ID SHAN1_HUMAN Reviewed; 2161 AA. AC Q9Y566; A8MXP5; B7WNY6; Q9NYW9; DT 26-JUL-2002, integrated into UniProtKB/Swiss-Prot. DT 05-MAY-2009, sequence version 2. DT 24-JUL-2024, entry version 209. DE RecName: Full=SH3 and multiple ankyrin repeat domains protein 1; DE Short=Shank1; DE AltName: Full=Somatostatin receptor-interacting protein; DE Short=SSTR-interacting protein; DE Short=SSTRIP; GN Name=SHANK1; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), AND INTERACTION WITH RP SSTR2. RC TISSUE=Fetal brain, Hippocampus, and Thalamus; RX PubMed=10551867; DOI=10.1074/jbc.274.46.32997; RA Zitzer H., Hoenck H.-H., Baechner D., Richter D., Kreienkamp H.-J.; RT "Somatostatin receptor interacting protein defines a novel family of RT multidomain proteins present in human and rodent brain."; RL J. Biol. Chem. 274:32997-33001(1999). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15057824; DOI=10.1038/nature02399; RA Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., RA Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., RA Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., RA Carrano A.V., Caoile C., Chan Y.M., Christensen M., Cleland C.A., RA Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., RA Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., RA Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., RA Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., RA Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., RA McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., RA Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., RA Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., RA She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., RA Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., RA Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., RA Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., RA Rubin E.M., Lucas S.M.; RT "The DNA sequence and biology of human chromosome 19."; RL Nature 428:529-535(2004). RN [3] RP REVIEW. RX PubMed=10806096; DOI=10.1242/jcs.113.11.1851; RA Sheng M., Kim E.; RT "The Shank family of scaffold proteins."; RL J. Cell Sci. 113:1851-1856(2000). RN [4] RP INTERACTION WITH BAIAP2. RX PubMed=12504591; DOI=10.1006/mcne.2002.1201; RA Soltau M., Richter D., Kreienkamp H.-J.; RT "The insulin receptor substrate IRSp53 links postsynaptic shank1 to the RT small G-protein cdc42."; RL Mol. Cell. Neurosci. 21:575-583(2002). RN [5] RP VARIANTS [LARGE SCALE ANALYSIS] ASP-569 AND ARG-2026. RX PubMed=16959974; DOI=10.1126/science.1133427; RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., RA Velculescu V.E.; RT "The consensus coding sequences of human breast and colorectal cancers."; RL Science 314:268-274(2006). CC -!- FUNCTION: Seems to be an adapter protein in the postsynaptic density CC (PSD) of excitatory synapses that interconnects receptors of the CC postsynaptic membrane including NMDA-type and metabotropic glutamate CC receptors via complexes with GKAP/PSD-95 and Homer, respectively, and CC the actin-based cytoskeleton. Plays a role in the structural and CC functional organization of the dendritic spine and synaptic junction. CC -!- SUBUNIT: May homomultimerize via its SAM domain (By similarity). CC Interacts with the C-terminus of SSTR2 via the PDZ domain. Interacts CC with IGSF9, SHARPIN, SPTAN1, HOMER1 and DLGAP1/GKAP isoforms 1 and 2 CC (By similarity). Part of a complex with DLG4/PSD-95 and DLGAP1/GKAP (By CC similarity). Interacts with BAIAP2. Interacts with HOMER1 and HOMER3 CC (By similarity). {ECO:0000250, ECO:0000250|UniProtKB:Q9WV48, CC ECO:0000269|PubMed:10551867, ECO:0000269|PubMed:12504591}. CC -!- INTERACTION: CC Q9Y566; Q9BYF1: ACE2; NbExp=2; IntAct=EBI-3442234, EBI-7730807; CC Q9Y566; Q15349: RPS6KA2; NbExp=2; IntAct=EBI-3442234, EBI-1384149; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250}. Postsynaptic density CC {ECO:0000250}. Synapse {ECO:0000250}. Note=Colocalizes with alpha- CC latrotoxin receptor 1. {ECO:0000250}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=3; CC Name=1; Synonyms=A; CC IsoId=Q9Y566-1; Sequence=Displayed; CC Name=2; Synonyms=B; CC IsoId=Q9Y566-2; Sequence=VSP_006069, VSP_006070; CC Name=3; CC IsoId=Q9Y566-3; Sequence=VSP_006071; CC -!- TISSUE SPECIFICITY: Expressed in brain particularly in the amygdala, CC hippocampus, substantia nigra and thalamus. Isoform 2 seems to be CC expressed ubiquitously. CC -!- SIMILARITY: Belongs to the SHANK family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF163302; AAD45121.1; -; mRNA. DR EMBL; AF226728; AAF35887.1; -; mRNA. DR EMBL; AC008743; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AC010325; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR CCDS; CCDS12799.1; -. [Q9Y566-1] DR RefSeq; NP_057232.2; NM_016148.3. [Q9Y566-1] DR RefSeq; XP_006723296.1; XM_006723233.3. DR RefSeq; XP_011525316.1; XM_011527014.2. [Q9Y566-3] DR PDB; 6CPI; NMR; -; A=554-613. DR PDB; 6YWZ; X-ray; 2.12 A; A/B=654-762. DR PDB; 6YX0; X-ray; 1.57 A; A/B=654-762. DR PDB; 6YX1; X-ray; 1.80 A; A/B=654-762. DR PDB; 6YX2; X-ray; 1.62 A; A/B=654-762. DR PDB; 7A00; X-ray; 1.78 A; A/B=654-762. DR PDBsum; 6CPI; -. DR PDBsum; 6YWZ; -. DR PDBsum; 6YX0; -. DR PDBsum; 6YX1; -. DR PDBsum; 6YX2; -. DR PDBsum; 7A00; -. DR AlphaFoldDB; Q9Y566; -. DR SMR; Q9Y566; -. DR BioGRID; 119171; 28. DR DIP; DIP-40834N; -. DR ELM; Q9Y566; -. DR IntAct; Q9Y566; 41. DR MINT; Q9Y566; -. DR STRING; 9606.ENSP00000293441; -. DR GlyCosmos; Q9Y566; 4 sites, 1 glycan. DR GlyGen; Q9Y566; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; Q9Y566; -. DR PhosphoSitePlus; Q9Y566; -. DR BioMuta; SHANK1; -. DR DMDM; 229462779; -. DR MassIVE; Q9Y566; -. DR PaxDb; 9606-ENSP00000293441; -. DR PeptideAtlas; Q9Y566; -. DR ProteomicsDB; 86293; -. [Q9Y566-1] DR ProteomicsDB; 86294; -. [Q9Y566-2] DR ProteomicsDB; 86295; -. [Q9Y566-3] DR ABCD; Q9Y566; 2 sequenced antibodies. DR Antibodypedia; 18886; 239 antibodies from 27 providers. DR DNASU; 50944; -. DR Ensembl; ENST00000293441.6; ENSP00000293441.1; ENSG00000161681.17. [Q9Y566-1] DR Ensembl; ENST00000359082.3; ENSP00000351984.2; ENSG00000161681.17. [Q9Y566-3] DR GeneID; 50944; -. DR KEGG; hsa:50944; -. DR MANE-Select; ENST00000293441.6; ENSP00000293441.1; NM_016148.5; NP_057232.2. DR UCSC; uc002psw.2; human. [Q9Y566-1] DR AGR; HGNC:15474; -. DR CTD; 50944; -. DR DisGeNET; 50944; -. DR GeneCards; SHANK1; -. DR HGNC; HGNC:15474; SHANK1. DR HPA; ENSG00000161681; Tissue enriched (brain). DR MalaCards; SHANK1; -. DR MIM; 604999; gene. DR neXtProt; NX_Q9Y566; -. DR OpenTargets; ENSG00000161681; -. DR PharmGKB; PA37965; -. DR VEuPathDB; HostDB:ENSG00000161681; -. DR eggNOG; KOG0504; Eukaryota. DR eggNOG; KOG4375; Eukaryota. DR GeneTree; ENSGT00940000153561; -. DR HOGENOM; CLU_001824_1_0_1; -. DR InParanoid; Q9Y566; -. DR OMA; ENCRPTE; -. DR OrthoDB; 2247290at2759; -. DR PhylomeDB; Q9Y566; -. DR TreeFam; TF324593; -. DR PathwayCommons; Q9Y566; -. DR Reactome; R-HSA-6794361; Neurexins and neuroligins. DR SignaLink; Q9Y566; -. DR SIGNOR; Q9Y566; -. DR BioGRID-ORCS; 50944; 6 hits in 1150 CRISPR screens. DR ChiTaRS; SHANK1; human. DR GeneWiki; SHANK1; -. DR GenomeRNAi; 50944; -. DR Pharos; Q9Y566; Tbio. DR PRO; PR:Q9Y566; -. DR Proteomes; UP000005640; Chromosome 19. DR RNAct; Q9Y566; Protein. DR Bgee; ENSG00000161681; Expressed in anterior cingulate cortex and 130 other cell types or tissues. DR ExpressionAtlas; Q9Y566; baseline and differential. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0030425; C:dendrite; NAS:UniProtKB. DR GO; GO:0043197; C:dendritic spine; ISS:BHF-UCL. DR GO; GO:0060076; C:excitatory synapse; ISS:BHF-UCL. DR GO; GO:0098978; C:glutamatergic synapse; IEA:Ensembl. DR GO; GO:0016020; C:membrane; IDA:UniProtKB. DR GO; GO:0043005; C:neuron projection; ISS:BHF-UCL. DR GO; GO:0005886; C:plasma membrane; IDA:HPA. DR GO; GO:0014069; C:postsynaptic density; ISS:BHF-UCL. DR GO; GO:0045211; C:postsynaptic membrane; ISS:BHF-UCL. DR GO; GO:0098685; C:Schaffer collateral - CA1 synapse; IEA:Ensembl. DR GO; GO:0071532; F:ankyrin repeat binding; ISS:BHF-UCL. DR GO; GO:0042802; F:identical protein binding; ISS:BHF-UCL. DR GO; GO:0035255; F:ionotropic glutamate receptor binding; ISS:BHF-UCL. DR GO; GO:0044877; F:protein-containing complex binding; ISS:BHF-UCL. DR GO; GO:0097110; F:scaffold protein binding; ISS:BHF-UCL. DR GO; GO:0017124; F:SH3 domain binding; ISS:BHF-UCL. DR GO; GO:0031877; F:somatostatin receptor binding; ISS:BHF-UCL. DR GO; GO:0098919; F:structural constituent of postsynaptic density; IEA:Ensembl. DR GO; GO:0030160; F:synaptic receptor adaptor activity; ISS:BHF-UCL. DR GO; GO:0030534; P:adult behavior; IMP:BHF-UCL. DR GO; GO:0008306; P:associative learning; ISS:BHF-UCL. DR GO; GO:0060997; P:dendritic spine morphogenesis; ISS:BHF-UCL. DR GO; GO:0050894; P:determination of affect; IMP:BHF-UCL. DR GO; GO:0046959; P:habituation; IEA:Ensembl. DR GO; GO:0007616; P:long-term memory; ISS:BHF-UCL. DR GO; GO:0032232; P:negative regulation of actin filament bundle assembly; ISS:BHF-UCL. DR GO; GO:0050885; P:neuromuscular process controlling balance; ISS:BHF-UCL. DR GO; GO:0042048; P:olfactory behavior; IEA:Ensembl. DR GO; GO:0060999; P:positive regulation of dendritic spine development; ISS:BHF-UCL. DR GO; GO:2000463; P:positive regulation of excitatory postsynaptic potential; ISS:BHF-UCL. DR GO; GO:0035418; P:protein localization to synapse; ISS:BHF-UCL. DR GO; GO:0065003; P:protein-containing complex assembly; ISS:BHF-UCL. DR GO; GO:2000311; P:regulation of AMPA receptor activity; ISS:BHF-UCL. DR GO; GO:0060013; P:righting reflex; IEA:Ensembl. DR GO; GO:0035176; P:social behavior; IMP:BHF-UCL. DR GO; GO:0060074; P:synapse maturation; ISS:BHF-UCL. DR GO; GO:0071625; P:vocalization behavior; IMP:BHF-UCL. 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 InterPro; IPR051569; SHANK. 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 3D-structure; Alternative splicing; ANK repeat; Cytoplasm; Differentiation; KW Methylation; Neurogenesis; Phosphoprotein; Reference proteome; Repeat; KW SH3 domain; Synapse. FT CHAIN 1..2161 FT /note="SH3 and multiple ankyrin repeat domains protein 1" FT /id="PRO_0000174671" FT REPEAT 212..245 FT /note="ANK 1" FT REPEAT 246..278 FT /note="ANK 2" FT REPEAT 279..312 FT /note="ANK 3" FT REPEAT 313..345 FT /note="ANK 4" FT REPEAT 346..378 FT /note="ANK 5" FT REPEAT 379..395 FT /note="ANK 6" FT DOMAIN 554..613 FT /note="SH3" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00192" FT DOMAIN 663..757 FT /note="PDZ" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143" FT DOMAIN 2098..2161 FT /note="SAM" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00184" FT REGION 1..53 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 412..433 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 455..546 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 832..886 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 909..1229 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1241..1289 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1353..1720 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1734..1785 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1827..1860 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1892..1983 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 1996..2023 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 459..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 1125..1147 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1158..1183 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1201..1220 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1373..1390 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1513..1530 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1582..1613 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1616..1636 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1643..1670 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1685..1703 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1840..1856 FT /note="Pro residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1911..1941 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 1963..1983 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 186 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 540 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 544 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 671 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 791 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 890 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 950 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 1051 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 1090 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 1101 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 1253 FT /note="Asymmetric dimethylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 1287 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 1423 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 1436 FT /note="Phosphoserine" FT /evidence="ECO:0000250|UniProtKB:Q9WV48" FT MOD_RES 1895 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 2016 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 2036 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT MOD_RES 2074 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:D3YZU1" FT VAR_SEQ 1..613 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10551867" FT /id="VSP_006069" FT VAR_SEQ 614..654 FT /note="RSQESKQESRSDKAKRLFRHYTVGSYDSFDAPSLMDGIGPG -> MQLMALE FT QRFGSGLPGGGQPLCLMMSSPLPPPPPHFSCLPA (in isoform 2)" FT /evidence="ECO:0000303|PubMed:10551867" FT /id="VSP_006070" FT VAR_SEQ 646..654 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:10551867" FT /id="VSP_006071" FT VARIANT 6 FT /note="A -> V (in dbSNP:rs10423744)" FT /id="VAR_055318" FT VARIANT 569 FT /note="A -> D (in a colorectal cancer sample; somatic FT mutation)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036541" FT VARIANT 1504 FT /note="V -> A (in dbSNP:rs3745521)" FT /id="VAR_022123" FT VARIANT 2026 FT /note="G -> R (in a colorectal cancer sample; somatic FT mutation; dbSNP:rs200040610)" FT /evidence="ECO:0000269|PubMed:16959974" FT /id="VAR_036542" FT CONFLICT 927 FT /note="S -> Y (in Ref. 1; AAD45121/AAF35887)" FT /evidence="ECO:0000305" FT CONFLICT 937 FT /note="P -> T (in Ref. 1; AAD45121/AAF35887)" FT /evidence="ECO:0000305" FT CONFLICT 969 FT /note="S -> T (in Ref. 1; AAD45121/AAF35887)" FT /evidence="ECO:0000305" FT CONFLICT 1085 FT /note="F -> I (in Ref. 1; AAD45121/AAF35887)" FT /evidence="ECO:0000305" FT CONFLICT 1133 FT /note="T -> S (in Ref. 1; AAD45121/AAF35887)" FT /evidence="ECO:0000305" FT CONFLICT 1832 FT /note="S -> C (in Ref. 1; AAD45121/AAF35887)" FT /evidence="ECO:0000305" FT STRAND 559..563 FT /evidence="ECO:0007829|PDB:6CPI" FT STRAND 569..572 FT /evidence="ECO:0007829|PDB:6CPI" FT STRAND 580..586 FT /evidence="ECO:0007829|PDB:6CPI" FT STRAND 591..596 FT /evidence="ECO:0007829|PDB:6CPI" FT STRAND 599..604 FT /evidence="ECO:0007829|PDB:6CPI" FT HELIX 605..607 FT /evidence="ECO:0007829|PDB:6CPI" FT STRAND 656..667 FT /evidence="ECO:0007829|PDB:6YX0" FT STRAND 675..680 FT /evidence="ECO:0007829|PDB:6YX0" FT STRAND 694..696 FT /evidence="ECO:0007829|PDB:6YX2" FT STRAND 699..705 FT /evidence="ECO:0007829|PDB:6YX0" FT HELIX 710..714 FT /evidence="ECO:0007829|PDB:6YX0" FT STRAND 721..725 FT /evidence="ECO:0007829|PDB:6YX0" FT HELIX 735..744 FT /evidence="ECO:0007829|PDB:6YX0" FT TURN 745..747 FT /evidence="ECO:0007829|PDB:6YX0" FT STRAND 748..757 FT /evidence="ECO:0007829|PDB:6YX0" SQ SEQUENCE 2161 AA; 224959 MW; 94BDE56D3D5F319D CRC64; MTHSPATSED EERHSASECP EGGSESDSSP DGPGRGPRGT RGQGSGAPGS LASVRGLQGR SMSVPDDAHF SMMVFRIGIP DLHQTKCLRF NPDATIWTAK QQVLCALSES LQDVLNYGLF QPATSGRDAN FLEEERLLRE YPQSFEKGVP YLEFRYKTRV YKQTNLDEKQ LAKLHTKTGL KKFLEYVQLG TSDKVARLLD KGLDPNYHDS DSGETPLTLA AQTEGSVEVI RTLCLGGAHI DFRARDGMTA LHKAACARHC LALTALLDLG GSPNYKDRRG LTPLFHTAMV GGDPRCCELL LFNRAQLGIA DENGWQEIHQ ACQRGHSQHL EHLLFYGAEP GAQNASGNTA LHICALYNKE TCARILLYRG ADKDVKNNNG QTPFQVAVIA GNFELGELIR NHREQDVVPF QESPKYAARR RGPPGTGLTV PPALLRANSD TSMALPDWMV FSAPGAASSG APGPTSGSQG QSQPSAPTTK LSSGTLRSAS SPRGARARSP SRGRHPEDAK RQPRGRPSSS GTPREGPAGG TGGSGGPGGS LGSRGRRRKL YSAVPGRSFM AVKSYQAQAE GEISLSKGEK IKVLSIGEGG FWEGQVKGRV GWFPSDCLEE VANRSQESKQ ESRSDKAKRL FRHYTVGSYD SFDAPSLMDG IGPGSDYIIK EKTVLLQKKD SEGFGFVLRG AKAQTPIEEF TPTPAFPALQ YLESVDEGGV AWRAGLRMGD FLIEVNGQNV VKVGHRQVVN MIRQGGNTLM VKVVMVTRHP DMDEAVHKKA PQQAKRLPPP TISLRSKSMT SELEEMEYEQ QPAPVPSMEK KRTVYQMALN KLDEILAAAQ QTISASESPG PGGLASLGKH RPKGFFATES SFDPHHRAQP SYERPSFLPP GPGLMLRQKS IGAAEDDRPY LAPPAMKFSR SLSVPGSEDI PPPPTTSPPE PPYSTPPVPS SSGRLTPSPR GGPFNPGSGG PLPASSPASF DGPSPPDTRV GSREKSLYHS GPLPPAHHHP PHHHHHHAPP PQPHHHHAHP PHPPEMETGG SPDDPPPRLA LGPQPSLRGW RGGGPSPTPG APSPSHHGSA GGGGGSSQGP ALRYFQLPPR AASAAMYVPA RSGRGRKGPL VKQTKVEGEP QKGGGLPPAP SPTSPASPQP PPAVAAPSEK NSIPIPTIII KAPSTSSSGR SSQGSSTEAE PPTQPEPTGG GGGGGSSPSP APAMSPVPPS PSPVPTPASP SGPATLDFTS QFGAALVGAA RREGGWQNEA RRRSTLFLST DAGDEDGGDG GLGTGAAPGP RLRHSKSIDE GMFSAEPYLR LESAGSGAGY GGYGAGSRAY GGGGGSSAFT SFLPPRPLVH PLTGKALDPA SPLGLALAAR ERALKESSEG GGAPQPPPRP PSPRYEAPPP TPHHHSPHAH HEPVLRLWGA SPPDPARREL GYRAGLGSQE KSLPASPPAA RRSLLHRLPP TAPGVGPLLL QLGTEPPAPH PGVSKPWRSA APEEPERLPL HVRFLENCQP RAPVTSGRGP PSEDGPGVPP PSPRRSVPPS PTSPRASEEN GLPLLVLPPP APSVDVEDGE FLFVEPLPPP LEFSNSFEKP ESPLTPGPPH PLPDTPAPAT PLPPVPPPAV AAAPPTLDST ASSLTSYDSE VATLTQGASA APGDPHPPGP PAPAAPAPAA PQPGPDPPPG TDSGIEEVDS RSSSDHPLET ISSASTLSSL SAEGGGSAGG GGGAGAGVAS GPELLDTYVA YLDGQAFGGS STPGPPYPPQ LMTPSKLRGR ALGASGGLRP GPSGGLRDPV TPTSPTVSVT GAGTDGLLAL RACSGPPTAG VAGGPVAVEP EVPPVPLPTA SSLPRKLLPW EEGPGPPPPP LPGPLAQPQA SALATVKASI ISELSSKLQQ FGGSSAAGGA LPWARGGSGG GGDSHHGGAS YVPERTSSLQ RQRLSDDSQS SLLSKPVSSL FQNWPKPPLP PLPTGTGVSP TAAAAPGATS PSASSSSTST RHLQGVEFEM RPPLLRRAPS PSLLPASEHK VSPAPRPSSL PILPSGPLYP GLFDIRGSPT GGAGGSADPF APVFVPPHPG ISGGLGGALS GASRSLSPTR LLSLPPDKPF GAKPLGFWTK FDVADWLEWL GLAEHRAQFL DHEIDGSHLP ALTKEDYVDL GVTRVGHRMN IDRALKFFLE R //