CPLM 1.0 - Compendium of Protein Lysine Modification
TagContent
CPLM ID CPLM-010426
UniProt Accession
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
 Reelin 
Protein Synonyms/Alias
  
Gene Name
 RELN 
Gene Synonyms/Alias
  
Created Date
 July 27, 2013 
Organism
 Homo sapiens (Human) 
NCBI Taxa ID
 9606 
Lysine Modification
Position
Peptide
Type
References
299ADWIQLEKIRAPSNVacetylation[1]
Reference
 [1] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 
Functional Description
 Extracellular matrix serine protease that plays a role in layering of neurons in the cerebral cortex and cerebellum. Regulates microtubule function in neurons and neuronal migration. Affects migration of sympathetic preganglionic neurons in the spinal cord, where it seems to act as a barrier to neuronal migration. Enzymatic activity is important for the modulation of cell adhesion. Binding to the extracellular domains of lipoprotein receptors VLDLR and LRP8/APOER2 induces tyrosine phosphorylation of DAB1 and modulation of TAU phosphorylation (By similarity). 
Sequence Annotation
 DOMAIN 26 190 Reelin.
 REPEAT 592 603 BNR 1.
 DOMAIN 670 701 EGF-like 1.
 REPEAT 798 809 BNR 2.
 REPEAT 951 962 BNR 3.
 DOMAIN 1029 1060 EGF-like 2.
 REPEAT 1156 1167 BNR 4.
 REPEAT 1322 1333 BNR 5.
 DOMAIN 1408 1441 EGF-like 3.
 REPEAT 1534 1545 BNR 6.
 REPEAT 1685 1696 BNR 7.
 DOMAIN 1764 1795 EGF-like 4.
 REPEAT 1883 1894 BNR 8.
 REPEAT 2042 2053 BNR 9.
 DOMAIN 2128 2160 EGF-like 5.
 REPEAT 2249 2260 BNR 10.
 REPEAT 2398 2409 BNR 11.
 DOMAIN 2477 2508 EGF-like 6.
 REPEAT 2597 2608 BNR 12.
 REPEAT 2777 2788 BNR 13.
 DOMAIN 2852 2883 EGF-like 7.
 REPEAT 2978 2989 BNR 14.
 REPEAT 3142 3154 BNR 15.
 DOMAIN 3227 3259 EGF-like 8.
 REPEAT 3362 3373 BNR 16.
 METAL 2060 2060 Zinc 1 (By similarity).
 METAL 2073 2073 Zinc 1 (By similarity).
 METAL 2178 2178 Zinc 1 (By similarity).
 METAL 2263 2263 Zinc 1 (By similarity).
 METAL 2396 2396 Zinc 2 (By similarity).
 METAL 2398 2398 Zinc 2 (By similarity).
 METAL 2459 2459 Zinc 2 (By similarity).
 CARBOHYD 140 140 N-linked (GlcNAc...) (Potential).
 CARBOHYD 257 257 N-linked (GlcNAc...) (Potential).
 CARBOHYD 289 289 N-linked (GlcNAc...) (Potential).
 CARBOHYD 305 305 N-linked (GlcNAc...).
 CARBOHYD 628 628 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1266 1266 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1599 1599 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1749 1749 N-linked (GlcNAc...) (Potential).
 CARBOHYD 1920 1920 N-linked (GlcNAc...).
 CARBOHYD 2144 2144 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2268 2268 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2316 2316 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2568 2568 N-linked (GlcNAc...) (Potential).
 CARBOHYD 2961 2961 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3015 3015 N-linked (GlcNAc...).
 CARBOHYD 3072 3072 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3184 3184 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3411 3411 N-linked (GlcNAc...) (Potential).
 CARBOHYD 3438 3438 N-linked (GlcNAc...) (Potential).
 DISULFID 40 126 By similarity.
 DISULFID 154 178 By similarity.
 DISULFID 539 580 By similarity.
 DISULFID 608 613 By similarity.
 DISULFID 674 684 By similarity.
 DISULFID 691 700 By similarity.
 DISULFID 894 936 By similarity.
 DISULFID 967 974 By similarity.
 DISULFID 1033 1043 By similarity.
 DISULFID 1050 1059 By similarity.
 DISULFID 1270 1309 By similarity.
 DISULFID 1338 1347 By similarity.
 DISULFID 1632 1672 By similarity.
 DISULFID 1701 1708 By similarity.
 DISULFID 2132 2142 By similarity.
 DISULFID 2136 2148 By similarity.
 DISULFID 2150 2159 By similarity.
 DISULFID 2194 2234 By similarity.
 DISULFID 2347 2386 By similarity.
 DISULFID 2392 2558 By similarity.
 DISULFID 2543 2583 By similarity.
 DISULFID 2793 2800 By similarity.
 DISULFID 2856 2866 By similarity.
 DISULFID 2860 2871 By similarity.
 DISULFID 2873 2882 By similarity.
 DISULFID 2918 2965 By similarity.
 DISULFID 3159 3169 By similarity.
 DISULFID 3231 3241 By similarity.
 DISULFID 3235 3247 By similarity.
 DISULFID 3249 3258 By similarity.
 DISULFID 3295 3345 By similarity.  
Keyword
 Alternative splicing; Calcium; Cell adhesion; Complete proteome; Developmental protein; Disulfide bond; EGF-like domain; Extracellular matrix; Glycoprotein; Hydrolase; Lissencephaly; Metal-binding; Polymorphism; Protease; Reference proteome; Repeat; Secreted; Serine protease; Signal; Zinc. 
Sequence Source
 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 
Protein Length
 3460 AA 
Protein Sequence
MERSGWARQT FLLALLLGAT LRARAAAGYY PRFSPFFFLC THHGELEGDG EQGEVLISLH 60
IAGNPTYYVP GQEYHVTIST STFFDGLLVT GLYTSTSVQA SQSIGGSSAF GFGIMSDHQF 120
GNQFMCSVVA SHVSHLPTTN LSFIWIAPPA GTGCVNFMAT ATHRGQVIFK DALAQQLCEQ 180
GAPTDVTVHP HLAEIHSDSI ILRDDFDSYH QLQLNPNIWV ECNNCETGEQ CGAIMHGNAV 240
TFCEPYGPRE LITTGLNTTT ASVLQFSIGS GSCRFSYSDP SIIVLYAKNN SADWIQLEKI 300
RAPSNVSTII HILYLPEDAK GENVQFQWKQ ENLRVGEVYE ACWALDNILI INSAHRQVVL 360
EDSLDPVDTG NWLFFPGATV KHSCQSDGNS IYFHGNEGSE FNFATTRDVD LSTEDIQEQW 420
SEEFESQPTG WDVLGAVIGT ECGTIESGLS MVFLKDGERK LCTPSMDTTG YGNLRFYFVM 480
GGICDPGNSH ENDIILYAKI EGRKEHITLD TLSYSSYKVP SLVSVVINPE LQTPATKFCL 540
RQKNHQGHNR NVWAVDFFHV LPVLPSTMSH MIQFSINLGC GTHQPGNSVS LEFSTNHGRS 600
WSLLHTECLP EICAGPHLPH STVYSSENYS GWNRITIPLP NAALTRNTRI RWRQTGPILG 660
NMWAIDNVYI GPSCLKFCSG RGQCTRHGCK CDPGFSGPAC EMASQTFPMF ISESFGSSRL 720
SSYHNFYSIR GAEVSFGCGV LASGKALVFN KDGRRQLITS FLDSSQSRFL QFTLRLGSKS 780
VLSTCRAPDQ PGEGVLLHYS YDNGITWKLL EHYSYLSYHE PRIISVELPG DAKQFGIQFR 840
WWQPYHSSQR EDVWAIDEII MTSVLFNSIS LDFTNLVEVT QSLGFYLGNV QPYCGHDWTL 900
CFTGDSKLAS SMRYVETQSM QIGASYMIQF SLVMGCGQKY TPHMDNQVKL EYSTNHGLTW 960
HLVQEECLPS MPSCQEFTSA SIYHASEFTQ WRRVIVLLPQ KTWSSATRFR WSQSYYTAQD 1020
EWALDSIYIG QQCPNMCSGH GSCDHGICRC DQGYQGTECH PEAALPSTIM SDFENQNGWE 1080
SDWQEVIGGE IVKPEQGCGV ISSGSSLYFS KAGKRQLVSW DLDTSWVDFV QFYIQIGGES 1140
ASCNKPDSRE EGVLLQYSNN GGIQWHLLAE MYFSDFSKPR FVYLELPAAA KTPCTRFRWW 1200
QPVFSGEDYD QWAVDDIIIL SEKQKQIIPV INPTLPQNFY EKPAFDYPMN QMSVWLMLAN 1260
EGMVKNETFC AATPSAMIFG KSDGDRFAVT RDLTLKPGYV LQFKLNIGCA NQFSSTAPVL 1320
LQYSHDAGMS WFLVKEGCYP ASAGKGCEGN SRELSEPTMY HTGDFEEWTR ITIVIPRSLA 1380
SSKTRFRWIQ ESSSQKNVPP FGLDGVYISE PCPSYCSGHG DCISGVCFCD LGYTAAQGTC 1440
VSNVPNHNEM FDRFEGKLSP LWYKITGAQV GTGCGTLNDG KSLYFNGPGK REARTVPLDT 1500
RNIRLVQFYI QIGSKTSGIT CIKPRTRNEG LIVQYSNDNG ILWHLLRELD FMSFLEPQII 1560
SIDLPQDAKT PATAFRWWQP QHGKHSAQWA LDDVLIGMND SSQTGFQDKF DGSIDLQANW 1620
YRIQGGQVDI DCLSMDTALI FTENIGKPRY AETWDFHVSA STFLQFEMSM GCSKPFSNSH 1680
SVQLQYSLNN GKDWHLVTEE CVPPTIGCLH YTESSIYTSE RFQNWKRITV YLPLSTISPR 1740
TRFRWIQANY TVGADSWAID NVVLASGCPW MCSGRGICDA GRCVCDRGFG GPYCVPVVPL 1800
PSILKDDFNG NLHPDLWPEV YGAERGNLNG ETIKSGTSLI FKGEGLRMLI SRDLDCTNTM 1860
YVQFSLRFIA KSTPERSHSI LLQFSISGGI TWHLMDEFYF PQTTNILFIN VPLPYTAQTN 1920
ATRFRLWQPY NNGKKEEIWI VDDFIIDGNN VNNPVMLLDT FDFGPREDNW FFYPGGNIGL 1980
YCPYSSKGAP EEDSAMVFVS NEVGEHSITT RDLNVNENTI IQFEINVGCS TDSSSADPVR 2040
LEFSRDFGAT WHLLLPLCYH SSSHVSSLCS TEHHPSSTYY AGTMQGWRRE VVHFGKLHLC 2100
GSVRFRWYQG FYPAGSQPVT WAIDNVYIGP QCEEMCNGQG SCINGTKCIC DPGYSGPTCK 2160
ISTKNPDFLK DDFEGQLESD RFLLMSGGKP SRKCGILSSG NNLFFNEDGL RMLMTRDLDL 2220
SHARFVQFFM RLGCGKGVPD PRSQPVLLQY SLNGGLSWSL LQEFLFSNSS NVGRYIALEI 2280
PLKARSGSTR LRWWQPSENG HFYSPWVIDQ ILIGGNISGN TVLEDDFTTL DSRKWLLHPG 2340
GTKMPVCGST GDALVFIEKA STRYVVSTDV AVNEDSFLQI DFAASCSVTD SCYAIELEYS 2400
VDLGLSWHPL VRDCLPTNVE CSRYHLQRIL VSDTFNKWTR ITLPLPPYTR SQATRFRWHQ 2460
PAPFDKQQTW AIDNVYIGDG CIDMCSGHGR CIQGNCVCDE QWGGLYCDDP ETSLPTQLKD 2520
NFNRAPSSQN WLTVNGGKLS TVCGAVASGM ALHFSGGCSR LLVTVDLNLT NAEFIQFYFM 2580
YGCLITPNNR NQGVLLEYSV NGGITWNLLM EIFYDQYSKP GFVNILLPPD AKEIATRFRW 2640
WQPRHDGLDQ NDWAIDNVLI SGSADQRTVM LDTFSSAPVP QHERSPADAG PVGRIAFDMF 2700
MEDKTSVNEH WLFHDDCTVE RFCDSPDGVM LCGSHDGREV YAVTHDLTPT EGWIMQFKIS 2760
VGCKVSEKIA QNQIHVQYST DFGVSWNYLV PQCLPADPKC SGSVSQPSVF FPTKGWKRIT 2820
YPLPESLVGN PVRFRFYQKY SDMQWAIDNF YLGPGCLDNC RGHGDCLREQ CICDPGYSGP 2880
NCYLTHTLKT FLKERFDSEE IKPDLWMSLE GGSTCTECGI LAEDTALYFG GSTVRQAVTQ 2940
DLDLRGAKFL QYWGRIGSEN NMTSCHRPIC RKEGVLLDYS TDGGITWTLL HEMDYQKYIS 3000
VRHDYILLPE DALTNTTRLR WWQPFVISNG IVVSGVERAQ WALDNILIGG AEINPSQLVD 3060
TFDDEGTSHE ENWSFYPNAV RTAGFCGNPS FHLYWPNKKK DKTHNALSSR ELIIQPGYMM 3120
QFKIVVGCEA TSCGDLHSVM LEYTKDARSD SWQLVQTQCL PSSSNSIGCS PFQFHEATIY 3180
NSVNSSSWKR ITIQLPDHVS SSATQFRWIQ KGEETEKQSW AIDHVYIGEA CPKLCSGHGY 3240
CTTGAICICD ESFQGDDCSV FSHDLPSYIK DNFESARVTE ANWETIQGGV IGSGCGQLAP 3300
YAHGDSLYFN GCQIRQAATK PLDLTRASKI MFVLQIGSMS QTDSCNSDLS GPHAVDKAVL 3360
LQYSVNNGIT WHVIAQHQPK DFTQAQRVSY NVPLEARMKG VLLRWWQPRH NGTGHDQWAL 3420
DHVEVVLVST RKQNYMMNFS RQHGLRHFYN RRRRSLRRYP 3460 
Gene Ontology
 GO:0005737; C:cytoplasm; ISS:UniProtKB.
 GO:0030425; C:dendrite; ISS:UniProtKB.
 GO:0005615; C:extracellular space; ISS:UniProtKB.
 GO:0005578; C:proteinaceous extracellular matrix; IEA:UniProtKB-SubCell.
 GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
 GO:0004712; F:protein serine/threonine/tyrosine kinase activity; ISS:UniProtKB.
 GO:0008236; F:serine-type peptidase activity; IEA:UniProtKB-KW.
 GO:0070326; F:very-low-density lipoprotein particle receptor binding; ISS:BHF-UCL.
 GO:0008306; P:associative learning; IEA:Compara.
 GO:0007411; P:axon guidance; ISS:UniProtKB.
 GO:0007155; P:cell adhesion; IEA:UniProtKB-KW.
 GO:0021800; P:cerebral cortex tangential migration; ISS:UniProtKB.
 GO:0016358; P:dendrite development; IEA:Compara.
 GO:0010001; P:glial cell differentiation; ISS:UniProtKB.
 GO:0021766; P:hippocampus development; ISS:BHF-UCL.
 GO:0007616; P:long-term memory; IEA:Compara.
 GO:0097114; P:N-methyl-D-aspartate receptor clustering; IEA:Compara.
 GO:0001764; P:neuron migration; ISS:UniProtKB.
 GO:0018108; P:peptidyl-tyrosine phosphorylation; ISS:UniProtKB.
 GO:2000969; P:positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity; ISS:BHF-UCL.
 GO:0032793; P:positive regulation of CREB transcription factor activity; ISS:BHF-UCL.
 GO:0061003; P:positive regulation of dendritic spine morphogenesis; ISS:BHF-UCL.
 GO:2000463; P:positive regulation of excitatory postsynaptic membrane potential; ISS:BHF-UCL.
 GO:1900273; P:positive regulation of long-term synaptic potentiation; ISS:BHF-UCL.
 GO:0010976; P:positive regulation of neuron projection development; ISS:BHF-UCL.
 GO:0014068; P:positive regulation of phosphatidylinositol 3-kinase cascade; IEA:Compara.
 GO:0061098; P:positive regulation of protein tyrosine kinase activity; ISS:BHF-UCL.
 GO:0051057; P:positive regulation of small GTPase mediated signal transduction; ISS:UniProtKB.
 GO:0090129; P:positive regulation of synapse maturation; ISS:BHF-UCL.
 GO:0051968; P:positive regulation of synaptic transmission, glutamatergic; ISS:BHF-UCL.
 GO:0032008; P:positive regulation of TOR signaling cascade; IEA:Compara.
 GO:0097119; P:postsynaptic density protein 95 clustering; IEA:Compara.
 GO:0006508; P:proteolysis; IEA:UniProtKB-KW.
 GO:0097120; P:receptor localization to synapse; IEA:Compara.
 GO:0038026; P:reelin-mediated signaling pathway; ISS:BHF-UCL.
 GO:0050795; P:regulation of behavior; ISS:BHF-UCL.
 GO:2000310; P:regulation of N-methyl-D-aspartate selective glutamate receptor activity; ISS:BHF-UCL.
 GO:0048265; P:response to pain; ISS:UniProtKB.
 GO:0021511; P:spinal cord patterning; ISS:UniProtKB.
 GO:0021517; P:ventral spinal cord development; IEA:Compara. 
Interpro
 IPR000742; EG-like_dom.
 IPR013032; EGF-like_CS.
 IPR002861; Reeler_dom.
 IPR011040; Sialidases. 
Pfam
 PF02014; Reeler 
SMART
 SM00181; EGF 
PROSITE
 PS00022; EGF_1
 PS01186; EGF_2
 PS50026; EGF_3
 PS51019; REELIN 
PRINTS