CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-012269
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
83ELRENLLKSLPASLSubiquitination[1]
185PDGIGQLKQLSILKVubiquitination[1]
232RSLGKLTKLTNLNVDubiquitination[1]
386AEEAAAEKRGLQRRAubiquitination[1]
Reference
 [1] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661] 
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
MQLVELDVSR NDIPEIPESI KFCKALEIAD FSGNPLSRLP DGFTQLRSLA HLALNDVSLQ 60
ALPGDVGNLA NLVTLELREN LLKSLPASLS FLVKLEQLDL GGNDLEVLPD TLGALPNLRE 120
LWLDRNQLSA LPPELGNLRR LVCLDVSENR LEELPAELGG LVLLTDLLLS QNLLRRLPDG 180
IGQLKQLSIL KVDQNRLCEV TEAIGDCENL SELILTENLL MALPRSLGKL TKLTNLNVDR 240
NHLEALPPEI GGCVALSVLS LRDNRLAVLP PELAHTTELH VLDVAGNRLQ SLPFALTHLN 300
LKALWLAENQ AQPMLRFQTE DDARTGEKVL TCYLLPQQPP PSLEDAGQQG SLSETWSDAP 360
PSRVSVIQFL EAPIGDEDAE EAAAEKRGLQ RRATPHPSEL KVMKRSIEGR RSEACPCQPD 420
SGSPLPAEEE KRLSAESGLS EDSRPSASTV SEAEPEGPSA EAQGGSQQEA TTAGGEEDAE 480
EDYQEPTVHF AEDALLPGDD REIEEGQPEA PWTLPGGRQR LIRKDTPHYK KHFKISKLPQ 540
PEAVVALLQG MQPDGEGPVA PGGWHNGPHA PWAPRAQKEE EEEEEGSPQE EEVEEEEENR 600
AEEEEASTEE EDKEGAVVSA PSVKGVSFDQ ANNLLIEPAR IEEEELTLTI LRQTGGLGIS 660
IAGGKGSTPY KGDDEGIFIS RVSEEGPAAR AGVRVGDKLL EVNGVALQGA EHHEAVEALR 720
GAGTAVQMRV WRERMVEPEN AVTITPLRPE DDYSPRERRG GGLRLPLLPP ESPGPLRQRH 780
VACLARSERG LGFSIAGGKG STPYRAGDAG IFVSRIAEGG AAHRAGTLQV GDRVLSINGV 840
DVTEARHDHA VSLLTAASPT IALLLEREAG GPLPPSPLPH SSPPTAAVAT TSITTATPGV 900
PGLPSLAPSL LAAALEGPYP VEEIRLPRAG GPLGLSIVGG SDHSSHPFGV QEPGVFISKV 960
LPRGLAARSG LRVGDRILAV NGQDVRDATH QEAVSALLRP CLELSLLVRR DPAPPGLREL 1020
CIQKAPGERL GISIRGGARG HAGNPRDPTD EGIFISKVSP TGAAGRDGRL RVGLRLLEVN 1080
QQSLLGLTHG EAVQLLRSVG DTLTVLVCDG FEASTDAALE VSPGVIANPF AAGIGHRNSL 1140
ESISSIDREL SPEGPGKEKE LPGQTLHWGP EATEAAGRGL QPLKLDYRAL AAVPSAGSVQ 1200
RVPSGAAGGK MAESPCSPSG QQPPSPPSPD ELPANVKQAY RAFAAVPTSH PPEDAPAQPP 1260
TPGPAASPEQ LSFRERQKYF ELEVRVPQAE GPPKRVSLVG ADDLRKMQEE EARKLQQKRA 1320
QMLREAAEAG AEARLALDGE TLGEEEQEDE QPPWASPSPT SRQSPASPPP LGGGAPVRTA 1380
KAERRHQERL RVQSPEPPAP ERALSPAELR ALEAEKRALW RAARMKSLEQ DALRAQMVLS 1440
RSQEGRGTRG PLERLAEAPS PAPTPSPTPV EDLGPQTSTS PGRLSPDFAE ELRSLEPSPS 1500
PGPQEEDGEV ALVLLGRPSP GAVGPEDVAL CSSRRPVRPG RRGLGPVPS 1549 
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