SASH3_MOUSE
ID SASH3_MOUSE Reviewed; 380 AA.
AC Q8K352; Q3TBX0; Q9DBV2;
DT 24-OCT-2003, integrated into UniProtKB/Swiss-Prot.
DT 24-OCT-2003, sequence version 2.
DT 03-AUG-2022, entry version 143.
DE RecName: Full=SAM and SH3 domain-containing protein 3;
DE AltName: Full=SH3 protein expressed in lymphocytes;
GN Name=Sash3; Synonyms=Sly;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND TISSUE SPECIFICITY.
RC TISSUE=T-cell lymphoma;
RX PubMed=11470164; DOI=10.1016/s0167-4781(01)00242-1;
RA Beer S., Simins A.B., Schuster A., Holzmann B.;
RT "Molecular cloning and characterization of a novel SH3 protein (SLY)
RT preferentially expressed in lymphoid cells.";
RL Biochim. Biophys. Acta 1520:89-93(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J, and NOD; TISSUE=Dendritic cell, Lung, and Spleen;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 104-380.
RC STRAIN=C57BL/6J; TISSUE=Mammary gland;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42; SER-97; THR-318 AND
RP SER-320, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Lung, and Spleen;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: May function as a signaling adapter protein in lymphocytes.
CC {ECO:0000269|PubMed:11470164}.
CC -!- TISSUE SPECIFICITY: Preferentially expressed in lymphoid tissues.
CC Expressed in bone marrow, thymus, spleen, lymph nodes and Peyer patches
CC of gut. In the spleen and lymph nodes, expressed in both T- and B-
CC cells. In the thymus, in the medulla and cortex.
CC {ECO:0000269|PubMed:11470164}.
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DR EMBL; AJ306422; CAC67499.1; -; mRNA.
DR EMBL; AK004734; BAB23516.1; -; mRNA.
DR EMBL; AK156202; BAE33623.1; -; mRNA.
DR EMBL; AK171017; BAE42187.1; -; mRNA.
DR EMBL; BC028773; AAH28773.1; -; mRNA.
DR CCDS; CCDS40959.1; -.
DR RefSeq; NP_001300678.1; NM_001313749.1.
DR RefSeq; NP_083049.1; NM_028773.4.
DR PDB; 6FXF; X-ray; 2.05 A; A=254-317.
DR PDB; 6G8O; NMR; -; A/B=254-321.
DR PDBsum; 6FXF; -.
DR PDBsum; 6G8O; -.
DR AlphaFoldDB; Q8K352; -.
DR SMR; Q8K352; -.
DR BioGRID; 216514; 1.
DR MINT; Q8K352; -.
DR STRING; 10090.ENSMUSP00000033427; -.
DR iPTMnet; Q8K352; -.
DR PhosphoSitePlus; Q8K352; -.
DR EPD; Q8K352; -.
DR jPOST; Q8K352; -.
DR MaxQB; Q8K352; -.
DR PaxDb; Q8K352; -.
DR PeptideAtlas; Q8K352; -.
DR PRIDE; Q8K352; -.
DR ProteomicsDB; 256731; -.
DR Antibodypedia; 381; 51 antibodies from 17 providers.
DR DNASU; 74131; -.
DR Ensembl; ENSMUST00000033427; ENSMUSP00000033427; ENSMUSG00000031101.
DR GeneID; 74131; -.
DR KEGG; mmu:74131; -.
DR UCSC; uc009tbw.1; mouse.
DR CTD; 54440; -.
DR MGI; MGI:1921381; Sash3.
DR VEuPathDB; HostDB:ENSMUSG00000031101; -.
DR eggNOG; KOG4384; Eukaryota.
DR GeneTree; ENSGT00940000160111; -.
DR HOGENOM; CLU_027875_0_0_1; -.
DR InParanoid; Q8K352; -.
DR OMA; DKEPTQK; -.
DR OrthoDB; 278880at2759; -.
DR PhylomeDB; Q8K352; -.
DR TreeFam; TF350709; -.
DR BioGRID-ORCS; 74131; 1 hit in 71 CRISPR screens.
DR ChiTaRS; Sly; mouse.
DR PRO; PR:Q8K352; -.
DR Proteomes; UP000000589; Chromosome X.
DR RNAct; Q8K352; protein.
DR Bgee; ENSMUSG00000031101; Expressed in thymus and 118 other tissues.
DR Genevisible; Q8K352; MM.
DR GO; GO:0005737; C:cytoplasm; IDA:MGI.
DR GO; GO:0005634; C:nucleus; IDA:MGI.
DR GO; GO:0001782; P:B cell homeostasis; IMP:MGI.
DR GO; GO:0042100; P:B cell proliferation; IMP:MGI.
DR GO; GO:0043367; P:CD4-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0048873; P:homeostasis of number of cells within a tissue; IMP:MGI.
DR GO; GO:0002821; P:positive regulation of adaptive immune response; IMP:MGI.
DR GO; GO:0030890; P:positive regulation of B cell proliferation; IMP:MGI.
DR GO; GO:0043372; P:positive regulation of CD4-positive, alpha-beta T cell differentiation; IMP:MGI.
DR GO; GO:0002639; P:positive regulation of immunoglobulin production; IMP:MGI.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:MGI.
DR GO; GO:0032733; P:positive regulation of interleukin-10 production; IMP:MGI.
DR GO; GO:0032743; P:positive regulation of interleukin-2 production; IMP:MGI.
DR GO; GO:0032753; P:positive regulation of interleukin-4 production; IMP:MGI.
DR GO; GO:0051251; P:positive regulation of lymphocyte activation; IMP:MGI.
DR GO; GO:0046622; P:positive regulation of organ growth; IMP:MGI.
DR GO; GO:0002726; P:positive regulation of T cell cytokine production; IMP:MGI.
DR GO; GO:0042102; P:positive regulation of T cell proliferation; IMP:MGI.
DR GO; GO:0032760; P:positive regulation of tumor necrosis factor production; IMP:MGI.
DR GO; GO:0042098; P:T cell proliferation; IMP:MGI.
DR CDD; cd11968; SH3_SASH3; 1.
DR Gene3D; 1.10.150.50; -; 1.
DR InterPro; IPR021090; rSAM/SH3_domain-containing.
DR InterPro; IPR001660; SAM.
DR InterPro; IPR013761; SAM/pointed_sf.
DR InterPro; IPR035722; SASH3.
DR InterPro; IPR035721; SASH3_SH3.
DR InterPro; IPR036028; SH3-like_dom_sf.
DR InterPro; IPR001452; SH3_domain.
DR PANTHER; PTHR12301:SF5; PTHR12301:SF5; 1.
DR Pfam; PF00536; SAM_1; 1.
DR Pfam; PF07653; SH3_2; 1.
DR Pfam; PF12485; SLY; 1.
DR SMART; SM00454; SAM; 1.
DR SMART; SM00326; SH3; 1.
DR SUPFAM; SSF47769; SSF47769; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR PROSITE; PS50105; SAM_DOMAIN; 1.
DR PROSITE; PS50002; SH3; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Phosphoprotein; Reference proteome; SH3 domain.
FT CHAIN 1..380
FT /note="SAM and SH3 domain-containing protein 3"
FT /id="PRO_0000071963"
FT DOMAIN 173..234
FT /note="SH3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192"
FT DOMAIN 252..316
FT /note="SAM"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184"
FT REGION 1..76
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 96..168
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 318..380
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..19
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 140..154
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 341..366
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 27
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75995"
FT MOD_RES 34
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75995"
FT MOD_RES 42
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 61
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75995"
FT MOD_RES 97
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75995"
FT MOD_RES 110
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75995"
FT MOD_RES 112
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O75995"
FT MOD_RES 113
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75995"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75995"
FT MOD_RES 318
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT CONFLICT 318
FT /note="T -> TA (in Ref. 3; AAH28773)"
FT /evidence="ECO:0000305"
FT HELIX 257..263
FT /evidence="ECO:0007829|PDB:6FXF"
FT HELIX 267..269
FT /evidence="ECO:0007829|PDB:6FXF"
FT HELIX 270..275
FT /evidence="ECO:0007829|PDB:6FXF"
FT HELIX 281..284
FT /evidence="ECO:0007829|PDB:6FXF"
FT HELIX 289..294
FT /evidence="ECO:0007829|PDB:6FXF"
FT HELIX 300..316
FT /evidence="ECO:0007829|PDB:6FXF"
SQ SEQUENCE 380 AA; 41609 MW; 8A3F19F0D79F66EB CRC64;
MLRRKPSNAS DKEPTQKKKL SLQRSSSFKD FAKSKPSSPV VSEKEFNLDD NIPEDDSGVL
TPEDSGKSGK KLGKKWRAVI SRTMNRKMGK MMVKALSEEM GDTLEEGSAS PTSPDCSLDS
PGPEKMALAF TEQEEREPPS LSRQTSTGSE LCSPGPGSGS FLEESPAPQY TGPFCGRARV
HTDFTPSPYD HDSLKLQKGD VIQIVEKPPV GTWLGLLNGK LGSFKFIYVD VLPEEAVGPV
RPSRRQSKGK RPKPKTLHEL LERIGLEEHT STLLLNGYQT LEDFKELRET HLNELNIMDP
QHRAKLLTAA ELLLDYDTGS EEAEEGAESS QEPVAHTVSE PKVDIPRDSG CFEGSESGRD
EAELAGTEEQ LQGLSLSGAP
