LOCUS       NP_057232               2161 aa            linear   PRI 27-APR-2025
DEFINITION  SH3 and multiple ankyrin repeat domains protein 1 [Homo sapiens].
ACCESSION   NP_057232 XP_006723296
VERSION     NP_057232.2
DBSOURCE    REFSEQ: accession NM_016148.5
KEYWORDS    RefSeq; MANE Select.
SOURCE      Homo sapiens (human)
  ORGANISM  Homo sapiens
            Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
            Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
            Catarrhini; Hominidae; Homo.
REFERENCE   1  (residues 1 to 2161)
  AUTHORS   Qin,Y., Du,Y., Chen,L., Liu,Y., Xu,W., Liu,Y., Li,Y., Leng,J.,
            Wang,Y., Zhang,X.Y., Feng,J., Zhang,F., Jin,L., Qiu,Z., Gong,X. and
            Wang,H.
  TITLE     A recurrent SHANK1 mutation implicated in autism spectrum disorder
            causes autistic-like core behaviors in mice via downregulation of
            mGluR1-IP3R1-calcium signaling
  JOURNAL   Mol Psychiatry 27 (7), 2985-2998 (2022)
   PUBMED   35388181
  REMARK    GeneRIF: A recurrent SHANK1 mutation implicated in autism spectrum
            disorder causes autistic-like core behaviors in mice via
            downregulation of mGluR1-IP3R1-calcium signaling.
            Erratum:[Mol Psychiatry. 2022 Sep;27(9):3922. doi:
            10.1038/s41380-022-01605-8. PMID: 35538194]
REFERENCE   2  (residues 1 to 2161)
  AUTHORS   Caillet-Saguy,C. and Wolff,N.
  TITLE     PDZ-Containing Proteins Targeted by the ACE2 Receptor
  JOURNAL   Viruses 13 (11), 2281 (2021)
   PUBMED   34835087
  REMARK    Publication Status: Online-Only
REFERENCE   3  (residues 1 to 2161)
  AUTHORS   May,H.J., Jeong,J., Revah-Politi,A., Cohen,J.S., Chassevent,A.,
            Baptista,J., Baugh,E.H., Bier,L., Bottani,A., Carminho A
            Rodrigues,M.T., Conlon,C., Fluss,J., Guipponi,M., Kim,C.A.,
            Matsumoto,N., Person,R., Primiano,M., Rankin,J., Shinawi,M.,
            Smith-Hicks,C., Telegrafi,A., Toy,S., Uchiyama,Y., Aggarwal,V.,
            Goldstein,D.B., Roche,K.W. and Anyane-Yeboa,K.
  TITLE     Truncating variants in the SHANK1 gene are associated with a
            spectrum of neurodevelopmental disorders
  JOURNAL   Genet Med 23 (10), 1912-1921 (2021)
   PUBMED   34113010
  REMARK    GeneRIF: Truncating variants in the SHANK1 gene are associated with
            a spectrum of neurodevelopmental disorders.
REFERENCE   4  (residues 1 to 2161)
  AUTHORS   Kliche,J., Kuss,H., Ali,M. and Ivarsson,Y.
  TITLE     Cytoplasmic short linear motifs in ACE2 and integrin beta3 link
            SARS-CoV-2 host cell receptors to mediators of endocytosis and
            autophagy
  JOURNAL   Sci Signal 14 (665) (2021)
   PUBMED   33436498
  REMARK    Publication Status: Online-Only
REFERENCE   5  (residues 1 to 2161)
  AUTHORS   Fu,Y., Liu,D., Guo,J., Long,H., Xiao,W., Xiao,W., Feng,L., Luo,Z.
            and Xiao,B.
  TITLE     Dynamic Change of Shanks Gene mRNA Expression and DNA Methylation
            in Epileptic Rat Model and Human Patients
  JOURNAL   Mol Neurobiol 57 (9), 3712-3726 (2020)
   PUBMED   32564287
  REMARK    GeneRIF: Dynamic Change of Shanks Gene mRNA Expression and DNA
            Methylation in Epileptic Rat Model and Human Patients.
REFERENCE   6  (residues 1 to 2161)
  AUTHORS   Tobaben,S., Sudhof,T.C. and Stahl,B.
  TITLE     The G protein-coupled receptor CL1 interacts directly with proteins
            of the Shank family
  JOURNAL   J Biol Chem 275 (46), 36204-36210 (2000)
   PUBMED   10958799
REFERENCE   7  (residues 1 to 2161)
  AUTHORS   Sheng,M. and Kim,E.
  TITLE     The Shank family of scaffold proteins
  JOURNAL   J Cell Sci 113 (Pt 11), 1851-1856 (2000)
   PUBMED   10806096
  REMARK    Review article
REFERENCE   8  (residues 1 to 2161)
  AUTHORS   Zitzer,H., Honck,H.H., Bachner,D., Richter,D. and Kreienkamp,H.J.
  TITLE     Somatostatin receptor interacting protein defines a novel family of
            multidomain proteins present in human and rodent brain
  JOURNAL   J Biol Chem 274 (46), 32997-33001 (1999)
   PUBMED   10551867
REFERENCE   9  (residues 1 to 2161)
  AUTHORS   Tu,J.C., Xiao,B., Naisbitt,S., Yuan,J.P., Petralia,R.S.,
            Brakeman,P., Doan,A., Aakalu,V.K., Lanahan,A.A., Sheng,M. and
            Worley,P.F.
  TITLE     Coupling of mGluR/Homer and PSD-95 complexes by the Shank family of
            postsynaptic density proteins
  JOURNAL   Neuron 23 (3), 583-592 (1999)
   PUBMED   10433269
REFERENCE   10 (residues 1 to 2161)
  AUTHORS   Naisbitt,S., Kim,E., Tu,J.C., Xiao,B., Sala,C., Valtschanoff,J.,
            Weinberg,R.J., Worley,P.F. and Sheng,M.
  TITLE     Shank, a novel family of postsynaptic density proteins that binds
            to the NMDA receptor/PSD-95/GKAP complex and cortactin
  JOURNAL   Neuron 23 (3), 569-582 (1999)
   PUBMED   10433268
COMMENT     VALIDATED REFSEQ: This record has undergone validation or
            preliminary review. The reference sequence was derived from
            AC010325.7, EU872208.1, AF163302.1 and AC008743.9.
            
            On or before Jun 15, 2017 this sequence version replaced
            XP_006723296.1, NP_057232.1.
            
            Summary: This gene encodes a member of the SHANK (SH3 domain and
            ankyrin repeat containing) family of proteins. Members of this
            family act as scaffold proteins that are required for the
            development and function of neuronal synapses. Deletions in this
            gene may be associated with autism spectrum disorder in males.
            [provided by RefSeq, Apr 2016].
            
            Sequence Note: This RefSeq record was created from transcript and
            genomic sequence data to make the sequence consistent with the
            reference genome assembly. The genomic coordinates used for the
            transcript record were based on transcript alignments and RNA-seq
            data.
            
            Publication Note:  This RefSeq record includes a subset of the
            publications that are available for this gene. Please see the Gene
            record to access additional publications.
            
            ##Evidence-Data-START##
            CDS exon combination :: AF163302.1 [ECO:0000331]
            RNAseq introns       :: mixed sample support SAMEA1965299,
                                    SAMEA1966682 [ECO:0006172]
            ##Evidence-Data-END##
            
            ##RefSeq-Attributes-START##
            inferred exon combination :: based on alignments, homology
            MANE Ensembl match        :: ENST00000293441.6/ ENSP00000293441.1
            RefSeq Select criteria    :: based on manual assertion,
                                         conservation, expression
            ##RefSeq-Attributes-END##
FEATURES             Location/Qualifiers
     source          1..2161
                     /organism="Homo sapiens"
                     /db_xref="taxon:9606"
                     /chromosome="19"
                     /map="19q13.33"
     Protein         1..2161
                     /product="SH3 and multiple ankyrin repeat domains protein
                     1"
                     /note="somatostatin receptor-interacting protein;
                     SSTR-interacting protein"
                     /calculated_mol_wt=224829
     Region          1..53
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          70..158
                     /region_name="FERM_F0_SHANK1"
                     /note="FERM (Four.1 protein, Ezrin, Radixin, Moesin)
                     domain, F0 sub-domain, found in SH3 and multiple ankyrin
                     repeat domains protein 1 (SHANK1); cd17175"
                     /db_xref="CDD:340695"
     Region          166..407
                     /region_name="ANKYR"
                     /note="Ankyrin repeat [Signal transduction mechanisms];
                     COG0666"
                     /db_xref="CDD:440430"
     Site            186
                     /site_type="phosphorylation"
                     /note="Phosphotyrosine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          212..245
                     /region_name="ANK 1"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          212..244
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Site            order(246,248,252..253,256..258,260..261,265,268,277,279,
                     281,319..320,323..325,327..328,332,335,344,346,348,
                     352..353,356..358,360..361,365,368,377)
                     /site_type="other"
                     /note="oligomer interface [polypeptide binding]"
                     /db_xref="CDD:293786"
     Region          246..278
                     /region_name="ANK 2"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          246..277
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          279..344
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          279..312
                     /region_name="ANK 3"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          313..345
                     /region_name="ANK 4"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          346..378
                     /region_name="ANK 5"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          346..377
                     /region_name="ANK repeat"
                     /note="ANK repeat [structural motif]"
                     /db_xref="CDD:293786"
     Region          379..395
                     /region_name="ANK 6"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          412..433
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          455..546
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            540
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            544
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          557..608
                     /region_name="SH3"
                     /note="Src Homology 3 domain superfamily; cl17036"
                     /db_xref="CDD:473055"
     Site            order(563,565,568,572,590..591,604,606..607)
                     /site_type="other"
                     /note="peptide ligand binding site [polypeptide binding]"
                     /db_xref="CDD:212690"
     Region          656..757
                     /region_name="PDZ_SHANK1_3-like"
                     /note="PDZ domain of SH3 and multiple ankyrin repeat
                     domains protein 1 (SHANK1), SHANK2, SHANK3, and related
                     domains; cd06746"
                     /db_xref="CDD:467228"
     Site            order(656..661,691..694,729,731,754)
                     /site_type="other"
                     /note="homodimer interface [polypeptide binding]"
                     /db_xref="CDD:467228"
     Site            671
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            order(673..679,703,706,735,739,742..743)
                     /site_type="other"
                     /note="peptide binding site [polypeptide binding]"
                     /db_xref="CDD:467228"
     Site            791
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          832..886
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            890
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          909..1229
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            950
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            1051
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            1090
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            1101
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          1241..1289
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            1253
                     /site_type="methylation"
                     /note="Asymmetric dimethylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            1287
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          1353..1720
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            1423
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            1436
                     /site_type="phosphorylation"
                     /note="Phosphoserine.
                     /evidence=ECO:0000250|UniProtKB:Q9WV48; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          1734..1785
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          1827..1860
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          1892..1983
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            1895
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          1996..2023
                     /region_name="Disordered.
                     /evidence=ECO:0000256|SAM:MobiDB-lite"
                     /note="propagated from UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            2016
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            2036
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Site            2074
                     /site_type="methylation"
                     /note="Omega-N-methylarginine.
                     /evidence=ECO:0000250|UniProtKB:D3YZU1; propagated from
                     UniProtKB/Swiss-Prot (Q9Y566.2)"
     Region          2094..2159
                     /region_name="SAM_Shank1,2,3"
                     /note="SAM domain of Shank1,2,3 family proteins; cd09506"
                     /db_xref="CDD:188905"
     Site            order(2097..2099,2101,2115..2116,2129)
                     /site_type="other"
                     /note="polymer interface (interfiber) [polypeptide
                     binding]"
                     /db_xref="CDD:188905"
     Site            order(2114..2115,2147)
                     /site_type="other"
                     /note="Zn binding site [ion binding]"
                     /db_xref="CDD:188905"
     Site            order(2138,2140,2145)
                     /site_type="other"
                     /note="polymer interface (intrafiber) [polypeptide
                     binding]"
                     /db_xref="CDD:188905"
     CDS             1..2161
                     /gene="SHANK1"
                     /gene_synonym="SPANK-1; SSTRIP; synamon"
                     /coded_by="NM_016148.5:441..6926"
                     /db_xref="CCDS:CCDS12799.1"
                     /db_xref="GeneID:50944"
                     /db_xref="HGNC:HGNC:15474"
                     /db_xref="MIM:604999"
ORIGIN      
        1 mthspatsed eerhsasecp eggsesdssp dgpgrgprgt rgqgsgapgs lasvrglqgr
       61 smsvpddahf smmvfrigip dlhqtkclrf npdatiwtak qqvlcalses lqdvlnyglf
      121 qpatsgrdan fleeerllre ypqsfekgvp ylefryktrv ykqtnldekq laklhtktgl
      181 kkfleyvqlg tsdkvarlld kgldpnyhds dsgetpltla aqtegsvevi rtlclggahi
      241 dfrardgmta lhkaacarhc laltalldlg gspnykdrrg ltplfhtamv ggdprccell
      301 lfnraqlgia dengwqeihq acqrghsqhl ehllfygaep gaqnasgnta lhicalynke
      361 tcarillyrg adkdvknnng qtpfqvavia gnfelgelir nhreqdvvpf qespkyaarr
      421 rgppgtgltv ppallransd tsmalpdwmv fsapgaassg apgptsgsqg qsqpsapttk
      481 lssgtlrsas sprgararsp srgrhpedak rqprgrpsss gtpregpagg tggsggpggs
      541 lgsrgrrrkl ysavpgrsfm avksyqaqae geislskgek ikvlsigegg fwegqvkgrv
      601 gwfpsdclee vanrsqeskq esrsdkakrl frhytvgsyd sfdapslmdg igpgsdyiik
      661 ektvllqkkd segfgfvlrg akaqtpieef tptpafpalq ylesvdeggv awraglrmgd
      721 flievngqnv vkvghrqvvn mirqggntlm vkvvmvtrhp dmdeavhkka pqqakrlppp
      781 tislrsksmt seleemeyeq qpapvpsmek krtvyqmaln kldeilaaaq qtisasespg
      841 pgglaslgkh rpkgffates sfdphhraqp syerpsflpp gpglmlrqks igaaeddrpy
      901 lappamkfsr slsvpgsedi ppppttsppe ppystppvps ssgrltpspr ggpfnpgsgg
      961 plpasspasf dgpsppdtrv gsrekslyhs gplppahhhp phhhhhhapp pqphhhhahp
     1021 phppemetgg spddppprla lgpqpslrgw rgggpsptpg apspshhgsa gggggssqgp
     1081 alryfqlppr aasaamyvpa rsgrgrkgpl vkqtkvegep qkggglppap sptspaspqp
     1141 ppavaapsek nsipiptiii kapstsssgr ssqgssteae pptqpeptgg gggggsspsp
     1201 apamspvpps pspvptpasp sgpatldfts qfgaalvgaa rreggwqnea rrrstlflst
     1261 dagdedggdg glgtgaapgp rlrhskside gmfsaepylr lesagsgagy ggygagsray
     1321 gggggssaft sflpprplvh pltgkaldpa splglalaar eralkesseg ggapqppprp
     1381 pspryeappp tphhhsphah hepvlrlwga sppdparrel gyraglgsqe kslpasppaa
     1441 rrsllhrlpp tapgvgplll qlgteppaph pgvskpwrsa apeeperlpl hvrflencqp
     1501 rapvtsgrgp psedgpgvpp psprrsvpps ptspraseen glpllvlppp apsvdvedge
     1561 flfveplppp lefsnsfekp espltpgpph plpdtpapat plppvpppav aaapptldst
     1621 assltsydse vatltqgasa apgdphppgp papaapapaa pqpgpdpppg tdsgieevds
     1681 rsssdhplet issastlssl saegggsagg gggagagvas gpelldtyva yldgqafggs
     1741 stpgppyppq lmtpsklrgr algasgglrp gpsgglrdpv tptsptvsvt gagtdgllal
     1801 racsgpptag vaggpvavep evppvplpta sslprkllpw eegpgppppp lpgplaqpqa
     1861 salatvkasi iselssklqq fggssaagga lpwarggsgg ggdshhggas yvpertsslq
     1921 rqrlsddsqs sllskpvssl fqnwpkpplp plptgtgvsp taaaapgats psasssstst
     1981 rhlqgvefem rppllrraps psllpasehk vspaprpssl pilpsgplyp glfdirgspt
     2041 ggaggsadpf apvfvpphpg isgglggals gasrslsptr llslppdkpf gakplgfwtk
     2101 fdvadwlewl glaehraqfl dheidgshlp altkedyvdl gvtrvghrmn idralkffle
     2161 r
//
