Q14160 · SCRIB_HUMAN
- ProteinProtein scribble homolog
- GeneSCRIB
- StatusUniProtKB reviewed (Swiss-Prot)
- Organism
- Amino acids1655 (go to sequence)
- Protein existenceEvidence at protein level
- Annotation score5/5
Function
function
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 annotations | all molecular function | virus receptor activity | dna binding | rna binding | cytoskeletal motor activity | catalytic activity | gtpase activity | structural molecule activity | transporter activity | cytoskeletal protein binding | lipid binding | cyclase activity | antioxidant activity | oxidoreductase activity | transferase activity | hydrolase activity | lyase activity | isomerase activity | ligase activity | protein tag activity | cargo receptor activity | histone binding | protein folding chaperone | translation regulator activity | nutrient reservoir activity | receptor ligand activity | molecular transducer activity | molecular adaptor activity | toxin activity | cell adhesion mediator activity | molecular function regulator activity | virus coreceptor activity | catalytic activity, acting on a protein | catalytic activity, acting on dna | catalytic activity, acting on rna | molecular carrier activity | transcription regulator activity | general transcription initiation factor activity | molecular sensor activity | molecular sequestering activity | atp-dependent activity | other molecular function | all biological process | mitotic cell cycle | cytokinesis | cytoplasmic translation | immune system process | muscle system process | circulatory system process | renal system process | respiratory system process | carbohydrate metabolic process | generation of precursor metabolites and energy | dna replication | dna repair | dna recombination | chromatin organization | dna-templated transcription | regulation of dna-templated transcription | trna metabolic process | protein folding | protein glycosylation | amino acid metabolic process | modified amino acid metabolic process | lipid metabolic process | vitamin metabolic process | sulfur compound metabolic process | intracellular protein transport | nucleocytoplasmic transport | autophagy | inflammatory response | mitochondrion organization | cytoskeleton organization | microtubule-based movement | peroxisome organization | lysosome organization | chromosome segregation | cell adhesion | establishment or maintenance of cell polarity | programmed cell death | photosynthesis | mrna metabolic process | snrna metabolic process | vesicle-mediated transport | reproductive process | digestive system process | signaling | cell differentiation | protein catabolic process | extracellular matrix organization | regulatory ncrna-mediated gene silencing | telomere organization | cell junction organization | wound healing | ribosome biogenesis | cilium organization | anatomical structure development | cell motility | nervous system process | endocrine process | protein maturation | transmembrane transport | nucleobase-containing small molecule metabolic process | hepaticobiliary system process | membrane organization | protein-containing complex assembly | cell wall organization or biogenesis | nitrogen cycle metabolic process | protein localization to plasma membrane | defense response to other organism | detoxification | meiotic nuclear division | mitotic nuclear division | mitochondrial gene expression | carbohydrate derivative metabolic process | other biological process | all cellular component | nuclear chromosome | extracellular region | extracellular space | cell wall | nucleus | nuclear envelope | nucleoplasm | chromosome | nucleolus | mitochondrion | lysosome | endosome | vacuole | peroxisome | endoplasmic reticulum | golgi apparatus | lipid droplet | microtubule organizing center | cytosol | ribosome | cytoskeleton | plasma membrane | cilium | plastid | thylakoid | external encapsulating structure | extracellular matrix | cytoplasmic vesicle | organelle | other cellular component | |||
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Keywords
- Molecular function
- Biological process
Enzyme and pathway databases
Protein family/group databases
Names & Taxonomy
Protein names
- Recommended nameProtein scribble homolog
- Short namesScribble; hScrib
- Alternative names
Gene names
Organism names
- Organism
- Taxonomic lineageEukaryota > Metazoa > Chordata > Craniata > Vertebrata > Euteleostomi > Mammalia > Eutheria > Euarchontoglires > Primates > Haplorrhini > Catarrhini > Hominidae > Homo
Accessions
- Primary accessionQ14160
- Secondary accessions
Proteomes
Organism-specific databases
Subcellular Location
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
- Cellular component
Disease & Variants
Involvement in disease
Neural tube defects (NTD)
- Note
- DescriptionCongenital 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 alsoMIM:182940
Natural variants in NTD
Variant ID | Position(s) | Change | Description | |
---|---|---|---|---|
VAR_067219 | 454 | P>S | in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane; dbSNP:rs1302482009 | |
VAR_067220 | 1535 | R>Q | in 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.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Mutagenesis | 4 | Loss 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. | ||||
Sequence: C → S | ||||||
Mutagenesis | 10 | Loss 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. | ||||
Sequence: C → S | ||||||
Mutagenesis | 22 | No effect on palmitoylation. | ||||
Sequence: C → S | ||||||
Mutagenesis | 305 | Decreased 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. | ||||
Sequence: P → L | ||||||
Natural variant | VAR_019429 | 422 | in dbSNP:rs6558394 | |||
Sequence: P → L | ||||||
Natural variant | VAR_067219 | 454 | in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane; dbSNP:rs1302482009 | |||
Sequence: P → S | ||||||
Mutagenesis | 738 | Loss of anti-proliferative activity. | ||||
Sequence: L → R | ||||||
Mutagenesis | 738-739 | Alters interaction with LPP. | ||||
Sequence: LG → AE | ||||||
Mutagenesis | 872-873 | Alters interaction with LPP. | ||||
Sequence: LG → AE | ||||||
Mutagenesis | 1014-1015 | Loss of interaction with LPP and TRIP6. | ||||
Sequence: LG → AE | ||||||
Mutagenesis | 1111-1112 | Alters interaction with LPP. | ||||
Sequence: LG → AE | ||||||
Natural variant | VAR_067220 | 1535 | in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane; dbSNP:rs782428100 | |||
Sequence: R → Q |
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.
Keywords
- Disease
Organism-specific databases
Miscellaneous
Genetic variation databases
PTM/Processing
Features
Showing features for chain, modified residue (large scale data), modified residue.
Type | ID | Position(s) | Source | Description | |||
---|---|---|---|---|---|---|---|
Chain | PRO_0000188303 | 1-1655 | UniProt | Protein scribble homolog | |||
Sequence: MLKCIPLWRCNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELGGLVLLTDLLLSQNLLRRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLMALPRSLGKLTKLTNLNVDRNHLEALPPEIGGCVALSVLSLRDNRLAVLPPELAHTTELHVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDARTGEKVLTCYLLPQQPPPSLEDAGQQGSLSETWSDAPPSRVSVIQFLEAPIGDEDAEEAAAEKRGLQRRATPHPSELKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPSAEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKEEEEEEEGSPQEEEEEEEEENRAEEEEASTEEEDKEGAVVSAPSVKGVSFDQANNLLIEPARIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERRGGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVGGSDHSSHPFGVQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDVRDATHQEAVSALLRPCLELSLLVRRDPAPPGLRELCIQKAPGERLGISIRGGARGHAGNPRDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFEASTDAALEVSPGVIANPFAAGIGHRNSLESISSIDRELSPEGPGKEKELPGQTLHWGPEATEAAGRGLQPLKLDYRALAAVPSAGSVQRVPSGAAGGKMAESPCSPSGQQPPSPPSPDELPANVKQAYRAFAAVPTSHPPEDAPAQPPTPGPAASPEQLSFRERQKYFELEVRVPQAEGPPKRVSLVGADDLRKMQEEEARKLQQKRAQMLREAAEAGAEARLALDGETLGEEEQEDEQPPWASPSPTSRQSPASPPPLGGGAPVRTAKAERRHQERLRVQSPEPPAPERALSPAELRALEAEKRALWRAARMKSLEQDALRAQMVLSRSQEGRGTRGPLERLAEAPSPAPTPSPTPVEDLGPQTSTSPGRLPLSGKKFDYRAFAALPSSRPVYDIQSPDFAEELRSLEPSPSPGPQEEDGEVALVLLGRPSPGAVGPEDVALCSSRRPVRPGRRGLGPVPS | |||||||
Modified residue (large scale data) | 23 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 35 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 37 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 37 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 378 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 432 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 446 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 475 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 475 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 502 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 504 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 504 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 515 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 668 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 688 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 688 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 689 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 689 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 703 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 708 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 708 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 741 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 749 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 761 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 764 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 764 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 824 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 826 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 826 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 834 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 835 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 835 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 853 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 853 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 875 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 875 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 883 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 939 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 939 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 941 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1140 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1140 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1220 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1220 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1223 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1223 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1225 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1226 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1226 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1232 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1232 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1276 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1276 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1279 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1279 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1285 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1295 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1295 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1298 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1298 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1300 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1306 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1306 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1309 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1309 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1342 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1342 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1348 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1348 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1353 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1360 | PRIDE | Phosphotyrosine | ||||
Sequence: Y | |||||||
Modified residue | 1378 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1378 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1437 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1437 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1439 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1445 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1445 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1448 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1448 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1475 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1475 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1486 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1486 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1508 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1508 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1523 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1541 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1541 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue | 1545 | UniProt | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1545 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1547 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1547 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1549 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1558 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue (large scale data) | 1559 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1560 | PRIDE | Phosphothreonine | ||||
Sequence: T | |||||||
Modified residue | 1561 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1561 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1566 | PRIDE | Phosphoserine | ||||
Sequence: P | |||||||
Modified residue (large scale data) | 1575 | PRIDE | Phosphoserine | ||||
Sequence: R | |||||||
Modified residue (large scale data) | 1579 | PRIDE | Phosphoserine | ||||
Sequence: A | |||||||
Modified residue (large scale data) | 1581 | PRIDE | Phosphoserine | ||||
Sequence: P | |||||||
Modified residue | 1591 | UniProt | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1600 | PRIDE | Phosphoserine | ||||
Sequence: S | |||||||
Modified residue (large scale data) | 1613 | PRIDE | Phosphoserine | ||||
Sequence: D |
Post-translational modification
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
- PTM
Proteomic databases
PTM databases
Expression
Tissue specificity
Gene expression databases
Organism-specific databases
Interaction
Subunit
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).
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
Protein-protein interaction databases
Miscellaneous
Structure
Family & Domains
Features
Showing features for region, repeat, compositional bias, coiled coil, domain.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Region | 1-818 | Sufficient for targeting to adherens junction and to inhibit cell proliferation | ||||
Sequence: MLKCIPLWRCNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELGGLVLLTDLLLSQNLLRRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLMALPRSLGKLTKLTNLNVDRNHLEALPPEIGGCVALSVLSLRDNRLAVLPPELAHTTELHVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDARTGEKVLTCYLLPQQPPPSLEDAGQQGSLSETWSDAPPSRVSVIQFLEAPIGDEDAEEAAAEKRGLQRRATPHPSELKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPSAEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKEEEEEEEGSPQEEEEEEEEENRAEEEEASTEEEDKEGAVVSAPSVKGVSFDQANNLLIEPARIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVE | ||||||
Repeat | 37-58 | LRR 1 | ||||
Sequence: SLEELLLDANQLRELPKPFFRL | ||||||
Repeat | 60-81 | LRR 2 | ||||
Sequence: NLRKLGLSDNEIQRLPPEVANF | ||||||
Repeat | 83-104 | LRR 3 | ||||
Sequence: QLVELDVSRNDIPEIPESIKFC | ||||||
Repeat | 106-127 | LRR 4 | ||||
Sequence: ALEIADFSGNPLSRLPDGFTQL | ||||||
Repeat | 129-150 | LRR 5 | ||||
Sequence: SLAHLALNDVSLQALPGDVGNL | ||||||
Repeat | 152-174 | LRR 6 | ||||
Sequence: NLVTLELRENLLKSLPASLSFLV | ||||||
Repeat | 175-197 | LRR 7 | ||||
Sequence: KLEQLDLGGNDLEVLPDTLGALP | ||||||
Repeat | 198-219 | LRR 8 | ||||
Sequence: NLRELWLDRNQLSALPPELGNL | ||||||
Repeat | 221-243 | LRR 9 | ||||
Sequence: RLVCLDVSENRLEELPAELGGLV | ||||||
Repeat | 244-265 | LRR 10 | ||||
Sequence: LLTDLLLSQNLLRRLPDGIGQL | ||||||
Repeat | 267-288 | LRR 11 | ||||
Sequence: QLSILKVDQNRLCEVTEAIGDC | ||||||
Repeat | 290-312 | LRR 12 | ||||
Sequence: NLSELILTENLLMALPRSLGKLT | ||||||
Repeat | 313-334 | LRR 13 | ||||
Sequence: KLTNLNVDRNHLEALPPEIGGC | ||||||
Repeat | 336-357 | LRR 14 | ||||
Sequence: ALSVLSLRDNRLAVLPPELAHT | ||||||
Repeat | 359-381 | LRR 15 | ||||
Sequence: ELHVLDVAGNRLQSLPFALTHLN | ||||||
Repeat | 382-402 | LRR 16 | ||||
Sequence: LKALWLAENQAQPMLRFQTED | ||||||
Region | 417-440 | Disordered | ||||
Sequence: PQQPPPSLEDAGQQGSLSETWSDA | ||||||
Compositional bias | 423-440 | Polar residues | ||||
Sequence: SLEDAGQQGSLSETWSDA | ||||||
Coiled coil | 458-474 | |||||
Sequence: EDAEEAAAEKRGLQRRA | ||||||
Region | 459-606 | Disordered | ||||
Sequence: DAEEAAAEKRGLQRRATPHPSELKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPSAEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQRLIRKD | ||||||
Compositional bias | 460-492 | Basic and acidic residues | ||||
Sequence: AEEAAAEKRGLQRRATPHPSELKVMKRSIEGRR | ||||||
Compositional bias | 520-534 | Polar residues | ||||
Sequence: LSEDSRPSASTVSEA | ||||||
Compositional bias | 565-588 | Basic and acidic residues | ||||
Sequence: QEPTVHFAEDALLPGDDREIEEGQ | ||||||
Region | 628-702 | Disordered | ||||
Sequence: LLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKEEEEEEEGSPQEEEEEEEEENRAEEEEASTEEEDKEGAVVSAP | ||||||
Coiled coil | 656-701 | |||||
Sequence: RAQKEEEEEEEGSPQEEEEEEEEENRAEEEEASTEEEDKEGAVVSA | ||||||
Compositional bias | 664-692 | Acidic residues | ||||
Sequence: EEEGSPQEEEEEEEEENRAEEEEASTEEE | ||||||
Region | 717-1229 | Interaction with ARHGEF7 | ||||
Sequence: IEPARIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERRGGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVGGSDHSSHPFGVQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDVRDATHQEAVSALLRPCLELSLLVRRDPAPPGLRELCIQKAPGERLGISIRGGARGHAGNPRDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFEASTDAALEVSPGVIANPFAAGIGHRNSLESISSIDR | ||||||
Domain | 728-815 | PDZ 1 | ||||
Sequence: TLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRER | ||||||
Region | 728-1194 | Required for interaction with VIM | ||||
Sequence: TLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERRGGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVGGSDHSSHPFGVQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDVRDATHQEAVSALLRPCLELSLLVRRDPAPPGLRELCIQKAPGERLGISIRGGARGHAGNPRDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFEA | ||||||
Region | 827-853 | Disordered | ||||
Sequence: PLRPEDDYSPRERRGGGLRLPLLPPES | ||||||
Domain | 862-950 | PDZ 2 | ||||
Sequence: VACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREA | ||||||
Domain | 1004-1093 | PDZ 3 | ||||
Sequence: EIRLPRAGGPLGLSIVGGSDHSSHPFGVQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDVRDATHQEAVSALLRPCLELSLLVRRDP | ||||||
Domain | 1100-1194 | PDZ 4 | ||||
Sequence: ELCIQKAPGERLGISIRGGARGHAGNPRDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFEA | ||||||
Region | 1105-1117 | Interaction with tick-borne encephalitis virus RNA-directed RNA polymerase NS5 | ||||
Sequence: KAPGERLGISIRG | ||||||
Region | 1227-1246 | Disordered | ||||
Sequence: IDRELSPEGPGKEKELPGQT | ||||||
Region | 1277-1489 | Disordered | ||||
Sequence: AGSVQRVPSGAAGGKMAESPCSPSGQQPPSPPSPDELPANVKQAYRAFAAVPTSHPPEDAPAQPPTPGPAASPEQLSFRERQKYFELEVRVPQAEGPPKRVSLVGADDLRKMQEEEARKLQQKRAQMLREAAEAGAEARLALDGETLGEEEQEDEQPPWASPSPTSRQSPASPPPLGGGAPVRTAKAERRHQERLRVQSPEPPAPERALSPAE | ||||||
Compositional bias | 1333-1347 | Pro residues | ||||
Sequence: PEDAPAQPPTPGPAA | ||||||
Coiled coil | 1379-1419 | |||||
Sequence: LVGADDLRKMQEEEARKLQQKRAQMLREAAEAGAEARLALD | ||||||
Compositional bias | 1380-1402 | Basic and acidic residues | ||||
Sequence: VGADDLRKMQEEEARKLQQKRAQ | ||||||
Compositional bias | 1439-1453 | Pro residues | ||||
Sequence: SPTSRQSPASPPPLG | ||||||
Region | 1520-1630 | Disordered | ||||
Sequence: LSRSQEGRGTRGPLERLAEAPSPAPTPSPTPVEDLGPQTSTSPGRLPLSGKKFDYRAFAALPSSRPVYDIQSPDFAEELRSLEPSPSPGPQEEDGEVALVLLGRPSPGAVG |
Sequence similarities
Keywords
- Domain
Phylogenomic databases
Family and domain databases
Sequence & Isoforms
- Sequence statusComplete
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.
- Name3
- Length1,655
- Mass (Da)177,724
- Last updated2024-10-02 v6
- Checksum578827D6C352A4FC
Q14160-1
- Name1
- Differences from canonical
- 1566-1590: Missing
Q14160-2
- Name2
- SynonymsVariant N1
- Differences from canonical
- 1-81: Missing
- 1566-1590: Missing
Computationally mapped potential isoform sequences
There are 8 potential isoforms mapped to this entry
Entry | Entry name | Gene name | Length | ||
---|---|---|---|---|---|
C0HLS1 | OSCRI_HUMAN | SCRIB | 120 | ||
H0YDF9 | H0YDF9_HUMAN | SCRIB | 140 | ||
H0YCG0 | H0YCG0_HUMAN | SCRIB | 650 | ||
A0A0G2JNZ2 | A0A0G2JNZ2_HUMAN | SCRIB | 1630 | ||
A0A0G2JPP5 | A0A0G2JPP5_HUMAN | SCRIB | 1655 | ||
A0A0G2JMS7 | A0A0G2JMS7_HUMAN | SCRIB | 1549 | ||
A0A669KB89 | A0A669KB89_HUMAN | SCRIB | 1658 | ||
A0A669KAX5 | A0A669KAX5_HUMAN | SCRIB | 214 |
Features
Showing features for alternative sequence, compositional bias, sequence conflict.
Type | ID | Position(s) | Description | |||
---|---|---|---|---|---|---|
Alternative sequence | VSP_062396 | 1-81 | in isoform 2 | |||
Sequence: Missing | ||||||
Compositional bias | 423-440 | Polar residues | ||||
Sequence: SLEDAGQQGSLSETWSDA | ||||||
Compositional bias | 460-492 | Basic and acidic residues | ||||
Sequence: AEEAAAEKRGLQRRATPHPSELKVMKRSIEGRR | ||||||
Compositional bias | 520-534 | Polar residues | ||||
Sequence: LSEDSRPSASTVSEA | ||||||
Compositional bias | 565-588 | Basic and acidic residues | ||||
Sequence: QEPTVHFAEDALLPGDDREIEEGQ | ||||||
Compositional bias | 664-692 | Acidic residues | ||||
Sequence: EEEGSPQEEEEEEEEENRAEEEEASTEEE | ||||||
Compositional bias | 1333-1347 | Pro residues | ||||
Sequence: PEDAPAQPPTPGPAA | ||||||
Compositional bias | 1380-1402 | Basic and acidic residues | ||||
Sequence: VGADDLRKMQEEEARKLQQKRAQ | ||||||
Compositional bias | 1439-1453 | Pro residues | ||||
Sequence: SPTSRQSPASPPPLG | ||||||
Sequence conflict | 1489 | in Ref. 2; AAL38976 | ||||
Sequence: E → K | ||||||
Alternative sequence | VSP_062397 | 1566-1590 | in isoform 2 and isoform 1 | |||
Sequence: Missing |
Keywords
- Coding sequence diversity
- Technical term
Sequence databases
Nucleotide Sequence | Protein Sequence | Molecule Type | Status | |
---|---|---|---|---|
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 |