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Protein scribble homolog (Scribble) (hScrib) (Protein LAP4)

 SCRIB_HUMAN             Reviewed;        1630 AA.
Q14160; Q6P496; Q7Z5D1; Q8WWV8; Q96C69; Q96GG1;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
13-OCT-2009, sequence version 4.
22-NOV-2017, entry version 183.
RecName: Full=Protein scribble homolog;
Short=Scribble;
Short=hScrib;
AltName: Full=Protein LAP4;
Name=SCRIB; Synonyms=CRIB1, KIAA0147, LAP4, SCRB1, VARTUL;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH LPP,
SUBCELLULAR LOCATION, MUTAGENESIS OF 738-LEU--GLY-739;
872-LEU--GLY-873; 1014-LEU--GLY-1015 AND 1111-LEU--GLY-1112, AND
VARIANT LEU-422.
PubMed=15649318; DOI=10.1186/1471-2121-6-1;
Petit M.M.R., Meulemans S.M.P., Alen P., Ayoubi T.A.Y., Jansen E.,
Van de Ven W.J.M.;
"The tumor suppressor Scrib interacts with the zyxin-related protein
LPP, which shuttles between cell adhesion sites and the nucleus.";
BMC Cell Biol. 6:1-1(2005).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-422, SUBCELLULAR
LOCATION, MUTAGENESIS OF PRO-305, AND TISSUE SPECIFICITY.
PubMed=15806148; DOI=10.1038/sj.onc.1208632;
Navarro C., Nola S., Audebert S., Santoni M.-J., Arsanto J.-P.,
Ginestier C., Marchetto S., Jacquemier J., Isnardon D., Le Bivic A.,
Birnbaum D., Borg J.-P.;
"Junctional recruitment of mammalian Scribble relies on E-cadherin
engagement.";
Oncogene 24:4330-4339(2005).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), AND VARIANT LEU-422.
Petit M.M.R., Alen P., Meulemans S.M.P., Van de Wouwer E.,
Ayoubi T.A.Y., Van de Ven W.J.M., Jansen E.;
"The human Scrib N1 variant encoded by the SCRIB gene contains 13
leucine-rich repeats and 4 PDZ domains.";
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-422.
TISSUE=Bone marrow, and Brain;
PubMed=8590280; DOI=10.1093/dnares/2.4.167;
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.;
"Prediction of the coding sequences of unidentified human genes. IV.
The coding sequences of 40 new genes (KIAA0121-KIAA0160) deduced by
analysis of cDNA clones from human cell line KG-1.";
DNA Res. 2:167-174(1995).
[5]
SEQUENCE REVISION.
PubMed=12168954; DOI=10.1093/dnares/9.3.99;
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
"Construction of expression-ready cDNA clones for KIAA genes: manual
curation of 330 KIAA cDNA clones.";
DNA Res. 9:99-106(2002).
[6]
SEQUENCE REVISION.
Ohara O., Nagase T., Kikuno R., Nomura N.;
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16421571; DOI=10.1038/nature04406;
Nusbaum C., Mikkelsen T.S., Zody M.C., Asakawa S., Taudien S.,
Garber M., Kodira C.D., Schueler M.G., Shimizu A., Whittaker C.A.,
Chang J.L., Cuomo C.A., Dewar K., FitzGerald M.G., Yang X.,
Allen N.R., Anderson S., Asakawa T., Blechschmidt K., Bloom T.,
Borowsky M.L., Butler J., Cook A., Corum B., DeArellano K.,
DeCaprio D., Dooley K.T., Dorris L. III, Engels R., Gloeckner G.,
Hafez N., Hagopian D.S., Hall J.L., Ishikawa S.K., Jaffe D.B.,
Kamat A., Kudoh J., Lehmann R., Lokitsang T., Macdonald P.,
Major J.E., Matthews C.D., Mauceli E., Menzel U., Mihalev A.H.,
Minoshima S., Murayama Y., Naylor J.W., Nicol R., Nguyen C.,
O'Leary S.B., O'Neill K., Parker S.C.J., Polley A., Raymond C.K.,
Reichwald K., Rodriguez J., Sasaki T., Schilhabel M., Siddiqui R.,
Smith C.L., Sneddon T.P., Talamas J.A., Tenzin P., Topham K.,
Venkataraman V., Wen G., Yamazaki S., Young S.K., Zeng Q.,
Zimmer A.R., Rosenthal A., Birren B.W., Platzer M., Shimizu N.,
Lander E.S.;
"DNA sequence and analysis of human chromosome 8.";
Nature 439:331-335(2006).
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 799-1630 (ISOFORM 1), AND
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1206-1630 (ISOFORM 3).
TISSUE=Lung carcinoma, and Neuroblastoma;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
INTERACTION WITH UBE3A AND HPV E6, UBIQUITINATION, AND SUBCELLULAR
LOCATION.
PubMed=11027293; DOI=10.1128/MCB.20.21.8244-8253.2000;
Nakagawa S., Huibregtse J.M.;
"Human scribble (Vartul) is targeted for ubiquitin-mediated
degradation by the high-risk papillomavirus E6 proteins and the E6AP
ubiquitin-protein ligase.";
Mol. Cell. Biol. 20:8244-8253(2000).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=15144186; DOI=10.1021/ac035352d;
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M.,
Peters E.C.;
"Robust phosphoproteomic profiling of tyrosine phosphorylation sites
from human T cells using immobilized metal affinity chromatography and
tandem mass spectrometry.";
Anal. Chem. 76:2763-2772(2004).
[11]
FUNCTION, INTERACTION WITH ARHGEF7 AND GIT1, AND SUBCELLULAR LOCATION.
PubMed=15182672; DOI=10.1016/j.cub.2004.05.051;
Audebert S., Navarro C., Nourry C., Chasserot-Golaz S., Lecine P.,
Bellaiche Y., Dupont J.-L., Premont R.T., Sempere C., Strub J.-M.,
Van Dorsselaer A., Vitale N., Borg J.-P.;
"Mammalian Scribble forms a tight complex with the betaPIX exchange
factor.";
Curr. Biol. 14:987-995(2004).
[12]
FUNCTION, AND INTERACTION WITH TSHR.
PubMed=15775968; DOI=10.1038/sj.emboj.7600616;
Lahuna O., Quellari M., Achard C., Nola S., Meduri G., Navarro C.,
Vitale N., Borg J.-P., Misrahi M.;
"Thyrotropin receptor trafficking relies on the hScrib-betaPIX-GIT1-
ARF6 pathway.";
EMBO J. 24:1364-1374(2005).
[13]
INTERACTION WITH TJP2.
PubMed=15975580; DOI=10.1016/j.febslet.2005.05.062;
Metais J.-Y., Navarro C., Santoni M.-J., Audebert S., Borg J.-P.;
"hScrib interacts with ZO-2 at the cell-cell junctions of epithelial
cells.";
FEBS Lett. 579:3725-3730(2005).
[14]
INTERACTION WITH TRIP6.
PubMed=16137684; DOI=10.1016/j.febslet.2005.08.012;
Petit M.M.R., Crombez K.R.M.O., Vervenne H.B.V.K., Weyns N.,
Van de Ven W.J.M.;
"The tumor suppressor Scrib selectively interacts with specific
members of the zyxin family of proteins.";
FEBS Lett. 579:5061-5068(2005).
[15]
FUNCTION IN CELL ADHESION.
PubMed=16344308; DOI=10.1083/jcb.200506094;
Qin Y., Capaldo C., Gumbiner B.M., Macara I.G.;
"The mammalian Scribble polarity protein regulates epithelial cell
adhesion and migration through E-cadherin.";
J. Cell Biol. 171:1061-1071(2005).
[16]
FUNCTION IN CELL PROLIFERATION, AND SUBCELLULAR LOCATION.
PubMed=16965391; DOI=10.1111/j.1349-7006.2006.00315.x;
Nagasaka K., Nakagawa S., Yano T., Takizawa S., Matsumoto Y.,
Tsuruga T., Nakagawa K., Minaguchi T., Oda K., Hiraike-Wada O.,
Ooishi H., Yasugi T., Taketani Y.;
"Human homolog of Drosophila tumor suppressor Scribble negatively
regulates cell-cycle progression from G1 to S phase by localizing at
the basolateral membrane in epithelial cells.";
Cancer Sci. 97:1217-1225(2006).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-853; SER-1306; SER-1309
AND SER-1378, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[18]
INTERACTION WITH APC, AND SUBCELLULAR LOCATION.
PubMed=16611247; DOI=10.1111/j.1365-2443.2006.00954.x;
Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K.,
Yasugi T., Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T.,
Taketani Y.;
"Human scribble, a novel tumor suppressor identified as a target of
high-risk HPV E6 for ubiquitin-mediated degradation, interacts with
adenomatous polyposis coli.";
Genes Cells 11:453-464(2006).
[19]
FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION, AND MUTAGENESIS OF
PRO-305.
PubMed=19041750; DOI=10.1016/j.cell.2008.09.045;
Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B.,
Allred C., Muthuswamy S.K.;
"Deregulation of scribble promotes mammary tumorigenesis and reveals a
role for cell polarity in carcinoma.";
Cell 135:865-878(2008).
[20]
FUNCTION IN CELL MIGRATION, AND INTERACTION WITH PAK1 AND PAK2.
PubMed=18716323; DOI=10.1093/hmg/ddn248;
Nola S., Sebbagh M., Marchetto S., Osmani N., Nourry C., Audebert S.,
Navarro C., Rachel R., Montcouquiol M., Sans N.,
Etienne-Manneville S., Borg J.-P., Santoni M.-J.;
"Scrib regulates PAK activity during the cell migration process.";
Hum. Mol. Genet. 17:3552-3565(2008).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1475 AND SER-1566, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[22]
FUNCTION.
PubMed=18641685; DOI=10.1038/onc.2008.219;
Dow L.E., Elsum I.A., King C.L., Kinross K.M., Richardson H.E.,
Humbert P.O.;
"Loss of human Scribble cooperates with H-Ras to promote cell invasion
through deregulation of MAPK signalling.";
Oncogene 27:5988-6001(2008).
[23]
INTERACTION WITH TICK-BORNE ENCEPHALITIS VIRUS RNA-DIRECTED RNA
POLYMERASE NS5.
PubMed=18042258; DOI=10.1111/j.1462-5822.2007.01076.x;
Werme K., Wigerius M., Johansson M.;
"Tick-borne encephalitis virus NS5 associates with membrane protein
scribble and impairs interferon-stimulated JAK-STAT signalling.";
Cell. Microbiol. 10:696-712(2008).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-826; SER-939; SER-1223;
SER-1232; SER-1306; SER-1309; THR-1342; SER-1348; SER-1437; SER-1547
AND SER-1566, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[26]
INTERACTION WITH MCC.
PubMed=19555689; DOI=10.1016/j.febslet.2009.06.034;
Arnaud C., Sebbagh M., Nola S., Audebert S., Bidaut G., Hermant A.,
Gayet O., Dusetti N.J., Ollendorff V., Santoni M.J., Borg J.P.,
Lecine P.;
"MCC, a new interacting protein for Scrib, is required for cell
migration in epithelial cells.";
FEBS Lett. 583:2326-2332(2009).
[27]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1348 AND SER-1448, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
Mann M., Daub H.;
"Large-scale proteomics analysis of the human kinome.";
Mol. Cell. Proteomics 8:1751-1764(2009).
[28]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-826; SER-1220; THR-1342;
SER-1348; SER-1475; SER-1547 AND SER-1566, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[29]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-826; SER-835; SER-853;
SER-939; SER-1140; SER-1220; SER-1232; THR-1342; SER-1348; SER-1378;
SER-1448; SER-1475; SER-1486 AND SER-1566, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[30]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[31]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688; THR-689; SER-1220;
SER-1309 AND SER-1378, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[32]
INTERACTION WITH MCC, AND SUBCELLULAR LOCATION.
PubMed=22480440; DOI=10.1016/j.bbamcr.2012.03.011;
Pangon L., Van Kralingen C., Abas M., Daly R.J., Musgrove E.A.,
Kohonen-Corish M.R.;
"The PDZ-binding motif of MCC is phosphorylated at position -1 and
controls lamellipodia formation in colon epithelial cells.";
Biochim. Biophys. Acta 1823:1058-1067(2012).
[33]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-37; THR-378; THR-475;
SER-504; SER-708; SER-853; SER-875; SER-1140; SER-1220; SER-1223;
SER-1226; SER-1232; SER-1276; SER-1279; SER-1306; SER-1309; SER-1348;
SER-1378; SER-1448; SER-1475; SER-1486; SER-1508; SER-1541; SER-1561
AND SER-1566, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[34]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-504; SER-764; SER-853;
SER-1140; SER-1220; SER-1295; SER-1298; SER-1306; SER-1309; SER-1378;
SER-1445; SER-1448; SER-1486; SER-1508; THR-1545 AND SER-1566, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[35]
INTERACTION WITH DLG5; STK4 AND LATS1, AND SUBCELLULAR LOCATION.
PubMed=28169360; DOI=10.1038/srep42125;
Liu J., Li J., Li P., Wang Y., Liang Z., Jiang Y., Li J., Feng C.,
Wang R., Chen H., Zhou C., Zhang J., Yang J., Liu P.;
"Loss of DLG5 promotes breast cancer malignancy by inhibiting the
Hippo signaling pathway.";
Sci. Rep. 7:42125-42125(2017).
[36]
STRUCTURE BY NMR OF 718-814; 860-951 AND 1096-1193.
RIKEN structural genomics initiative (RSGI);
"Solution structure of the first, second and fourth PDZ domain of
human scribble (KIAA0147 protein).";
Submitted (NOV-2005) to the PDB data bank.
[37]
VARIANTS NTD SER-454 AND GLN-1535, AND CHARACTERIZATION OF VARIANTS
NTD SER-454 AND GLN-1535.
PubMed=22095531; DOI=10.1002/humu.21662;
Robinson A., Escuin S., Doudney K., Vekemans M., Stevenson R.E.,
Greene N.D., Copp A.J., Stanier P.;
"Mutations in the planar cell polarity genes CELSR1 and SCRIB are
associated with the severe neural tube defect craniorachischisis.";
Hum. Mutat. 33:440-447(2012).
-!- FUNCTION: Scaffold protein involved in different aspects of
polarized cells differentiation regulating epithelial and neuronal
morphogenesis. Most probably functions in the establishment of
apico-basal cell polarity. May function in cell proliferation
regulating progression from G1 to S phase and as a positive
regulator of apoptosis for instance during acinar morphogenesis of
the mammary epithelium. May also function in cell migration and
adhesion and hence regulate cell invasion through MAPK signaling.
May play a role in exocytosis and in the targeting synaptic
vesicles to synapses. Functions as an activator of Rac GTPase
activity. {ECO:0000269|PubMed:15182672,
ECO:0000269|PubMed:15775968, ECO:0000269|PubMed:16344308,
ECO:0000269|PubMed:16965391, ECO:0000269|PubMed:18641685,
ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750}.
-!- SUBUNIT: Interacts (via PDZ domains) with VANGL2. Interacts with
CTNNB1 and MAPK12 (By similarity). Interacts with UBE3A and HPV
E6. Interacts with PAK1 and PAK2. Interacts with ARHGEF7 and GIT1;
interacts directly with ARHGEF7. Interacts (via PDZ domains) with
LPP and TRIP6; the interaction is direct. Interacts (via PDZ
domains) with TJP2. Interacts (via PDZ domains) with APC; may
mediate APC targeting to adherens junctions of epithelial cells.
Interacts (via PDZ domains) with TSHR; regulates TSHR trafficking
and function. Interacts (via PDZ domains 1 and 3) with MCC.
Interacts (via fourth PDZ domain) with tick-borne encephalitis
virus NS5 protein; this interaction inhibits SCRIB and downstream
STAT1 phosphorylation, thereby preventing activation of JAK-STAT
signaling pathway. Interacts with DLG5 (PubMed:28169360).
Interacts with STK4/MST1 and LATS1 in the presence of DLG5
(PubMed:28169360). {ECO:0000250|UniProtKB:Q80U72,
ECO:0000269|PubMed:11027293, ECO:0000269|PubMed:15182672,
ECO:0000269|PubMed:15649318, ECO:0000269|PubMed:15775968,
ECO:0000269|PubMed:15975580, ECO:0000269|PubMed:16137684,
ECO:0000269|PubMed:16611247, ECO:0000269|PubMed:18042258,
ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19555689,
ECO:0000269|PubMed:22480440, ECO:0000269|PubMed:28169360}.
-!- SUBUNIT: (Microbial infection) Interacts with tick-borne
encephalitis virus RNA-directed RNA polymerase NS5; this
interaction targets viral NS5 to the cell membrane periphery and
nucleus, thereby allowing efficient host nuclear STAT1 inhibition.
{ECO:0000269|PubMed:18042258}.
-!- INTERACTION:
B7Z2Y1:-; NbExp=3; IntAct=EBI-357345, EBI-11791049;
P25054:APC; NbExp=4; IntAct=EBI-357345, EBI-727707;
Q14155:ARHGEF7; NbExp=9; IntAct=EBI-357345, EBI-717515;
O00429:DNM1L; NbExp=2; IntAct=EBI-357345, EBI-724571;
P03126:E6 (xeno); NbExp=7; IntAct=EBI-357345, EBI-1177242;
P06427:E6 (xeno); NbExp=2; IntAct=EBI-357345, EBI-11737184;
P06463:E6 (xeno); NbExp=3; IntAct=EBI-357345, EBI-1186926;
Q9QXA3:Fat1 (xeno); NbExp=5; IntAct=EBI-357345, EBI-6980218;
P33402:GUCY1A2; NbExp=3; IntAct=EBI-357345, EBI-6911715;
P22460:KCNA5; NbExp=2; IntAct=EBI-357345, EBI-6426121;
P53778:MAPK12; NbExp=3; IntAct=EBI-357345, EBI-602406;
P27361:MAPK3; NbExp=2; IntAct=EBI-357345, EBI-73995;
P23508:MCC; NbExp=8; IntAct=EBI-357345, EBI-307531;
Q96DL1:NXPE2; NbExp=2; IntAct=EBI-357345, EBI-11791121;
O60346:PHLPP1; NbExp=2; IntAct=EBI-357345, EBI-2511516;
Q99569:PKP4; NbExp=3; IntAct=EBI-357345, EBI-726447;
P48065:SLC6A12; NbExp=2; IntAct=EBI-357345, EBI-3843589;
P0C213:tax (xeno); NbExp=2; IntAct=EBI-357345, EBI-11793850;
P0C222:tax (xeno); NbExp=2; IntAct=EBI-357345, EBI-11794384;
P16473:TSHR; NbExp=3; IntAct=EBI-357345, EBI-13939599;
-!- SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:28169360};
Peripheral membrane protein. Cell junction, adherens junction.
Cell projection, lamellipodium. Cytoplasm. Note=Targeting to cell-
cell junctions which is CDH1-dependent is required for the pro-
apoptotic activity. Localizes to neuronal post- and pre-synaptic
regions.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q14160-1; Sequence=Displayed;
Name=2; Synonyms=Variant N1;
IsoId=Q14160-2; Sequence=VSP_010906;
Note=No experimental confirmation available.;
Name=3;
IsoId=Q14160-3; Sequence=VSP_010908;
-!- TISSUE SPECIFICITY: Expressed in kidney, skeletal muscles, liver,
lung, breast, intestine, placenta and skin mainly in epithelial
cells (at protein level). {ECO:0000269|PubMed:15806148}.
-!- PTM: Ubiquitinated; targeted for UBE3A-dependent
multiubiquitination in the presence of high-risk HPV E6 proteins
and degraded. {ECO:0000269|PubMed:11027293}.
-!- DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital
malformations of the central nervous system and adjacent
structures related to defective neural tube closure during the
first trimester of pregnancy. Failure of neural tube closure can
occur at any level of the embryonic axis. Common NTD forms include
anencephaly, myelomeningocele and spina bifida, which result from
the failure of fusion in the cranial and spinal region of the
neural tube. NTDs have a multifactorial etiology encompassing both
genetic and environmental components.
{ECO:0000269|PubMed:22095531}. Note=The disease is caused by
mutations affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
{ECO:0000305}.
-----------------------------------------------------------------------
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EMBL; AF240677; AAP88017.1; -; mRNA.
EMBL; AY062238; AAL38976.1; -; mRNA.
EMBL; AF271734; AAP88018.2; -; mRNA.
EMBL; D63481; BAA09768.3; -; mRNA.
EMBL; AC105219; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC009490; AAH09490.2; -; mRNA.
EMBL; BC014632; AAH14632.2; -; mRNA.
CCDS; CCDS6411.1; -. [Q14160-1]
CCDS; CCDS6412.1; -. [Q14160-3]
RefSeq; NP_056171.3; NM_015356.4.
RefSeq; NP_874365.3; NM_182706.4.
UniGene; Hs.436329; -.
PDB; 1UJU; NMR; -; A=1096-1193.
PDB; 1WHA; NMR; -; A=860-951.
PDB; 1X5Q; NMR; -; A=718-814.
PDB; 2W4F; X-ray; 1.30 A; A=725-815.
PDB; 4WYT; X-ray; 2.60 A; A=992-1203.
PDB; 4WYU; X-ray; 2.50 A; A/B=992-1203.
PDBsum; 1UJU; -.
PDBsum; 1WHA; -.
PDBsum; 1X5Q; -.
PDBsum; 2W4F; -.
PDBsum; 4WYT; -.
PDBsum; 4WYU; -.
ProteinModelPortal; Q14160; -.
SMR; Q14160; -.
BioGrid; 117060; 59.
CORUM; Q14160; -.
DIP; DIP-31259N; -.
ELM; Q14160; -.
IntAct; Q14160; 105.
MINT; MINT-147371; -.
STRING; 9606.ENSP00000349486; -.
iPTMnet; Q14160; -.
PhosphoSitePlus; Q14160; -.
SwissPalm; Q14160; -.
BioMuta; SCRIB; -.
DMDM; 261260101; -.
EPD; Q14160; -.
MaxQB; Q14160; -.
PaxDb; Q14160; -.
PeptideAtlas; Q14160; -.
PRIDE; Q14160; -.
DNASU; 23513; -.
Ensembl; ENST00000320476; ENSP00000322938; ENSG00000180900.
Ensembl; ENST00000356994; ENSP00000349486; ENSG00000180900.
Ensembl; ENST00000377533; ENSP00000366756; ENSG00000180900.
GeneID; 23513; -.
KEGG; hsa:23513; -.
UCSC; uc003yzo.1; human. [Q14160-1]
CTD; 23513; -.
DisGeNET; 23513; -.
EuPathDB; HostDB:ENSG00000180900.16; -.
GeneCards; SCRIB; -.
HGNC; HGNC:30377; SCRIB.
HPA; CAB015463; -.
HPA; CAB022081; -.
HPA; HPA023557; -.
HPA; HPA064312; -.
MalaCards; SCRIB; -.
MIM; 182940; phenotype.
MIM; 607733; gene.
neXtProt; NX_Q14160; -.
PharmGKB; PA134936275; -.
eggNOG; ENOG410KCZ0; Eukaryota.
eggNOG; COG4886; LUCA.
HOGENOM; HOG000113281; -.
InParanoid; Q14160; -.
KO; K16175; -.
OrthoDB; EOG091G01EF; -.
PhylomeDB; Q14160; -.
TreeFam; TF351429; -.
Reactome; R-HSA-4608870; Asymmetric localization of PCP proteins.
SignaLink; Q14160; -.
ChiTaRS; SCRIB; human.
EvolutionaryTrace; Q14160; -.
GeneWiki; SCRIB; -.
GenomeRNAi; 23513; -.
PRO; PR:Q14160; -.
Proteomes; UP000005640; Chromosome 8.
Bgee; ENSG00000180900; -.
CleanEx; HS_SCRIB; -.
ExpressionAtlas; Q14160; baseline and differential.
Genevisible; Q14160; HS.
GO; GO:0016323; C:basolateral plasma membrane; IBA:GO_Central.
GO; GO:0030054; C:cell junction; IDA:HPA.
GO; GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
GO; GO:0044291; C:cell-cell contact zone; IEA:Ensembl.
GO; GO:0005911; C:cell-cell junction; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005886; C:plasma membrane; IDA:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
GO; GO:0098793; C:presynapse; IEA:GOC.
GO; GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL.
GO; GO:0045296; F:cadherin binding; IDA:BHF-UCL.
GO; GO:0004385; F:guanylate kinase activity; IBA:GO_Central.
GO; GO:0035255; F:ionotropic glutamate receptor binding; IBA:GO_Central.
GO; GO:0090630; P:activation of GTPase activity; IMP:UniProtKB.
GO; GO:0060561; P:apoptotic process involved in morphogenesis; IMP:UniProtKB.
GO; GO:0043615; P:astrocyte cell migration; IEA:Ensembl.
GO; GO:0008105; P:asymmetric protein localization; IEA:Ensembl.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; IDA:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; IGI:UniProtKB.
GO; GO:0007268; P:chemical synaptic transmission; IBA:GO_Central.
GO; GO:0021747; P:cochlear nucleus development; IEA:Ensembl.
GO; GO:0035089; P:establishment of apical/basal cell polarity; IMP:UniProtKB.
GO; GO:0045197; P:establishment or maintenance of epithelial cell apical/basal polarity; IBA:GO_Central.
GO; GO:0060603; P:mammary gland duct morphogenesis; ISS:UniProtKB.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB.
GO; GO:0001843; P:neural tube closure; IMP:UniProtKB.
GO; GO:0098968; P:neurotransmitter receptor transport postsynaptic membrane to endosome; IEA:Ensembl.
GO; GO:0098887; P:neurotransmitter receptor transport, endosome to postsynaptic membrane; IEA:Ensembl.
GO; GO:0050918; P:positive chemotaxis; IMP:UniProtKB.
GO; GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB.
GO; GO:0001921; P:positive regulation of receptor recycling; IMP:UniProtKB.
GO; GO:0071896; P:protein localization to adherens junction; IMP:BHF-UCL.
GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
GO; GO:0039563; P:suppression by virus of host STAT1 activity; IEA:UniProtKB-KW.
GO; GO:0039564; P:suppression by virus of host STAT2 activity; IEA:UniProtKB-KW.
GO; GO:0039502; P:suppression by virus of host type I interferon-mediated signaling pathway; IEA:UniProtKB-KW.
GO; GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl.
GO; GO:0016080; P:synaptic vesicle targeting; IEA:Ensembl.
GO; GO:0042060; P:wound healing; IEA:Ensembl.
Gene3D; 3.80.10.10; -; 4.
InterPro; IPR001611; Leu-rich_rpt.
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp.
InterPro; IPR032675; LRR_dom_sf.
InterPro; IPR001478; PDZ.
InterPro; IPR036034; PDZ_sf.
Pfam; PF13855; LRR_8; 2.
Pfam; PF00595; PDZ; 4.
SMART; SM00369; LRR_TYP; 11.
SMART; SM00228; PDZ; 4.
SUPFAM; SSF50156; SSF50156; 4.
SUPFAM; SSF52058; SSF52058; 2.
PROSITE; PS51450; LRR; 13.
PROSITE; PS50106; PDZ; 4.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell junction; Cell membrane;
Cell projection; Coiled coil; Complete proteome; Cytoplasm;
Developmental protein; Differentiation; Disease mutation;
Host-virus interaction;
Inhibition of host innate immune response by virus;
Inhibition of host interferon signaling pathway by virus;
Inhibition of host STAT1 by virus; Inhibition of host STAT2 by virus;
Leucine-rich repeat; Membrane; Phosphoprotein; Polymorphism;
Reference proteome; Repeat; Ubl conjugation; Viral immunoevasion.
CHAIN 1 1630 Protein scribble homolog.
/FTId=PRO_0000188303.
REPEAT 37 58 LRR 1.
REPEAT 60 81 LRR 2.
REPEAT 83 104 LRR 3.
REPEAT 106 127 LRR 4.
REPEAT 129 150 LRR 5.
REPEAT 152 174 LRR 6.
REPEAT 175 197 LRR 7.
REPEAT 198 219 LRR 8.
REPEAT 221 243 LRR 9.
REPEAT 244 265 LRR 10.
REPEAT 267 288 LRR 11.
REPEAT 290 312 LRR 12.
REPEAT 313 334 LRR 13.
REPEAT 336 357 LRR 14.
REPEAT 359 381 LRR 15.
REPEAT 382 402 LRR 16.
DOMAIN 728 815 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 862 950 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1004 1093 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1100 1194 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 1 818 Sufficient for targeting to adherens
junction and to inhibit cell
proliferation.
REGION 717 1229 Interaction with ARHGEF7.
{ECO:0000269|PubMed:15182672}.
REGION 1105 1117 Interaction with tick-borne encephalitis
virus RNA-directed RNA polymerase NS5.
{ECO:0000269|PubMed:18042258}.
COILED 458 474 {ECO:0000255}.
COILED 656 701 {ECO:0000255}.
COILED 1379 1419 {ECO:0000255}.
COMPBIAS 660 695 Glu-rich.
COMPBIAS 1296 1349 Pro-rich.
MOD_RES 37 37 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 378 378 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 475 475 Phosphothreonine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 504 504 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 688 688 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 689 689 Phosphothreonine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 708 708 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 764 764 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 826 826 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 835 835 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 853 853 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 875 875 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 939 939 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 1140 1140 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1220 1220 Phosphoserine.
{ECO:0000244|PubMed:15144186,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1223 1223 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
MOD_RES 1226 1226 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1232 1232 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1276 1276 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1279 1279 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1295 1295 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1298 1298 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1306 1306 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1309 1309 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1342 1342 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231}.
MOD_RES 1348 1348 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1378 1378 Phosphoserine.
{ECO:0000244|PubMed:17081983,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1437 1437 Phosphoserine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 1445 1445 Phosphoserine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1448 1448 Phosphoserine.
{ECO:0000244|PubMed:19369195,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1475 1475 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 1486 1486 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1508 1508 Phosphoserine.
{ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 1541 1541 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1545 1545 Phosphothreonine.
{ECO:0000244|PubMed:24275569}.
MOD_RES 1547 1547 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332}.
MOD_RES 1561 1561 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 1566 1566 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
VAR_SEQ 1 81 Missing (in isoform 2).
{ECO:0000303|Ref.3}.
/FTId=VSP_010906.
VAR_SEQ 1565 1565 L -> LPLSGKKFDYRAFAALPSSRPVYDIQ (in
isoform 3).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010908.
VARIANT 422 422 P -> L (in dbSNP:rs6558394).
{ECO:0000269|PubMed:15649318,
ECO:0000269|PubMed:15806148,
ECO:0000269|PubMed:8590280,
ECO:0000269|Ref.3}.
/FTId=VAR_019429.
VARIANT 454 454 P -> S (in NTD; protein interactions not
affected by the mutation; shows reduced
protein localization to the cell
membrane). {ECO:0000269|PubMed:22095531}.
/FTId=VAR_067219.
VARIANT 1535 1535 R -> Q (in NTD; protein interactions not
affected by the mutation; shows reduced
protein localization to the cell
membrane). {ECO:0000269|PubMed:22095531}.
/FTId=VAR_067220.
MUTAGEN 305 305 P->L: Loss of pro-apoptotic function and
of the targeting to cell-cell junctions.
Targeted to the cytoplasm. Alters
interaction with TJP2.
{ECO:0000269|PubMed:15806148,
ECO:0000269|PubMed:19041750}.
MUTAGEN 738 739 LG->AE: Alters interaction with LPP.
{ECO:0000269|PubMed:15649318}.
MUTAGEN 738 738 L->R: Loss of anti-proliferative
activity.
MUTAGEN 872 873 LG->AE: Alters interaction with LPP.
{ECO:0000269|PubMed:15649318}.
MUTAGEN 1014 1015 LG->AE: Loss of interaction with LPP and
TRIP6. {ECO:0000269|PubMed:15649318}.
MUTAGEN 1111 1112 LG->AE: Alters interaction with LPP.
{ECO:0000269|PubMed:15649318}.
CONFLICT 674 674 V -> E (in Ref. 1; AAP88017, 2; AAL38976,
3; AAP88018 and 4; BAA09768).
{ECO:0000305}.
CONFLICT 1489 1489 E -> K (in Ref. 2; AAL38976).
{ECO:0000305}.
STRAND 726 732 {ECO:0000244|PDB:2W4F}.
STRAND 737 744 {ECO:0000244|PDB:2W4F}.
STRAND 757 763 {ECO:0000244|PDB:2W4F}.
HELIX 768 772 {ECO:0000244|PDB:2W4F}.
STRAND 779 783 {ECO:0000244|PDB:2W4F}.
HELIX 793 801 {ECO:0000244|PDB:2W4F}.
STRAND 805 812 {ECO:0000244|PDB:2W4F}.
STRAND 860 865 {ECO:0000244|PDB:1WHA}.
STRAND 875 877 {ECO:0000244|PDB:1WHA}.
STRAND 893 896 {ECO:0000244|PDB:1WHA}.
HELIX 903 906 {ECO:0000244|PDB:1WHA}.
STRAND 914 920 {ECO:0000244|PDB:1WHA}.
HELIX 928 935 {ECO:0000244|PDB:1WHA}.
STRAND 942 948 {ECO:0000244|PDB:1WHA}.
STRAND 997 1000 {ECO:0000244|PDB:4WYU}.
STRAND 1002 1008 {ECO:0000244|PDB:4WYU}.
STRAND 1010 1012 {ECO:0000244|PDB:4WYU}.
STRAND 1016 1020 {ECO:0000244|PDB:4WYU}.
STRAND 1022 1024 {ECO:0000244|PDB:4WYT}.
TURN 1027 1030 {ECO:0000244|PDB:4WYU}.
STRAND 1031 1033 {ECO:0000244|PDB:4WYU}.
STRAND 1036 1041 {ECO:0000244|PDB:4WYU}.
HELIX 1046 1050 {ECO:0000244|PDB:4WYU}.
STRAND 1057 1061 {ECO:0000244|PDB:4WYU}.
HELIX 1071 1079 {ECO:0000244|PDB:4WYU}.
STRAND 1083 1090 {ECO:0000244|PDB:4WYU}.
STRAND 1099 1104 {ECO:0000244|PDB:4WYU}.
STRAND 1113 1117 {ECO:0000244|PDB:4WYU}.
STRAND 1119 1122 {ECO:0000244|PDB:1UJU}.
STRAND 1126 1128 {ECO:0000244|PDB:4WYT}.
STRAND 1134 1139 {ECO:0000244|PDB:4WYU}.
STRAND 1141 1143 {ECO:0000244|PDB:4WYT}.
HELIX 1144 1148 {ECO:0000244|PDB:4WYU}.
STRAND 1156 1160 {ECO:0000244|PDB:4WYU}.
HELIX 1170 1178 {ECO:0000244|PDB:4WYU}.
STRAND 1183 1189 {ECO:0000244|PDB:4WYU}.
SEQUENCE 1630 AA; 174885 MW; D71E024FBC4F72D1 CRC64;
MLKCIPLWRC NRHVESVDKR HCSLQAVPEE IYRYSRSLEE LLLDANQLRE LPKPFFRLLN
LRKLGLSDNE IQRLPPEVAN FMQLVELDVS RNDIPEIPES IKFCKALEIA DFSGNPLSRL
PDGFTQLRSL AHLALNDVSL QALPGDVGNL ANLVTLELRE NLLKSLPASL SFLVKLEQLD
LGGNDLEVLP DTLGALPNLR ELWLDRNQLS ALPPELGNLR RLVCLDVSEN RLEELPAELG
GLVLLTDLLL SQNLLRRLPD GIGQLKQLSI LKVDQNRLCE VTEAIGDCEN LSELILTENL
LMALPRSLGK LTKLTNLNVD RNHLEALPPE IGGCVALSVL SLRDNRLAVL PPELAHTTEL
HVLDVAGNRL QSLPFALTHL NLKALWLAEN QAQPMLRFQT EDDARTGEKV LTCYLLPQQP
PPSLEDAGQQ GSLSETWSDA PPSRVSVIQF LEAPIGDEDA EEAAAEKRGL QRRATPHPSE
LKVMKRSIEG RRSEACPCQP DSGSPLPAEE EKRLSAESGL SEDSRPSAST VSEAEPEGPS
AEAQGGSQQE ATTAGGEEDA EEDYQEPTVH FAEDALLPGD DREIEEGQPE APWTLPGGRQ
RLIRKDTPHY KKHFKISKLP QPEAVVALLQ GMQPDGEGPV APGGWHNGPH APWAPRAQKE
EEEEEEGSPQ EEEVEEEEEN RAEEEEASTE EEDKEGAVVS APSVKGVSFD QANNLLIEPA
RIEEEELTLT ILRQTGGLGI SIAGGKGSTP YKGDDEGIFI SRVSEEGPAA RAGVRVGDKL
LEVNGVALQG AEHHEAVEAL RGAGTAVQMR VWRERMVEPE NAVTITPLRP EDDYSPRERR
GGGLRLPLLP PESPGPLRQR HVACLARSER GLGFSIAGGK GSTPYRAGDA GIFVSRIAEG
GAAHRAGTLQ VGDRVLSING VDVTEARHDH AVSLLTAASP TIALLLEREA GGPLPPSPLP
HSSPPTAAVA TTSITTATPG VPGLPSLAPS LLAAALEGPY PVEEIRLPRA GGPLGLSIVG
GSDHSSHPFG VQEPGVFISK VLPRGLAARS GLRVGDRILA VNGQDVRDAT HQEAVSALLR
PCLELSLLVR RDPAPPGLRE LCIQKAPGER LGISIRGGAR GHAGNPRDPT DEGIFISKVS
PTGAAGRDGR LRVGLRLLEV NQQSLLGLTH GEAVQLLRSV GDTLTVLVCD GFEASTDAAL
EVSPGVIANP FAAGIGHRNS LESISSIDRE LSPEGPGKEK ELPGQTLHWG PEATEAAGRG
LQPLKLDYRA LAAVPSAGSV QRVPSGAAGG KMAESPCSPS GQQPPSPPSP DELPANVKQA
YRAFAAVPTS HPPEDAPAQP PTPGPAASPE QLSFRERQKY FELEVRVPQA EGPPKRVSLV
GADDLRKMQE EEARKLQQKR AQMLREAAEA GAEARLALDG ETLGEEEQED EQPPWASPSP
TSRQSPASPP PLGGGAPVRT AKAERRHQER LRVQSPEPPA PERALSPAEL RALEAEKRAL
WRAARMKSLE QDALRAQMVL SRSQEGRGTR GPLERLAEAP SPAPTPSPTP VEDLGPQTST
SPGRLSPDFA EELRSLEPSP SPGPQEEDGE VALVLLGRPS PGAVGPEDVA LCSSRRPVRP
GRRGLGPVPS


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