SHAN1_HUMAN
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 03-AUG-2022, entry version 199.
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}.
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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; 25.
DR DIP; DIP-40834N; -.
DR ELM; Q9Y566; -.
DR IntAct; Q9Y566; 26.
DR MINT; Q9Y566; -.
DR STRING; 9606.ENSP00000293441; -.
DR GlyGen; Q9Y566; 4 sites, 1 O-linked glycan (4 sites).
DR iPTMnet; Q9Y566; -.
DR PhosphoSitePlus; Q9Y566; -.
DR BioMuta; SHANK1; -.
DR DMDM; 229462779; -.
DR EPD; Q9Y566; -.
DR MassIVE; Q9Y566; -.
DR MaxQB; Q9Y566; -.
DR PaxDb; Q9Y566; -.
DR PeptideAtlas; Q9Y566; -.
DR PRIDE; 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; 232 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 CTD; 50944; -.
DR DisGeNET; 50944; -.
DR GeneCards; SHANK1; -.
DR HGNC; HGNC:15474; SHANK1.
DR HPA; ENSG00000161681; Tissue enriched (brain).
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; DYEPAMG; -.
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 1070 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 129 other tissues.
DR ExpressionAtlas; Q9Y566; baseline and differential.
DR Genevisible; Q9Y566; HS.
DR GO; GO:0070161; C:anchoring junction; IEA:UniProtKB-KW.
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:0008022; F:protein C-terminus 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: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 Gene3D; 1.10.150.50; -; 1.
DR Gene3D; 1.25.40.20; -; 1.
DR Gene3D; 2.30.42.10; -; 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 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; SSF47769; SSF47769; 1.
DR SUPFAM; SSF48403; SSF48403; 1.
DR SUPFAM; SSF50044; SSF50044; 1.
DR SUPFAM; SSF50156; SSF50156; 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
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