CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-022397
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Cadherin EGF LAG seven-pass G-type receptor 3 
Protein Synonyms/Alias
 Cadherin family member 11; Epidermal growth factor-like protein 1; EGF-like protein 1; Flamingo homolog 1; hFmi1; Multiple epidermal growth factor-like domains protein 2; Multiple EGF-like domains protein 2 
Gene Name
 CELSR3 
Gene Synonyms/Alias
 CDHF11; EGFL1; FMI1; KIAA0812; MEGF2 
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
2062TNGQCHCKEFHYRPRubiquitination[1]
2131VLYDACPKSLRSGVWubiquitination[1]
2143GVWWPQTKFGVLATVubiquitination[1]
2197LDGLELNKTALDTMEubiquitination[1]
2206ALDTMEAKKLAQRLRubiquitination[2]
2207LDTMEAKKLAQRLREubiquitination[1, 2]
2477LQTANRSKAICVQWDubiquitination[1, 2]
2790MPACLGRKAAPEEARubiquitination[1]
Reference
 [1] 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]
 [2] Integrated proteomic analysis of post-translational modifications by serial enrichment.
 Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
 Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302] 
Functional Description
 Receptor that may have an important role in cell/cell signaling during nervous system formation. 
Sequence Annotation
 DOMAIN 326 433 Cadherin 1.
 DOMAIN 434 545 Cadherin 2.
 DOMAIN 546 651 Cadherin 3.
 DOMAIN 652 756 Cadherin 4.
 DOMAIN 757 858 Cadherin 5.
 DOMAIN 859 961 Cadherin 6.
 DOMAIN 962 1067 Cadherin 7.
 DOMAIN 1068 1169 Cadherin 8.
 DOMAIN 1170 1265 Cadherin 9.
 DOMAIN 1375 1433 EGF-like 1; calcium-binding.
 DOMAIN 1435 1471 EGF-like 2; calcium-binding.
 DOMAIN 1475 1514 EGF-like 3; calcium-binding.
 DOMAIN 1515 1719 Laminin G-like 1.
 DOMAIN 1722 1758 EGF-like 4; calcium-binding.
 DOMAIN 1764 1944 Laminin G-like 2.
 DOMAIN 1946 1982 EGF-like 5; calcium-binding.
 DOMAIN 1983 2020 EGF-like 6; calcium-binding.
 DOMAIN 2021 2053 EGF-like 7; calcium-binding.
 DOMAIN 2055 2090 EGF-like 8; calcium-binding.
 DOMAIN 2077 2124 Laminin EGF-like.
 DOMAIN 2477 2529 GPS.
 MOD_RES 1963 1963 (3R)-3-hydroxyaspartate (Potential).
 MOD_RES 2126 2126 Phosphotyrosine (By similarity).
 MOD_RES 3051 3051 Phosphotyrosine (By similarity).
 MOD_RES 3097 3097 Phosphoserine (By similarity).
 CARBOHYD 632 632 N-linked (GlcNAc...) (Potential).
 CARBOHYD 847 847 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1182 1182 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1222 1222 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1317 1317 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1327 1327 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1649 1649 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1713 1713 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1770 1770 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2053 2053 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2177 2177 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2196 2196 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2386 2386 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2474 2474 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2506 2506 N-linked (GlcNAc...) (Potential).
 DISULFID 1379 1390 By similarity.
 DISULFID 1384 1421 By similarity.
 DISULFID 1423 1432 By similarity.
 DISULFID 1439 1450 By similarity.
 DISULFID 1444 1459 By similarity.
 DISULFID 1461 1470 By similarity.
 DISULFID 1479 1490 By similarity.
 DISULFID 1484 1500 By similarity.
 DISULFID 1502 1513 By similarity.
 DISULFID 1693 1719 By similarity.
 DISULFID 1726 1737 By similarity.
 DISULFID 1731 1746 By similarity.
 DISULFID 1748 1757 By similarity.
 DISULFID 1915 1944 By similarity.
 DISULFID 1950 1961 By similarity.
 DISULFID 1955 1970 By similarity.
 DISULFID 1972 1981 By similarity.
 DISULFID 1985 1996 By similarity.
 DISULFID 1990 2008 By similarity.
 DISULFID 2010 2019 By similarity.
 DISULFID 2027 2040 By similarity.
 DISULFID 2042 2052 By similarity.
 DISULFID 2059 2074 By similarity.
 DISULFID 2061 2077 By similarity.
 DISULFID 2079 2089 By similarity.
 DISULFID 2098 2107 By similarity.
 DISULFID 2110 2122 By similarity.  
Keyword
 Alternative splicing; Calcium; Cell membrane; Complete proteome; Developmental protein; Disulfide bond; EGF-like domain; G-protein coupled receptor; Glycoprotein; Hydroxylation; Laminin EGF-like domain; Membrane; Phosphoprotein; Polymorphism; Receptor; Reference proteome; Repeat; Signal; Transducer; Transmembrane; Transmembrane helix. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3312 AA 
Protein Sequence
MMARRPPWRG LGGRSTPILL LLLLSLFPLS QEELGGGGHQ GWDPGLAATT GPRAHIGGGA 60
LALCPESSGV REDGGPGLGV REPIFVGLRG RRQSARNSRG PPEQPNEELG IEHGVQPLGS 120
RERETGQGPG SVLYWRPEVS SCGRTGPLQR GSLSPGALSS GVPGSGNSSP LPSDFLIRHH 180
GPKPVSSQRN AGTGSRKRVG TARCCGELWA TGSKGQGERA TTSGAERTAP RRNCLPGASG 240
SGPELDSAPR TARTAPASGS APRESRTAPE PAPKRMRSRG LFRCRFLPQR PGPRPPGLPA 300
RPEARKVTSA NRARFRRAAN RHPQFPQYNY QTLVPENEAA GTAVLRVVAQ DPDAGEAGRL 360
VYSLAALMNS RSLELFSIDP QSGLIRTAAA LDRESMERHY LRVTAQDHGS PRLSATTMVA 420
VTVADRNDHS PVFEQAQYRE TLRENVEEGY PILQLRATDG DAPPNANLRY RFVGPPAARA 480
AAAAAFEIDP RSGLISTSGR VDREHMESYE LVVEASDQGQ EPGPRSATVR VHITVLDEND 540
NAPQFSEKRY VAQVREDVRP HTVVLRVTAT DRDKDANGLV HYNIISGNSR GHFAIDSLTG 600
EIQVVAPLDF EAEREYALRI RAQDAGRPPL SNNTGLASIQ VVDINDHIPI FVSTPFQVSV 660
LENAPLGHSV IHIQAVDADH GENARLEYSL TGVAPDTPFV INSATGWVSV SGPLDRESVE 720
HYFFGVEARD HGSPPLSASA SVTVTVLDVN DNRPEFTMKE YHLRLNEDAA VGTSVVSVTA 780
VDRDANSAIS YQITGGNTRN RFAISTQGGV GLVTLALPLD YKQERYFKLV LTASDRALHD 840
HCYVHINITD ANTHRPVFQS AHYSVSVNED RPMGSTIVVI SASDDDVGEN ARITYLLEDN 900
LPQFRIDADS GAITLQAPLD YEDQVTYTLA ITARDNGIPQ KADTTYVEVM VNDVNDNAPQ 960
FVASHYTGLV SEDAPPFTSV LQISATDRDA HANGRVQYTF QNGEDGDGDF TIEPTSGIVR 1020
TVRRLDREAV SVYELTAYAV DRGVPPLRTP VSIQVMVQDV NDNAPVFPAE EFEVRVKENS 1080
IVGSVVAQIT AVDPDEGPNA HIMYQIVEGN IPELFQMDIF SGELTALIDL DYEARQEYVI 1140
VVQATSAPLV SRATVHVRLV DQNDNSPVLN NFQILFNNYV SNRSDTFPSG IIGRIPAYDP 1200
DVSDHLFYSF ERGNELQLLV VNQTSGELRL SRKLDNNRPL VASMLVTVTD GLHSVTAQCV 1260
LRVVIITEEL LANSLTVRLE NMWQERFLSP LLGRFLEGVA AVLATPAEDV FIFNIQNDTD 1320
VGGTVLNVSF SALAPRGAGA GAAGPWFSSE ELQEQLYVRR AALAARSLLD VLPFDDNVCL 1380
REPCENYMKC VSVLRFDSSA PFLASASTLF RPIQPIAGLR CRCPPGFTGD FCETELDLCY 1440
SNPCRNGGAC ARREGGYTCV CRPRFTGEDC ELDTEAGRCV PGVCRNGGTC TDAPNGGFRC 1500
QCPAGGAFEG PRCEVAARSF PPSSFVMFRG LRQRFHLTLS LSFATVQQSG LLFYNGRLNE 1560
KHDFLALELV AGQVRLTYST GESNTVVSPT VPGGLSDGQW HTVHLRYYNK PRTDALGGAQ 1620
GPSKDKVAVL SVDDCDVAVA LQFGAEIGNY SCAAAGVQTS SKKSLDLTGP LLLGGVPNLP 1680
ENFPVSHKDF IGCMRDLHID GRRVDMAAFV ANNGTMAGCQ AKLHFCDSGP CKNSGFCSER 1740
WGSFSCDCPV GFGGKDCQLT MAHPHHFRGN GTLSWNFGSD MAVSVPWYLG LAFRTRATQG 1800
VLMQVQAGPH STLLCQLDRG LLSVTVTRGS GRASHLLLDQ VTVSDGRWHD LRLELQEEPG 1860
GRRGHHVLMV SLDFSLFQDT MAVGSELQGL KVKQLHVGGL PPGSAEEAPQ GLVGCIQGVW 1920
LGSTPSGSPA LLPPSHRVNA EPGCVVTNAC ASGPCPPHAD CRDLWQTFSC TCQPGYYGPG 1980
CVDACLLNPC QNQGSCRHLP GAPHGYTCDC VGGYFGHHCE HRMDQQCPRG WWGSPTCGPC 2040
NCDVHKGFDP NCNKTNGQCH CKEFHYRPRG SDSCLPCDCY PVGSTSRSCA PHSGQCPCRP 2100
GALGRQCNSC DSPFAEVTAS GCRVLYDACP KSLRSGVWWP QTKFGVLATV PCPRGALGAA 2160
VRLCDEAQGW LEPDLFNCTS PAFRELSLLL DGLELNKTAL DTMEAKKLAQ RLREVTGHTD 2220
HYFSQDVRVT ARLLAHLLAF ESHQQGFGLT ATQDAHFNEN LLWAGSALLA PETGDLWAAL 2280
GQRAPGGSPG SAGLVRHLEE YAATLARNME LTYLNPMGLV TPNIMLSIDR MEHPSSPRGA 2340
RRYPRYHSNL FRGQDAWDPH THVLLPSQSP RPSPSEVLPT SSSIENSTTS SVVPPPAPPE 2400
PEPGISIIIL LVYRTLGGLL PAQFQAERRG ARLPQNPVMN SPVVSVAVFH GRNFLRGILE 2460
SPISLEFRLL QTANRSKAIC VQWDPPGLAE QHGVWTARDC ELVHRNGSHA RCRCSRTGTF 2520
GVLMDASPRE RLEGDLELLA VFTHVVVAVS VAALVLTAAI LLSLRSLKSN VRGIHANVAA 2580
ALGVAELLFL LGIHRTHNQL VCTAVAILLH YFFLSTFAWL FVQGLHLYRM QVEPRNVDRG 2640
AMRFYHALGW GVPAVLLGLA VGLDPEGYGN PDFCWISVHE PLIWSFAGPV VLVIVMNGTM 2700
FLLAARTSCS TGQREAKKTS ALTLRSSFLL LLLVSASWLF GLLAVNHSIL AFHYLHAGLC 2760
GLQGLAVLLL FCVLNADARA AWMPACLGRK AAPEEARPAP GLGPGAYNNT ALFEESGLIR 2820
ITLGASTVSS VSSARSGRTQ DQDSQRGRSY LRDNVLVRHG SAADHTDHSL QAHAGPTDLD 2880
VAMFHRDAGA DSDSDSDLSL EEERSLSIPS SESEDNGRTR GRFQRPLCRA AQSERLLTHP 2940
KDVDGNDLLS YWPALGECEA APCALQTWGS ERRLGLDTSK DAANNNQPDP ALTSGDETSL 3000
GRAQRQRKGI LKNRLQYPLV PQTRGAPELS WCRAATLGHR AVPAASYGRI YAGGGTGSLS 3060
QPASRYSSRE QLDLLLRRQL SRERLEEAPA PVLRPLSRPG SQECMDAAPG RLEPKDRGST 3120
LPRRQPPRDY PGAMAGRFGS RDALDLGAPR EWLSTLPPPR RTRDLDPQPP PLPLSPQRQL 3180
SRDPLLPSRP LDSLSRSSNS REQLDQVPSR HPSREALGPL PQLLRAREDS VSGPSHGPST 3240
EQLDILSSIL ASFNSSALSS VQSSSTPLGP HTTATPSATA SVLGPSTPRS ATSHSISELS 3300
PDSEVPRSEG HS 3312 
Gene Ontology
 GO:0016021; C:integral to membrane; TAS:GDB.
 GO:0005886; C:plasma membrane; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0004930; F:G-protein coupled receptor activity; TAS:GDB.
 GO:0007413; P:axonal fasciculation; IEA:Compara.
 GO:0007156; P:homophilic cell adhesion; IEA:InterPro.
 GO:0001764; P:neuron migration; IEA:Compara.
 GO:0007218; P:neuropeptide signaling pathway; IEA:InterPro. 
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.
 IPR013032; EGF-like_CS.
 IPR002049; EGF_laminin.
 IPR017981; GPCR_2-like.
 IPR001879; GPCR_2_extracellular_dom.
 IPR000832; GPCR_2_secretin-like.
 IPR017983; GPCR_2_secretin-like_CS.
 IPR000203; GPS_dom.
 IPR001791; Laminin_G. 
Pfam
 PF00002; 7tm_2
 PF00028; Cadherin
 PF12003; DUF3497
 PF00008; EGF
 PF01825; GPS
 PF02793; HRM
 PF00053; Laminin_EGF
 PF02210; Laminin_G_2 
SMART
 SM00112; CA
 SM00181; EGF
 SM00180; EGF_Lam
 SM00303; GPS
 SM00008; HormR
 SM00282; LamG 
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.