SCRIB_MOUSE
ID SCRIB_MOUSE Reviewed; 1612 AA.
AC Q80U72; Q6P5H7; Q7TPH8; Q80VB1; Q8CI48; Q8VII1; Q922S3;
DT 19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
DT 19-JUL-2004, sequence version 2.
DT 03-AUG-2022, entry version 178.
DE RecName: Full=Protein scribble homolog;
DE Short=Scribble;
DE AltName: Full=Protein LAP4;
GN Name=Scrib; Synonyms=Kiaa0147, Lap4, Scrib1;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum;
RA Mattock K.L., Kurschner C.;
RT "Molecular cloning of mouse Scribble cDNA.";
RL Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Brain;
RX PubMed=12693553; DOI=10.1093/dnares/10.1.35;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
RA Nakajima D., Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: II.
RT The complete nucleotide sequences of 400 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 10:35-48(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 694-1336 (ISOFORM 1).
RX PubMed=15649318; DOI=10.1186/1471-2121-6-1;
RA Petit M.M.R., Meulemans S.M.P., Alen P., Ayoubi T.A.Y., Jansen E.,
RA Van de Ven W.J.M.;
RT "The tumor suppressor Scrib interacts with the zyxin-related protein LPP,
RT which shuttles between cell adhesion sites and the nucleus.";
RL BMC Cell Biol. 6:1-1(2005).
RN [5]
RP FUNCTION, AND DEVELOPMENTAL STAGE.
RX PubMed=12499390; DOI=10.1093/hmg/ddg014;
RA Murdoch J.N., Henderson D.J., Doudney K., Gaston-Massuet C., Phillips H.M.,
RA Paternotte C., Arkell R., Stanier P., Copp A.J.;
RT "Disruption of scribble (Scrb1) causes severe neural tube defects in the
RT circletail mouse.";
RL Hum. Mol. Genet. 12:87-98(2003).
RN [6]
RP INTERACTION WITH ARHGEF7 AND GIT1, AND TISSUE SPECIFICITY.
RX PubMed=15182672; DOI=10.1016/j.cub.2004.05.051;
RA Audebert S., Navarro C., Nourry C., Chasserot-Golaz S., Lecine P.,
RA Bellaiche Y., Dupont J.-L., Premont R.T., Sempere C., Strub J.-M.,
RA Van Dorsselaer A., Vitale N., Borg J.-P.;
RT "Mammalian Scribble forms a tight complex with the betaPIX exchange
RT factor.";
RL Curr. Biol. 14:987-995(2004).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1548, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic brain;
RX PubMed=15345747; DOI=10.1074/mcp.m400085-mcp200;
RA Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
RT "Phosphoproteomic analysis of the developing mouse brain.";
RL Mol. Cell. Proteomics 3:1093-1101(2004).
RN [8]
RP INTERACTION WITH MAPK12.
RX PubMed=15878399; DOI=10.1016/j.bbamcr.2004.11.008;
RA Court N.W., Ingley E., Klinken S.P., Bogoyevitch M.A.;
RT "Outer membrane protein 25-a mitochondrial anchor and inhibitor of stress-
RT activated protein kinase-3.";
RL Biochim. Biophys. Acta 1744:68-75(2005).
RN [9]
RP TISSUE SPECIFICITY.
RX PubMed=15806148; DOI=10.1038/sj.onc.1208632;
RA Navarro C., Nola S., Audebert S., Santoni M.-J., Arsanto J.-P.,
RA Ginestier C., Marchetto S., Jacquemier J., Isnardon D., Le Bivic A.,
RA Birnbaum D., Borg J.-P.;
RT "Junctional recruitment of mammalian Scribble relies on E-cadherin
RT engagement.";
RL Oncogene 24:4330-4339(2005).
RN [10]
RP INTERACTION WITH APC AND CTNNB1, AND SUBCELLULAR LOCATION.
RX PubMed=16611247; DOI=10.1111/j.1365-2443.2006.00954.x;
RA Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K., Yasugi T.,
RA Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T., Taketani Y.;
RT "Human scribble, a novel tumor suppressor identified as a target of high-
RT risk HPV E6 for ubiquitin-mediated degradation, interacts with adenomatous
RT polyposis coli.";
RL Genes Cells 11:453-464(2006).
RN [11]
RP INTERACTION WITH VANGL2.
RX PubMed=16687519; DOI=10.1523/jneurosci.4680-05.2006;
RA Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A.,
RA Rachel R.A., Copeland N.G., Jenkins N.A., Bogani D., Murdoch J.,
RA Warchol M.E., Wenthold R.J., Kelley M.W.;
RT "Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms for
RT planar cell polarity in mammals.";
RL J. Neurosci. 26:5265-5275(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-674; THR-675 AND SER-1206,
RP AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=17242355; DOI=10.1073/pnas.0609836104;
RA Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
RT "Large-scale phosphorylation analysis of mouse liver.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
RN [13]
RP FUNCTION, INTERACTION WITH CRTAM, SUBCELLULAR LOCATION, AND TISSUE
RP SPECIFICITY.
RX PubMed=18329370; DOI=10.1016/j.cell.2008.01.013;
RA Yeh J.H., Sidhu S.S., Chan A.C.;
RT "Regulation of a late phase of T cell polarity and effector functions by
RT Crtam.";
RL Cell 132:846-859(2008).
RN [14]
RP FUNCTION.
RX PubMed=19041750; DOI=10.1016/j.cell.2008.09.045;
RA Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C.,
RA Muthuswamy S.K.;
RT "Deregulation of scribble promotes mammary tumorigenesis and reveals a role
RT for cell polarity in carcinoma.";
RL Cell 135:865-878(2008).
RN [15]
RP FUNCTION IN CELL MIGRATION, AND INTERACTION WITH PAK1 AND PAK2.
RX PubMed=18716323; DOI=10.1093/hmg/ddn248;
RA Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
RA Navarro C., Rachel R., Montcouquiol M., Sans N., Etienne-Manneville S.,
RA Borg J.-P., Santoni M.-J.;
RT "Scrib regulates PAK activity during the cell migration process.";
RL Hum. Mol. Genet. 17:3552-3565(2008).
RN [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1206 AND SER-1548, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
RA Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
RA Thibault P.;
RT "The phagosomal proteome in interferon-gamma-activated macrophages.";
RL Immunity 30:143-154(2009).
RN [17]
RP FUNCTION, AND INTERACTION WITH CTNNB1.
RX PubMed=19458197; DOI=10.1091/mbc.e08-12-1172;
RA Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.;
RT "Scribble interacts with beta-catenin to localize synaptic vesicles to
RT synapses.";
RL Mol. Biol. Cell 20:3390-3400(2009).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583; THR-674; THR-675;
RP SER-925; SER-1206; SER-1292; SER-1361; SER-1457; SER-1490; SER-1529;
RP SER-1543 AND SER-1548, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1320
RP (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1299 (ISOFORM
RP 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas,
RC Spleen, and Testis;
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 [19]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1312 (ISOFORM 3), METHYLATION
RP [LARGE SCALE ANALYSIS] AT ARG-1291 (ISOFORM 4), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, and Embryo;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
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).
CC -!- FUNCTION: Scaffold protein involved in different aspects of polarized
CC cell differentiation regulating epithelial and neuronal morphogenesis
CC and T-cell polarization (PubMed:12499390, PubMed:18716323,
CC PubMed:19041750, PubMed:18329370). Via its interaction with CRTAM,
CC required for the late phase polarization of a subset of CD4+ T-cells,
CC which in turn regulates TCR-mediated proliferation and IFNG and IL22
CC production (PubMed:18329370). Most probably functions in the
CC establishment of apico-basal cell polarity (PubMed:19041750). May
CC function in cell proliferation regulating progression from G1 to S
CC phase and as a positive regulator of apoptosis for instance during
CC acinar morphogenesis of the mammary epithelium (PubMed:19041750). May
CC also function in cell migration and adhesion and hence regulate cell
CC invasion through MAPK signaling (PubMed:18716323). May play a role in
CC exocytosis and in the targeting of synaptic vesicles to synapses
CC (PubMed:19458197). Functions as an activator of Rac GTPase activity.
CC {ECO:0000269|PubMed:12499390, ECO:0000269|PubMed:18329370,
CC ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750,
CC ECO:0000269|PubMed:19458197}.
CC -!- SUBUNIT: Interacts with UBE3A (By similarity). Interacts with PAK1 and
CC PAK2 (PubMed:18716323). Interacts (via PDZ domains) with VANGL2
CC (PubMed:16687519). Interacts (via PDZ domains) with LPP and TRIP6; the
CC interaction is direct (By similarity). Interacts (via PDZ domains) with
CC TJP2 (By similarity). Interacts (via PDZ domains) with APC; may mediate
CC APC targeting to adherens junctions of epithelial cells
CC (PubMed:16611247). Interacts (via PDZ domains) with TSHR; regulates
CC TSHR trafficking and function (By similarity). Interacts with ARHGEF7
CC and GIT1; interacts directly with ARHGEF7 (PubMed:15182672). Interacts
CC with CTNNB1 (PubMed:16611247, PubMed:19458197). Interacts with MAPK12
CC (PubMed:15878399). Interacts (via PDZ domains 1 and 3) with MCC (By
CC similarity). Interacts with DLG5 (By similarity). Interacts with
CC STK4/MST1 and LATS1 in the presence of DLG5 (By similarity). Interacts
CC (via PDZ domain 3) with CRTAM (via PDZ-binding motif); the interaction
CC promotes CRTAM and SCRIB polarization in a subset of CD4+ T-cells
CC (PubMed:18329370). {ECO:0000250|UniProtKB:Q14160,
CC ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:15878399,
CC ECO:0000269|PubMed:16611247, ECO:0000269|PubMed:16687519,
CC ECO:0000269|PubMed:18329370, ECO:0000269|PubMed:18716323,
CC ECO:0000269|PubMed:19458197}.
CC -!- INTERACTION:
CC Q80U72; Q149L7: Crtam; NbExp=4; IntAct=EBI-1766028, EBI-1766072;
CC Q80U72; O60346: PHLPP1; Xeno; NbExp=2; IntAct=EBI-1766028, EBI-2511516;
CC -!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:18329370};
CC Peripheral membrane protein {ECO:0000269|PubMed:18329370}. Cell
CC junction {ECO:0000250|UniProtKB:Q14160}. Cell junction, adherens
CC junction {ECO:0000250|UniProtKB:Q14160}. Cell projection, lamellipodium
CC {ECO:0000250|UniProtKB:Q14160}. Cytoplasm
CC {ECO:0000250|UniProtKB:Q14160}. Postsynapse
CC {ECO:0000250|UniProtKB:Q14160}. Presynapse
CC {ECO:0000250|UniProtKB:Q14160}. Note=Targeting to cell-cell junctions
CC which is CDH1-dependent is required for the pro-apoptotic activity (By
CC similarity). In a subset of CD4+ T-cells, colocalizes with CRTAM at the
CC immunological synapse during the late phase of T-cell activation
CC (PubMed:18329370). {ECO:0000250|UniProtKB:Q14160,
CC ECO:0000269|PubMed:18329370}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q80U72-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q80U72-2; Sequence=VSP_010911;
CC Name=3;
CC IsoId=Q80U72-3; Sequence=VSP_010910, VSP_010911;
CC Name=4;
CC IsoId=Q80U72-4; Sequence=VSP_010909, VSP_010910;
CC -!- TISSUE SPECIFICITY: Expressed in CD4+ T-cells (at protein level)
CC (PubMed:18329370). Found in a wide range of tissues including liver,
CC kidney and spleen (PubMed:15806148). Also expressed in the brain (at
CC protein level) (PubMed:15182672, PubMed:15806148).
CC {ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:15806148,
CC ECO:0000269|PubMed:18329370}.
CC -!- DEVELOPMENTAL STAGE: First detected at 7.5 dpc in the neuroepithelium
CC at the time of initial neural tube closure. Also expressed in cranial
CC mesenchyme, branchial arches, somitic mesoderm and lateral mesoderm. At
CC later stages it is expressed in the eyelid epithelium, submandibular
CC glands, whisker and hair follicles, sympathetic glanglia, inner ear,
CC thymus, testis, kidney, esophagus, lung, stomach, trigeminal and dorsal
CC root glanglia. {ECO:0000269|PubMed:12499390}.
CC -!- PTM: Ubiquitinated; targeted for UBE3A-dependent multiubiquitination
CC and degraded. {ECO:0000250}.
CC -!- PTM: Palmitoylated. Could be depalmitoylated by LYPLA1 and/or LYPLA2.
CC Palmitoylation of SCRIB by ZDHHC7 is required for its localization to
CC cell-cell junctions, function in the establishement of epithelial cell
CC polarity and the regulation of downstream signaling pathways important
CC for epithelial cell differentiation. {ECO:0000250|UniProtKB:Q14160}.
CC -!- MISCELLANEOUS: The circletail (Crc) mice exhibit craniorachischisis, a
CC severe form of neural tube defect. This is due to a single base
CC insertion in the Scrib gene creating a frameshift which leads to
CC synthesis of a truncated protein.
CC -!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAC65493.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AF441233; AAL32469.1; -; mRNA.
DR EMBL; AK122211; BAC65493.1; ALT_INIT; mRNA.
DR EMBL; BC006859; AAH06859.1; -; mRNA.
DR EMBL; BC037480; AAH37480.1; -; mRNA.
DR EMBL; BC049942; AAH49942.1; -; mRNA.
DR EMBL; BC062888; AAH62888.1; -; mRNA.
DR EMBL; AF271735; AAP88019.1; -; mRNA.
DR CCDS; CCDS27560.1; -. [Q80U72-3]
DR CCDS; CCDS79381.1; -. [Q80U72-1]
DR CCDS; CCDS79382.1; -. [Q80U72-2]
DR RefSeq; NP_001297471.1; NM_001310542.1. [Q80U72-2]
DR RefSeq; NP_001297472.1; NM_001310543.1. [Q80U72-1]
DR RefSeq; NP_598850.1; NM_134089.2. [Q80U72-3]
DR RefSeq; XP_017171844.1; XM_017316355.1. [Q80U72-4]
DR AlphaFoldDB; Q80U72; -.
DR SMR; Q80U72; -.
DR BioGRID; 222921; 10.
DR CORUM; Q80U72; -.
DR DIP; DIP-40660N; -.
DR IntAct; Q80U72; 15.
DR MINT; Q80U72; -.
DR STRING; 10090.ENSMUSP00000002603; -.
DR iPTMnet; Q80U72; -.
DR PhosphoSitePlus; Q80U72; -.
DR SwissPalm; Q80U72; -.
DR EPD; Q80U72; -.
DR jPOST; Q80U72; -.
DR MaxQB; Q80U72; -.
DR PaxDb; Q80U72; -.
DR PeptideAtlas; Q80U72; -.
DR PRIDE; Q80U72; -.
DR ProteomicsDB; 261137; -. [Q80U72-1]
DR ProteomicsDB; 261138; -. [Q80U72-2]
DR ProteomicsDB; 261139; -. [Q80U72-3]
DR ProteomicsDB; 261140; -. [Q80U72-4]
DR Antibodypedia; 43533; 135 antibodies from 27 providers.
DR DNASU; 105782; -.
DR Ensembl; ENSMUST00000002603; ENSMUSP00000002603; ENSMUSG00000022568. [Q80U72-3]
DR Ensembl; ENSMUST00000063747; ENSMUSP00000068056; ENSMUSG00000022568. [Q80U72-1]
DR Ensembl; ENSMUST00000109946; ENSMUSP00000105572; ENSMUSG00000022568. [Q80U72-2]
DR GeneID; 105782; -.
DR KEGG; mmu:105782; -.
DR UCSC; uc007wig.1; mouse. [Q80U72-3]
DR UCSC; uc007wih.1; mouse. [Q80U72-2]
DR UCSC; uc007wii.1; mouse. [Q80U72-1]
DR CTD; 23513; -.
DR MGI; MGI:2145950; Scrib.
DR VEuPathDB; HostDB:ENSMUSG00000022568; -.
DR eggNOG; KOG0619; Eukaryota.
DR GeneTree; ENSGT00940000154025; -.
DR HOGENOM; CLU_000288_18_20_1; -.
DR InParanoid; Q80U72; -.
DR OMA; NNFHPKQ; -.
DR OrthoDB; 284114at2759; -.
DR PhylomeDB; Q80U72; -.
DR TreeFam; TF351429; -.
DR Reactome; R-MMU-9013148; CDC42 GTPase cycle.
DR Reactome; R-MMU-9013406; RHOQ GTPase cycle.
DR Reactome; R-MMU-9013409; RHOJ GTPase cycle.
DR Reactome; R-MMU-9696264; RND3 GTPase cycle.
DR Reactome; R-MMU-9696270; RND2 GTPase cycle.
DR BioGRID-ORCS; 105782; 9 hits in 76 CRISPR screens.
DR ChiTaRS; Scrib; mouse.
DR PRO; PR:Q80U72; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q80U72; protein.
DR Bgee; ENSMUSG00000022568; Expressed in ear vesicle and 265 other tissues.
DR ExpressionAtlas; Q80U72; baseline and differential.
DR Genevisible; Q80U72; MM.
DR GO; GO:0005912; C:adherens junction; ISS:UniProtKB.
DR GO; GO:0016324; C:apical plasma membrane; TAS:MGI.
DR GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
DR GO; GO:0030054; C:cell junction; ISO:MGI.
DR GO; GO:0031252; C:cell leading edge; ISO:MGI.
DR GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
DR GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0099147; C:extrinsic component of postsynaptic density membrane; ISO:MGI.
DR GO; GO:0098978; C:glutamatergic synapse; ISO:MGI.
DR GO; GO:0001772; C:immunological synapse; IDA:UniProtKB.
DR GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
DR GO; GO:0035748; C:myelin sheath abaxonal region; IDA:BHF-UCL.
DR GO; GO:0005654; C:nucleoplasm; ISO:MGI.
DR GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
DR GO; GO:0014069; C:postsynaptic density; ISO:MGI.
DR GO; GO:0045211; C:postsynaptic membrane; ISO:MGI.
DR GO; GO:0042734; C:presynaptic membrane; ISO:MGI.
DR GO; GO:0034750; C:Scrib-APC-beta-catenin complex; ISO:MGI.
DR GO; GO:0090630; P:activation of GTPase activity; ISS:UniProtKB.
DR GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISS:UniProtKB.
DR GO; GO:0043615; P:astrocyte cell migration; ISO:MGI.
DR GO; GO:0002093; P:auditory receptor cell morphogenesis; IGI:MGI.
DR GO; GO:0060088; P:auditory receptor cell stereocilium organization; IGI:MGI.
DR GO; GO:0048593; P:camera-type eye morphogenesis; TAS:MGI.
DR GO; GO:0016477; P:cell migration; IMP:UniProtKB.
DR GO; GO:0008283; P:cell population proliferation; ISS:UniProtKB.
DR GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
DR GO; GO:0021747; P:cochlear nucleus development; IGI:MGI.
DR GO; GO:0003382; P:epithelial cell morphogenesis; TAS:MGI.
DR GO; GO:0035089; P:establishment of apical/basal cell polarity; ISS:UniProtKB.
DR GO; GO:0001768; P:establishment of T cell polarity; IDA:UniProtKB.
DR GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
DR GO; GO:0060122; P:inner ear receptor cell stereocilium organization; IMP:MGI.
DR GO; GO:0060603; P:mammary gland duct morphogenesis; IMP:UniProtKB.
DR GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
DR GO; GO:0046007; P:negative regulation of activated T cell proliferation; IMP:UniProtKB.
DR GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
DR GO; GO:0001843; P:neural tube closure; IMP:MGI.
DR GO; GO:0098968; P:neurotransmitter receptor transport postsynaptic membrane to endosome; ISO:MGI.
DR GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; ISO:MGI.
DR GO; GO:0030859; P:polarized epithelial cell differentiation; ISO:MGI.
DR GO; GO:0050918; P:positive chemotaxis; IMP:UniProtKB.
DR GO; GO:0043065; P:positive regulation of apoptotic process; ISS:UniProtKB.
DR GO; GO:0032729; P:positive regulation of interferon-gamma production; IMP:UniProtKB.
DR GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
DR GO; GO:0036342; P:post-anal tail morphogenesis; IMP:MGI.
DR GO; GO:0008104; P:protein localization; IMP:MGI.
DR GO; GO:0071896; P:protein localization to adherens junction; ISO:MGI.
DR GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
DR GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
DR GO; GO:0099149; P:regulation of postsynaptic neurotransmitter receptor internalization; ISO:MGI.
DR GO; GO:0048488; P:synaptic vesicle endocytosis; IDA:SynGO.
DR GO; GO:0016080; P:synaptic vesicle targeting; IMP:UniProtKB.
DR GO; GO:0099003; P:vesicle-mediated transport in synapse; ISO:MGI.
DR GO; GO:0042060; P:wound healing; IGI:MGI.
DR Gene3D; 2.30.42.10; -; 4.
DR Gene3D; 3.80.10.10; -; 4.
DR InterPro; IPR001611; Leu-rich_rpt.
DR InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
DR InterPro; IPR032675; LRR_dom_sf.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR Pfam; PF13855; LRR_8; 2.
DR Pfam; PF00595; PDZ; 4.
DR SMART; SM00369; LRR_TYP; 12.
DR SMART; SM00228; PDZ; 4.
DR SUPFAM; SSF50156; SSF50156; 4.
DR PROSITE; PS51450; LRR; 13.
DR PROSITE; PS50106; PDZ; 4.
PE 1: Evidence at protein level;
KW Alternative splicing; Cell junction; Cell membrane; Cell projection;
KW Coiled coil; Cytoplasm; Developmental protein; Differentiation;
KW Leucine-rich repeat; Lipoprotein; Membrane; Methylation; Palmitate;
KW Phosphoprotein; Reference proteome; Repeat; Synapse; Ubl conjugation.
FT CHAIN 1..1612
FT /note="Protein scribble homolog"
FT /id="PRO_0000188304"
FT REPEAT 37..58
FT /note="LRR 1"
FT REPEAT 60..81
FT /note="LRR 2"
FT REPEAT 83..104
FT /note="LRR 3"
FT REPEAT 106..127
FT /note="LRR 4"
FT REPEAT 129..150
FT /note="LRR 5"
FT REPEAT 152..174
FT /note="LRR 6"
FT REPEAT 175..197
FT /note="LRR 7"
FT REPEAT 198..219
FT /note="LRR 8"
FT REPEAT 221..243
FT /note="LRR 9"
FT REPEAT 244..265
FT /note="LRR 10"
FT REPEAT 267..288
FT /note="LRR 11"
FT REPEAT 290..312
FT /note="LRR 12"
FT REPEAT 313..334
FT /note="LRR 13"
FT REPEAT 336..357
FT /note="LRR 14"
FT REPEAT 359..381
FT /note="LRR 15"
FT REPEAT 382..402
FT /note="LRR 16"
FT DOMAIN 714..801
FT /note="PDZ 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 848..936
FT /note="PDZ 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 990..1079
FT /note="PDZ 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT DOMAIN 1086..1180
FT /note="PDZ 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 1..804
FT /note="Sufficient for targeting to adherens junction and to
FT inhibit cell proliferation"
FT /evidence="ECO:0000250"
FT REGION 422..615
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 635..689
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 703..1215
FT /note="Interaction with ARHGEF7"
FT /evidence="ECO:0000250"
FT REGION 1213..1246
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1263..1297
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1310..1473
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1500..1550
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1579..1612
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 455..475
FT /evidence="ECO:0000255"
FT COILED 653..687
FT /evidence="ECO:0000255"
FT COILED 1362..1393
FT /evidence="ECO:0000255"
FT COMPBIAS 423..443
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 461..497
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 562..585
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 656..679
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1266..1285
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1363..1385
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 37
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 378
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 475
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 583
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 674
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 675
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:21183079"
FT MOD_RES 694
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 750
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 812
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 821
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 861
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 925
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1126
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1206
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17242355,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT MOD_RES 1209
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1212
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1218
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1262
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1284
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1325
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1331
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1361
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1427
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1430
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1457
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1468
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1490
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1523
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1527
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q14160"
FT MOD_RES 1529
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1543
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1548
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:15345747,
FT ECO:0007744|PubMed:19144319, ECO:0007744|PubMed:21183079"
FT VAR_SEQ 692..712
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_010909"
FT VAR_SEQ 1289
FT /note="Q -> QTKPGVIQPLAQAWPRNSPAPRGRGGPCS (in isoform 3 and
FT isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_010910"
FT VAR_SEQ 1547
FT /note="L -> LPLSGKKFDYRAFAALPSSRPVYDIQ (in isoform 2 and
FT isoform 3)"
FT /evidence="ECO:0000303|PubMed:12693553,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.1"
FT /id="VSP_010911"
FT CONFLICT 588
FT /note="P -> L (in Ref. 3; AAH62888)"
FT /evidence="ECO:0000305"
FT CONFLICT 676..683
FT /note="EEDDKEEA -> GRVGGRVG (in Ref. 3; AAH06859)"
FT /evidence="ECO:0000305"
FT CONFLICT 947..949
FT /note="HSS -> RVR (in Ref. 3; AAH37480)"
FT /evidence="ECO:0000305"
FT CONFLICT 1080
FT /note="P -> H (in Ref. 4; AAP88019)"
FT /evidence="ECO:0000305"
FT CONFLICT 1109
FT /note="A -> T (in Ref. 4; AAP88019)"
FT /evidence="ECO:0000305"
FT MOD_RES Q80U72-3:1312
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q80U72-3:1320
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES Q80U72-4:1291
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES Q80U72-4:1299
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
SQ SEQUENCE 1612 AA; 174059 MW; 8C85DB322D738EDE CRC64;
MLKCIPLWRC NRHVESVDKR HCSLQVVPEE IYRYSRSLEE LLLDANQLRE LPKPFFRLLN
LRKLGLSDNE IQRLPPEVAN FMQLVELDVS RNDIPEIPES IKFCKALEIA DFSGNPLSRL
PDGFTQLRSL AHLALNDVSL QALPGDVGNL ANLVTLELRE NLLKSLPASL SFLVKLEQLD
LGGNDLEVLP DTLGALPNLR ELWLDRNQLS ALPPELGNLR RLVCLDVSEN RLEELPVELG
GLALLTDLLL SQNLLQRLPE GIGQLKQLSI LKVDQNRLCE VTEAIGDCEN LSELILTENL
LTALPHSLGK LTKLTNLNVD RNHLEVLPPE IGGCVALSVL SLRDNRLAVL PPELAHTAEL
HVLDVAGNRL RSLPFALTHL NLKALWLAEN QAQPMLRFQT EDDAQTGEKV LTCYLLPQQP
LPSLEDAGQQ SSPSESCSDA PLSRVSVIQF EDTLEGEEDA EEAAAEKRGL QRRATPHPSE
LKVMKRGIEE RRNEAFVCKP DPSPPSPSEE EKRLSAESAL SGGSVPSAST ASEGEPEILP
AEVQGLGQHE AMPAQEEYTE DDYNEPTVHF AEDTLIPRED GESEEGQPEA AWPLPSGRQR
LIRKDTPHYK KHFKISKLPQ PEAVVALLQG VQTDREGPTA GWHNGPHTPW APRAHEEEEE
EEEENRDEEE GEATTEEDDK EEAVASAPSV KGVSFDQANN LLIEPARIEE EELTLTIVRQ
TGGLGISIAG GKGSTPYKGD DEGIFISRVS EEGPAARAGV RVGDKLLEVN GVALQDAEHH
EAVEALRGAG AAVQMRVWRE RMVEPENAVT ITPLRPEDDY SPREWRGGGL RLPLLQPETP
VSLRQRHAAC LVRSEKGLGF SIAGGKGSTP YRAGDGGIFI SRIAEGGAAH RAGTLQVGDR
VLSINGVDMT EARHDHAVSL LTAASPTISL LLERETGGTY PPSPPPHSSP TPAATVAATV
STAVPGEPLL PRLSPSLLAT ALEGPYPVEE ICLPRAGGPL GLSIVGGSDH SSHPFGVQDP
GVFISKVLPR GLAARCGLRV GDRILAVNGQ DVREATHQEA VSALLRPCLE LCLLVRRDPP
PPGMRELCIQ KAPGEKLGIS IRGGAKGHAG NPCDPTDEGI FISKVSPTGA AGRDGRLRVG
LRLLEVNQQS LLGLTHAEAV QLLRSVGDTL TVLVCDGFDT STTTALEVSP GVIANPFAAG
LGHRNSLESI SSIDRELSPE GPGKEKELAS QALPWESESA ETTGRNLEPL KLDYRALAAL
PSAGSLQRGP SATTGGKTTE APCSPGSQQP PSPDELPANV KQAYRAFAAV PTVHPPENSA
TQPPTPGPAA SPEQLSFRER QKYFELEVRV PQAEGPPKRV SLVGADDLRK MQEEEARKLQ
QKRAQMLREE AVTSGPDMGL ASDRESPDDQ QEAEQPWAVP SHAGGSSPSS PPPLGGNAPV
RTAKAERRHQ ERLRMQSPEL PAPERALSPA ERRALEAEKR ALWRAARMKS LEQDALRAQM
VLSKSQEGRG KRGPLERLAE APSPAPTPSP TPLEDFGLQT SASPGRLSPD FVEELRTLEA
SPSPGSQEED GEVALVLLGR PSPGAVGPED MTLCSSRRSV RPGRRGLGPV PS
