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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
     R
 
 
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