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Protein scribble homolog (Scribble) (Protein LAP4)

 SCRIB_MOUSE             Reviewed;        1612 AA.
Q80U72; Q6P5H7; Q7TPH8; Q80VB1; Q8CI48; Q8VII1; Q922S3;
19-JUL-2004, integrated into UniProtKB/Swiss-Prot.
19-JUL-2004, sequence version 2.
28-MAR-2018, entry version 150.
RecName: Full=Protein scribble homolog;
Short=Scribble;
AltName: Full=Protein LAP4;
Name=Scrib; Synonyms=Kiaa0147, Lap4, Scrib1;
Mus musculus (Mouse).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha;
Muroidea; Muridae; Murinae; Mus; Mus.
NCBI_TaxID=10090;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
STRAIN=C57BL/6J; TISSUE=Cerebellum;
Mattock K.L., Kurschner C.;
"Molecular cloning of mouse Scribble cDNA.";
Submitted (OCT-2001) to the EMBL/GenBank/DDBJ databases.
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Brain;
PubMed=12693553; DOI=10.1093/dnares/10.1.35;
Okazaki N., Kikuno R., Ohara R., Inamoto S., Aizawa H., Yuasa S.,
Nakajima D., Nagase T., Ohara O., Koga H.;
"Prediction of the coding sequences of mouse homologues of KIAA gene:
II. The complete nucleotide sequences of 400 mouse KIAA-homologous
cDNAs identified by screening of terminal sequences of cDNA clones
randomly sampled from size-fractionated libraries.";
DNA Res. 10:35-48(2003).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
STRAIN=C57BL/6J; TISSUE=Brain, and Mammary tumor;
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).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 694-1336 (ISOFORM 1).
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).
[5]
FUNCTION, AND DEVELOPMENTAL STAGE.
PubMed=12499390; DOI=10.1093/hmg/ddg014;
Murdoch J.N., Henderson D.J., Doudney K., Gaston-Massuet C.,
Phillips H.M., Paternotte C., Arkell R., Stanier P., Copp A.J.;
"Disruption of scribble (Scrb1) causes severe neural tube defects in
the circletail mouse.";
Hum. Mol. Genet. 12:87-98(2003).
[6]
INTERACTION WITH ARHGEF7 AND GIT1.
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).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1548, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Embryonic brain;
PubMed=15345747; DOI=10.1074/mcp.M400085-MCP200;
Ballif B.A., Villen J., Beausoleil S.A., Schwartz D., Gygi S.P.;
"Phosphoproteomic analysis of the developing mouse brain.";
Mol. Cell. Proteomics 3:1093-1101(2004).
[8]
INTERACTION WITH MAPK12.
PubMed=15878399; DOI=10.1016/j.bbamcr.2004.11.008;
Court N.W., Ingley E., Klinken S.P., Bogoyevitch M.A.;
"Outer membrane protein 25-a mitochondrial anchor and inhibitor of
stress-activated protein kinase-3.";
Biochim. Biophys. Acta 1744:68-75(2005).
[9]
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).
[10]
INTERACTION WITH APC AND CTNNB1, 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).
[11]
INTERACTION WITH VANGL2.
PubMed=16687519; DOI=10.1523/JNEUROSCI.4680-05.2006;
Montcouquiol M., Sans N., Huss D., Kach J., Dickman J.D., Forge A.,
Rachel R.A., Copeland N.G., Jenkins N.A., Bogani D., Murdoch J.,
Warchol M.E., Wenthold R.J., Kelley M.W.;
"Asymmetric localization of Vangl2 and Fz3 indicate novel mechanisms
for planar cell polarity in mammals.";
J. Neurosci. 26:5265-5275(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-674; THR-675 AND
SER-1206, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Liver;
PubMed=17242355; DOI=10.1073/pnas.0609836104;
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.;
"Large-scale phosphorylation analysis of mouse liver.";
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007).
[13]
FUNCTION.
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).
[14]
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).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1206 AND SER-1548, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19144319; DOI=10.1016/j.immuni.2008.11.006;
Trost M., English L., Lemieux S., Courcelles M., Desjardins M.,
Thibault P.;
"The phagosomal proteome in interferon-gamma-activated macrophages.";
Immunity 30:143-154(2009).
[16]
FUNCTION, AND INTERACTION WITH CTNNB1.
PubMed=19458197; DOI=10.1091/mbc.E08-12-1172;
Sun Y., Aiga M., Yoshida E., Humbert P.O., Bamji S.X.;
"Scribble interacts with beta-catenin to localize synaptic vesicles to
synapses.";
Mol. Biol. Cell 20:3390-3400(2009).
[17]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-583; THR-674; THR-675;
SER-925; SER-1206; SER-1292; SER-1361; SER-1457; SER-1490; SER-1529;
SER-1543 AND SER-1548, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
SER-1320 (ISOFORM 3), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT
SER-1299 (ISOFORM 4), AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
SCALE ANALYSIS].
TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung,
Pancreas, Spleen, and Testis;
PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
"A tissue-specific atlas of mouse protein phosphorylation and
expression.";
Cell 143:1174-1189(2010).
[18]
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1312 (ISOFORM 3),
METHYLATION [LARGE SCALE ANALYSIS] AT ARG-1291 (ISOFORM 4), AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Brain, and Embryo;
PubMed=24129315; DOI=10.1074/mcp.O113.027870;
Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V.,
Aguiar M., Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C.,
Vemulapalli V., Bedford M.T., Comb M.J.;
"Immunoaffinity enrichment and mass spectrometry analysis of protein
methylation.";
Mol. Cell. Proteomics 13:372-387(2014).
-!- 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:12499390,
ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750,
ECO:0000269|PubMed:19458197}.
-!- SUBUNIT: Interacts with UBE3A. Interacts with PAK1 and PAK2.
Interacts (via PDZ domains) with LPP and TRIP6; the interaction is
direct. Interacts (via PDZ domains) with TJP2. Interacts (via PDZ
domains) with TSHR; regulates TSHR trafficking and function (By
similarity). Interacts (via PDZ domains) with VANGL2. Interacts
with ARHGEF7 and GIT1; interacts directly with ARHGEF7. Interacts
(via PDZ domains) with APC; may mediate APC targeting to adherens
junctions of epithelial cells. Interacts with CTNNB1 and MAPK12.
Interacts (via PDZ domains 1 and 3) with MCC (By similarity).
Interacts with DLG5 (By similarity). Interacts with STK4/MST1 and
LATS1 in the presence of DLG5 (By similarity).
{ECO:0000250|UniProtKB:Q14160, ECO:0000269|PubMed:15182672,
ECO:0000269|PubMed:15878399, ECO:0000269|PubMed:16611247,
ECO:0000269|PubMed:16687519, ECO:0000269|PubMed:18716323,
ECO:0000269|PubMed:19458197}.
-!- INTERACTION:
Q149L7:Crtam; NbExp=4; IntAct=EBI-1766028, EBI-1766072;
O60346:PHLPP1 (xeno); NbExp=2; IntAct=EBI-1766028, EBI-2511516;
-!- SUBCELLULAR LOCATION: Cell membrane
{ECO:0000250|UniProtKB:Q14160}; Peripheral membrane protein
{ECO:0000250}. Cell junction, adherens junction {ECO:0000250}.
Cytoplasm {ECO:0000250}. Cell projection, lamellipodium
{ECO:0000250}. 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 (By
similarity). {ECO:0000250}.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=4;
Name=1;
IsoId=Q80U72-1; Sequence=Displayed;
Name=2;
IsoId=Q80U72-2; Sequence=VSP_010911;
Name=3;
IsoId=Q80U72-3; Sequence=VSP_010910, VSP_010911;
Note=Contains a phosphoserine at position 1320. Contains a
omega-N-methylarginine at position 1312.
{ECO:0000244|PubMed:21183079, ECO:0000244|PubMed:24129315};
Name=4;
IsoId=Q80U72-4; Sequence=VSP_010909, VSP_010910;
Note=No experimental confirmation available. Contains a
phosphoserine at position 1299. Contains a
omega-N-methylarginine at position 1291.
{ECO:0000244|PubMed:21183079, ECO:0000244|PubMed:24129315};
-!- TISSUE SPECIFICITY: Found in a wide range of tissues including
liver, brain, kidney and spleen. {ECO:0000269|PubMed:15806148}.
-!- DEVELOPMENTAL STAGE: First detected at E7.5 in the neuroepithelium
at the time of initial neural tube closure. Also expressed in
cranial mesenchyme, branchial arches, somitic mesoderm and lateral
mesoderm. At later stages it is expressed in the eyelid
epithelium, submandibular glands, whisker and hair follicles,
sympathetic glanglia, inner ear, thymus, testis, kidney,
esophagus, lung, stomach, trigeminal and dorsal root glanglia.
{ECO:0000269|PubMed:12499390}.
-!- PTM: Ubiquitinated; targeted for UBE3A-dependent
multiubiquitination and degraded. {ECO:0000250}.
-!- MISCELLANEOUS: The circletail (Crc) mice exhibit
craniorachishicisis a severe form of neural tube defect. This is
due to a single base insertion in the Scrib gene creating a
frameshift which leads to synthesis of a truncated protein.
-!- SIMILARITY: Belongs to the LAP (LRR and PDZ) protein family.
{ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=BAC65493.1; Type=Erroneous initiation; Evidence={ECO:0000305};
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EMBL; AF441233; AAL32469.1; -; mRNA.
EMBL; AK122211; BAC65493.1; ALT_INIT; mRNA.
EMBL; BC006859; AAH06859.1; -; mRNA.
EMBL; BC037480; AAH37480.1; -; mRNA.
EMBL; BC049942; AAH49942.1; -; mRNA.
EMBL; BC062888; AAH62888.1; -; mRNA.
EMBL; AF271735; AAP88019.1; -; mRNA.
CCDS; CCDS27560.1; -. [Q80U72-3]
CCDS; CCDS79381.1; -. [Q80U72-1]
CCDS; CCDS79382.1; -. [Q80U72-2]
RefSeq; NP_001297471.1; NM_001310542.1. [Q80U72-2]
RefSeq; NP_001297472.1; NM_001310543.1. [Q80U72-1]
RefSeq; NP_598850.1; NM_134089.2. [Q80U72-3]
RefSeq; XP_017171844.1; XM_017316355.1. [Q80U72-4]
UniGene; Mm.25568; -.
ProteinModelPortal; Q80U72; -.
SMR; Q80U72; -.
BioGrid; 222921; 7.
CORUM; Q80U72; -.
DIP; DIP-40660N; -.
IntAct; Q80U72; 14.
MINT; Q80U72; -.
STRING; 10090.ENSMUSP00000002603; -.
iPTMnet; Q80U72; -.
PhosphoSitePlus; Q80U72; -.
SwissPalm; Q80U72; -.
PaxDb; Q80U72; -.
PeptideAtlas; Q80U72; -.
PRIDE; Q80U72; -.
Ensembl; ENSMUST00000002603; ENSMUSP00000002603; ENSMUSG00000022568. [Q80U72-3]
Ensembl; ENSMUST00000063747; ENSMUSP00000068056; ENSMUSG00000022568. [Q80U72-1]
Ensembl; ENSMUST00000109946; ENSMUSP00000105572; ENSMUSG00000022568. [Q80U72-2]
GeneID; 105782; -.
KEGG; mmu:105782; -.
UCSC; uc007wig.1; mouse. [Q80U72-3]
UCSC; uc007wih.1; mouse. [Q80U72-2]
UCSC; uc007wii.1; mouse. [Q80U72-1]
CTD; 23513; -.
MGI; MGI:2145950; Scrib.
eggNOG; ENOG410KCZ0; Eukaryota.
eggNOG; COG4886; LUCA.
GeneTree; ENSGT00840000129686; -.
InParanoid; Q80U72; -.
KO; K16175; -.
OMA; QVGMRIL; -.
OrthoDB; EOG091G01EF; -.
PhylomeDB; Q80U72; -.
TreeFam; TF351429; -.
ChiTaRS; Scrib; mouse.
PRO; PR:Q80U72; -.
Proteomes; UP000000589; Chromosome 15.
Bgee; ENSMUSG00000022568; -.
CleanEx; MM_SCRIB; -.
ExpressionAtlas; Q80U72; baseline and differential.
Genevisible; Q80U72; MM.
GO; GO:0016323; C:basolateral plasma membrane; IDA:MGI.
GO; GO:0030054; C:cell junction; ISO:MGI.
GO; GO:0005913; C:cell-cell adherens junction; ISS:UniProtKB.
GO; GO:0044291; C:cell-cell contact zone; IDA:MGI.
GO; GO:0005911; C:cell-cell junction; ISS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0030027; C:lamellipodium; IEA:UniProtKB-SubCell.
GO; GO:0035748; C:myelin sheath abaxonal region; IDA:BHF-UCL.
GO; GO:0005654; C:nucleoplasm; ISO:MGI.
GO; GO:0005886; C:plasma membrane; ISS:UniProtKB.
GO; GO:0014069; C:postsynaptic density; IBA:GO_Central.
GO; GO:0045211; C:postsynaptic membrane; IBA:GO_Central.
GO; GO:0042734; C:presynaptic membrane; IEA:Ensembl.
GO; GO:0034750; C:Scrib-APC-beta-catenin complex; ISO:MGI.
GO; GO:0045296; F:cadherin binding; ISO:MGI.
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; ISS:UniProtKB.
GO; GO:0060561; P:apoptotic process involved in morphogenesis; ISS:UniProtKB.
GO; GO:0043615; P:astrocyte cell migration; IEA:Ensembl.
GO; GO:0002093; P:auditory receptor cell morphogenesis; IGI:MGI.
GO; GO:0060088; P:auditory receptor cell stereocilium organization; IGI:MGI.
GO; GO:0016477; P:cell migration; IMP:UniProtKB.
GO; GO:0008283; P:cell proliferation; ISS:UniProtKB.
GO; GO:0098609; P:cell-cell adhesion; ISS:UniProtKB.
GO; GO:0021747; P:cochlear nucleus development; IGI:MGI.
GO; GO:0035089; P:establishment of apical/basal cell polarity; ISS:UniProtKB.
GO; GO:0060603; P:mammary gland duct morphogenesis; IMP:UniProtKB.
GO; GO:0016331; P:morphogenesis of embryonic epithelium; IMP:MGI.
GO; GO:0045930; P:negative regulation of mitotic cell cycle; ISS:UniProtKB.
GO; GO:0001843; P:neural tube closure; IMP:MGI.
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; ISS:UniProtKB.
GO; GO:0001921; P:positive regulation of receptor recycling; ISO:MGI.
GO; GO:0008104; P:protein localization; IMP:MGI.
GO; GO:0071896; P:protein localization to adherens junction; ISO:MGI.
GO; GO:0043113; P:receptor clustering; IBA:GO_Central.
GO; GO:0097120; P:receptor localization to synapse; IBA:GO_Central.
GO; GO:0048488; P:synaptic vesicle endocytosis; IMP:UniProtKB.
GO; GO:0016080; P:synaptic vesicle targeting; IMP:UniProtKB.
GO; GO:0042060; P:wound healing; IGI:MGI.
Gene3D; 3.80.10.10; -; 2.
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; 3.
Pfam; PF00595; PDZ; 4.
SMART; SM00369; LRR_TYP; 12.
SMART; SM00228; PDZ; 4.
SUPFAM; SSF50156; SSF50156; 4.
PROSITE; PS51450; LRR; 13.
PROSITE; PS50106; PDZ; 4.
1: Evidence at protein level;
Alternative splicing; Cell junction; Cell membrane; Cell projection;
Coiled coil; Complete proteome; Cytoplasm; Developmental protein;
Differentiation; Leucine-rich repeat; Membrane; Methylation;
Phosphoprotein; Reference proteome; Repeat; Ubl conjugation.
CHAIN 1 1612 Protein scribble homolog.
/FTId=PRO_0000188304.
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 714 801 PDZ 1. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 848 936 PDZ 2. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 990 1079 PDZ 3. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
DOMAIN 1086 1180 PDZ 4. {ECO:0000255|PROSITE-
ProRule:PRU00143}.
REGION 1 804 Sufficient for targeting to adherens
junction and to inhibit cell
proliferation. {ECO:0000250}.
REGION 703 1215 Interaction with ARHGEF7. {ECO:0000250}.
COILED 455 475 {ECO:0000255}.
COILED 653 687 {ECO:0000255}.
COILED 1362 1393 {ECO:0000255}.
COMPBIAS 656 682 Glu-rich.
COMPBIAS 656 664 Poly-Glu.
COMPBIAS 709 712 Poly-Glu.
COMPBIAS 1079 1082 Poly-Pro.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 378 378 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 475 475 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 583 583 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 674 674 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 675 675 Phosphothreonine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:21183079}.
MOD_RES 694 694 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 750 750 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 812 812 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 821 821 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 861 861 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 925 925 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1126 1126 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1206 1206 Phosphoserine.
{ECO:0000244|PubMed:17242355,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
MOD_RES 1209 1209 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1212 1212 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1218 1218 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1262 1262 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1265 1265 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1284 1284 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1292 1292 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1325 1325 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1331 1331 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1361 1361 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1427 1427 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1430 1430 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1457 1457 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1468 1468 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1490 1490 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1523 1523 Phosphoserine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1527 1527 Phosphothreonine.
{ECO:0000250|UniProtKB:Q14160}.
MOD_RES 1529 1529 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1543 1543 Phosphoserine.
{ECO:0000244|PubMed:21183079}.
MOD_RES 1548 1548 Phosphoserine.
{ECO:0000244|PubMed:15345747,
ECO:0000244|PubMed:19144319,
ECO:0000244|PubMed:21183079}.
VAR_SEQ 692 712 Missing (in isoform 4).
{ECO:0000303|PubMed:15489334}.
/FTId=VSP_010909.
VAR_SEQ 1289 1289 Q -> QTKPGVIQPLAQAWPRNSPAPRGRGGPCS (in
isoform 3 and isoform 4).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1}.
/FTId=VSP_010910.
VAR_SEQ 1547 1547 L -> LPLSGKKFDYRAFAALPSSRPVYDIQ (in
isoform 2 and isoform 3).
{ECO:0000303|PubMed:12693553,
ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.1}.
/FTId=VSP_010911.
CONFLICT 588 588 P -> L (in Ref. 3; AAH62888).
{ECO:0000305}.
CONFLICT 676 683 EEDDKEEA -> GRVGGRVG (in Ref. 3;
AAH06859). {ECO:0000305}.
CONFLICT 947 949 HSS -> RVR (in Ref. 3; AAH37480).
{ECO:0000305}.
CONFLICT 1080 1080 P -> H (in Ref. 4; AAP88019).
{ECO:0000305}.
CONFLICT 1109 1109 A -> T (in Ref. 4; AAP88019).
{ECO:0000305}.
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


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