT1; human.
GeneWiki; SIT1; -.
GenomeRNAi; 27240; -.
PRO; PR:Q9Y3P8; -.
Proteomes; UP000005640; Chromosome 9.
Bgee; ENSG00000137078; Expressed in 111 organ(s), highest expression level in leukocyte.
CleanEx; HS_SIT1; -.
ExpressionAtlas; Q9Y3P8; baseline and differential.
Genevisible; Q9Y3P8; HS.
GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
GO; GO:0005887; C:integral component of plasma membrane; TAS:HGNC.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0019900; F:kinase binding; IPI:UniProtKB.
GO; GO:0042169; F:SH2 domain binding; TAS:HGNC.
GO; GO:0002250; P:adaptive immune response; IEA:UniProtKB-KW.
GO; GO:0050863; P:regulation of T cell activation; IDA:UniProtKB.
GO; GO:0007165; P:signal transduction; TAS:ProtInc.
GO; GO:0043029; P:T cell homeostasis; IEA:InterPro.
InterPro; IPR033269; Sit1.
PANTHER; PTHR15604; PTHR15604; 1.
ProDom; PD358400; PD358400; 1.
1: Evidence at protein level;
Adaptive immunity; Cell membrane; Complete proteome;
Direct protein sequencing; Disulfide bond; Glycoprotein; Immunity;
Membrane; Phosphoprotein; Reference proteome; Signal; Transmembrane;
Transmembrane helix.
SIGNAL 1 24 {ECO:0000255}.
CHAIN 25 196 Signaling threshold-regulating
transmembrane adapter 1.
/FTId=PRO_0000045152.
TOPO_DOM 25 40 Extracellular. {ECO:0000255}.
TRANSMEM 41 61 Helical. {ECO:0000255}.
TOPO_DOM 62 196 Cytoplasmic. {ECO:0000255}.
REGION 90 93 Interaction with GRB2.
{ECO:0000269|PubMed:11433379}.
REGION 146 151 Interaction with PTPN11.
REGION 169 172 Interaction with CSK.
{ECO:0000269|PubMed:11433379}.
REGION 188 191 Interaction with GRB2.
{ECO:0000269|PubMed:11433379}.
MOD_RES 80 80 Phosphoserine.
{ECO:0000244|PubMed:15144186}.
MOD_RES 83 83 Phosphoserine.
{ECO:0000250|UniProtKB:Q5M869}.
MOD_RES 90 90 Phosphotyrosine.
{ECO:0000244|PubMed:15144186,
ECO:0000269|PubMed:11433379}.
MOD_RES 102 102 Phosphoserine.
{ECO:0000244|PubMed:19690332}.
MOD_RES 127 127 Phosphotyrosine.
{ECO:0000305|PubMed:11433379}.
MOD_RES 144 144 Phosphothreonine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332}.
MOD_RES 148 148 Phosphotyrosine.
{ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:10209036,
ECO:0000269|PubMed:11433379}.
MOD_RES 169 169 Phosphotyrosine.
{ECO:0000305|PubMed:11433379}.
MOD_RES 182 182 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332}.
MOD_RES 188 188 Phosphotyrosine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332,
ECO:0000269|PubMed:11433379}.
CARBOHYD 26 26 N-linked (GlcNAc...) asparagine.
{ECO:0000269|PubMed:10209036}.
DISULFID 27 27 Interchain. {ECO:0000305}.
MUTAGEN 26 26 N->Q: Abolishes glycosylation.
{ECO:0000269|PubMed:10209036}.
MUTAGEN 90 90 Y->F: Reduces interaction with GRB2.
Abolishes interaction with GRB2; when
associated with F-188.
{ECO:0000269|PubMed:11433379}.
MUTAGEN 127 127 Y->F: No effect on interaction with
PTPN11 or GRB2.
{ECO:0000269|PubMed:11433379}.
MUTAGEN 148 148 Y->F: Reduces interaction with PTPN11, no
effect on inhibition of NF-AT activation.
{ECO:0000269|PubMed:10209036,
ECO:0000269|PubMed:11433379}.
MUTAGEN 169 169 Y->F: Abolishes interaction with CSK and
impairs inhibition of NF-AT activation.
{ECO:0000269|PubMed:11433379}.
MUTAGEN 188 188 Y->F: Reduces interaction with GRB2.
Abolishes interaction with GRB2; when
associated with F-90.
{ECO:0000269|PubMed:11433379}.
SEQUENCE 196 AA; 21126 MW; 2A0C48C9466F7F07 CRC64;
MNQADPRLRA VCLWTLTSAA MSRGDNCTDL LALGIPSITQ AWGLWVLLGA VTLLFLISLA
AHLSQWTRGR SRSHPGQGRS GESVEEVPLY GNLHYLQTGR LSQDPEPDQQ DPTLGGPARA
AEEVMCYTSL QLRPPQGRIP GPGTPVKYSE VVLDSEPKSQ ASGPEPELYA SVCAQTRRAR
ASFPDQAYAN SQPAAS


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