Q14160 · SCRIB_HUMAN

  • Protein
    Protein scribble homolog
  • Gene
    SCRIB
  • Status
    UniProtKB reviewed (Swiss-Prot)
  • Amino acids
  • Protein existence
    Evidence at protein level
  • Annotation score
    5/5

Function

function

Scaffold protein involved in different aspects of polarized cell differentiation regulating epithelial and neuronal morphogenesis and T-cell polarization (PubMed:15182672, PubMed:16344308, PubMed:16965391, PubMed:18641685, PubMed:18716323, PubMed:19041750, PubMed:27380321).
Via its interaction with CRTAM, required for the late phase polarization of a subset of CD4+ T-cells, which in turn regulates TCR-mediated proliferation and IFNG and IL22 production (By similarity).
Plays a role in cell directional movement, cell orientation, cell sheet organization and Golgi complex polarization at the cell migration front (By similarity).
Promotes epithelial cell layer barrier function via maintaining cell-cell adhesion (By similarity).
Most probably functions in the establishment of apico-basal cell polarity (PubMed:16344308, PubMed:19041750).
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 (PubMed:16965391, PubMed:19041750).
May regulate cell invasion via MAPK-mediated cell migration and adhesion (PubMed:18641685, PubMed:18716323).
May play a role in exocytosis and in the targeting of synaptic vesicles to synapses (PubMed:15182672).
Functions as an activator of Rac GTPase activity (PubMed:15182672).

GO annotations

all annotationsall molecular functionvirus receptor activitydna bindingrna bindingcytoskeletal motor activitycatalytic activitygtpase activitystructural molecule activitytransporter activitycytoskeletal protein bindinglipid bindingcyclase activityantioxidant activityoxidoreductase activitytransferase activityhydrolase activitylyase activityisomerase activityligase activityprotein tag activitycargo receptor activityhistone bindingprotein folding chaperonetranslation regulator activitynutrient reservoir activityreceptor ligand activitymolecular transducer activitymolecular adaptor activitytoxin activitycell adhesion mediator activitymolecular function regulator activityvirus coreceptor activitycatalytic activity, acting on a proteincatalytic activity, acting on dnacatalytic activity, acting on rnamolecular carrier activitytranscription regulator activitygeneral transcription initiation factor activitymolecular sensor activitymolecular sequestering activityatp-dependent activityother molecular functionall biological processmitotic cell cyclecytokinesiscytoplasmic translationimmune system processmuscle system processcirculatory system processrenal system processrespiratory system processcarbohydrate metabolic processgeneration of precursor metabolites and energydna replicationdna repairdna recombinationchromatin organizationdna-templated transcriptionregulation of dna-templated transcriptiontrna metabolic processprotein foldingprotein glycosylationamino acid metabolic processmodified amino acid metabolic processlipid metabolic processvitamin metabolic processsulfur compound metabolic processintracellular protein transportnucleocytoplasmic transportautophagyinflammatory responsemitochondrion organizationcytoskeleton organizationmicrotubule-based movementperoxisome organizationlysosome organizationchromosome segregationcell adhesionestablishment or maintenance of cell polarityprogrammed cell deathphotosynthesismrna metabolic processsnrna metabolic processvesicle-mediated transportreproductive processdigestive system processsignalingcell differentiationprotein catabolic processextracellular matrix organizationregulatory ncrna-mediated gene silencingtelomere organizationcell junction organizationwound healingribosome biogenesiscilium organizationanatomical structure developmentcell motilitynervous system processendocrine processprotein maturationtransmembrane transportnucleobase-containing small molecule metabolic processhepaticobiliary system processmembrane organizationprotein-containing complex assemblycell wall organization or biogenesisnitrogen cycle metabolic processprotein localization to plasma membranedefense response to other organismdetoxificationmeiotic nuclear divisionmitotic nuclear divisionmitochondrial gene expressioncarbohydrate derivative metabolic processother biological processall cellular componentnuclear chromosomeextracellular regionextracellular spacecell wallnucleusnuclear envelopenucleoplasmchromosomenucleolusmitochondrionlysosomeendosomevacuoleperoxisomeendoplasmic reticulumgolgi apparatuslipid dropletmicrotubule organizing centercytosolribosomecytoskeletonplasma membraneciliumplastidthylakoidexternal encapsulating structureextracellular matrixcytoplasmic vesicleorganelleother cellular component
Cell color indicative of number of GO terms
AspectTerm
Cellular Componentadherens junction
Cellular Componentbasolateral plasma membrane
Cellular Componentcell junction
Cellular Componentcell-cell contact zone
Cellular Componentcell-cell junction
Cellular Componentcytoplasm
Cellular Componentextracellular exosome
Cellular Componentextrinsic component of postsynaptic density membrane
Cellular Componentglutamatergic synapse
Cellular Componentimmunological synapse
Cellular Componentlamellipodium
Cellular Componentmyelin sheath abaxonal region
Cellular Componentnucleoplasm
Cellular Componentplasma membrane
Cellular Componentpostsynaptic density
Cellular Componentpresynapse
Cellular ComponentScrib-APC-beta-catenin complex
Molecular Functioncadherin binding
Molecular Functionprotein kinase binding
Molecular Functionsignaling adaptor activity
Biological Processactivation of GTPase activity
Biological Processapoptotic process involved in morphogenesis
Biological Processastrocyte cell migration
Biological Processauditory receptor cell stereocilium organization
Biological Processcell migration
Biological Processcell population proliferation
Biological Processcell-cell adhesion
Biological Processcochlear nucleus development
Biological Processepithelial structure maintenance
Biological Processestablishment of apical/basal cell polarity
Biological Processestablishment of T cell polarity
Biological Processestablishment or maintenance of epithelial cell apical/basal polarity
Biological Processmammary gland duct morphogenesis
Biological Processnegative regulation of activated T cell proliferation
Biological Processnegative regulation of mitotic cell cycle
Biological Processneural tube closure
Biological Processneurotransmitter receptor transport postsynaptic membrane to endosome
Biological Processneurotransmitter receptor transport, endosome to postsynaptic membrane
Biological Processpolarized epithelial cell differentiation
Biological Processpositive chemotaxis
Biological Processpositive regulation of apoptotic process
Biological Processpositive regulation of receptor recycling
Biological Processpositive regulation of type II interferon production
Biological Processpost-anal tail morphogenesis
Biological Processprotein localization to adherens junction
Biological Processreceptor clustering
Biological Processregulation of postsynaptic neurotransmitter receptor internalization
Biological Processsynaptic vesicle endocytosis
Biological Processsynaptic vesicle targeting
Biological Processwound healing

Keywords

Enzyme and pathway databases

Protein family/group databases

Names & Taxonomy

Protein names

  • Recommended name
    Protein scribble homolog
  • Short names
    Scribble; hScrib
  • Alternative names
    • Protein LAP4

Gene names

    • Name
      SCRIB
    • Synonyms
      CRIB1, KIAA0147, LAP4, SCRB1, VARTUL

Organism names

  • Taxonomic identifier
  • Taxonomic lineage
    Eukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo

Accessions

  • Primary accession
    Q14160
  • Secondary accessions
    • Q6P496
    • Q7Z5D1
    • Q8WWV8
    • Q96C69
    • Q96GG1

Proteomes

Organism-specific databases

Subcellular Location

Cell membrane
; Peripheral membrane protein
Cell junction
Cytoplasm
Postsynapse
Presynapse
Note: Targeting to cell-cell junctions which is CDH1-dependent is required for the pro-apoptotic activity. In a subset of CD4+ T-cells, colocalizes with CRTAM at the immunological synapse during the late phase of T-cell activation (By similarity).
Localized to small puncta throughout the cytoplasm and cell membrane when in the presence of SNAIL1 (By similarity).
Localized along the length of perinuclear emanating vimentin bundles and at vimentin-positive fibrils at the cell periphery (PubMed:19386766).
Localized to the lateral plasma membrane during the establishment and maturation of cell-cell contacts (PubMed:19386766).

Keywords

Disease & Variants

Involvement in disease

Neural tube defects (NTD)

  • Note
    • The disease is caused by variants affecting the gene represented in this entry
  • Description
    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.
  • See also
    MIM:182940
Natural variants in NTD
Variant IDPosition(s)ChangeDescription
VAR_067219454P>Sin NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane; dbSNP:rs1302482009
VAR_0672201535R>Qin NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane; dbSNP:rs782428100

Features

Showing features for mutagenesis, natural variant.

TypeIDPosition(s)Description
Mutagenesis4Loss of palmitoylation. Loss of palmitoylation, localization to cell-cell junctions and function in epithelial cell polarization and signaling pathways regulation; when associated with S-10.
Mutagenesis10Loss of palmitoylation. Loss of palmitoylation, localization to cell-cell junctions and function in epithelial cell polarization and signaling pathways regulation; when associated with S-4.
Mutagenesis22No effect on palmitoylation.
Mutagenesis305Decreased palmitoylation. Loss of localization at the plasma membrane. Loss of targeting to cell-cell junctions. Alters interaction with TJP2. Loss of pro-apoptotic function. Loss of function in epithelial cell polarization and signaling pathways regulation. Abolishes interaction with YES1 in the closed conformation and instead facilitates SCRIB interaction with YES1 in an open conformation.
Natural variantVAR_019429422in dbSNP:rs6558394
Natural variantVAR_067219454in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane; dbSNP:rs1302482009
Mutagenesis738Loss of anti-proliferative activity.
Mutagenesis738-739Alters interaction with LPP.
Mutagenesis872-873Alters interaction with LPP.
Mutagenesis1014-1015Loss of interaction with LPP and TRIP6.
Mutagenesis1111-1112Alters interaction with LPP.
Natural variantVAR_0672201535in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane; dbSNP:rs782428100

Variants

We now provide the "Disease & Variants" viewer in its own tab.

The viewer provides 3,859 variants from UniProt as well as other sources including ClinVar and dbSNP.

Go to variant viewer

Keywords

Organism-specific databases

Miscellaneous

Genetic variation databases

PTM/Processing

Features

Showing features for chain, modified residue (large scale data), modified residue.

TypeIDPosition(s)SourceDescription
ChainPRO_00001883031-1655UniProtProtein scribble homolog
Modified residue (large scale data)23PRIDEPhosphoserine
Modified residue (large scale data)35PRIDEPhosphoserine
Modified residue37UniProtPhosphoserine
Modified residue (large scale data)37PRIDEPhosphoserine
Modified residue378UniProtPhosphothreonine
Modified residue (large scale data)432PRIDEPhosphoserine
Modified residue (large scale data)446PRIDEPhosphoserine
Modified residue475UniProtPhosphothreonine
Modified residue (large scale data)475PRIDEPhosphothreonine
Modified residue (large scale data)502PRIDEPhosphoserine
Modified residue504UniProtPhosphoserine
Modified residue (large scale data)504PRIDEPhosphoserine
Modified residue (large scale data)515PRIDEPhosphoserine
Modified residue (large scale data)668PRIDEPhosphoserine
Modified residue688UniProtPhosphoserine
Modified residue (large scale data)688PRIDEPhosphoserine
Modified residue689UniProtPhosphothreonine
Modified residue (large scale data)689PRIDEPhosphothreonine
Modified residue (large scale data)703PRIDEPhosphoserine
Modified residue708UniProtPhosphoserine
Modified residue (large scale data)708PRIDEPhosphoserine
Modified residue (large scale data)741PRIDEPhosphoserine
Modified residue (large scale data)749PRIDEPhosphothreonine
Modified residue (large scale data)761PRIDEPhosphoserine
Modified residue764UniProtPhosphoserine
Modified residue (large scale data)764PRIDEPhosphoserine
Modified residue (large scale data)824PRIDEPhosphothreonine
Modified residue826UniProtPhosphothreonine
Modified residue (large scale data)826PRIDEPhosphothreonine
Modified residue (large scale data)834PRIDEPhosphotyrosine
Modified residue835UniProtPhosphoserine
Modified residue (large scale data)835PRIDEPhosphoserine
Modified residue853UniProtPhosphoserine
Modified residue (large scale data)853PRIDEPhosphoserine
Modified residue875UniProtPhosphoserine
Modified residue (large scale data)875PRIDEPhosphoserine
Modified residue (large scale data)883PRIDEPhosphothreonine
Modified residue939UniProtPhosphoserine
Modified residue (large scale data)939PRIDEPhosphoserine
Modified residue (large scale data)941PRIDEPhosphothreonine
Modified residue1140UniProtPhosphoserine
Modified residue (large scale data)1140PRIDEPhosphoserine
Modified residue1220UniProtPhosphoserine
Modified residue (large scale data)1220PRIDEPhosphoserine
Modified residue1223UniProtPhosphoserine
Modified residue (large scale data)1223PRIDEPhosphoserine
Modified residue (large scale data)1225PRIDEPhosphoserine
Modified residue1226UniProtPhosphoserine
Modified residue (large scale data)1226PRIDEPhosphoserine
Modified residue1232UniProtPhosphoserine
Modified residue (large scale data)1232PRIDEPhosphoserine
Modified residue1276UniProtPhosphoserine
Modified residue (large scale data)1276PRIDEPhosphoserine
Modified residue1279UniProtPhosphoserine
Modified residue (large scale data)1279PRIDEPhosphoserine
Modified residue (large scale data)1285PRIDEPhosphoserine
Modified residue1295UniProtPhosphoserine
Modified residue (large scale data)1295PRIDEPhosphoserine
Modified residue1298UniProtPhosphoserine
Modified residue (large scale data)1298PRIDEPhosphoserine
Modified residue (large scale data)1300PRIDEPhosphoserine
Modified residue1306UniProtPhosphoserine
Modified residue (large scale data)1306PRIDEPhosphoserine
Modified residue1309UniProtPhosphoserine
Modified residue (large scale data)1309PRIDEPhosphoserine
Modified residue1342UniProtPhosphothreonine
Modified residue (large scale data)1342PRIDEPhosphothreonine
Modified residue1348UniProtPhosphoserine
Modified residue (large scale data)1348PRIDEPhosphoserine
Modified residue (large scale data)1353PRIDEPhosphoserine
Modified residue (large scale data)1360PRIDEPhosphotyrosine
Modified residue1378UniProtPhosphoserine
Modified residue (large scale data)1378PRIDEPhosphoserine
Modified residue1437UniProtPhosphoserine
Modified residue (large scale data)1437PRIDEPhosphoserine
Modified residue (large scale data)1439PRIDEPhosphoserine
Modified residue1445UniProtPhosphoserine
Modified residue (large scale data)1445PRIDEPhosphoserine
Modified residue1448UniProtPhosphoserine
Modified residue (large scale data)1448PRIDEPhosphoserine
Modified residue1475UniProtPhosphoserine
Modified residue (large scale data)1475PRIDEPhosphoserine
Modified residue1486UniProtPhosphoserine
Modified residue (large scale data)1486PRIDEPhosphoserine
Modified residue1508UniProtPhosphoserine
Modified residue (large scale data)1508PRIDEPhosphoserine
Modified residue (large scale data)1523PRIDEPhosphoserine
Modified residue1541UniProtPhosphoserine
Modified residue (large scale data)1541PRIDEPhosphoserine
Modified residue1545UniProtPhosphothreonine
Modified residue (large scale data)1545PRIDEPhosphothreonine
Modified residue1547UniProtPhosphoserine
Modified residue (large scale data)1547PRIDEPhosphoserine
Modified residue (large scale data)1549PRIDEPhosphothreonine
Modified residue (large scale data)1558PRIDEPhosphothreonine
Modified residue (large scale data)1559PRIDEPhosphoserine
Modified residue (large scale data)1560PRIDEPhosphothreonine
Modified residue1561UniProtPhosphoserine
Modified residue (large scale data)1561PRIDEPhosphoserine
Modified residue (large scale data)1566PRIDEPhosphoserine
Modified residue (large scale data)1575PRIDEPhosphoserine
Modified residue (large scale data)1579PRIDEPhosphoserine
Modified residue (large scale data)1581PRIDEPhosphoserine
Modified residue1591UniProtPhosphoserine
Modified residue (large scale data)1600PRIDEPhosphoserine
Modified residue (large scale data)1613PRIDEPhosphoserine

Post-translational modification

Ubiquitinated; targeted for UBE3A-dependent multiubiquitination in the presence of high-risk HPV E6 proteins and degraded.
Palmitoylated (PubMed:27380321).
Could be depalmitoylated by LYPLA1 and/or LYPLA2 (PubMed:27380321).
Palmitoylation of SCRIB by ZDHHC7 is required for its localization to cell-cell junctions, function in the establishement of epithelial cell polarity and the regulation of downstream signaling pathways important for epithelial cell differentiation (PubMed:27380321).

Keywords

Proteomic databases

PTM databases

Expression

Tissue specificity

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

Gene expression databases

Organism-specific databases

Interaction

Subunit

Interacts with UBE3A (PubMed:11027293).
Interacts with PAK1 and PAK2 (PubMed:18716323).
Interacts (via PDZ domains) with VANGL2 (By similarity).
Interacts (via PDZ domains) with LPP and TRIP6; the interaction is direct (PubMed:15649318, PubMed:16137684).
Interacts (via PDZ domains) with TJP2 (PubMed:15975580).
Interacts (via PDZ domains) with APC; may mediate APC targeting to adherens junctions of epithelial cells (PubMed:16611247).
Interacts (via PDZ domains) with TSHR; regulates TSHR trafficking and function (PubMed:15775968).
Interacts with ARHGEF7 and GIT1; interacts directly with ARHGEF7 (PubMed:15182672).
Interacts with CTNNB1 (By similarity).
Interacts with MAPK12 (By similarity).
Interacts (via PDZ domains 1 and 3) with MCC (PubMed:19555689, PubMed:22480440).
Interacts with DLG5 (PubMed:28169360).
Interacts with STK4/MST1 and LATS1 in the presence of DLG5 (PubMed:28169360).
Interacts (via PDZ domain 3) with CRTAM (via PDZ-binding motif); the interaction promotes CRTAM and SCRIB polarization in a subset of CD4+ T-cells (By similarity).
Interacts with YES1, when YES1 is in a closed conformation; the interaction facilitates YES1 autophosphorylation (PubMed:33730553).
Interacts (via PDZ domains) with VIM; the interaction protects SCRIB from proteasomal degradation and facilitates SCRIB localization to intermediate filaments, the interaction is reduced by cell contact inhibition (PubMed:19386766).
(Microbial infection) Interacts (via fourth PDZ domain) with tick-borne encephalitis virus RNA-directed RNA polymerase NS5; this interaction targets viral NS5 to the cell membrane periphery and nucleus and prevents STAT1 phosphorylation, and thus, the activation of the JAK-STAT signaling pathway (PubMed:18042258).
Interacts with HPV E6 (PubMed:11027293).
Interacts with influenza A virus protein NS1; the interaction results in the translocation of SCRIB from the cell membrane to perinuclear puncta (PubMed:21849460).

Binary interactions

TypeEntry 1Entry 2Number of experimentsIntact
BINARY Q14160ADAM22 Q9P0K13EBI-357345, EBI-1567236
BINARY Q14160ADRA1D P2510019EBI-357345, EBI-489993
BINARY Q14160APC P250545EBI-357345, EBI-727707
BINARY Q14160ARHGEF16 Q5VV412EBI-357345, EBI-1057448
BINARY Q14160ARHGEF7 Q1415515EBI-357345, EBI-717515
BINARY Q14160ATP2B1 P200202EBI-357345, EBI-5279998
BINARY Q14160ATP2B2 Q018142EBI-357345, EBI-1174243
BINARY Q14160 B7Z2Y13EBI-357345, EBI-11791049
BINARY Q14160CRHR1 P349983EBI-357345, EBI-3870393
BINARY Q14160CTNND2 Q9UQB32EBI-357345, EBI-7266482
BINARY Q14160CYSLTR2 Q9NS753EBI-357345, EBI-3843579
BINARY Q14160DNAAF11 Q86X452EBI-357345, EBI-9379658
BINARY Q14160DNM1L O004292EBI-357345, EBI-724571
XENO Q14160E6 P031268EBI-357345, EBI-1177242
XENO Q14160E6 P064273EBI-357345, EBI-11737184
XENO Q14160E6 P064634EBI-357345, EBI-1186926
XENO Q14160E6 P248352EBI-357345, EBI-11793707
BINARY Q14160FAM163B P0C2L33EBI-357345, EBI-11793223
BINARY Q14160FASTKD5 Q7L8L62EBI-357345, EBI-747570
XENO Q14160Fat1 Q9QXA35EBI-357345, EBI-6980218
BINARY Q14160FRMPD4 Q14CM02EBI-357345, EBI-311279
BINARY Q14160GUCY1A2 P334026EBI-357345, EBI-6911715
BINARY Q14160KCNA5 P224602EBI-357345, EBI-6426121
BINARY Q14160KCNJ12 Q145002EBI-357345, EBI-11794596
BINARY Q14160KCNJ2 P632522EBI-357345, EBI-703457
BINARY Q14160KCNJ4 P480502EBI-357345, EBI-706117
BINARY Q14160MAPK12 P537786EBI-357345, EBI-602406
BINARY Q14160MAPK3 P273612EBI-357345, EBI-73995
BINARY Q14160MCC P2350815EBI-357345, EBI-307531
BINARY Q14160NET1 Q7Z6282EBI-357345, EBI-2511306
BINARY Q14160NXPE2 Q96DL12EBI-357345, EBI-11791121
BINARY Q14160PHLPP1 O603464EBI-357345, EBI-2511516
BINARY Q14160PKP4 Q995694EBI-357345, EBI-726447
BINARY Q14160RALBP1 Q153112EBI-357345, EBI-749285
BINARY Q14160RPS6KA1 Q154183EBI-357345, EBI-963034
BINARY Q14160RPS6KA2 Q153499EBI-357345, EBI-1384149
BINARY Q14160SLC15A5 A6NIM62EBI-357345, EBI-11792220
BINARY Q14160SLC6A12 P480652EBI-357345, EBI-3843589
BINARY Q14160TANC1 Q9C0D54EBI-357345, EBI-11023211
XENO Q14160tax P0C2132EBI-357345, EBI-11793850
XENO Q14160tax P0C2222EBI-357345, EBI-11794384
BINARY Q14160TSHR P164733EBI-357345, EBI-13939599
BINARY Q14160VEPH1 Q14D042EBI-357345, EBI-1043669
BINARY Q14160WTIP A6NIX22EBI-357345, EBI-20730502
BINARY Q14160WWTR1 Q9GZV53EBI-357345, EBI-747743
BINARY Q14160YAP1 P469372EBI-357345, EBI-1044059
View interactors in UniProtKB
View CPX-6168 in Complex Portal

Protein-protein interaction databases

Miscellaneous

Family & Domains

Features

Showing features for region, repeat, compositional bias, coiled coil, domain.

TypeIDPosition(s)Description
Region1-818Sufficient for targeting to adherens junction and to inhibit cell proliferation
Repeat37-58LRR 1
Repeat60-81LRR 2
Repeat83-104LRR 3
Repeat106-127LRR 4
Repeat129-150LRR 5
Repeat152-174LRR 6
Repeat175-197LRR 7
Repeat198-219LRR 8
Repeat221-243LRR 9
Repeat244-265LRR 10
Repeat267-288LRR 11
Repeat290-312LRR 12
Repeat313-334LRR 13
Repeat336-357LRR 14
Repeat359-381LRR 15
Repeat382-402LRR 16
Region417-440Disordered
Compositional bias423-440Polar residues
Coiled coil458-474
Region459-606Disordered
Compositional bias460-492Basic and acidic residues
Compositional bias520-534Polar residues
Compositional bias565-588Basic and acidic residues
Region628-702Disordered
Coiled coil656-701
Compositional bias664-692Acidic residues
Region717-1229Interaction with ARHGEF7
Domain728-815PDZ 1
Region728-1194Required for interaction with VIM
Region827-853Disordered
Domain862-950PDZ 2
Domain1004-1093PDZ 3
Domain1100-1194PDZ 4
Region1105-1117Interaction with tick-borne encephalitis virus RNA-directed RNA polymerase NS5
Region1227-1246Disordered
Region1277-1489Disordered
Compositional bias1333-1347Pro residues
Coiled coil1379-1419
Compositional bias1380-1402Basic and acidic residues
Compositional bias1439-1453Pro residues
Region1520-1630Disordered

Sequence similarities

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

Keywords

Phylogenomic databases

Family and domain databases

Sequence & Isoforms

Align isoforms (3)
  • Sequence status
    Complete

This entry describes 3 isoforms produced by Alternative splicing.

Q14160-3

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.

  • Length
    1,655
  • Mass (Da)
    177,724
  • Last updated
    2024-10-02 v6
  • Checksum
    578827D6C352A4FC
MLKCIPLWRCNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELGGLVLLTDLLLSQNLLRRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLMALPRSLGKLTKLTNLNVDRNHLEALPPEIGGCVALSVLSLRDNRLAVLPPELAHTTELHVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDARTGEKVLTCYLLPQQPPPSLEDAGQQGSLSETWSDAPPSRVSVIQFLEAPIGDEDAEEAAAEKRGLQRRATPHPSELKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPSAEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKEEEEEEEGSPQEEEEEEEEENRAEEEEASTEEEDKEGAVVSAPSVKGVSFDQANNLLIEPARIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERRGGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVGGSDHSSHPFGVQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDVRDATHQEAVSALLRPCLELSLLVRRDPAPPGLRELCIQKAPGERLGISIRGGARGHAGNPRDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFEASTDAALEVSPGVIANPFAAGIGHRNSLESISSIDRELSPEGPGKEKELPGQTLHWGPEATEAAGRGLQPLKLDYRALAAVPSAGSVQRVPSGAAGGKMAESPCSPSGQQPPSPPSPDELPANVKQAYRAFAAVPTSHPPEDAPAQPPTPGPAASPEQLSFRERQKYFELEVRVPQAEGPPKRVSLVGADDLRKMQEEEARKLQQKRAQMLREAAEAGAEARLALDGETLGEEEQEDEQPPWASPSPTSRQSPASPPPLGGGAPVRTAKAERRHQERLRVQSPEPPAPERALSPAELRALEAEKRALWRAARMKSLEQDALRAQMVLSRSQEGRGTRGPLERLAEAPSPAPTPSPTPVEDLGPQTSTSPGRLPLSGKKFDYRAFAALPSSRPVYDIQSPDFAEELRSLEPSPSPGPQEEDGEVALVLLGRPSPGAVGPEDVALCSSRRPVRPGRRGLGPVPS

Q14160-1

Q14160-2

  • Name
    2
  • Synonyms
    Variant N1
  • See also
    sequence in UniParc or sequence clusters in UniRef
  • Differences from canonical

Computationally mapped potential isoform sequences

There are 8 potential isoforms mapped to this entry

View all
EntryEntry nameGene nameLength
C0HLS1OSCRI_HUMANSCRIB120
H0YDF9H0YDF9_HUMANSCRIB140
H0YCG0H0YCG0_HUMANSCRIB650
A0A0G2JNZ2A0A0G2JNZ2_HUMANSCRIB1630
A0A0G2JPP5A0A0G2JPP5_HUMANSCRIB1655
A0A0G2JMS7A0A0G2JMS7_HUMANSCRIB1549
A0A669KB89A0A669KB89_HUMANSCRIB1658
A0A669KAX5A0A669KAX5_HUMANSCRIB214

Features

Showing features for alternative sequence, compositional bias, sequence conflict.

TypeIDPosition(s)Description
Alternative sequenceVSP_0623961-81in isoform 2
Compositional bias423-440Polar residues
Compositional bias460-492Basic and acidic residues
Compositional bias520-534Polar residues
Compositional bias565-588Basic and acidic residues
Compositional bias664-692Acidic residues
Compositional bias1333-1347Pro residues
Compositional bias1380-1402Basic and acidic residues
Compositional bias1439-1453Pro residues
Sequence conflict1489in Ref. 2; AAL38976
Alternative sequenceVSP_0623971566-1590in isoform 2 and isoform 1

Keywords

Sequence databases

Nucleotide SequenceProtein SequenceMolecule TypeStatus
AF240677
EMBL· GenBank· DDBJ
AAP88017.1
EMBL· GenBank· DDBJ
mRNA
AY062238
EMBL· GenBank· DDBJ
AAL38976.1
EMBL· GenBank· DDBJ
mRNA
AF271734
EMBL· GenBank· DDBJ
AAP88018.2
EMBL· GenBank· DDBJ
mRNA
D63481
EMBL· GenBank· DDBJ
BAA09768.3
EMBL· GenBank· DDBJ
mRNA
AC105219
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
KF458881
EMBL· GenBank· DDBJ
-Genomic DNA No translation available.
BC009490
EMBL· GenBank· DDBJ
AAH09490.2
EMBL· GenBank· DDBJ
mRNA
BC014632
EMBL· GenBank· DDBJ
AAH14632.2
EMBL· GenBank· DDBJ
mRNA

Genome annotation databases

Similar Proteins

Disclaimer

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