SCRIB
entrez
23513
canonical
uniprot
Q14160
canonical
ensembl
ENSG00000180900
resolver
ensembl
ENSG00000274287
resolver
ensp
ENSP00000322938
resolver
ensp
ENSP00000349486
resolver
ensp
ENSP00000482406
resolver
ensp
ENSP00000484041
resolver
enst
ENST00000612204
resolver
enst
ENST00000622455
resolver
genesymbol
SCRIB
resolver
genesymbol_syn
CRIB1
resolver
genesymbol_syn
KIAA0147
resolver
genesymbol_syn
LAP4
resolver
genesymbol_syn
SCRB1
resolver
genesymbol_syn
VARTUL
resolver
hgnc
HGNC:30377
resolver
uniprot
A0A0G2JNZ2
resolver
uniprot
A0A0G2JPP5
resolver
uniprot
A0PJK8
resolver
uniprot
Q6P496
resolver
uniprot
Q7Z5D1
resolver
uniprot
Q8WWV8
resolver
uniprot
Q96C69
resolver
uniprot
Q96GG1
resolver
uniprot_entry
A0A0G2JNZ2_HUMAN
resolver
uniprot_entry
A0A0G2JPP5_HUMAN
resolver
uniprot_entry
A0PJK8_HUMAN
resolver
uniprot_entry
SCRIB_HUMAN
resolver
uniprot_sec
Q6P496
resolver
uniprot_sec
Q7Z5D1
resolver
uniprot_sec
Q8WWV8
resolver
uniprot_sec
Q96C69
resolver
uniprot_sec
Q96GG1
resolver
amino_acid_sequence
MLKCIPLWRCNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLNLRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRLPDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLDLGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELGGLVLLTDLLLSQNLLRRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENLLMALPRSLGKLTKLTNLNVDRNHLEALPPEIGGCVALSVLSLRDNRLAVLPPELAHTTELHVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDARTGEKVLTCYLLPQQPPPSLEDAGQQGSLSETWSDAPPSRVSVIQFLEAPIGDEDAEEAAAEKRGLQRRATPHPSELKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPSAEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQRLIRKDTPHYKKHFKISKLPQPEAVVALLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKEEEEEEEGSPQEEEEEEEEENRAEEEEASTEEEDKEGAVVSAPSVKGVSFDQANNLLIEPARIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKLLEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERRGGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEGGAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLPHSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVGGSDHSSHPFGVQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDVRDATHQEAVSALLRPCLELSLLVRRDPAPPGLRELCIQKAPGERLGISIRGGARGHAGNPRDPTDEGIFISKVSPTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFEASTDAALEVSPGVIANPFAAGIGHRNSLESISSIDRELSPEGPGKEKELPGQTLHWGPEATEAAGRGLQPLKLDYRALAAVPSAGSVQRVPSGAAGGKMAESPCSPSGQQPPSPPSPDELPANVKQAYRAFAAVPTSHPPEDAPAQPPTPGPAASPEQLSFRERQKYFELEVRVPQAEGPPKRVSLVGADDLRKMQEEEARKLQQKRAQMLREAAEAGAEARLALDGETLGEEEQEDEQPPWASPSPTSRQSPASPPPLGGGAPVRTAKAERRHQERLRVQSPEPPAPERALSPAELRALEAEKRALWRAARMKSLEQDALRAQMVLSRSQEGRGTRGPLERLAEAPSPAPTPSPTPVEDLGPQTSTSPGRLPLSGKKFDYRAFAALPSSRPVYDIQSPDFAEELRSLEPSPSPGPQEEDGEVALVLLGRPSPGAVGPEDVALCSSRRPVRPGRRGLGPVPS
uniprot
proteins
disease_involvement
DISEASE: Neural tube defects (NTD) [MIM:182940]: Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. {ECO:0000269|PubMed:22095531}. Note=The disease is caused by variants affecting the gene represented in this entry.
uniprot
proteins
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). {ECO:0000250|UniProtKB:A0A8P0N4K0, ECO:0000250|UniProtKB:Q80U72, ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:16344308, ECO:0000269|PubMed:16965391, ECO:0000269|PubMed:18641685, ECO:0000269|PubMed:18716323, ECO:0000269|PubMed:19041750, ECO:0000269|PubMed:27380321}.
uniprot
proteins
mass_dalton
177724
uniprot
proteins
mutagenesis
MUTAGEN 4; /note="C->S: 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."; /evidence="ECO:0000269|PubMed:27380321"; MUTAGEN 10; /note="C->S: 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."; /evidence="ECO:0000269|PubMed:27380321"; MUTAGEN 22; /note="C->S: No effect on palmitoylation."; /evidence="ECO:0000269|PubMed:27380321"; MUTAGEN 305; /note="P->L: 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."; /evidence="ECO:0000269|PubMed:15182672, ECO:0000269|PubMed:15806148, ECO:0000269|PubMed:19041750, ECO:0000269|PubMed:27380321, ECO:0000269|PubMed:33730553"; MUTAGEN 738..739; /note="LG->AE: Alters interaction with LPP."; /evidence="ECO:0000269|PubMed:15649318"; MUTAGEN 738; /note="L->R: Loss of anti-proliferative activity."; MUTAGEN 872..873; /note="LG->AE: Alters interaction with LPP."; /evidence="ECO:0000269|PubMed:15649318"; MUTAGEN 1014..1015; /note="LG->AE: Loss of interaction with LPP and TRIP6."; /evidence="ECO:0000269|PubMed:15649318"; MUTAGEN 1111..1112; /note="LG->AE: Alters interaction with LPP."; /evidence="ECO:0000269|PubMed:15649318
uniprot
proteins
post_translational_modification
PTM: Ubiquitinated; targeted for UBE3A-dependent multiubiquitination in the presence of high-risk HPV E6 proteins and degraded. {ECO:0000269|PubMed:11027293}.; PTM: 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). {ECO:0000269|PubMed:27380321}.
uniprot
proteins
protein_family
LAP (LRR and PDZ) protein family
uniprot
proteins
pubmed
11027293
uniprot
proteins
pubmed
12168954
uniprot
proteins
pubmed
15144186
uniprot
proteins
pubmed
15182672
uniprot
proteins
pubmed
15489334
uniprot
proteins
pubmed
15649318
uniprot
proteins
pubmed
15775968
uniprot
proteins
pubmed
15806148
uniprot
proteins
pubmed
15975580
uniprot
proteins
pubmed
16137684
uniprot
proteins
pubmed
16344308
uniprot
proteins
pubmed
16421571
uniprot
proteins
pubmed
16611247
uniprot
proteins
pubmed
16965391
uniprot
proteins
pubmed
17081983
uniprot
proteins
pubmed
18042258
uniprot
proteins
pubmed
18220336
uniprot
proteins
pubmed
18641685
uniprot
proteins
pubmed
18669648
uniprot
proteins
pubmed
18716323
uniprot
proteins
pubmed
19041750
uniprot
proteins
pubmed
19369195
uniprot
proteins
pubmed
19386766
uniprot
proteins
pubmed
19413330
uniprot
proteins
pubmed
19555689
uniprot
proteins
pubmed
19690332
uniprot
proteins
pubmed
20068231
uniprot
proteins
pubmed
21269460
uniprot
proteins
pubmed
21406692
uniprot
proteins
pubmed
21849460
uniprot
proteins
pubmed
22095531
uniprot
proteins
pubmed
22480440
uniprot
proteins
pubmed
23186163
uniprot
proteins
pubmed
24275569
uniprot
proteins
pubmed
27380321
uniprot
proteins
pubmed
28169360
uniprot
proteins
pubmed
33730553
uniprot
proteins
pubmed
35670457
uniprot
proteins
pubmed
8590280
uniprot
proteins
sequence_length
1655
uniprot
proteins
subcellular_location
SUBCELLULAR LOCATION: Cell membrane {ECO:0000269|PubMed:19386766, ECO:0000269|PubMed:21849460, ECO:0000269|PubMed:28169360}; Peripheral membrane protein. Cell junction {ECO:0000269|PubMed:27380321}. Cell junction, adherens junction. Cell projection, lamellipodium. Cytoplasm {ECO:0000269|PubMed:19386766}. Postsynapse {ECO:0000269|PubMed:15182672}. Presynapse {ECO:0000269|PubMed:15182672}. 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). {ECO:0000250|UniProtKB:A0A8P0N4K0, ECO:0000250|UniProtKB:Q80U72, ECO:0000269|PubMed:19386766}.
uniprot
proteins