Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-01282
Entry Name
UniProt Accession
Theoretical PI
5.01
Molecular Weight
174884.98
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Protein scribble homolog
Protein Synonyms/Alias
Scribble; hScrib; Protein LAP4;
Gene Name
SCRIB
Gene Synonyms/Alias
CRIB1; KIAA0147; LAP4; SCRB1; VARTUL;
Created Date
19-JUL-2004
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
4
Canonical
****MLKCIPLWRCN
[1]
S-Palmitoylation
10
Canonical
KCIPLWRCNRHVESV
[1]
S-Palmitoylation
1297
Canonical
GKMAESPCSPSGQQP
[1]
S-Palmitoylation
1612
Canonical
GPEDVALCSSRRPVR
[1]
S-Palmitoylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Predicted from GPS-Lipid
Functional Description
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.
Sequence Annotation
Domain: 728 815 PDZ 1.
Domain: 862 950 PDZ 2.
Domain: 1004 1093 PDZ 3.
Domain: 1100 1194 PDZ 4.
Region: 1 818 Sufficient for targeting to adherensjunction and to inhibit cellproliferation.
Region: 717 1229 Interaction with ARHGEF7.
Modified residue: 688 688 Phosphoserine.
Modified residue: 689 689 Phosphothreonine.
Modified residue: 826 826 Phosphothreonine.
Modified residue: 835 835 Phosphoserine.
Modified residue: 853 853 Phosphoserine.
Modified residue: 939 939 Phosphoserine.
Modified residue: 1140 1140 Phosphoserine.
Modified residue: 1220 1220 Phosphoserine.
Modified residue: 1223 1223 Phosphoserine.
Modified residue: 1232 1232 Phosphoserine.
Modified residue: 1306 1306 Phosphoserine.
Modified residue: 1309 1309 Phosphoserine.
Modified residue: 1342 1342 Phosphothreonine.
Modified residue: 1348 1348 Phosphoserine.
Modified residue: 1378 1378 Phosphoserine.
Modified residue: 1437 1437 Phosphoserine.
Modified residue: 1448 1448 Phosphoserine.
Modified residue: 1475 1475 Phosphoserine.
Modified residue: 1486 1486 Phosphoserine.
Modified residue: 1547 1547 Phosphoserine.
Modified residue: 1566 1566 Phosphoserine.
Protein Length
1630 AA.
Protein Sequence
(Canonical)
MLKCIPLWRC NRHVESVDKR HCSLQAVPEE IYRYSRSLEE LLLDANQLRE LPKPFFRLLN  60
LRKLGLSDNE IQRLPPEVAN FMQLVELDVS RNDIPEIPES IKFCKALEIA DFSGNPLSRL  120
PDGFTQLRSL AHLALNDVSL QALPGDVGNL ANLVTLELRE NLLKSLPASL SFLVKLEQLD  180
LGGNDLEVLP DTLGALPNLR ELWLDRNQLS ALPPELGNLR RLVCLDVSEN RLEELPAELG  240
GLVLLTDLLL SQNLLRRLPD GIGQLKQLSI LKVDQNRLCE VTEAIGDCEN LSELILTENL  300
LMALPRSLGK LTKLTNLNVD RNHLEALPPE IGGCVALSVL SLRDNRLAVL PPELAHTTEL  360
HVLDVAGNRL QSLPFALTHL NLKALWLAEN QAQPMLRFQT EDDARTGEKV LTCYLLPQQP  420
PPSLEDAGQQ GSLSETWSDA PPSRVSVIQF LEAPIGDEDA EEAAAEKRGL QRRATPHPSE  480
LKVMKRSIEG RRSEACPCQP DSGSPLPAEE EKRLSAESGL SEDSRPSAST VSEAEPEGPS  540
AEAQGGSQQE ATTAGGEEDA EEDYQEPTVH FAEDALLPGD DREIEEGQPE APWTLPGGRQ  600
RLIRKDTPHY KKHFKISKLP QPEAVVALLQ GMQPDGEGPV APGGWHNGPH APWAPRAQKE  660
EEEEEEGSPQ EEEVEEEEEN RAEEEEASTE EEDKEGAVVS APSVKGVSFD QANNLLIEPA  720
RIEEEELTLT ILRQTGGLGI SIAGGKGSTP YKGDDEGIFI SRVSEEGPAA RAGVRVGDKL  780
LEVNGVALQG AEHHEAVEAL RGAGTAVQMR VWRERMVEPE NAVTITPLRP EDDYSPRERR  840
GGGLRLPLLP PESPGPLRQR HVACLARSER GLGFSIAGGK GSTPYRAGDA GIFVSRIAEG  900
GAAHRAGTLQ VGDRVLSING VDVTEARHDH AVSLLTAASP TIALLLEREA GGPLPPSPLP  960
HSSPPTAAVA TTSITTATPG VPGLPSLAPS LLAAALEGPY PVEEIRLPRA GGPLGLSIVG  1020
GSDHSSHPFG VQEPGVFISK VLPRGLAARS GLRVGDRILA VNGQDVRDAT HQEAVSALLR  1080
PCLELSLLVR RDPAPPGLRE LCIQKAPGER LGISIRGGAR GHAGNPRDPT DEGIFISKVS  1140
PTGAAGRDGR LRVGLRLLEV NQQSLLGLTH GEAVQLLRSV GDTLTVLVCD GFEASTDAAL  1200
EVSPGVIANP FAAGIGHRNS LESISSIDRE LSPEGPGKEK ELPGQTLHWG PEATEAAGRG  1260
LQPLKLDYRA LAAVPSAGSV QRVPSGAAGG KMAESPCSPS GQQPPSPPSP DELPANVKQA  1320
YRAFAAVPTS HPPEDAPAQP PTPGPAASPE QLSFRERQKY FELEVRVPQA EGPPKRVSLV  1380
GADDLRKMQE EEARKLQQKR AQMLREAAEA GAEARLALDG ETLGEEEQED EQPPWASPSP  1440
TSRQSPASPP PLGGGAPVRT AKAERRHQER LRVQSPEPPA PERALSPAEL RALEAEKRAL  1500
WRAARMKSLE QDALRAQMVL SRSQEGRGTR GPLERLAEAP SPAPTPSPTP VEDLGPQTST  1560
SPGRLSPDFA EELRSLEPSP SPGPQEEDGE VALVLLGRPS PGAVGPEDVA LCSSRRPVRP  1620
GRRGLGPVPS                                                         1630
FASTA
(Canonical)
>LipidDB-9606-01282|Q14160
MLKCIPLWRCNRHVESVDKRHCSLQAVPEEIYRYSRSLEELLLDANQLRELPKPFFRLLN
LRKLGLSDNEIQRLPPEVANFMQLVELDVSRNDIPEIPESIKFCKALEIADFSGNPLSRL
PDGFTQLRSLAHLALNDVSLQALPGDVGNLANLVTLELRENLLKSLPASLSFLVKLEQLD
LGGNDLEVLPDTLGALPNLRELWLDRNQLSALPPELGNLRRLVCLDVSENRLEELPAELG
GLVLLTDLLLSQNLLRRLPDGIGQLKQLSILKVDQNRLCEVTEAIGDCENLSELILTENL
LMALPRSLGKLTKLTNLNVDRNHLEALPPEIGGCVALSVLSLRDNRLAVLPPELAHTTEL
HVLDVAGNRLQSLPFALTHLNLKALWLAENQAQPMLRFQTEDDARTGEKVLTCYLLPQQP
PPSLEDAGQQGSLSETWSDAPPSRVSVIQFLEAPIGDEDAEEAAAEKRGLQRRATPHPSE
LKVMKRSIEGRRSEACPCQPDSGSPLPAEEEKRLSAESGLSEDSRPSASTVSEAEPEGPS
AEAQGGSQQEATTAGGEEDAEEDYQEPTVHFAEDALLPGDDREIEEGQPEAPWTLPGGRQ
RLIRKDTPHYKKHFKISKLPQPEAVVALLQGMQPDGEGPVAPGGWHNGPHAPWAPRAQKE
EEEEEEGSPQEEEVEEEEENRAEEEEASTEEEDKEGAVVSAPSVKGVSFDQANNLLIEPA
RIEEEELTLTILRQTGGLGISIAGGKGSTPYKGDDEGIFISRVSEEGPAARAGVRVGDKL
LEVNGVALQGAEHHEAVEALRGAGTAVQMRVWRERMVEPENAVTITPLRPEDDYSPRERR
GGGLRLPLLPPESPGPLRQRHVACLARSERGLGFSIAGGKGSTPYRAGDAGIFVSRIAEG
GAAHRAGTLQVGDRVLSINGVDVTEARHDHAVSLLTAASPTIALLLEREAGGPLPPSPLP
HSSPPTAAVATTSITTATPGVPGLPSLAPSLLAAALEGPYPVEEIRLPRAGGPLGLSIVG
GSDHSSHPFGVQEPGVFISKVLPRGLAARSGLRVGDRILAVNGQDVRDATHQEAVSALLR
PCLELSLLVRRDPAPPGLRELCIQKAPGERLGISIRGGARGHAGNPRDPTDEGIFISKVS
PTGAAGRDGRLRVGLRLLEVNQQSLLGLTHGEAVQLLRSVGDTLTVLVCDGFEASTDAAL
EVSPGVIANPFAAGIGHRNSLESISSIDRELSPEGPGKEKELPGQTLHWGPEATEAAGRG
LQPLKLDYRALAAVPSAGSVQRVPSGAAGGKMAESPCSPSGQQPPSPPSPDELPANVKQA
YRAFAAVPTSHPPEDAPAQPPTPGPAASPEQLSFRERQKYFELEVRVPQAEGPPKRVSLV
GADDLRKMQEEEARKLQQKRAQMLREAAEAGAEARLALDGETLGEEEQEDEQPPWASPSP
TSRQSPASPPPLGGGAPVRTAKAERRHQERLRVQSPEPPAPERALSPAELRALEAEKRAL
WRAARMKSLEQDALRAQMVLSRSQEGRGTRGPLERLAEAPSPAPTPSPTPVEDLGPQTST
SPGRLSPDFAEELRSLEPSPSPGPQEEDGEVALVLLGRPSPGAVGPEDVALCSSRRPVRP
GRRGLGPVPS
Gene Ontology
GO:0016323; C:basolateral plasma membrane; IEA:Ensembl
GO:0042995; C:cell projection; IEA:UniProtKB-KW
GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB
GO:0005911; C:cell-cell junction; IDA:UniProtKB
GO:0070062; C:extracellular vesicular exosome; IDA:UniProt
GO:0035748; C:myelin sheath abaxonal region; IEA:Ensembl
GO:0005886; C:plasma membrane; IDA:UniProtKB
GO:0034750; C:Scrib-APC-beta-catenin complex; IDA:BHF-UCL
GO:0032863; P:activation of Rac GTPase activity; IMP:UniProtKB
GO:0060561; P:apoptotic process involved in morphogenesis; IMP:UniProtKB
GO:0043615; P:astrocyte cell migration; IEA:Ensembl
GO:0008105; P:asymmetric protein localization; IEA:Ensembl
GO:0060088; P:auditory receptor cell stereocilium organization; IEA:Ensembl
GO:0016477; P:cell migration; IMP:UniProtKB
GO:0008283; P:cell proliferation; IDA:UniProtKB
GO:0021747; P:cochlear nucleus development; IEA:Ensembl
GO:0035089; P:establishment of apical/basal cell polarity; IMP:UniProtKB
GO:0060603; P:mammary gland duct morphogenesis; ISS:UniProtKB
GO:0045930; P:negative regulation of mitotic cell cycle; IDA:UniProtKB
GO:0001843; P:neural tube closure; IMP:UniProtKB
GO:0050918; P:positive chemotaxis; IMP:UniProtKB
GO:0043065; P:positive regulation of apoptotic process; IMP:UniProtKB
GO:0001921; P:positive regulation of receptor recycling; IMP:UniProtKB
GO:0071896; P:protein localization to adherens junction; IMP:BHF-UCL
GO:0016337; P:single organismal cell-cell adhesion; IGI:UniProtKB
GO:0048488; P:synaptic vesicle endocytosis; IEA:Ensembl
GO:0016080; P:synaptic vesicle targeting; IEA:Ensembl
GO:0016032; P:viral process; IEA:UniProtKB-KW
GO:0042060; P:wound healing; IEA:Ensembl
Interpro
InterPro; IPR001611; Leu-rich_rpt
InterPro; IPR025875; Leu-rich_rpt_4
InterPro; IPR003591; Leu-rich_rpt_typical-subtyp
InterPro; IPR001478; PDZ
Pfam
Pfam; PF12799; LRR_4;
Pfam; PF13855; LRR_8;
Pfam; PF00595; PDZ;
SMART
SMART; SM00369; LRR_TYP;
SMART; SM00228; PDZ;
PROSITE
PROSITE; PS51450; LRR;
PROSITE; PS50106; PDZ;
PRINTS