ID   D3YZU4_MOUSE            Unreviewed;      2159 AA.
AC   D3YZU4;
DT   20-APR-2010, integrated into UniProtKB/TrEMBL.
DT   20-APR-2010, sequence version 1.
DT   27-MAR-2024, entry version 102.
DE   SubName: Full=SH3 and multiple ankyrin repeat domains 1 {ECO:0000313|Ensembl:ENSMUSP00000103568.2};
GN   Name=Shank1 {ECO:0000313|Ensembl:ENSMUSP00000103568.2,
GN   ECO:0000313|MGI:MGI:3613677};
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 {ECO:0000313|Ensembl:ENSMUSP00000103568.2, ECO:0000313|Proteomes:UP000000589};
RN   [1] {ECO:0007829|PubMed:16452087}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=16452087; DOI=10.1074/mcp.T500041-MCP200;
RA   Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.;
RT   "Comprehensive identification of phosphorylation sites in postsynaptic
RT   density preparations.";
RL   Mol. Cell. Proteomics 5:914-922(2006).
RN   [2] {ECO:0007829|PubMed:18034455}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18034455; DOI=10.1021/pr0701254;
RA   Ballif B.A., Carey G.R., Sunyaev S.R., Gygi S.P.;
RT   "Large-scale identification and evolution indexing of tyrosine
RT   phosphorylation sites from murine brain.";
RL   J. Proteome Res. 7:311-318(2008).
RN   [3] {ECO:0000313|Ensembl:ENSMUSP00000103568.2, ECO:0000313|Proteomes:UP000000589}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000103568.2,
RC   ECO:0000313|Proteomes:UP000000589};
RX   PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA   Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA   Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA   Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA   Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA   Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA   Eichler E.E., Ponting C.P.;
RT   "Lineage-specific biology revealed by a finished genome assembly of the
RT   mouse.";
RL   PLoS Biol. 7:E1000112-E1000112(2009).
RN   [4] {ECO:0007829|PubMed:21183079}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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).
RN   [5] {ECO:0007829|PubMed:24129315}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24129315;
RA   Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA   Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA   Bedford M.T., Comb M.J.;
RT   "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT   methylation.";
RL   Mol. Cell. Proteomics 13:372-387(2014).
RN   [6] {ECO:0000313|Ensembl:ENSMUSP00000103568.2}
RP   IDENTIFICATION.
RC   STRAIN=C57BL/6J {ECO:0000313|Ensembl:ENSMUSP00000103568.2};
RG   Ensembl;
RL   Submitted (NOV-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Postsynaptic density
CC       {ECO:0000256|ARBA:ARBA00034105}.
CC   -!- SIMILARITY: Belongs to the SHANK family.
CC       {ECO:0000256|ARBA:ARBA00010508}.
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DR   RefSeq; XP_006540928.1; XM_006540865.3.
DR   SMR; D3YZU4; -.
DR   IntAct; D3YZU4; 2.
DR   MINT; D3YZU4; -.
DR   MaxQB; D3YZU4; -.
DR   PeptideAtlas; D3YZU4; -.
DR   ProteomicsDB; 344850; -.
DR   Antibodypedia; 18886; 245 antibodies from 27 providers.
DR   Ensembl; ENSMUST00000107935.8; ENSMUSP00000103568.2; ENSMUSG00000038738.16.
DR   GeneID; 243961; -.
DR   AGR; MGI:3613677; -.
DR   CTD; 50944; -.
DR   MGI; MGI:3613677; Shank1.
DR   VEuPathDB; HostDB:ENSMUSG00000038738; -.
DR   GeneTree; ENSGT00940000153561; -.
DR   OrthoDB; 2247290at2759; -.
DR   BioGRID-ORCS; 243961; 3 hits in 77 CRISPR screens.
DR   Proteomes; UP000000589; Chromosome 7.
DR   Bgee; ENSMUSG00000038738; Expressed in prefrontal cortex and 140 other cell types or tissues.
DR   ExpressionAtlas; D3YZU4; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:UniProt.
DR   GO; GO:0120025; C:plasma membrane bounded cell projection; IEA:UniProt.
DR   GO; GO:0014069; C:postsynaptic density; IEA:UniProtKB-SubCell.
DR   GO; GO:0050808; P:synapse organization; IEA:UniProt.
DR   CDD; cd17175; FERM_F0_SHANK1; 1.
DR   CDD; cd00992; PDZ_signaling; 1.
DR   CDD; cd09506; SAM_Shank1_2_3; 1.
DR   Gene3D; 2.30.42.10; -; 1.
DR   Gene3D; 1.25.40.20; Ankyrin repeat-containing domain; 1.
DR   Gene3D; 2.30.30.40; SH3 Domains; 1.
DR   Gene3D; 1.10.150.50; Transcription Factor, Ets-1; 1.
DR   InterPro; IPR002110; Ankyrin_rpt.
DR   InterPro; IPR036770; Ankyrin_rpt-contain_sf.
DR   InterPro; IPR001478; PDZ.
DR   InterPro; IPR041489; PDZ_6.
DR   InterPro; IPR036034; PDZ_sf.
DR   InterPro; IPR001660; SAM.
DR   InterPro; IPR013761; SAM/pointed_sf.
DR   InterPro; IPR036028; SH3-like_dom_sf.
DR   InterPro; IPR001452; SH3_domain.
DR   PANTHER; PTHR24135; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN; 1.
DR   PANTHER; PTHR24135:SF3; SH3 AND MULTIPLE ANKYRIN REPEAT DOMAINS PROTEIN 1; 1.
DR   Pfam; PF12796; Ank_2; 2.
DR   Pfam; PF17820; PDZ_6; 1.
DR   Pfam; PF00536; SAM_1; 1.
DR   Pfam; PF07653; SH3_2; 1.
DR   SMART; SM00248; ANK; 6.
DR   SMART; SM00228; PDZ; 1.
DR   SMART; SM00454; SAM; 1.
DR   SMART; SM00326; SH3; 1.
DR   SUPFAM; SSF48403; Ankyrin repeat; 1.
DR   SUPFAM; SSF50156; PDZ domain-like; 1.
DR   SUPFAM; SSF47769; SAM/Pointed domain; 1.
DR   SUPFAM; SSF50044; SH3-domain; 1.
DR   PROSITE; PS50297; ANK_REP_REGION; 1.
DR   PROSITE; PS50088; ANK_REPEAT; 3.
DR   PROSITE; PS50106; PDZ; 1.
DR   PROSITE; PS50105; SAM_DOMAIN; 1.
DR   PROSITE; PS50002; SH3; 1.
PE   1: Evidence at protein level;
KW   ANK repeat {ECO:0000256|PROSITE-ProRule:PRU00023};
KW   Cytoplasm {ECO:0000256|ARBA:ARBA00022490};
KW   Proteomics identification {ECO:0007829|MaxQB:D3YZU4,
KW   ECO:0007829|PeptideAtlas:D3YZU4};
KW   Reference proteome {ECO:0000313|Proteomes:UP000000589};
KW   Repeat {ECO:0000256|ARBA:ARBA00022737};
KW   SH3 domain {ECO:0000256|ARBA:ARBA00022443, ECO:0000256|PROSITE-
KW   ProRule:PRU00192}; Synapse {ECO:0000256|ARBA:ARBA00023018}.
FT   REPEAT          246..278
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          313..345
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   REPEAT          346..378
FT                   /note="ANK"
FT                   /evidence="ECO:0000256|PROSITE-ProRule:PRU00023"
FT   DOMAIN          554..613
FT                   /note="SH3"
FT                   /evidence="ECO:0000259|PROSITE:PS50002"
FT   DOMAIN          663..757
FT                   /note="PDZ"
FT                   /evidence="ECO:0000259|PROSITE:PS50106"
FT   DOMAIN          2096..2159
FT                   /note="SAM"
FT                   /evidence="ECO:0000259|PROSITE:PS50105"
FT   REGION          1..63
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          413..432
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          454..546
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          833..886
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          909..1225
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1237..1282
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1353..1409
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1492..1717
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1732..1782
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1820..1858
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1890..1980
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1994..2021
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1..20
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        454..495
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        500..514
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        917..938
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        996..1017
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1025..1042
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1058..1076
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1130..1149
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1157..1181
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1197..1216
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1369..1392
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1580..1611
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1614..1631
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1639..1668
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1683..1703
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1838..1854
FT                   /note="Pro residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1909..1940
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1953..1980
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   2159 AA;  225350 MW;  78EA8FD9E436C06F CRC64;
     MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPQGT RGRGSGAPGN LASTRGLQGR
     SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF
     QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL
     KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI
     DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL
     LYNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE
     TCARILLYRG ANKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR
     RGPPGAGLTV PPALLRANSD TSMALPDWMV FSAPGASSSG TPGPTSGSQG QSQPSAPSTK
     LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPRDGPAGG TGGSGGPGGS
     LGSRGRRRKL YSAVPGRSFM AVKSYQAQGE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV
     GWFPSDCLEE VANRSQEGRQ ESRSDKAKRL FRHYTVGSYD SFDAPSLIDG IDSGSDYIIK
     EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD
     FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA SQQAKRLPPP
     AISLRSKSMT SELEEMEYEQ QPAAVPSMEK KRTVYQMALN KLDEILAAAQ QTISASESPG
     PGGLASLGKH RPKGFFATES SFDPHHRSQP SYDRPSFLPP GPGLMLRQKS IGAAEDDRPY
     LAPPAMKFSR SLSVPGSEDI PPPPTTSPPE PPYSTPPAPS SSGRLTPSPR GGPFNPGSGG
     PLPASSPSSF DGPSPPDPRS GGREKSLYHS GALPPAHHHP PHHHHHHAPP PQPHHHHAHP
     PHPPEMETGG SPDDPPPRLA LGPQPSLRGW RGGGPSPTSG APSPSHHSSS GGSSGPAQAP
     ALRYFQLPPR AASAAMYVPA RSGRGRKGPL VKQTKVEGEP QKGSLPPASS PTSPALPRSE
     PPPAGPSEKN SIPIPTIIIK APSTSSSGRS SQGSSTEAEP PTQPDGAGGG GSSPSPAPAT
     SPVPPSPSPV PTPASPSGPA TLDFTSQFGA ALVGAARREG GWQNEARRRS TLFLSTDAGD
     EDGGDSGLGP GAPPGPRLRH SKSIDEGMFS AEPYLRLESG GSSGGYGAYA AGSRAYGGSG
     SSSAFTSFLP PRPLVHPLTG KALDPASPLG LALAARERAL KESSEGGVTP QPPPRPPSPR
     YDAPPPTLHH HSPHSPHSPH ARHEPVLRLW GDPARRELGY RAGLGSQEKA LTASPPAARR
     SLLHRLPPTA PGVGPLLLQL GPEPPTPHPG VSKAWRTAAP EEPERLPLHV RFLENCQARP
     PPAGTRGSST EDGPGVPPPS PRRVLPTSPT SPRGNEENGL PLLVLPPPAP SVDVDDGEFL
     FAEPLPPPLE FSNSFEKPES PLTPGPPHPL PDPPSPATPL PAAPPPAVAA APPTLDSTAS
     SLTSYDSEVA TLTQGAPAAP GDPPAPGPPA PAAPAPPAPQ PGPDPPPGTD SGIEEVDSRS
     SSDHPLETIS SASTLSSLSA EGGGNTGGVA GGGAGVASGT ELLDTYVAYL DGQAFGGSGT
     PGPPYPPQLM TPSKLRGRAL GTSGNLRPGP SGGLRDPVTP TSPTVSVTGA GTDGLLALSA
     CSGPSTAGVA GGPVAVEPEV PPVPLPTASS LPRKLLPWEE GPGPPPPPLP GPLSQPQASA
     LATVKASIIS ELSSKLQQFG GASTAGGALP WARGGSGGST DSHHGGASYI PERTSSLQRQ
     RLSEDSQTSL LSKPSSSIFQ NWPKPPLPPL PTGSGVSSST AAAPGATSPS ASSASASTRH
     LQGVEFEMRP PLLRRAPSPS LLPASDHKVS PAPRPSSLPI LPSGPLYPGL FDIRSSPTGG
     AGGSADPFAP VFVPPHPGIS GGLGGALSGA SRSLSPTRLL SLPPDKPFGA KPLGFWTKFD
     VADWLEWLGL SEHRAQFLDH EIDGSHLPAL TKEDYVDLGV TRVGHRMNID RALKFFLER
//