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Q14160

- SCRIB_HUMAN

UniProt

Q14160 - SCRIB_HUMAN

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Protein

Protein scribble homolog

Gene

SCRIB

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

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 - 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. auditory receptor cell stereocilium organization Source: Ensembl
  6. cell migration Source: UniProtKB
  7. cell proliferation Source: UniProtKB
  8. cochlear nucleus development Source: Ensembl
  9. establishment of apical/basal cell polarity Source: UniProtKB
  10. mammary gland duct morphogenesis Source: UniProtKB
  11. negative regulation of mitotic cell cycle Source: UniProtKB
  12. neural tube closure Source: UniProtKB
  13. positive chemotaxis Source: UniProtKB
  14. positive regulation of apoptotic process Source: UniProtKB
  15. positive regulation of receptor recycling Source: UniProtKB
  16. protein localization to adherens junction Source: BHF-UCL
  17. single organismal cell-cell adhesion Source: UniProtKB
  18. synaptic vesicle endocytosis Source: Ensembl
  19. synaptic vesicle targeting Source: Ensembl
  20. viral process Source: UniProtKB-KW
  21. wound healing Source: Ensembl
Complete GO annotation...

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. cell projection Source: UniProtKB-KW
  5. extracellular vesicular exosome Source: UniProt
  6. myelin sheath abaxonal region Source: Ensembl
  7. plasma membrane Source: UniProtKB
  8. Scrib-APC-beta-catenin complex Source: BHF-UCL
Complete GO annotation...

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. 2 Publications
Mutagenesisi738 – 7392LG → AE: Alters interaction with LPP. 1 Publication
Mutagenesisi738 – 7381L → R: Loss of anti-proliferative activity.
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

BgeeiQ14160.
CleanExiHS_SCRIB.
ExpressionAtlasiQ14160. baseline and differential.
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. 25 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.
InParanoidiQ14160.
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

        10         20         30         40         50
MLKCIPLWRC NRHVESVDKR HCSLQAVPEE IYRYSRSLEE LLLDANQLRE
60 70 80 90 100
LPKPFFRLLN LRKLGLSDNE IQRLPPEVAN FMQLVELDVS RNDIPEIPES
110 120 130 140 150
IKFCKALEIA DFSGNPLSRL PDGFTQLRSL AHLALNDVSL QALPGDVGNL
160 170 180 190 200
ANLVTLELRE NLLKSLPASL SFLVKLEQLD LGGNDLEVLP DTLGALPNLR
210 220 230 240 250
ELWLDRNQLS ALPPELGNLR RLVCLDVSEN RLEELPAELG GLVLLTDLLL
260 270 280 290 300
SQNLLRRLPD GIGQLKQLSI LKVDQNRLCE VTEAIGDCEN LSELILTENL
310 320 330 340 350
LMALPRSLGK LTKLTNLNVD RNHLEALPPE IGGCVALSVL SLRDNRLAVL
360 370 380 390 400
PPELAHTTEL HVLDVAGNRL QSLPFALTHL NLKALWLAEN QAQPMLRFQT
410 420 430 440 450
EDDARTGEKV LTCYLLPQQP PPSLEDAGQQ GSLSETWSDA PPSRVSVIQF
460 470 480 490 500
LEAPIGDEDA EEAAAEKRGL QRRATPHPSE LKVMKRSIEG RRSEACPCQP
510 520 530 540 550
DSGSPLPAEE EKRLSAESGL SEDSRPSAST VSEAEPEGPS AEAQGGSQQE
560 570 580 590 600
ATTAGGEEDA EEDYQEPTVH FAEDALLPGD DREIEEGQPE APWTLPGGRQ
610 620 630 640 650
RLIRKDTPHY KKHFKISKLP QPEAVVALLQ GMQPDGEGPV APGGWHNGPH
660 670 680 690 700
APWAPRAQKE EEEEEEGSPQ EEEVEEEEEN RAEEEEASTE EEDKEGAVVS
710 720 730 740 750
APSVKGVSFD QANNLLIEPA RIEEEELTLT ILRQTGGLGI SIAGGKGSTP
760 770 780 790 800
YKGDDEGIFI SRVSEEGPAA RAGVRVGDKL LEVNGVALQG AEHHEAVEAL
810 820 830 840 850
RGAGTAVQMR VWRERMVEPE NAVTITPLRP EDDYSPRERR GGGLRLPLLP
860 870 880 890 900
PESPGPLRQR HVACLARSER GLGFSIAGGK GSTPYRAGDA GIFVSRIAEG
910 920 930 940 950
GAAHRAGTLQ VGDRVLSING VDVTEARHDH AVSLLTAASP TIALLLEREA
960 970 980 990 1000
GGPLPPSPLP HSSPPTAAVA TTSITTATPG VPGLPSLAPS LLAAALEGPY
1010 1020 1030 1040 1050
PVEEIRLPRA GGPLGLSIVG GSDHSSHPFG VQEPGVFISK VLPRGLAARS
1060 1070 1080 1090 1100
GLRVGDRILA VNGQDVRDAT HQEAVSALLR PCLELSLLVR RDPAPPGLRE
1110 1120 1130 1140 1150
LCIQKAPGER LGISIRGGAR GHAGNPRDPT DEGIFISKVS PTGAAGRDGR
1160 1170 1180 1190 1200
LRVGLRLLEV NQQSLLGLTH GEAVQLLRSV GDTLTVLVCD GFEASTDAAL
1210 1220 1230 1240 1250
EVSPGVIANP FAAGIGHRNS LESISSIDRE LSPEGPGKEK ELPGQTLHWG
1260 1270 1280 1290 1300
PEATEAAGRG LQPLKLDYRA LAAVPSAGSV QRVPSGAAGG KMAESPCSPS
1310 1320 1330 1340 1350
GQQPPSPPSP DELPANVKQA YRAFAAVPTS HPPEDAPAQP PTPGPAASPE
1360 1370 1380 1390 1400
QLSFRERQKY FELEVRVPQA EGPPKRVSLV GADDLRKMQE EEARKLQQKR
1410 1420 1430 1440 1450
AQMLREAAEA GAEARLALDG ETLGEEEQED EQPPWASPSP TSRQSPASPP
1460 1470 1480 1490 1500
PLGGGAPVRT AKAERRHQER LRVQSPEPPA PERALSPAEL RALEAEKRAL
1510 1520 1530 1540 1550
WRAARMKSLE QDALRAQMVL SRSQEGRGTR GPLERLAEAP SPAPTPSPTP
1560 1570 1580 1590 1600
VEDLGPQTST SPGRLSPDFA EELRSLEPSP SPGPQEEDGE VALVLLGRPS
1610 1620 1630
PGAVGPEDVA LCSSRRPVRP GRRGLGPVPS
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.
ENST00000356994; ENSP00000349486; ENSG00000180900.
ENST00000377533; ENSP00000366756; ENSG00000180900.
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. 25 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 .
ENST00000356994 ; ENSP00000349486 ; ENSG00000180900 .
ENST00000377533 ; ENSP00000366756 ; ENSG00000180900 .
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.
InParanoidi Q14160.
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

Bgeei Q14160.
CleanExi HS_SCRIB.
ExpressionAtlasi Q14160. baseline and differential.
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

« Hide 'large scale' publications
  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 29, 2014
This is version 149 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

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