CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012270
UniProt Accession
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
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
53NQLRELPKPFFRLLNubiquitination[1, 2]
63FRLLNLRKLGLSDNEubiquitination[1, 2]
105PESIKFCKALEIADFubiquitination[1, 3]
164ELRENLLKSLPASLSubiquitination[2]
266PDGIGQLKQLSILKVubiquitination[2]
272LKQLSILKVDQNRLCubiquitination[1, 2, 3]
313RSLGKLTKLTNLNVDubiquitination[3]
467AEEAAAEKRGLQRRAubiquitination[4]
880GFSIAGGKGSTPYRAubiquitination[3]
1105LRELCIQKAPGERLGubiquitination[3]
Reference
 [1] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965]
 [2] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789]
 [3] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
 Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
 J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931] 
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
 REPEAT 37 58 LRR 1.
 REPEAT 60 81 LRR 2.
 REPEAT 83 104 LRR 3.
 REPEAT 106 127 LRR 4.
 REPEAT 129 150 LRR 5.
 REPEAT 152 174 LRR 6.
 REPEAT 175 197 LRR 7.
 REPEAT 198 219 LRR 8.
 REPEAT 221 243 LRR 9.
 REPEAT 244 265 LRR 10.
 REPEAT 267 288 LRR 11.
 REPEAT 290 312 LRR 12.
 REPEAT 313 334 LRR 13.
 REPEAT 336 357 LRR 14.
 REPEAT 359 381 LRR 15.
 REPEAT 382 402 LRR 16.
 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 adherens
 REGION 717 1229 Interaction with ARHGEF7.
 MOD_RES 688 688 Phosphoserine.
 MOD_RES 689 689 Phosphothreonine.
 MOD_RES 826 826 Phosphothreonine.
 MOD_RES 835 835 Phosphoserine.
 MOD_RES 853 853 Phosphoserine.
 MOD_RES 939 939 Phosphoserine.
 MOD_RES 1140 1140 Phosphoserine.
 MOD_RES 1220 1220 Phosphoserine.
 MOD_RES 1223 1223 Phosphoserine.
 MOD_RES 1232 1232 Phosphoserine.
 MOD_RES 1306 1306 Phosphoserine.
 MOD_RES 1309 1309 Phosphoserine.
 MOD_RES 1342 1342 Phosphothreonine.
 MOD_RES 1348 1348 Phosphoserine.
 MOD_RES 1378 1378 Phosphoserine.
 MOD_RES 1437 1437 Phosphoserine.
 MOD_RES 1448 1448 Phosphoserine.
 MOD_RES 1475 1475 Phosphoserine.
 MOD_RES 1486 1486 Phosphoserine.
 MOD_RES 1547 1547 Phosphoserine.
 MOD_RES 1566 1566 Phosphoserine.  
Keyword
 3D-structure; Alternative splicing; Cell junction; Cell membrane; Coiled coil; Complete proteome; Cytoplasm; Developmental protein; Differentiation; Disease mutation; Host-virus interaction; Leucine-rich repeat; Membrane; Phosphoprotein; Polymorphism; Reference proteome; Repeat; Ubl conjugation. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 1630 AA 
Protein Sequence
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
SPGRLPLSGK KFDYRAFAAL PSSRPVYDIQ SPDFAEELRS LEPSPSPGPQ EEDGEVALVL 1620
LGRPSPGAVG PEDVALCSSR RPVRPGRRGL GPVPS 1655 
Gene Ontology
 GO:0016323; C:basolateral plasma membrane; IEA:Compara.
 GO:0005913; C:cell-cell adherens junction; IDA:UniProtKB.
 GO:0035748; C:myelin sheath abaxonal region; IEA:Compara.
 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:0008105; P:asymmetric protein localization; IEA:Compara.
 GO:0016477; P:cell migration; IMP:UniProtKB.
 GO:0008283; P:cell proliferation; IDA:UniProtKB.
 GO:0016337; P:cell-cell adhesion; IGI:UniProtKB.
 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:0048488; P:synaptic vesicle endocytosis; IEA:Compara.
 GO:0016080; P:synaptic vesicle targeting; IEA:Compara.
 GO:0019048; P:virus-host interaction; IEA:UniProtKB-KW.
 GO:0042060; P:wound healing; IEA:Compara. 
Interpro
 IPR001611; Leu-rich_rpt.
 IPR025875; Leu-rich_rpt_4.
 IPR003591; Leu-rich_rpt_typical-subtyp.
 IPR001478; PDZ. 
Pfam
 PF12799; LRR_4
 PF00595; PDZ 
SMART
 SM00369; LRR_TYP
 SM00228; PDZ 
PROSITE
 PS51450; LRR
 PS50106; PDZ 
PRINTS