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Q14160

- SCRIB_HUMAN

UniProt

Q14160 - SCRIB_HUMAN

Protein

Protein scribble homolog

Gene

SCRIB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 148 (01 Oct 2014)
      Sequence version 4 (13 Oct 2009)
      Previous versions | rss
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    Functioni

    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.7 Publications

    GO - Molecular functioni

    1. protein binding Source: UniProtKB

    GO - Biological processi

    1. activation of Rac GTPase activity Source: UniProtKB
    2. apoptotic process involved in morphogenesis Source: UniProtKB
    3. astrocyte cell migration Source: Ensembl
    4. asymmetric protein localization Source: Ensembl
    5. cell migration Source: UniProtKB
    6. cell proliferation Source: UniProtKB
    7. establishment of apical/basal cell polarity Source: UniProtKB
    8. mammary gland duct morphogenesis Source: UniProtKB
    9. negative regulation of mitotic cell cycle Source: UniProtKB
    10. neural tube closure Source: UniProtKB
    11. positive chemotaxis Source: UniProtKB
    12. positive regulation of apoptotic process Source: UniProtKB
    13. positive regulation of receptor recycling Source: UniProtKB
    14. protein localization to adherens junction Source: BHF-UCL
    15. single organismal cell-cell adhesion Source: UniProtKB
    16. synaptic vesicle endocytosis Source: Ensembl
    17. synaptic vesicle targeting Source: Ensembl
    18. viral process Source: UniProtKB-KW
    19. wound healing Source: Ensembl

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Host-virus interaction

    Enzyme and pathway databases

    ReactomeiREACT_172638. Asymmetric localization of PCP proteins.
    SignaLinkiQ14160.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Protein scribble homolog
    Short name:
    Scribble
    Short name:
    hScrib
    Alternative name(s):
    Protein LAP4
    Gene namesi
    Name:SCRIB
    Synonyms:CRIB1, KIAA0147, LAP4, SCRB1, VARTUL
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:30377. SCRIB.

    Subcellular locationi

    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.

    GO - Cellular componenti

    1. basolateral plasma membrane Source: Ensembl
    2. cell-cell adherens junction Source: UniProtKB
    3. cell-cell junction Source: UniProtKB
    4. extracellular vesicular exosome Source: UniProt
    5. lamellipodium Source: UniProtKB-SubCell
    6. myelin sheath abaxonal region Source: Ensembl
    7. plasma membrane Source: UniProtKB
    8. Scrib-APC-beta-catenin complex Source: BHF-UCL

    Keywords - Cellular componenti

    Cell junction, Cell membrane, Cell projection, Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    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.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti454 – 4541P → S in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. 1 Publication
    VAR_067219
    Natural varianti1535 – 15351R → Q in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. 1 Publication
    VAR_067220

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi305 – 3051P → L: Loss of pro-apoptotic function and of the targeting to cell-cell junctions. Targeted to the cytoplasm. Alters interaction with TJP2. 3 Publications
    Mutagenesisi738 – 7392LG → AE: Alters interaction with LPP. 1 Publication
    Mutagenesisi738 – 7381L → R: Loss of anti-proliferative activity. 1 Publication
    Mutagenesisi872 – 8732LG → AE: Alters interaction with LPP. 1 Publication
    Mutagenesisi1014 – 10152LG → AE: Loss of interaction with LPP and TRIP6. 1 Publication
    Mutagenesisi1111 – 11122LG → AE: Alters interaction with LPP. 1 Publication

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi182940. phenotype.
    PharmGKBiPA134936275.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16301630Protein scribble homologPRO_0000188303Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei688 – 6881Phosphoserine1 Publication
    Modified residuei689 – 6891Phosphothreonine1 Publication
    Modified residuei826 – 8261Phosphothreonine3 Publications
    Modified residuei835 – 8351Phosphoserine1 Publication
    Modified residuei853 – 8531Phosphoserine2 Publications
    Modified residuei939 – 9391Phosphoserine2 Publications
    Modified residuei1140 – 11401Phosphoserine1 Publication
    Modified residuei1220 – 12201Phosphoserine4 Publications
    Modified residuei1223 – 12231Phosphoserine1 Publication
    Modified residuei1232 – 12321Phosphoserine2 Publications
    Modified residuei1306 – 13061Phosphoserine2 Publications
    Modified residuei1309 – 13091Phosphoserine3 Publications
    Modified residuei1342 – 13421Phosphothreonine3 Publications
    Modified residuei1348 – 13481Phosphoserine4 Publications
    Modified residuei1378 – 13781Phosphoserine3 Publications
    Modified residuei1437 – 14371Phosphoserine1 Publication
    Modified residuei1448 – 14481Phosphoserine3 Publications
    Modified residuei1475 – 14751Phosphoserine3 Publications
    Modified residuei1486 – 14861Phosphoserine1 Publication
    Modified residuei1547 – 15471Phosphoserine2 Publications
    Modified residuei1566 – 15661Phosphoserine4 Publications

    Post-translational modificationi

    Ubiquitinated; targeted for UBE3A-dependent multiubiquitination in the presence of high-risk HPV E6 proteins and degraded.1 Publication

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiQ14160.
    PaxDbiQ14160.
    PRIDEiQ14160.

    PTM databases

    PhosphoSiteiQ14160.

    Expressioni

    Tissue specificityi

    Expressed in kidney, skeletal muscles, liver, lung, breast, intestine, placenta and skin mainly in epithelial cells (at protein level).1 Publication

    Gene expression databases

    ArrayExpressiQ14160.
    BgeeiQ14160.
    CleanExiHS_SCRIB.
    GenevestigatoriQ14160.

    Organism-specific databases

    HPAiCAB015463.
    CAB022081.
    HPA023557.

    Interactioni

    Subunit structurei

    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.By similarity11 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    APCP250544EBI-357345,EBI-727707
    ARHGEF7Q141554EBI-357345,EBI-717515
    E6P031265EBI-357345,EBI-1177242From a different organism.
    E6P064633EBI-357345,EBI-1186926From a different organism.
    MAPK3P273612EBI-357345,EBI-73995
    MCCP235088EBI-357345,EBI-307531
    PHLPP1O603462EBI-357345,EBI-2511516

    Protein-protein interaction databases

    BioGridi117060. 18 interactions.
    DIPiDIP-31259N.
    IntActiQ14160. 25 interactions.
    MINTiMINT-147371.
    STRINGi9606.ENSP00000349486.

    Structurei

    Secondary structure

    1
    1630
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Beta strandi726 – 7327
    Beta strandi737 – 7448
    Beta strandi757 – 7637
    Helixi768 – 7725
    Beta strandi779 – 7835
    Helixi793 – 8019
    Beta strandi805 – 8128
    Beta strandi860 – 8656
    Beta strandi875 – 8773
    Beta strandi893 – 8964
    Helixi903 – 9064
    Beta strandi914 – 9207
    Helixi928 – 9358
    Beta strandi942 – 9487
    Beta strandi1097 – 10993
    Beta strandi1101 – 11044
    Beta strandi1113 – 11164
    Beta strandi1119 – 11224
    Beta strandi1135 – 11395
    Helixi1144 – 11485
    Beta strandi1159 – 11624
    Helixi1170 – 11778
    Beta strandi1181 – 11866

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    1UJUNMR-A1096-1193[»]
    1WHANMR-A860-951[»]
    1X5QNMR-A718-814[»]
    2W4FX-ray1.30A725-815[»]
    ProteinModelPortaliQ14160.
    SMRiQ14160. Positions 718-814, 860-953, 1098-1194.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ14160.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Repeati37 – 5822LRR 1Add
    BLAST
    Repeati60 – 8122LRR 2Add
    BLAST
    Repeati83 – 10422LRR 3Add
    BLAST
    Repeati106 – 12722LRR 4Add
    BLAST
    Repeati129 – 15022LRR 5Add
    BLAST
    Repeati152 – 17423LRR 6Add
    BLAST
    Repeati175 – 19723LRR 7Add
    BLAST
    Repeati198 – 21922LRR 8Add
    BLAST
    Repeati221 – 24323LRR 9Add
    BLAST
    Repeati244 – 26522LRR 10Add
    BLAST
    Repeati267 – 28822LRR 11Add
    BLAST
    Repeati290 – 31223LRR 12Add
    BLAST
    Repeati313 – 33422LRR 13Add
    BLAST
    Repeati336 – 35722LRR 14Add
    BLAST
    Repeati359 – 38123LRR 15Add
    BLAST
    Repeati382 – 40221LRR 16Add
    BLAST
    Domaini728 – 81588PDZ 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini862 – 95089PDZ 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini1004 – 109390PDZ 3PROSITE-ProRule annotationAdd
    BLAST
    Domaini1100 – 119495PDZ 4PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 818818Sufficient for targeting to adherens junction and to inhibit cell proliferationAdd
    BLAST
    Regioni717 – 1229513Interaction with ARHGEF7Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili458 – 47417Sequence AnalysisAdd
    BLAST
    Coiled coili656 – 70146Sequence AnalysisAdd
    BLAST
    Coiled coili1379 – 141941Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi660 – 69536Glu-richAdd
    BLAST
    Compositional biasi1296 – 134954Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the LAP (LRR and PDZ) protein family.Curated
    Contains 16 LRR (leucine-rich) repeats.Curated
    Contains 4 PDZ (DHR) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Leucine-rich repeat, Repeat

    Phylogenomic databases

    eggNOGiCOG4886.
    HOGENOMiHOG000113281.
    KOiK16175.
    OMAiEGFTQLR.
    PhylomeDBiQ14160.
    TreeFamiTF351429.

    Family and domain databases

    Gene3Di2.30.42.10. 4 hits.
    InterProiIPR001611. Leu-rich_rpt.
    IPR025875. Leu-rich_rpt_4.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR001478. PDZ.
    [Graphical view]
    PfamiPF12799. LRR_4. 2 hits.
    PF13855. LRR_8. 1 hit.
    PF00595. PDZ. 4 hits.
    [Graphical view]
    SMARTiSM00369. LRR_TYP. 2 hits.
    SM00228. PDZ. 4 hits.
    [Graphical view]
    SUPFAMiSSF50156. SSF50156. 4 hits.
    PROSITEiPS51450. LRR. 13 hits.
    PS50106. PDZ. 4 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q14160-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MLKCIPLWRC NRHVESVDKR HCSLQAVPEE IYRYSRSLEE LLLDANQLRE     50
    LPKPFFRLLN LRKLGLSDNE IQRLPPEVAN FMQLVELDVS RNDIPEIPES 100
    IKFCKALEIA DFSGNPLSRL PDGFTQLRSL AHLALNDVSL QALPGDVGNL 150
    ANLVTLELRE NLLKSLPASL SFLVKLEQLD LGGNDLEVLP DTLGALPNLR 200
    ELWLDRNQLS ALPPELGNLR RLVCLDVSEN RLEELPAELG GLVLLTDLLL 250
    SQNLLRRLPD GIGQLKQLSI LKVDQNRLCE VTEAIGDCEN LSELILTENL 300
    LMALPRSLGK LTKLTNLNVD RNHLEALPPE IGGCVALSVL SLRDNRLAVL 350
    PPELAHTTEL HVLDVAGNRL QSLPFALTHL NLKALWLAEN QAQPMLRFQT 400
    EDDARTGEKV LTCYLLPQQP PPSLEDAGQQ GSLSETWSDA PPSRVSVIQF 450
    LEAPIGDEDA EEAAAEKRGL QRRATPHPSE LKVMKRSIEG RRSEACPCQP 500
    DSGSPLPAEE EKRLSAESGL SEDSRPSAST VSEAEPEGPS AEAQGGSQQE 550
    ATTAGGEEDA EEDYQEPTVH FAEDALLPGD DREIEEGQPE APWTLPGGRQ 600
    RLIRKDTPHY KKHFKISKLP QPEAVVALLQ GMQPDGEGPV APGGWHNGPH 650
    APWAPRAQKE EEEEEEGSPQ EEEVEEEEEN RAEEEEASTE EEDKEGAVVS 700
    APSVKGVSFD QANNLLIEPA RIEEEELTLT ILRQTGGLGI SIAGGKGSTP 750
    YKGDDEGIFI SRVSEEGPAA RAGVRVGDKL LEVNGVALQG AEHHEAVEAL 800
    RGAGTAVQMR VWRERMVEPE NAVTITPLRP EDDYSPRERR GGGLRLPLLP 850
    PESPGPLRQR HVACLARSER GLGFSIAGGK GSTPYRAGDA GIFVSRIAEG 900
    GAAHRAGTLQ VGDRVLSING VDVTEARHDH AVSLLTAASP TIALLLEREA 950
    GGPLPPSPLP HSSPPTAAVA TTSITTATPG VPGLPSLAPS LLAAALEGPY 1000
    PVEEIRLPRA GGPLGLSIVG GSDHSSHPFG VQEPGVFISK VLPRGLAARS 1050
    GLRVGDRILA VNGQDVRDAT HQEAVSALLR PCLELSLLVR RDPAPPGLRE 1100
    LCIQKAPGER LGISIRGGAR GHAGNPRDPT DEGIFISKVS PTGAAGRDGR 1150
    LRVGLRLLEV NQQSLLGLTH GEAVQLLRSV GDTLTVLVCD GFEASTDAAL 1200
    EVSPGVIANP FAAGIGHRNS LESISSIDRE LSPEGPGKEK ELPGQTLHWG 1250
    PEATEAAGRG LQPLKLDYRA LAAVPSAGSV QRVPSGAAGG KMAESPCSPS 1300
    GQQPPSPPSP DELPANVKQA YRAFAAVPTS HPPEDAPAQP PTPGPAASPE 1350
    QLSFRERQKY FELEVRVPQA EGPPKRVSLV GADDLRKMQE EEARKLQQKR 1400
    AQMLREAAEA GAEARLALDG ETLGEEEQED EQPPWASPSP TSRQSPASPP 1450
    PLGGGAPVRT AKAERRHQER LRVQSPEPPA PERALSPAEL RALEAEKRAL 1500
    WRAARMKSLE QDALRAQMVL SRSQEGRGTR GPLERLAEAP SPAPTPSPTP 1550
    VEDLGPQTST SPGRLSPDFA EELRSLEPSP SPGPQEEDGE VALVLLGRPS 1600
    PGAVGPEDVA LCSSRRPVRP GRRGLGPVPS 1630
    Length:1,630
    Mass (Da):174,885
    Last modified:October 13, 2009 - v4
    Checksum:iD71E024FBC4F72D1
    GO
    Isoform 2 (identifier: Q14160-2) [UniParc]FASTAAdd to Basket

    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.

    Show »
    Length:1,549
    Mass (Da):165,243
    Checksum:i88EE83BC4A132CD6
    GO
    Isoform 3 (identifier: Q14160-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,655
    Mass (Da):177,694
    Checksum:iBF9BD19ED0A577FA
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti674 – 6741V → E in AAP88017. (PubMed:15649318)Curated
    Sequence conflicti674 – 6741V → E in AAL38976. (PubMed:15806148)Curated
    Sequence conflicti674 – 6741V → E in AAP88018. 1 PublicationCurated
    Sequence conflicti674 – 6741V → E in BAA09768. (PubMed:8590280)Curated
    Sequence conflicti1489 – 14891E → K in AAL38976. (PubMed:15806148)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti422 – 4221P → L.4 Publications
    Corresponds to variant rs6558394 [ dbSNP | Ensembl ].
    VAR_019429
    Natural varianti454 – 4541P → S in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. 1 Publication
    VAR_067219
    Natural varianti1535 – 15351R → Q in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. 1 Publication
    VAR_067220

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 8181Missing in isoform 2. 1 PublicationVSP_010906Add
    BLAST
    Alternative sequencei1565 – 15651L → LPLSGKKFDYRAFAALPSSR PVYDIQ in isoform 3. 1 PublicationVSP_010908

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS6411.1. [Q14160-1]
    CCDS6412.1. [Q14160-3]
    RefSeqiNP_056171.3. NM_015356.4.
    NP_874365.3. NM_182706.4.
    UniGeneiHs.436329.

    Genome annotation databases

    EnsembliENST00000320476; ENSP00000322938; ENSG00000180900. [Q14160-1]
    ENST00000356994; ENSP00000349486; ENSG00000180900. [Q14160-3]
    ENST00000377533; ENSP00000366756; ENSG00000180900. [Q14160-2]
    GeneIDi23513.
    KEGGihsa:23513.
    UCSCiuc003yzo.1. human. [Q14160-3]
    uc003yzp.1. human. [Q14160-1]

    Polymorphism databases

    DMDMi261260101.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS6411.1. [Q14160-1 ]
    CCDS6412.1. [Q14160-3 ]
    RefSeqi NP_056171.3. NM_015356.4.
    NP_874365.3. NM_182706.4.
    UniGenei Hs.436329.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    1UJU NMR - A 1096-1193 [» ]
    1WHA NMR - A 860-951 [» ]
    1X5Q NMR - A 718-814 [» ]
    2W4F X-ray 1.30 A 725-815 [» ]
    ProteinModelPortali Q14160.
    SMRi Q14160. Positions 718-814, 860-953, 1098-1194.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 117060. 18 interactions.
    DIPi DIP-31259N.
    IntActi Q14160. 25 interactions.
    MINTi MINT-147371.
    STRINGi 9606.ENSP00000349486.

    PTM databases

    PhosphoSitei Q14160.

    Polymorphism databases

    DMDMi 261260101.

    Proteomic databases

    MaxQBi Q14160.
    PaxDbi Q14160.
    PRIDEi Q14160.

    Protocols and materials databases

    DNASUi 23513.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000320476 ; ENSP00000322938 ; ENSG00000180900 . [Q14160-1 ]
    ENST00000356994 ; ENSP00000349486 ; ENSG00000180900 . [Q14160-3 ]
    ENST00000377533 ; ENSP00000366756 ; ENSG00000180900 . [Q14160-2 ]
    GeneIDi 23513.
    KEGGi hsa:23513.
    UCSCi uc003yzo.1. human. [Q14160-3 ]
    uc003yzp.1. human. [Q14160-1 ]

    Organism-specific databases

    CTDi 23513.
    GeneCardsi GC08M144874.
    HGNCi HGNC:30377. SCRIB.
    HPAi CAB015463.
    CAB022081.
    HPA023557.
    MIMi 182940. phenotype.
    607733. gene.
    neXtProti NX_Q14160.
    PharmGKBi PA134936275.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG4886.
    HOGENOMi HOG000113281.
    KOi K16175.
    OMAi EGFTQLR.
    PhylomeDBi Q14160.
    TreeFami TF351429.

    Enzyme and pathway databases

    Reactomei REACT_172638. Asymmetric localization of PCP proteins.
    SignaLinki Q14160.

    Miscellaneous databases

    EvolutionaryTracei Q14160.
    GeneWikii SCRIB.
    GenomeRNAii 23513.
    NextBioi 45935.
    PROi Q14160.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q14160.
    Bgeei Q14160.
    CleanExi HS_SCRIB.
    Genevestigatori Q14160.

    Family and domain databases

    Gene3Di 2.30.42.10. 4 hits.
    InterProi IPR001611. Leu-rich_rpt.
    IPR025875. Leu-rich_rpt_4.
    IPR003591. Leu-rich_rpt_typical-subtyp.
    IPR001478. PDZ.
    [Graphical view ]
    Pfami PF12799. LRR_4. 2 hits.
    PF13855. LRR_8. 1 hit.
    PF00595. PDZ. 4 hits.
    [Graphical view ]
    SMARTi SM00369. LRR_TYP. 2 hits.
    SM00228. PDZ. 4 hits.
    [Graphical view ]
    SUPFAMi SSF50156. SSF50156. 4 hits.
    PROSITEi PS51450. LRR. 13 hits.
    PS50106. PDZ. 4 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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. 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.
      , 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. 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. 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. 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. 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. 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.

    Entry informationi

    Entry nameiSCRIB_HUMAN
    AccessioniPrimary (citable) accession number: Q14160
    Secondary accession number(s): Q6P496
    , Q7Z5D1, Q8WWV8, Q96C69, Q96GG1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 19, 2004
    Last sequence update: October 13, 2009
    Last modified: October 1, 2014
    This is version 148 of the entry and version 4 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3