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Q14160 (SCRIB_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 143. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Protein scribble homolog

Short name=Scribble
Short name=hScrib
Alternative name(s):
Protein LAP4
Gene names
Name:SCRIB
Synonyms:CRIB1, KIAA0147, LAP4, SCRB1, VARTUL
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1630 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.11 Ref.12 Ref.15 Ref.16 Ref.19 Ref.20 Ref.22

Subunit structure

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. Ref.1 Ref.9 Ref.11 Ref.12 Ref.13 Ref.14 Ref.18 Ref.20 Ref.23 Ref.26 Ref.32

Subcellular location

Cell membrane; Peripheral membrane protein. Cell junctionadherens junction. Cell projectionlamellipodium. 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. Ref.1 Ref.2 Ref.9 Ref.11 Ref.16 Ref.18 Ref.19 Ref.32

Tissue specificity

Expressed in kidney, skeletal muscles, liver, lung, breast, intestine, placenta and skin mainly in epithelial cells (at protein level). Ref.2

Post-translational modification

Ubiquitinated; targeted for UBE3A-dependent multiubiquitination in the presence of high-risk HPV E6 proteins and degraded. Ref.9

Involvement in 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.
Note: The disease is caused by mutations affecting the gene represented in this entry. Ref.34

Sequence similarities

Belongs to the LAP (LRR and PDZ) protein family.

Contains 16 LRR (leucine-rich) repeats.

Contains 4 PDZ (DHR) domains.

Ontologies

Keywords
   Biological processDifferentiation
Host-virus interaction
   Cellular componentCell junction
Cell membrane
Cell projection
Cytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
   DomainCoiled coil
Leucine-rich repeat
Repeat
   Molecular functionDevelopmental protein
   PTMPhosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processactivation of Rac GTPase activity

Inferred from mutant phenotype Ref.19. Source: UniProtKB

apoptotic process involved in morphogenesis

Inferred from mutant phenotype Ref.19. Source: UniProtKB

astrocyte cell migration

Inferred from electronic annotation. Source: Ensembl

asymmetric protein localization

Inferred from electronic annotation. Source: Ensembl

cell migration

Inferred from mutant phenotype Ref.20. Source: UniProtKB

cell proliferation

Inferred from direct assay Ref.16. Source: UniProtKB

cell-cell adhesion

Inferred from genetic interaction Ref.15. Source: UniProtKB

establishment of apical/basal cell polarity

Inferred from mutant phenotype Ref.19. Source: UniProtKB

mammary gland duct morphogenesis

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of mitotic cell cycle

Inferred from direct assay Ref.16. Source: UniProtKB

neural tube closure

Inferred from mutant phenotype Ref.34. Source: UniProtKB

positive chemotaxis

Inferred from mutant phenotype Ref.20. Source: UniProtKB

positive regulation of apoptotic process

Inferred from mutant phenotype Ref.19. Source: UniProtKB

positive regulation of receptor recycling

Inferred from mutant phenotype Ref.12. Source: UniProtKB

protein localization to adherens junction

Inferred from mutant phenotype Ref.18. Source: BHF-UCL

synaptic vesicle endocytosis

Inferred from electronic annotation. Source: Ensembl

synaptic vesicle targeting

Inferred from electronic annotation. Source: Ensembl

viral process

Inferred from electronic annotation. Source: UniProtKB-KW

wound healing

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentScrib-APC-beta-catenin complex

Inferred from direct assay Ref.18. Source: BHF-UCL

basolateral plasma membrane

Inferred from electronic annotation. Source: Ensembl

cell-cell adherens junction

Inferred from direct assay Ref.16. Source: UniProtKB

cell-cell junction

Inferred from direct assay Ref.1. Source: UniProtKB

extracellular vesicular exosome

Inferred from direct assay PubMed 20458337. Source: UniProt

lamellipodium

Inferred from electronic annotation. Source: UniProtKB-SubCell

myelin sheath abaxonal region

Inferred from electronic annotation. Source: Ensembl

plasma membrane

Inferred from direct assay Ref.11. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q14160-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: Q14160-2)

Also known as: Variant N1;

The sequence of this isoform differs from the canonical sequence as follows:
     1-81: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: Q14160-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1565-1565: L → LPLSGKKFDYRAFAALPSSRPVYDIQ

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16301630Protein scribble homolog
PRO_0000188303

Regions

Repeat37 – 5822LRR 1
Repeat60 – 8122LRR 2
Repeat83 – 10422LRR 3
Repeat106 – 12722LRR 4
Repeat129 – 15022LRR 5
Repeat152 – 17423LRR 6
Repeat175 – 19723LRR 7
Repeat198 – 21922LRR 8
Repeat221 – 24323LRR 9
Repeat244 – 26522LRR 10
Repeat267 – 28822LRR 11
Repeat290 – 31223LRR 12
Repeat313 – 33422LRR 13
Repeat336 – 35722LRR 14
Repeat359 – 38123LRR 15
Repeat382 – 40221LRR 16
Domain728 – 81588PDZ 1
Domain862 – 95089PDZ 2
Domain1004 – 109390PDZ 3
Domain1100 – 119495PDZ 4
Region1 – 818818Sufficient for targeting to adherens junction and to inhibit cell proliferation
Region717 – 1229513Interaction with ARHGEF7
Coiled coil458 – 47417 Potential
Coiled coil656 – 70146 Potential
Coiled coil1379 – 141941 Potential
Compositional bias660 – 69536Glu-rich
Compositional bias1296 – 134954Pro-rich

Amino acid modifications

Modified residue6881Phosphoserine Ref.31
Modified residue6891Phosphothreonine Ref.31
Modified residue8261Phosphothreonine Ref.24 Ref.28 Ref.29
Modified residue8351Phosphoserine Ref.29
Modified residue8531Phosphoserine Ref.17 Ref.29
Modified residue9391Phosphoserine Ref.24 Ref.29
Modified residue11401Phosphoserine Ref.29
Modified residue12201Phosphoserine Ref.10 Ref.28 Ref.29 Ref.31
Modified residue12231Phosphoserine Ref.24
Modified residue12321Phosphoserine Ref.24 Ref.29
Modified residue13061Phosphoserine Ref.17 Ref.24
Modified residue13091Phosphoserine Ref.17 Ref.24 Ref.31
Modified residue13421Phosphothreonine Ref.24 Ref.28 Ref.29
Modified residue13481Phosphoserine Ref.24 Ref.27 Ref.28 Ref.29
Modified residue13781Phosphoserine Ref.17 Ref.29 Ref.31
Modified residue14371Phosphoserine Ref.24
Modified residue14481Phosphoserine Ref.27 Ref.29 Ref.31
Modified residue14751Phosphoserine Ref.21 Ref.28 Ref.29
Modified residue14861Phosphoserine Ref.29
Modified residue15471Phosphoserine Ref.24 Ref.28
Modified residue15661Phosphoserine Ref.21 Ref.24 Ref.28 Ref.29

Natural variations

Alternative sequence1 – 8181Missing in isoform 2.
VSP_010906
Alternative sequence15651L → LPLSGKKFDYRAFAALPSSR PVYDIQ in isoform 3.
VSP_010908
Natural variant4221P → L. Ref.1 Ref.2 Ref.3 Ref.4
Corresponds to variant rs6558394 [ dbSNP | Ensembl ].
VAR_019429
Natural variant4541P → S in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. Ref.34
VAR_067219
Natural variant15351R → Q in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. Ref.34
VAR_067220

Experimental info

Mutagenesis3051P → L: Loss of pro-apoptotic function and of the targeting to cell-cell junctions. Targeted to the cytoplasm. Alters interaction with TJP2. Ref.2 Ref.19
Mutagenesis738 – 7392LG → AE: Alters interaction with LPP.
Mutagenesis7381L → R: Loss of anti-proliferative activity.
Mutagenesis872 – 8732LG → AE: Alters interaction with LPP.
Mutagenesis1014 – 10152LG → AE: Loss of interaction with LPP and TRIP6. Ref.1
Mutagenesis1111 – 11122LG → AE: Alters interaction with LPP. Ref.1
Sequence conflict6741V → E in AAP88017. Ref.1
Sequence conflict6741V → E in AAL38976. Ref.2
Sequence conflict6741V → E in AAP88018. Ref.3
Sequence conflict6741V → E in BAA09768. Ref.4
Sequence conflict14891E → K in AAL38976. Ref.2

Secondary structure

............................................... 1630
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 13, 2009. Version 4.
Checksum: D71E024FBC4F72D1

FASTA1,630174,885
        10         20         30         40         50         60 
MLKCIPLWRC NRHVESVDKR HCSLQAVPEE IYRYSRSLEE LLLDANQLRE LPKPFFRLLN 

        70         80         90        100        110        120 
LRKLGLSDNE IQRLPPEVAN FMQLVELDVS RNDIPEIPES IKFCKALEIA DFSGNPLSRL 

       130        140        150        160        170        180 
PDGFTQLRSL AHLALNDVSL QALPGDVGNL ANLVTLELRE NLLKSLPASL SFLVKLEQLD 

       190        200        210        220        230        240 
LGGNDLEVLP DTLGALPNLR ELWLDRNQLS ALPPELGNLR RLVCLDVSEN RLEELPAELG 

       250        260        270        280        290        300 
GLVLLTDLLL SQNLLRRLPD GIGQLKQLSI LKVDQNRLCE VTEAIGDCEN LSELILTENL 

       310        320        330        340        350        360 
LMALPRSLGK LTKLTNLNVD RNHLEALPPE IGGCVALSVL SLRDNRLAVL PPELAHTTEL 

       370        380        390        400        410        420 
HVLDVAGNRL QSLPFALTHL NLKALWLAEN QAQPMLRFQT EDDARTGEKV LTCYLLPQQP 

       430        440        450        460        470        480 
PPSLEDAGQQ GSLSETWSDA PPSRVSVIQF LEAPIGDEDA EEAAAEKRGL QRRATPHPSE 

       490        500        510        520        530        540 
LKVMKRSIEG RRSEACPCQP DSGSPLPAEE EKRLSAESGL SEDSRPSAST VSEAEPEGPS 

       550        560        570        580        590        600 
AEAQGGSQQE ATTAGGEEDA EEDYQEPTVH FAEDALLPGD DREIEEGQPE APWTLPGGRQ 

       610        620        630        640        650        660 
RLIRKDTPHY KKHFKISKLP QPEAVVALLQ GMQPDGEGPV APGGWHNGPH APWAPRAQKE 

       670        680        690        700        710        720 
EEEEEEGSPQ EEEVEEEEEN RAEEEEASTE EEDKEGAVVS APSVKGVSFD QANNLLIEPA 

       730        740        750        760        770        780 
RIEEEELTLT ILRQTGGLGI SIAGGKGSTP YKGDDEGIFI SRVSEEGPAA RAGVRVGDKL 

       790        800        810        820        830        840 
LEVNGVALQG AEHHEAVEAL RGAGTAVQMR VWRERMVEPE NAVTITPLRP EDDYSPRERR 

       850        860        870        880        890        900 
GGGLRLPLLP PESPGPLRQR HVACLARSER GLGFSIAGGK GSTPYRAGDA GIFVSRIAEG 

       910        920        930        940        950        960 
GAAHRAGTLQ VGDRVLSING VDVTEARHDH AVSLLTAASP TIALLLEREA GGPLPPSPLP 

       970        980        990       1000       1010       1020 
HSSPPTAAVA TTSITTATPG VPGLPSLAPS LLAAALEGPY PVEEIRLPRA GGPLGLSIVG 

      1030       1040       1050       1060       1070       1080 
GSDHSSHPFG VQEPGVFISK VLPRGLAARS GLRVGDRILA VNGQDVRDAT HQEAVSALLR 

      1090       1100       1110       1120       1130       1140 
PCLELSLLVR RDPAPPGLRE LCIQKAPGER LGISIRGGAR GHAGNPRDPT DEGIFISKVS 

      1150       1160       1170       1180       1190       1200 
PTGAAGRDGR LRVGLRLLEV NQQSLLGLTH GEAVQLLRSV GDTLTVLVCD GFEASTDAAL 

      1210       1220       1230       1240       1250       1260 
EVSPGVIANP FAAGIGHRNS LESISSIDRE LSPEGPGKEK ELPGQTLHWG PEATEAAGRG 

      1270       1280       1290       1300       1310       1320 
LQPLKLDYRA LAAVPSAGSV QRVPSGAAGG KMAESPCSPS GQQPPSPPSP DELPANVKQA 

      1330       1340       1350       1360       1370       1380 
YRAFAAVPTS HPPEDAPAQP PTPGPAASPE QLSFRERQKY FELEVRVPQA EGPPKRVSLV 

      1390       1400       1410       1420       1430       1440 
GADDLRKMQE EEARKLQQKR AQMLREAAEA GAEARLALDG ETLGEEEQED EQPPWASPSP 

      1450       1460       1470       1480       1490       1500 
TSRQSPASPP PLGGGAPVRT AKAERRHQER LRVQSPEPPA PERALSPAEL RALEAEKRAL 

      1510       1520       1530       1540       1550       1560 
WRAARMKSLE QDALRAQMVL SRSQEGRGTR GPLERLAEAP SPAPTPSPTP VEDLGPQTST 

      1570       1580       1590       1600       1610       1620 
SPGRLSPDFA EELRSLEPSP SPGPQEEDGE VALVLLGRPS PGAVGPEDVA LCSSRRPVRP 

      1630 
GRRGLGPVPS 

« Hide

Isoform 2 (Variant N1) [UniParc].

Checksum: 88EE83BC4A132CD6
Show »

FASTA1,549165,243
Isoform 3 [UniParc].

Checksum: BF9BD19ED0A577FA
Show »

FASTA1,655177,694

References

« Hide 'large scale' references
[1]"The tumor suppressor Scrib interacts with the zyxin-related protein LPP, which shuttles between cell adhesion sites and the nucleus."
Petit M.M.R., Meulemans S.M.P., Alen P., Ayoubi T.A.Y., Jansen E., Van de Ven W.J.M.
BMC Cell Biol. 6:1-1(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, VARIANT LEU-422.
[2]"Junctional recruitment of mammalian Scribble relies on E-cadherin engagement."
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.
Oncogene 24:4330-4339(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT LEU-422, SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-305, TISSUE SPECIFICITY.
[3]"The human Scrib N1 variant encoded by the SCRIB gene contains 13 leucine-rich repeats and 4 PDZ domains."
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.
Submitted (JUL-2008) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT LEU-422.
[4]"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."
Nagase T., Seki N., Tanaka A., Ishikawa K., Nomura N.
DNA Res. 2:167-174(1995) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), VARIANT LEU-422.
Tissue: Bone marrow and Brain.
[5]"Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
Cited for: SEQUENCE REVISION.
[6]Ohara O., Nagase T., Kikuno R., Nomura N.
Submitted (APR-2005) to the EMBL/GenBank/DDBJ databases
Cited for: SEQUENCE REVISION.
[7]"DNA sequence and analysis of human chromosome 8."
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. expand/collapse author list , 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.
Nature 439:331-335(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 799-1630 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1206-1630 (ISOFORM 3).
Tissue: Lung carcinoma and Neuroblastoma.
[9]"Human scribble (Vartul) is targeted for ubiquitin-mediated degradation by the high-risk papillomavirus E6 proteins and the E6AP ubiquitin-protein ligase."
Nakagawa S., Huibregtse J.M.
Mol. Cell. Biol. 20:8244-8253(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH UBE3A AND HPV E6, UBIQUITINATION, SUBCELLULAR LOCATION.
[10]"Robust phosphoproteomic profiling of tyrosine phosphorylation sites from human T cells using immobilized metal affinity chromatography and tandem mass spectrometry."
Brill L.M., Salomon A.R., Ficarro S.B., Mukherji M., Stettler-Gill M., Peters E.C.
Anal. Chem. 76:2763-2772(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1220, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[11]"Mammalian Scribble forms a tight complex with the betaPIX exchange factor."
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.
Curr. Biol. 14:987-995(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH ARHGEF7 AND GIT1, SUBCELLULAR LOCATION.
[12]"Thyrotropin receptor trafficking relies on the hScrib-betaPIX-GIT1-ARF6 pathway."
Lahuna O., Quellari M., Achard C., Nola S., Meduri G., Navarro C., Vitale N., Borg J.-P., Misrahi M.
EMBO J. 24:1364-1374(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, INTERACTION WITH TSHR.
[13]"hScrib interacts with ZO-2 at the cell-cell junctions of epithelial cells."
Metais J.-Y., Navarro C., Santoni M.-J., Audebert S., Borg J.-P.
FEBS Lett. 579:3725-3730(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TJP2.
[14]"The tumor suppressor Scrib selectively interacts with specific members of the zyxin family of proteins."
Petit M.M.R., Crombez K.R.M.O., Vervenne H.B.V.K., Weyns N., Van de Ven W.J.M.
FEBS Lett. 579:5061-5068(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TRIP6.
[15]"The mammalian Scribble polarity protein regulates epithelial cell adhesion and migration through E-cadherin."
Qin Y., Capaldo C., Gumbiner B.M., Macara I.G.
J. Cell Biol. 171:1061-1071(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL ADHESION.
[16]"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."
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.
Cancer Sci. 97:1217-1225(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL PROLIFERATION, SUBCELLULAR LOCATION.
[17]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-853; SER-1306; SER-1309 AND SER-1378, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[18]"Human scribble, a novel tumor suppressor identified as a target of high-risk HPV E6 for ubiquitin-mediated degradation, interacts with adenomatous polyposis coli."
Takizawa S., Nagasaka K., Nakagawa S., Yano T., Nakagawa K., Yasugi T., Takeuchi T., Kanda T., Huibregtse J.M., Akiyama T., Taketani Y.
Genes Cells 11:453-464(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH APC, SUBCELLULAR LOCATION.
[19]"Deregulation of scribble promotes mammary tumorigenesis and reveals a role for cell polarity in carcinoma."
Zhan L., Rosenberg A., Bergami K.C., Yu M., Xuan Z., Jaffe A.B., Allred C., Muthuswamy S.K.
Cell 135:865-878(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN APOPTOSIS, SUBCELLULAR LOCATION, MUTAGENESIS OF PRO-305.
[20]"Scrib regulates PAK activity during the cell migration process."
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.
Hum. Mol. Genet. 17:3552-3565(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION IN CELL MIGRATION, INTERACTION WITH PAK1 AND PAK2.
[21]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1475 AND SER-1566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[22]"Loss of human Scribble cooperates with H-Ras to promote cell invasion through deregulation of MAPK signalling."
Dow L.E., Elsum I.A., King C.L., Kinross K.M., Richardson H.E., Humbert P.O.
Oncogene 27:5988-6001(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[23]"Tick-borne encephalitis virus NS5 associates with membrane protein scribble and impairs interferon-stimulated JAK-STAT signalling."
Werme K., Wigerius M., Johansson M.
Cell. Microbiol. 10:696-712(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH TICK-BORNE ENCEPHALITIS VIRUS RNA-DIRECTED RNA POLYMERASE NS5.
[24]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[25]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[26]"MCC, a new interacting protein for Scrib, is required for cell migration in epithelial cells."
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.
FEBS Lett. 583:2326-2332(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCC.
[27]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1348 AND SER-1448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[28]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-826; SER-1220; THR-1342; SER-1348; SER-1475; SER-1547 AND SER-1566, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[29]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
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.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[30]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[31]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-688; THR-689; SER-1220; SER-1309; SER-1378 AND SER-1448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[32]"The PDZ-binding motif of MCC is phosphorylated at position -1 and controls lamellipodia formation in colon epithelial cells."
Pangon L., Van Kralingen C., Abas M., Daly R.J., Musgrove E.A., Kohonen-Corish M.R.
Biochim. Biophys. Acta 1823:1058-1067(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH MCC, SUBCELLULAR LOCATION.
[33]"Solution structure of the first, second and fourth PDZ domain of human scribble (KIAA0147 protein)."
RIKEN structural genomics initiative (RSGI)
Submitted (NOV-2005) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 718-814; 860-951 AND 1096-1193.
[34]"Mutations in the planar cell polarity genes CELSR1 and SCRIB are associated with the severe neural tube defect craniorachischisis."
Robinson A., Escuin S., Doudney K., Vekemans M., Stevenson R.E., Greene N.D., Copp A.J., Stanier P.
Hum. Mutat. 33:440-447(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: VARIANTS NTD SER-454 AND GLN-1535, CHARACTERIZATION OF VARIANTS NTD SER-454 AND GLN-1535.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF240677 mRNA. Translation: AAP88017.1.
AY062238 mRNA. Translation: AAL38976.1.
AF271734 mRNA. Translation: AAP88018.2.
D63481 mRNA. Translation: BAA09768.3.
AC105219 Genomic DNA. No translation available.
BC009490 mRNA. Translation: AAH09490.2.
BC014632 mRNA. Translation: AAH14632.2.
RefSeqNP_056171.3. NM_015356.4.
NP_874365.3. NM_182706.4.
UniGeneHs.436329.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1UJUNMR-A1096-1193[»]
1WHANMR-A860-951[»]
1X5QNMR-A718-814[»]
2W4FX-ray1.30A725-815[»]
ProteinModelPortalQ14160.
SMRQ14160. Positions 718-814, 860-953, 1098-1194.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid117060. 17 interactions.
DIPDIP-31259N.
IntActQ14160. 24 interactions.
MINTMINT-147371.
STRING9606.ENSP00000349486.

PTM databases

PhosphoSiteQ14160.

Polymorphism databases

DMDM261260101.

Proteomic databases

PaxDbQ14160.
PRIDEQ14160.

Protocols and materials databases

DNASU23513.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000320476; ENSP00000322938; ENSG00000180900. [Q14160-1]
ENST00000356994; ENSP00000349486; ENSG00000180900. [Q14160-3]
ENST00000377533; ENSP00000366756; ENSG00000180900. [Q14160-2]
ENST00000564122; ENSP00000456859; ENSG00000260968. [Q14160-2]
ENST00000567584; ENSP00000456561; ENSG00000260968. [Q14160-3]
ENST00000569114; ENSP00000455629; ENSG00000260968. [Q14160-1]
GeneID23513.
KEGGhsa:23513.
UCSCuc003yzo.1. human. [Q14160-3]
uc003yzp.1. human. [Q14160-1]

Organism-specific databases

CTD23513.
GeneCardsGC08M144874.
HGNCHGNC:30377. SCRIB.
HPACAB015463.
CAB022081.
HPA023557.
MIM182940. phenotype.
607733. gene.
neXtProtNX_Q14160.
PharmGKBPA134936275.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG4886.
HOGENOMHOG000113281.
KOK16175.
OMAEGFTQLR.
PhylomeDBQ14160.
TreeFamTF351429.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ14160.

Gene expression databases

ArrayExpressQ14160.
BgeeQ14160.
CleanExHS_SCRIB.
GenevestigatorQ14160.

Family and domain databases

Gene3D2.30.42.10. 4 hits.
InterProIPR001611. Leu-rich_rpt.
IPR025875. Leu-rich_rpt_4.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR001478. PDZ.
[Graphical view]
PfamPF12799. LRR_4. 2 hits.
PF00595. PDZ. 4 hits.
[Graphical view]
SMARTSM00369. LRR_TYP. 2 hits.
SM00228. PDZ. 4 hits.
[Graphical view]
SUPFAMSSF50156. SSF50156. 4 hits.
PROSITEPS51450. LRR. 13 hits.
PS50106. PDZ. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ14160.
GeneWikiSCRIB.
GenomeRNAi23513.
NextBio45935.
PROQ14160.
SOURCESearch...

Entry information

Entry nameSCRIB_HUMAN
AccessionPrimary (citable) accession number: Q14160
Secondary accession number(s): Q6P496 expand/collapse secondary AC list , Q7Z5D1, Q8WWV8, Q96C69, Q96GG1
Entry history
Integrated into UniProtKB/Swiss-Prot: July 19, 2004
Last sequence update: October 13, 2009
Last modified: April 16, 2014
This is version 143 of the entry and version 4 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 8

Human chromosome 8: entries, gene names and cross-references to MIM