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Protein

Protein scribble homolog

Gene

SCRIB

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: 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 - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

GO - Biological processi

  • activation of GTPase activity Source: UniProtKB
  • apoptotic process involved in morphogenesis Source: UniProtKB
  • astrocyte cell migration Source: Ensembl
  • asymmetric protein localization Source: Ensembl
  • auditory receptor cell stereocilium organization Source: Ensembl
  • cell migration Source: UniProtKB
  • cell proliferation Source: UniProtKB
  • cochlear nucleus development Source: Ensembl
  • establishment of apical/basal cell polarity Source: UniProtKB
  • mammary gland duct morphogenesis Source: UniProtKB
  • negative regulation of mitotic cell cycle Source: UniProtKB
  • neural tube closure Source: UniProtKB
  • positive chemotaxis Source: UniProtKB
  • positive regulation of apoptotic process Source: UniProtKB
  • positive regulation of receptor recycling Source: UniProtKB
  • protein localization to adherens junction Source: BHF-UCL
  • single organismal cell-cell adhesion Source: UniProtKB
  • synaptic vesicle endocytosis Source: Ensembl
  • synaptic vesicle targeting Source: Ensembl
  • viral process Source: UniProtKB-KW
  • wound healing Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Host-virus interaction

Enzyme and pathway databases

ReactomeiR-HSA-4608870. 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
Proteomesi
  • UP000005640 Componenti: Chromosome 8

Organism-specific databases

HGNCiHGNC:30377. SCRIB.

Subcellular locationi

GO - Cellular componenti

  • basolateral plasma membrane Source: Ensembl
  • cell-cell adherens junction Source: UniProtKB
  • cell-cell contact zone Source: Ensembl
  • cell-cell junction Source: UniProtKB
  • cell junction Source: HPA
  • cytoplasm Source: HPA
  • extracellular exosome Source: UniProtKB
  • lamellipodium Source: UniProtKB-SubCell
  • myelin sheath abaxonal region Source: Ensembl
  • nucleoplasm Source: HPA
  • plasma membrane Source: UniProtKB
  • presynapse Source: GOC
  • 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)1 Publication
The disease is caused by mutations affecting the gene represented in this entry.
Disease 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 also OMIM:182940
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_067219454P → S in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. 1 Publication1
Natural variantiVAR_0672201535R → Q in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. 1 Publication1

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi305P → L: Loss of pro-apoptotic function and of the targeting to cell-cell junctions. Targeted to the cytoplasm. Alters interaction with TJP2. 2 Publications1
Mutagenesisi738 – 739LG → AE: Alters interaction with LPP. 1 Publication2
Mutagenesisi738L → R: Loss of anti-proliferative activity. 1
Mutagenesisi872 – 873LG → AE: Alters interaction with LPP. 1 Publication2
Mutagenesisi1014 – 1015LG → AE: Loss of interaction with LPP and TRIP6. 1 Publication2
Mutagenesisi1111 – 1112LG → AE: Alters interaction with LPP. 1 Publication2

Keywords - Diseasei

Disease mutation

Organism-specific databases

DisGeNETi23513.
MalaCardsiSCRIB.
MIMi182940. phenotype.
PharmGKBiPA134936275.

Polymorphism and mutation databases

BioMutaiSCRIB.
DMDMi261260101.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00001883031 – 1630Protein scribble homologAdd BLAST1630

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei37PhosphoserineCombined sources1
Modified residuei378PhosphothreonineCombined sources1
Modified residuei475PhosphothreonineCombined sources1
Modified residuei504PhosphoserineCombined sources1
Modified residuei688PhosphoserineCombined sources1
Modified residuei689PhosphothreonineCombined sources1
Modified residuei708PhosphoserineCombined sources1
Modified residuei764PhosphoserineCombined sources1
Modified residuei826PhosphothreonineCombined sources1
Modified residuei835PhosphoserineCombined sources1
Modified residuei853PhosphoserineCombined sources1
Modified residuei875PhosphoserineCombined sources1
Modified residuei939PhosphoserineCombined sources1
Modified residuei1140PhosphoserineCombined sources1
Modified residuei1220PhosphoserineCombined sources1
Modified residuei1223PhosphoserineCombined sources1
Modified residuei1226PhosphoserineCombined sources1
Modified residuei1232PhosphoserineCombined sources1
Modified residuei1276PhosphoserineCombined sources1
Modified residuei1279PhosphoserineCombined sources1
Modified residuei1295PhosphoserineCombined sources1
Modified residuei1298PhosphoserineCombined sources1
Modified residuei1306PhosphoserineCombined sources1
Modified residuei1309PhosphoserineCombined sources1
Modified residuei1342PhosphothreonineCombined sources1
Modified residuei1348PhosphoserineCombined sources1
Modified residuei1378PhosphoserineCombined sources1
Modified residuei1437PhosphoserineCombined sources1
Modified residuei1445PhosphoserineCombined sources1
Modified residuei1448PhosphoserineCombined sources1
Modified residuei1475PhosphoserineCombined sources1
Modified residuei1486PhosphoserineCombined sources1
Modified residuei1508PhosphoserineCombined sources1
Modified residuei1541PhosphoserineCombined sources1
Modified residuei1545PhosphothreonineCombined sources1
Modified residuei1547PhosphoserineCombined sources1
Modified residuei1561PhosphoserineCombined sources1
Modified residuei1566PhosphoserineCombined sources1

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

EPDiQ14160.
MaxQBiQ14160.
PaxDbiQ14160.
PeptideAtlasiQ14160.
PRIDEiQ14160.

PTM databases

iPTMnetiQ14160.
PhosphoSitePlusiQ14160.
SwissPalmiQ14160.

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

BgeeiENSG00000180900.
CleanExiHS_SCRIB.
ExpressionAtlasiQ14160. baseline and differential.
GenevisibleiQ14160. HS.

Organism-specific databases

HPAiCAB015463.
CAB022081.
HPA023557.
HPA064312.

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

GO - Molecular functioni

  • cadherin binding involved in cell-cell adhesion Source: BHF-UCL

Protein-protein interaction databases

BioGridi117060. 52 interactors.
DIPiDIP-31259N.
IntActiQ14160. 49 interactors.
MINTiMINT-147371.
STRINGi9606.ENSP00000349486.

Structurei

Secondary structure

11630
Legend: HelixTurnBeta strandPDB Structure known for this area
Show more details
Feature keyPosition(s)DescriptionActionsGraphical viewLength
Beta strandi726 – 732Combined sources7
Beta strandi737 – 744Combined sources8
Beta strandi757 – 763Combined sources7
Helixi768 – 772Combined sources5
Beta strandi779 – 783Combined sources5
Helixi793 – 801Combined sources9
Beta strandi805 – 812Combined sources8
Beta strandi860 – 865Combined sources6
Beta strandi875 – 877Combined sources3
Beta strandi893 – 896Combined sources4
Helixi903 – 906Combined sources4
Beta strandi914 – 920Combined sources7
Helixi928 – 935Combined sources8
Beta strandi942 – 948Combined sources7
Beta strandi997 – 1000Combined sources4
Beta strandi1002 – 1008Combined sources7
Beta strandi1010 – 1012Combined sources3
Beta strandi1016 – 1020Combined sources5
Beta strandi1022 – 1024Combined sources3
Turni1027 – 1030Combined sources4
Beta strandi1031 – 1033Combined sources3
Beta strandi1036 – 1041Combined sources6
Helixi1046 – 1050Combined sources5
Beta strandi1057 – 1061Combined sources5
Helixi1071 – 1079Combined sources9
Beta strandi1083 – 1090Combined sources8
Beta strandi1099 – 1104Combined sources6
Beta strandi1113 – 1117Combined sources5
Beta strandi1119 – 1122Combined sources4
Beta strandi1126 – 1128Combined sources3
Beta strandi1134 – 1139Combined sources6
Beta strandi1141 – 1143Combined sources3
Helixi1144 – 1148Combined sources5
Beta strandi1156 – 1160Combined sources5
Helixi1170 – 1178Combined sources9
Beta strandi1183 – 1189Combined sources7

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UJUNMR-A1096-1193[»]
1WHANMR-A860-951[»]
1X5QNMR-A718-814[»]
2W4FX-ray1.30A725-815[»]
4WYTX-ray2.60A992-1203[»]
4WYUX-ray2.50A/B992-1203[»]
ProteinModelPortaliQ14160.
SMRiQ14160.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ14160.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati37 – 58LRR 1Add BLAST22
Repeati60 – 81LRR 2Add BLAST22
Repeati83 – 104LRR 3Add BLAST22
Repeati106 – 127LRR 4Add BLAST22
Repeati129 – 150LRR 5Add BLAST22
Repeati152 – 174LRR 6Add BLAST23
Repeati175 – 197LRR 7Add BLAST23
Repeati198 – 219LRR 8Add BLAST22
Repeati221 – 243LRR 9Add BLAST23
Repeati244 – 265LRR 10Add BLAST22
Repeati267 – 288LRR 11Add BLAST22
Repeati290 – 312LRR 12Add BLAST23
Repeati313 – 334LRR 13Add BLAST22
Repeati336 – 357LRR 14Add BLAST22
Repeati359 – 381LRR 15Add BLAST23
Repeati382 – 402LRR 16Add BLAST21
Domaini728 – 815PDZ 1PROSITE-ProRule annotationAdd BLAST88
Domaini862 – 950PDZ 2PROSITE-ProRule annotationAdd BLAST89
Domaini1004 – 1093PDZ 3PROSITE-ProRule annotationAdd BLAST90
Domaini1100 – 1194PDZ 4PROSITE-ProRule annotationAdd BLAST95

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni1 – 818Sufficient for targeting to adherens junction and to inhibit cell proliferationAdd BLAST818
Regioni717 – 1229Interaction with ARHGEF71 PublicationAdd BLAST513

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili458 – 474Sequence analysisAdd BLAST17
Coiled coili656 – 701Sequence analysisAdd BLAST46
Coiled coili1379 – 1419Sequence analysisAdd BLAST41

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi660 – 695Glu-richAdd BLAST36
Compositional biasi1296 – 1349Pro-richAdd BLAST54

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

eggNOGiENOG410KCZ0. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000113281.
InParanoidiQ14160.
KOiK16175.
OrthoDBiEOG091G01EF.
PhylomeDBiQ14160.
TreeFamiTF351429.

Family and domain databases

Gene3Di2.30.42.10. 4 hits.
3.80.10.10. 3 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR001478. PDZ.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
PF00595. PDZ. 4 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 11 hits.
SM00228. PDZ. 4 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 4 hits.
SSF52058. SSF52058. 2 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. AlignAdd to basket

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)DescriptionActionsGraphical viewLength
Sequence conflicti674V → E in AAP88017 (PubMed:15649318).Curated1
Sequence conflicti674V → E in AAL38976 (PubMed:15806148).Curated1
Sequence conflicti674V → E in AAP88018 (Ref. 3) Curated1
Sequence conflicti674V → E in BAA09768 (PubMed:8590280).Curated1
Sequence conflicti1489E → K in AAL38976 (PubMed:15806148).Curated1

Natural variant

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Natural variantiVAR_019429422P → L.4 PublicationsCorresponds to variant rs6558394dbSNPEnsembl.1
Natural variantiVAR_067219454P → S in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. 1 Publication1
Natural variantiVAR_0672201535R → Q in NTD; protein interactions not affected by the mutation; shows reduced protein localization to the cell membrane. 1 Publication1

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0109061 – 81Missing in isoform 2. 1 PublicationAdd BLAST81
Alternative sequenceiVSP_0109081565L → LPLSGKKFDYRAFAALPSSR PVYDIQ in isoform 3. 1 Publication1

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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. [Q14160-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
PDB entryMethodResolution (Å)ChainPositionsPDBsum
1UJUNMR-A1096-1193[»]
1WHANMR-A860-951[»]
1X5QNMR-A718-814[»]
2W4FX-ray1.30A725-815[»]
4WYTX-ray2.60A992-1203[»]
4WYUX-ray2.50A/B992-1203[»]
ProteinModelPortaliQ14160.
SMRiQ14160.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi117060. 52 interactors.
DIPiDIP-31259N.
IntActiQ14160. 49 interactors.
MINTiMINT-147371.
STRINGi9606.ENSP00000349486.

PTM databases

iPTMnetiQ14160.
PhosphoSitePlusiQ14160.
SwissPalmiQ14160.

Polymorphism and mutation databases

BioMutaiSCRIB.
DMDMi261260101.

Proteomic databases

EPDiQ14160.
MaxQBiQ14160.
PaxDbiQ14160.
PeptideAtlasiQ14160.
PRIDEiQ14160.

Protocols and materials databases

DNASUi23513.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi23513.
DisGeNETi23513.
GeneCardsiSCRIB.
HGNCiHGNC:30377. SCRIB.
HPAiCAB015463.
CAB022081.
HPA023557.
HPA064312.
MalaCardsiSCRIB.
MIMi182940. phenotype.
607733. gene.
neXtProtiNX_Q14160.
PharmGKBiPA134936275.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410KCZ0. Eukaryota.
COG4886. LUCA.
HOGENOMiHOG000113281.
InParanoidiQ14160.
KOiK16175.
OrthoDBiEOG091G01EF.
PhylomeDBiQ14160.
TreeFamiTF351429.

Enzyme and pathway databases

ReactomeiR-HSA-4608870. Asymmetric localization of PCP proteins.
SignaLinkiQ14160.

Miscellaneous databases

ChiTaRSiSCRIB. human.
EvolutionaryTraceiQ14160.
GeneWikiiSCRIB.
GenomeRNAii23513.
PROiQ14160.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000180900.
CleanExiHS_SCRIB.
ExpressionAtlasiQ14160. baseline and differential.
GenevisibleiQ14160. HS.

Family and domain databases

Gene3Di2.30.42.10. 4 hits.
3.80.10.10. 3 hits.
InterProiIPR032675. L_dom-like.
IPR001611. Leu-rich_rpt.
IPR003591. Leu-rich_rpt_typical-subtyp.
IPR001478. PDZ.
[Graphical view]
PfamiPF13855. LRR_8. 2 hits.
PF00595. PDZ. 4 hits.
[Graphical view]
SMARTiSM00369. LRR_TYP. 11 hits.
SM00228. PDZ. 4 hits.
[Graphical view]
SUPFAMiSSF50156. SSF50156. 4 hits.
SSF52058. SSF52058. 2 hits.
PROSITEiPS51450. LRR. 13 hits.
PS50106. PDZ. 4 hits.
[Graphical view]
ProtoNetiSearch...

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: November 30, 2016
This is version 173 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.