CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-021682
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cadherin EGF LAG seven-pass G-type receptor 2 
Protein Synonyms/Alias
 Cadherin family member 10; Epidermal growth factor-like protein 2; EGF-like protein 2; Flamingo homolog 3; Multiple epidermal growth factor-like domains protein 3; Multiple EGF-like domains protein 3 
Gene Name
 CELSR2 
Gene Synonyms/Alias
 CDHF10; EGFL2; KIAA0279; MEGF3 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
468PLDYETTKEYTLRVRubiquitination[1, 2]
676LALPLDYKLERQYVLubiquitination[1]
2121ALLDTANKRHWELIQubiquitination[1]
2637PDPALTTKSTLTSSYubiquitination[2]
2674HSTSRSGKSQPSYIPubiquitination[1]
Reference
 [1] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [2] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094
Functional Description
 Receptor that may have an important role in cell/cell signaling during nervous system formation. 
Sequence Annotation
 DOMAIN 182 289 Cadherin 1.
 DOMAIN 290 399 Cadherin 2.
 DOMAIN 400 505 Cadherin 3.
 DOMAIN 506 610 Cadherin 4.
 DOMAIN 611 712 Cadherin 5.
 DOMAIN 713 815 Cadherin 6.
 DOMAIN 816 921 Cadherin 7.
 DOMAIN 922 1023 Cadherin 8.
 DOMAIN 1028 1146 Cadherin 9.
 DOMAIN 1228 1286 EGF-like 1; calcium-binding.
 DOMAIN 1288 1324 EGF-like 2; calcium-binding.
 DOMAIN 1328 1366 EGF-like 3; calcium-binding.
 DOMAIN 1367 1571 Laminin G-like 1.
 DOMAIN 1574 1610 EGF-like 4; calcium-binding.
 DOMAIN 1614 1791 Laminin G-like 2.
 DOMAIN 1793 1828 EGF-like 5; calcium-binding.
 DOMAIN 1829 1867 EGF-like 6; calcium-binding.
 DOMAIN 1883 1922 EGF-like 7; calcium-binding.
 DOMAIN 1924 1971 Laminin EGF-like.
 DOMAIN 2316 2368 GPS.
 MOD_RES 1591 1591 (3R)-3-hydroxyasparagine (Potential).
 MOD_RES 1810 1810 (3R)-3-hydroxyasparagine (Potential).
 CARBOHYD 486 486 N-linked (GlcNAc...) (Potential).
 CARBOHYD 557 557 N-linked (GlcNAc...) (Potential).
 CARBOHYD 701 701 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1036 1036 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1076 1076 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1182 1182 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1212 1212 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1501 1501 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1565 1565 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1741 1741 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1827 1827 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1900 1900 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2024 2024 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2043 2043 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2061 2061 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2323 2323 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2345 2345 N-linked (GlcNAc...) (Potential).
 DISULFID 1232 1243 By similarity.
 DISULFID 1237 1274 By similarity.
 DISULFID 1276 1285 By similarity.
 DISULFID 1292 1303 By similarity.
 DISULFID 1297 1312 By similarity.
 DISULFID 1314 1323 By similarity.
 DISULFID 1332 1343 By similarity.
 DISULFID 1337 1353 By similarity.
 DISULFID 1355 1365 By similarity.
 DISULFID 1545 1571 By similarity.
 DISULFID 1578 1589 By similarity.
 DISULFID 1583 1598 By similarity.
 DISULFID 1600 1609 By similarity.
 DISULFID 1761 1791 By similarity.
 DISULFID 1797 1808 By similarity.
 DISULFID 1802 1817 By similarity.
 DISULFID 1819 1828 By similarity.
 DISULFID 1832 1843 By similarity.
 DISULFID 1837 1855 By similarity.
 DISULFID 1857 1866 By similarity.
 DISULFID 1887 1899 By similarity.
 DISULFID 1889 1906 By similarity.
 DISULFID 1908 1921 By similarity.
 DISULFID 1924 1936 By similarity.
 DISULFID 1926 1943 By similarity.
 DISULFID 1945 1954 By similarity.
 DISULFID 1957 1969 By similarity.  
Keyword
 Calcium; Cell membrane; Complete proteome; Developmental protein; Disulfide bond; EGF-like domain; G-protein coupled receptor; Glycoprotein; Hydroxylation; Laminin EGF-like domain; Membrane; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transducer; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 2923 AA 
Protein Sequence
MRSPATGVPL PTPPPPLLLL LLLLLPPPLL GDQVGPCRSL GSRGRGSSGA CAPMGWLCPS 60
SASNLWLYTS RCRDAGTELT GHLVPHHDGL RVWCPESEAH IPLPPAPEGC PWSCRLLGIG 120
GHLSPQGKLT LPEEHPCLKA PRLRCQSCKL AQAPGLRAGE RSPEESLGGR RKRNVNTAPQ 180
FQPPSYQATV PENQPAGTPV ASLRAIDPDE GEAGRLEYTM DALFDSRSNQ FFSLDPVTGA 240
VTTAEELDRE TKSTHVFRVT AQDHGMPRRS ALATLTILVT DTNDHDPVFE QQEYKESLRE 300
NLEVGYEVLT VRATDGDAPP NANILYRLLE GSGGSPSEVF EIDPRSGVIR TRGPVDREEV 360
ESYQLTVEAS DQGRDPGPRS TTAAVFLSVE DDNDNAPQFS EKRYVVQVRE DVTPGAPVLR 420
VTASDRDKGS NAVVHYSIMS GNARGQFYLD AQTGALDVVS PLDYETTKEY TLRVRAQDGG 480
RPPLSNVSGL VTVQVLDIND NAPIFVSTPF QATVLESVPL GYLVLHVQAI DADAGDNARL 540
EYRLAGVGHD FPFTINNGTG WISVAAELDR EEVDFYSFGV EARDHGTPAL TASASVSVTV 600
LDVNDNNPTF TQPEYTVRLN EDAAVGTSVV TVSAVDRDAH SVITYQITSG NTRNRFSITS 660
QSGGGLVSLA LPLDYKLERQ YVLAVTASDG TRQDTAQIVV NVTDANTHRP VFQSSHYTVN 720
VNEDRPAGTT VVLISATDED TGENARITYF MEDSIPQFRI DADTGAVTTQ AELDYEDQVS 780
YTLAITARDN GIPQKSDTTY LEILVNDVND NAPQFLRDSY QGSVYEDVPP FTSVLQISAT 840
DRDSGLNGRV FYTFQGGDDG DGDFIVESTS GIVRTLRRLD RENVAQYVLR AYAVDKGMPP 900
ARTPMEVTVT VLDVNDNPPV FEQDEFDVFV EENSPIGLAV ARVTATDPDE GTNAQIMYQI 960
VEGNIPEVFQ LDIFSGELTA LVDLDYEDRP EYVLVIQATS APLVSRATVH VRLLDRNDNP 1020
PVLGNFEILF NNYVTNRSSS FPGGAIGRVP AHDPDISDSL TYSFERGNEL SLVLLNASTG 1080
ELKLSRALDN NRPLEAIMSV LVSDGVHSVT AQCALRVTII TDEMLTHSIT LRLEDMSPER 1140
FLSPLLGLFI QAVAATLATP PDHVVVFNVQ RDTDAPGGHI LNVSLSVGQP PGPGGGPPFL 1200
PSEDLQERLY LNRSLLTAIS AQRVLPFDDN ICLREPCENY MRCVSVLRFD SSAPFIASSS 1260
VLFRPIHPVG GLRCRCPPGF TGDYCETEVD LCYSRPCGPH GRCRSREGGY TCLCRDGYTG 1320
EHCEVSARSG RCTPGVCKNG GTCVNLLVGG FKCDCPSGDF EKPYCQVTTR SFPAHSFITF 1380
RGLRQRFHFT LALSFATKER DGLLLYNGRF NEKHDFVALE VIQEQVQLTF SAGESTTTVS 1440
PFVPGGVSDG QWHTVQLKYY NKPLLGQTGL PQGPSEQKVA VVTVDGCDTG VALRFGSVLG 1500
NYSCAAQGTQ GGSKKSLDLT GPLLLGGVPD LPESFPVRMR QFVGCMRNLQ VDSRHIDMAD 1560
FIANNGTVPG CPAKKNVCDS NTCHNGGTCV NQWDAFSCEC PLGFGGKSCA QEMANPQHFL 1620
GSSLVAWHGL SLPISQPWYL SLMFRTRQAD GVLLQAITRG RSTITLQLRE GHVMLSVEGT 1680
GLQASSLRLE PGRANDGDWH HAQLALGASG GPGHAILSFD YGQQRAEGNL GPRLHGLHLS 1740
NITVGGIPGP AGGVARGFRG CLQGVRVSDT PEGVNSLDPS HGESINVEQG CSLPDPCDSN 1800
PCPANSYCSN DWDSYSCSCD PGYYGDNCTN VCDLNPCEHQ SVCTRKPSAP HGYTCECPPN 1860
YLGPYCETRI DQPCPRGWWG HPTCGPCNCD VSKGFDPDCN KTSGECHCKE NHYRPPGSPT 1920
CLLCDCYPTG SLSRVCDPED GQCPCKPGVI GRQCDRCDNP FAEVTTNGCE VNYDSCPRAI 1980
EAGIWWPRTR FGLPAAAPCP KGSFGTAVRH CDEHRGWLPP NLFNCTSITF SELKGFAERL 2040
QRNESGLDSG RSQQLALLLR NATQHTAGYF GSDVKVAYQL ATRLLAHEST QRGFGLSATQ 2100
DVHFTENLLR VGSALLDTAN KRHWELIQQT EGGTAWLLQH YEAYASALAQ NMRHTYLSPF 2160
TIVTPNIVIS VVRLDKGNFA GAKLPRYEAL RGEQPPDLET TVILPESVFR ETPPVVRPAG 2220
PGEAQEPEEL ARRQRRHPEL SQGEAVASVI IYRTLAGLLP HNYDPDKRSL RVPKRPIINT 2280
PVVSISVHDD EELLPRALDK PVTVQFRLLE TEERTKPICV FWNHSILVSG TGGWSARGCE 2340
VVFRNESHVS CQCNHMTSFA VLMDVSRREN GEILPLKTLT YVALGVTLAA LLLTFFFLTL 2400
LRILRSNQHG IRRNLTAALG LAQLVFLLGI NQADLPFACT VIAILLHFLY LCTFSWALLE 2460
ALHLYRALTE VRDVNTGPMR FYYMLGWGVP AFITGLAVGL DPEGYGNPDF CWLSIYDTLI 2520
WSFAGPVAFA VSMSVFLYIL AARASCAAQR QGFEKKGPVS GLQPSFAVLL LLSATWLLAL 2580
LSVNSDTLLF HYLFATCNCI QGPFIFLSYV VLSKEVRKAL KLACSRKPSP DPALTTKSTL 2640
TSSYNCPSPY ADGRLYQPYG DSAGSLHSTS RSGKSQPSYI PFLLREESAL NPGQGPPGLG 2700
DPGSLFLEGQ DQQHDPDTDS DSDLSLEDDQ SGSYASTHSS DSEEEEEEEE EEAAFPGEQG 2760
WDSLLGPGAE RLPLHSTPKD GGPGPGKAPW PGDFGTTAKE SSGNGAPEER LRENGDALSR 2820
EGSLGPLPGS SAQPHKGILK KKCLPTISEK SSLLRLPLEQ CTGSSRGSSA SEGSRGGPPP 2880
RPPPRQSLQE QLNGVMPIAM SIKAGTVDED SSGSEFLFFN FLH 2923 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:BHF-UCL.
 GO:0016021; C:integral to membrane; NAS:UniProtKB.
 GO:0005886; C:plasma membrane; ISS:BHF-UCL.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0004930; F:G-protein coupled receptor activity; NAS:UniProtKB.
 GO:0048813; P:dendrite morphogenesis; ISS:BHF-UCL.
 GO:0007156; P:homophilic cell adhesion; ISS:BHF-UCL.
 GO:0021999; P:neural plate anterior/posterior regionalization; ISS:BHF-UCL.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro.
 GO:0022407; P:regulation of cell-cell adhesion; ISS:BHF-UCL.
 GO:0006355; P:regulation of transcription, DNA-dependent; ISS:BHF-UCL.
 GO:0021591; P:ventricular system development; IEA:Compara.
 GO:0016055; P:Wnt receptor signaling pathway; ISS:BHF-UCL. 
Interpro
 IPR002126; Cadherin.
 IPR015919; Cadherin-like.
 IPR020894; Cadherin_CS.
 IPR008985; ConA-like_lec_gl_sf.
 IPR013320; ConA-like_subgrp.
 IPR022624; DUF3497.
 IPR000742; EG-like_dom.
 IPR001881; EGF-like_Ca-bd.
 IPR013032; EGF-like_CS.
 IPR000152; EGF-type_Asp/Asn_hydroxyl_site.
 IPR002049; EGF_laminin.
 IPR017981; GPCR_2-like.
 IPR001879; GPCR_2_extracellular_dom.
 IPR000832; GPCR_2_secretin-like.
 IPR000203; GPS_dom.
 IPR001791; Laminin_G.
 IPR001368; TNFR/NGFR_Cys_rich_reg. 
Pfam
 PF00002; 7tm_2
 PF00028; Cadherin
 PF12003; DUF3497
 PF00008; EGF
 PF01825; GPS
 PF00053; Laminin_EGF
 PF02210; Laminin_G_2 
SMART
 SM00112; CA
 SM00181; EGF
 SM00179; EGF_CA
 SM00180; EGF_Lam
 SM00303; GPS
 SM00008; HormR
 SM00282; LamG
 SM00208; TNFR 
PROSITE
 PS00010; ASX_HYDROXYL
 PS00232; CADHERIN_1
 PS50268; CADHERIN_2
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS01248; EGF_LAM_1
 PS50027; EGF_LAM_2
 PS00649; G_PROTEIN_RECEP_F2_1
 PS00650; G_PROTEIN_RECEP_F2_2
 PS50227; G_PROTEIN_RECEP_F2_3
 PS50261; G_PROTEIN_RECEP_F2_4
 PS50221; GPS
 PS50025; LAM_G_DOMAIN 
PRINTS
 PR00205; CADHERIN.
 PR00249; GPCRSECRETIN.