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P78509

- RELN_HUMAN

UniProt

P78509 - RELN_HUMAN

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Protein

Reelin

Gene

RELN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.By similarity

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi2060 – 20601Zinc 1By similarity
Metal bindingi2073 – 20731Zinc 1By similarity
Metal bindingi2178 – 21781Zinc 1By similarity
Metal bindingi2263 – 22631Zinc 1By similarity
Metal bindingi2396 – 23961Zinc 2By similarity
Metal bindingi2398 – 23981Zinc 2By similarity
Metal bindingi2459 – 24591Zinc 2By similarity

GO - Molecular functioni

  1. lipoprotein particle receptor binding Source: BHF-UCL
  2. metal ion binding Source: UniProtKB-KW
  3. protein serine/threonine/tyrosine kinase activity Source: UniProtKB
  4. serine-type peptidase activity Source: UniProtKB-KW
  5. very-low-density lipoprotein particle receptor binding Source: BHF-UCL

GO - Biological processi

  1. associative learning Source: Ensembl
  2. axon guidance Source: UniProtKB
  3. brain development Source: UniProtKB
  4. cell adhesion Source: UniProtKB-KW
  5. cell morphogenesis involved in differentiation Source: UniProtKB
  6. central nervous system development Source: UniProtKB
  7. cerebral cortex tangential migration Source: UniProtKB
  8. dendrite development Source: Ensembl
  9. glial cell differentiation Source: UniProtKB
  10. hippocampus development Source: BHF-UCL
  11. lateral motor column neuron migration Source: Ensembl
  12. layer formation in cerebral cortex Source: Ensembl
  13. long-term memory Source: Ensembl
  14. neuron migration Source: UniProtKB
  15. N-methyl-D-aspartate receptor clustering Source: Ensembl
  16. peptidyl-tyrosine phosphorylation Source: UniProtKB
  17. positive regulation of alpha-amino-3-hydroxy-5-methyl-4-isoxazole propionate selective glutamate receptor activity Source: BHF-UCL
  18. positive regulation of CREB transcription factor activity Source: BHF-UCL
  19. positive regulation of dendritic spine morphogenesis Source: BHF-UCL
  20. positive regulation of excitatory postsynaptic membrane potential Source: BHF-UCL
  21. positive regulation of lateral motor column neuron migration Source: Ensembl
  22. positive regulation of long-term synaptic potentiation Source: BHF-UCL
  23. positive regulation of neuron projection development Source: BHF-UCL
  24. positive regulation of peptidyl-tyrosine phosphorylation Source: BHF-UCL
  25. positive regulation of phosphatidylinositol 3-kinase signaling Source: Ensembl
  26. positive regulation of protein kinase activity Source: UniProtKB
  27. positive regulation of protein tyrosine kinase activity Source: BHF-UCL
  28. positive regulation of small GTPase mediated signal transduction Source: UniProtKB
  29. positive regulation of synapse maturation Source: BHF-UCL
  30. positive regulation of synaptic transmission, glutamatergic Source: BHF-UCL
  31. positive regulation of TOR signaling Source: Ensembl
  32. postsynaptic density protein 95 clustering Source: Ensembl
  33. receptor localization to synapse Source: Ensembl
  34. reelin-mediated signaling pathway Source: BHF-UCL
  35. regulation of behavior Source: BHF-UCL
  36. regulation of N-methyl-D-aspartate selective glutamate receptor activity Source: BHF-UCL
  37. regulation of synaptic transmission Source: BHF-UCL
  38. response to pain Source: UniProtKB
  39. spinal cord patterning Source: UniProtKB
  40. ventral spinal cord development Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein, Hydrolase, Protease, Serine protease

Keywords - Biological processi

Cell adhesion

Keywords - Ligandi

Calcium, Metal-binding, Zinc

Names & Taxonomyi

Protein namesi
Recommended name:
Reelin (EC:3.4.21.-)
Gene namesi
Name:RELN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:9957. RELN.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. dendrite Source: UniProtKB
  3. extracellular space Source: UniProtKB
  4. proteinaceous extracellular matrix Source: UniProtKB-KW
Complete GO annotation...

Keywords - Cellular componenti

Extracellular matrix, Secreted

Pathology & Biotechi

Involvement in diseasei

Lissencephaly 2 (LIS2) [MIM:257320]: A classic type lissencephaly associated with ataxia, mental retardation, seizures and abnormalities of the cerebellum, hippocampus and brainstem.1 Publication
Note: The disease is caused by mutations affecting the gene represented in this entry.

Keywords - Diseasei

Lissencephaly

Organism-specific databases

MIMi257320. phenotype.
Orphaneti89844. Lissencephaly syndrome, Norman-Roberts type.
PharmGKBiPA34323.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Signal peptidei1 – 2525Sequence AnalysisAdd
BLAST
Chaini26 – 34603435ReelinPRO_0000030304Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Disulfide bondi40 ↔ 126PROSITE-ProRule annotation
Glycosylationi140 – 1401N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi154 ↔ 178PROSITE-ProRule annotation
Glycosylationi257 – 2571N-linked (GlcNAc...)Sequence Analysis
Glycosylationi289 – 2891N-linked (GlcNAc...)Sequence Analysis
Glycosylationi305 – 3051N-linked (GlcNAc...)1 Publication
Disulfide bondi539 ↔ 580PROSITE-ProRule annotation
Disulfide bondi608 ↔ 613PROSITE-ProRule annotation
Glycosylationi628 – 6281N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi674 ↔ 684PROSITE-ProRule annotation
Disulfide bondi691 ↔ 700PROSITE-ProRule annotation
Disulfide bondi894 ↔ 936PROSITE-ProRule annotation
Disulfide bondi967 ↔ 974PROSITE-ProRule annotation
Disulfide bondi1033 ↔ 1043PROSITE-ProRule annotation
Disulfide bondi1050 ↔ 1059PROSITE-ProRule annotation
Glycosylationi1266 – 12661N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1270 ↔ 1309PROSITE-ProRule annotation
Disulfide bondi1338 ↔ 1347PROSITE-ProRule annotation
Glycosylationi1599 – 15991N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi1632 ↔ 1672PROSITE-ProRule annotation
Disulfide bondi1701 ↔ 1708PROSITE-ProRule annotation
Glycosylationi1749 – 17491N-linked (GlcNAc...)Sequence Analysis
Glycosylationi1920 – 19201N-linked (GlcNAc...)1 Publication
Disulfide bondi2100 – 2100InterchainPROSITE-ProRule annotation
Disulfide bondi2132 ↔ 2142PROSITE-ProRule annotation
Disulfide bondi2136 ↔ 2148PROSITE-ProRule annotation
Glycosylationi2144 – 21441N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2150 ↔ 2159PROSITE-ProRule annotation
Disulfide bondi2194 ↔ 2234PROSITE-ProRule annotation
Glycosylationi2268 – 22681N-linked (GlcNAc...)Sequence Analysis
Glycosylationi2316 – 23161N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2347 ↔ 2386PROSITE-ProRule annotation
Disulfide bondi2392 ↔ 2558PROSITE-ProRule annotation
Disulfide bondi2543 ↔ 2583PROSITE-ProRule annotation
Glycosylationi2568 – 25681N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi2793 ↔ 2800PROSITE-ProRule annotation
Disulfide bondi2856 ↔ 2866PROSITE-ProRule annotation
Disulfide bondi2860 ↔ 2871PROSITE-ProRule annotation
Disulfide bondi2873 ↔ 2882PROSITE-ProRule annotation
Disulfide bondi2918 ↔ 2965PROSITE-ProRule annotation
Glycosylationi2961 – 29611N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3015 – 30151N-linked (GlcNAc...)1 Publication
Glycosylationi3072 – 30721N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3159 ↔ 3169PROSITE-ProRule annotation
Glycosylationi3184 – 31841N-linked (GlcNAc...)Sequence Analysis
Disulfide bondi3231 ↔ 3241PROSITE-ProRule annotation
Disulfide bondi3235 ↔ 3247PROSITE-ProRule annotation
Disulfide bondi3249 ↔ 3258PROSITE-ProRule annotation
Disulfide bondi3295 ↔ 3345PROSITE-ProRule annotation
Glycosylationi3411 – 34111N-linked (GlcNAc...)Sequence Analysis
Glycosylationi3438 – 34381N-linked (GlcNAc...)Sequence Analysis

Keywords - PTMi

Disulfide bond, Glycoprotein

Proteomic databases

MaxQBiP78509.
PaxDbiP78509.
PRIDEiP78509.

PTM databases

PhosphoSiteiP78509.

Expressioni

Tissue specificityi

Abundantly produced during brain ontogenesis by the Cajal-Retzius cells and other pioneer neurons located in the telencephalic marginal zone and by granule cells of the external granular layer of the cerebellum. In adult brain, preferentially expressed in GABAergic interneurons of prefrontal cortices, temporal cortex, hippocampus and glutamatergic granule cells of cerebellum. Expression is reduced to about 50% in patients with schizophrenia. Also expressed in fetal and adult liver.1 Publication

Developmental stagei

Expressed in fetal and postnatal brain and liver. Expression in postnatal human brain is high in the cerebellum.

Gene expression databases

BgeeiP78509.
CleanExiHS_RELN.
ExpressionAtlasiP78509. baseline and differential.
GenevestigatoriP78509.

Organism-specific databases

HPAiCAB004556.

Interactioni

Subunit structurei

Oligomer of disulfide-linked homodimers. Binds to the ectodomains of VLDLR and LRP8/APOER2 By similarity.By similarity

Protein-protein interaction databases

BioGridi111630. 5 interactions.
MINTiMINT-155986.
STRINGi9606.ENSP00000392423.

Structurei

3D structure databases

ProteinModelPortaliP78509.
SMRiP78509. Positions 1293-1596, 1955-2661.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini26 – 190165ReelinPROSITE-ProRule annotationAdd
BLAST
Repeati592 – 60312BNR 1Add
BLAST
Domaini670 – 70132EGF-like 1PROSITE-ProRule annotationAdd
BLAST
Repeati798 – 80912BNR 2Add
BLAST
Repeati951 – 96212BNR 3Add
BLAST
Domaini1029 – 106032EGF-like 2PROSITE-ProRule annotationAdd
BLAST
Repeati1156 – 116712BNR 4Add
BLAST
Repeati1322 – 133312BNR 5Add
BLAST
Domaini1408 – 144134EGF-like 3PROSITE-ProRule annotationAdd
BLAST
Repeati1534 – 154512BNR 6Add
BLAST
Repeati1685 – 169612BNR 7Add
BLAST
Domaini1764 – 179532EGF-like 4PROSITE-ProRule annotationAdd
BLAST
Repeati1883 – 189412BNR 8Add
BLAST
Repeati2042 – 205312BNR 9Add
BLAST
Domaini2128 – 216033EGF-like 5PROSITE-ProRule annotationAdd
BLAST
Repeati2249 – 226012BNR 10Add
BLAST
Repeati2398 – 240912BNR 11Add
BLAST
Domaini2477 – 250832EGF-like 6PROSITE-ProRule annotationAdd
BLAST
Repeati2597 – 260812BNR 12Add
BLAST
Repeati2777 – 278812BNR 13Add
BLAST
Domaini2852 – 288332EGF-like 7PROSITE-ProRule annotationAdd
BLAST
Repeati2978 – 298912BNR 14Add
BLAST
Repeati3142 – 315413BNR 15Add
BLAST
Domaini3227 – 325933EGF-like 8PROSITE-ProRule annotationAdd
BLAST
Repeati3362 – 337312BNR 16Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi3431 – 346030Arg-rich (basic)Add
BLAST

Domaini

The basic C-terminal region is essential for secretion.By similarity

Sequence similaritiesi

Belongs to the reelin family.Curated
Contains 16 BNR repeats.Curated
Contains 8 EGF-like domains.PROSITE-ProRule annotation
Contains 1 reelin domain.PROSITE-ProRule annotation

Keywords - Domaini

EGF-like domain, Repeat, Signal

Phylogenomic databases

eggNOGiNOG45680.
GeneTreeiENSGT00580000081623.
HOVERGENiHBG023117.
InParanoidiP78509.
KOiK06249.
OMAiNWFFYPG.
OrthoDBiEOG7P2XR4.
PhylomeDBiP78509.
TreeFamiTF106479.

Family and domain databases

Gene3Di2.120.10.10. 2 hits.
InterProiIPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002861. Reeler_dom.
IPR011040. Sialidases.
[Graphical view]
PfamiPF12661. hEGF. 2 hits.
PF02014. Reeler. 1 hit.
[Graphical view]
SMARTiSM00181. EGF. 5 hits.
[Graphical view]
SUPFAMiSSF50939. SSF50939. 17 hits.
PROSITEiPS00022. EGF_1. 7 hits.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 5 hits.
PS51019. REELIN. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P78509-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MERSGWARQT FLLALLLGAT LRARAAAGYY PRFSPFFFLC THHGELEGDG
60 70 80 90 100
EQGEVLISLH IAGNPTYYVP GQEYHVTIST STFFDGLLVT GLYTSTSVQA
110 120 130 140 150
SQSIGGSSAF GFGIMSDHQF GNQFMCSVVA SHVSHLPTTN LSFIWIAPPA
160 170 180 190 200
GTGCVNFMAT ATHRGQVIFK DALAQQLCEQ GAPTDVTVHP HLAEIHSDSI
210 220 230 240 250
ILRDDFDSYH QLQLNPNIWV ECNNCETGEQ CGAIMHGNAV TFCEPYGPRE
260 270 280 290 300
LITTGLNTTT ASVLQFSIGS GSCRFSYSDP SIIVLYAKNN SADWIQLEKI
310 320 330 340 350
RAPSNVSTII HILYLPEDAK GENVQFQWKQ ENLRVGEVYE ACWALDNILI
360 370 380 390 400
INSAHRQVVL EDSLDPVDTG NWLFFPGATV KHSCQSDGNS IYFHGNEGSE
410 420 430 440 450
FNFATTRDVD LSTEDIQEQW SEEFESQPTG WDVLGAVIGT ECGTIESGLS
460 470 480 490 500
MVFLKDGERK LCTPSMDTTG YGNLRFYFVM GGICDPGNSH ENDIILYAKI
510 520 530 540 550
EGRKEHITLD TLSYSSYKVP SLVSVVINPE LQTPATKFCL RQKNHQGHNR
560 570 580 590 600
NVWAVDFFHV LPVLPSTMSH MIQFSINLGC GTHQPGNSVS LEFSTNHGRS
610 620 630 640 650
WSLLHTECLP EICAGPHLPH STVYSSENYS GWNRITIPLP NAALTRNTRI
660 670 680 690 700
RWRQTGPILG NMWAIDNVYI GPSCLKFCSG RGQCTRHGCK CDPGFSGPAC
710 720 730 740 750
EMASQTFPMF ISESFGSSRL SSYHNFYSIR GAEVSFGCGV LASGKALVFN
760 770 780 790 800
KDGRRQLITS FLDSSQSRFL QFTLRLGSKS VLSTCRAPDQ PGEGVLLHYS
810 820 830 840 850
YDNGITWKLL EHYSYLSYHE PRIISVELPG DAKQFGIQFR WWQPYHSSQR
860 870 880 890 900
EDVWAIDEII MTSVLFNSIS LDFTNLVEVT QSLGFYLGNV QPYCGHDWTL
910 920 930 940 950
CFTGDSKLAS SMRYVETQSM QIGASYMIQF SLVMGCGQKY TPHMDNQVKL
960 970 980 990 1000
EYSTNHGLTW HLVQEECLPS MPSCQEFTSA SIYHASEFTQ WRRVIVLLPQ
1010 1020 1030 1040 1050
KTWSSATRFR WSQSYYTAQD EWALDSIYIG QQCPNMCSGH GSCDHGICRC
1060 1070 1080 1090 1100
DQGYQGTECH PEAALPSTIM SDFENQNGWE SDWQEVIGGE IVKPEQGCGV
1110 1120 1130 1140 1150
ISSGSSLYFS KAGKRQLVSW DLDTSWVDFV QFYIQIGGES ASCNKPDSRE
1160 1170 1180 1190 1200
EGVLLQYSNN GGIQWHLLAE MYFSDFSKPR FVYLELPAAA KTPCTRFRWW
1210 1220 1230 1240 1250
QPVFSGEDYD QWAVDDIIIL SEKQKQIIPV INPTLPQNFY EKPAFDYPMN
1260 1270 1280 1290 1300
QMSVWLMLAN EGMVKNETFC AATPSAMIFG KSDGDRFAVT RDLTLKPGYV
1310 1320 1330 1340 1350
LQFKLNIGCA NQFSSTAPVL LQYSHDAGMS WFLVKEGCYP ASAGKGCEGN
1360 1370 1380 1390 1400
SRELSEPTMY HTGDFEEWTR ITIVIPRSLA SSKTRFRWIQ ESSSQKNVPP
1410 1420 1430 1440 1450
FGLDGVYISE PCPSYCSGHG DCISGVCFCD LGYTAAQGTC VSNVPNHNEM
1460 1470 1480 1490 1500
FDRFEGKLSP LWYKITGAQV GTGCGTLNDG KSLYFNGPGK REARTVPLDT
1510 1520 1530 1540 1550
RNIRLVQFYI QIGSKTSGIT CIKPRTRNEG LIVQYSNDNG ILWHLLRELD
1560 1570 1580 1590 1600
FMSFLEPQII SIDLPQDAKT PATAFRWWQP QHGKHSAQWA LDDVLIGMND
1610 1620 1630 1640 1650
SSQTGFQDKF DGSIDLQANW YRIQGGQVDI DCLSMDTALI FTENIGKPRY
1660 1670 1680 1690 1700
AETWDFHVSA STFLQFEMSM GCSKPFSNSH SVQLQYSLNN GKDWHLVTEE
1710 1720 1730 1740 1750
CVPPTIGCLH YTESSIYTSE RFQNWKRITV YLPLSTISPR TRFRWIQANY
1760 1770 1780 1790 1800
TVGADSWAID NVVLASGCPW MCSGRGICDA GRCVCDRGFG GPYCVPVVPL
1810 1820 1830 1840 1850
PSILKDDFNG NLHPDLWPEV YGAERGNLNG ETIKSGTSLI FKGEGLRMLI
1860 1870 1880 1890 1900
SRDLDCTNTM YVQFSLRFIA KSTPERSHSI LLQFSISGGI TWHLMDEFYF
1910 1920 1930 1940 1950
PQTTNILFIN VPLPYTAQTN ATRFRLWQPY NNGKKEEIWI VDDFIIDGNN
1960 1970 1980 1990 2000
VNNPVMLLDT FDFGPREDNW FFYPGGNIGL YCPYSSKGAP EEDSAMVFVS
2010 2020 2030 2040 2050
NEVGEHSITT RDLNVNENTI IQFEINVGCS TDSSSADPVR LEFSRDFGAT
2060 2070 2080 2090 2100
WHLLLPLCYH SSSHVSSLCS TEHHPSSTYY AGTMQGWRRE VVHFGKLHLC
2110 2120 2130 2140 2150
GSVRFRWYQG FYPAGSQPVT WAIDNVYIGP QCEEMCNGQG SCINGTKCIC
2160 2170 2180 2190 2200
DPGYSGPTCK ISTKNPDFLK DDFEGQLESD RFLLMSGGKP SRKCGILSSG
2210 2220 2230 2240 2250
NNLFFNEDGL RMLMTRDLDL SHARFVQFFM RLGCGKGVPD PRSQPVLLQY
2260 2270 2280 2290 2300
SLNGGLSWSL LQEFLFSNSS NVGRYIALEI PLKARSGSTR LRWWQPSENG
2310 2320 2330 2340 2350
HFYSPWVIDQ ILIGGNISGN TVLEDDFTTL DSRKWLLHPG GTKMPVCGST
2360 2370 2380 2390 2400
GDALVFIEKA STRYVVSTDV AVNEDSFLQI DFAASCSVTD SCYAIELEYS
2410 2420 2430 2440 2450
VDLGLSWHPL VRDCLPTNVE CSRYHLQRIL VSDTFNKWTR ITLPLPPYTR
2460 2470 2480 2490 2500
SQATRFRWHQ PAPFDKQQTW AIDNVYIGDG CIDMCSGHGR CIQGNCVCDE
2510 2520 2530 2540 2550
QWGGLYCDDP ETSLPTQLKD NFNRAPSSQN WLTVNGGKLS TVCGAVASGM
2560 2570 2580 2590 2600
ALHFSGGCSR LLVTVDLNLT NAEFIQFYFM YGCLITPNNR NQGVLLEYSV
2610 2620 2630 2640 2650
NGGITWNLLM EIFYDQYSKP GFVNILLPPD AKEIATRFRW WQPRHDGLDQ
2660 2670 2680 2690 2700
NDWAIDNVLI SGSADQRTVM LDTFSSAPVP QHERSPADAG PVGRIAFDMF
2710 2720 2730 2740 2750
MEDKTSVNEH WLFHDDCTVE RFCDSPDGVM LCGSHDGREV YAVTHDLTPT
2760 2770 2780 2790 2800
EGWIMQFKIS VGCKVSEKIA QNQIHVQYST DFGVSWNYLV PQCLPADPKC
2810 2820 2830 2840 2850
SGSVSQPSVF FPTKGWKRIT YPLPESLVGN PVRFRFYQKY SDMQWAIDNF
2860 2870 2880 2890 2900
YLGPGCLDNC RGHGDCLREQ CICDPGYSGP NCYLTHTLKT FLKERFDSEE
2910 2920 2930 2940 2950
IKPDLWMSLE GGSTCTECGI LAEDTALYFG GSTVRQAVTQ DLDLRGAKFL
2960 2970 2980 2990 3000
QYWGRIGSEN NMTSCHRPIC RKEGVLLDYS TDGGITWTLL HEMDYQKYIS
3010 3020 3030 3040 3050
VRHDYILLPE DALTNTTRLR WWQPFVISNG IVVSGVERAQ WALDNILIGG
3060 3070 3080 3090 3100
AEINPSQLVD TFDDEGTSHE ENWSFYPNAV RTAGFCGNPS FHLYWPNKKK
3110 3120 3130 3140 3150
DKTHNALSSR ELIIQPGYMM QFKIVVGCEA TSCGDLHSVM LEYTKDARSD
3160 3170 3180 3190 3200
SWQLVQTQCL PSSSNSIGCS PFQFHEATIY NSVNSSSWKR ITIQLPDHVS
3210 3220 3230 3240 3250
SSATQFRWIQ KGEETEKQSW AIDHVYIGEA CPKLCSGHGY CTTGAICICD
3260 3270 3280 3290 3300
ESFQGDDCSV FSHDLPSYIK DNFESARVTE ANWETIQGGV IGSGCGQLAP
3310 3320 3330 3340 3350
YAHGDSLYFN GCQIRQAATK PLDLTRASKI MFVLQIGSMS QTDSCNSDLS
3360 3370 3380 3390 3400
GPHAVDKAVL LQYSVNNGIT WHVIAQHQPK DFTQAQRVSY NVPLEARMKG
3410 3420 3430 3440 3450
VLLRWWQPRH NGTGHDQWAL DHVEVVLVST RKQNYMMNFS RQHGLRHFYN
3460
RRRRSLRRYP
Length:3,460
Mass (Da):388,388
Last modified:May 18, 2010 - v3
Checksum:i9A398EC17FA4EE1B
GO
Isoform 2 (identifier: P78509-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3428-3429: Missing.

Show »
Length:3,458
Mass (Da):388,201
Checksum:iA67B9EAF1DAE6F69
GO
Isoform 3 (identifier: P78509-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     3428-3460: Missing.

Show »
Length:3,427
Mass (Da):384,093
Checksum:iE9DF2AE0AC29DB8C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti752 – 7521D → E in AAC51105. (PubMed:9049633)Curated

Polymorphismi

A polymorphic GGC triplet repeat located in the 5'-UTR region of RELN gene, which harbors in the normal population 8 to 10 repeats, is significantly increased in autistic patients to carry 4 to 23 additional repeats.

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti978 – 9781T → A.
Corresponds to variant rs3025962 [ dbSNP | Ensembl ].
VAR_047977
Natural varianti997 – 9971L → V.
Corresponds to variant rs362691 [ dbSNP | Ensembl ].
VAR_047978
Natural varianti1703 – 17031P → R.
Corresponds to variant rs2229860 [ dbSNP | Ensembl ].
VAR_057712

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei3428 – 346033Missing in isoform 3. CuratedVSP_005576Add
BLAST
Alternative sequencei3428 – 34292Missing in isoform 2. CuratedVSP_005575

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U79716 mRNA. Translation: AAC51105.1.
AC002067 Genomic DNA. Translation: AAM49151.1.
AC006981 Genomic DNA. No translation available.
AC073208 Genomic DNA. Translation: AAP22355.1.
AC005101 Genomic DNA. Translation: AAP22330.1.
AC000121 Genomic DNA. Translation: AAB46357.2.
AC006316 Genomic DNA. Translation: AAD29127.1.
AC005064 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24410.1.
CH236947 Genomic DNA. Translation: EAL24411.1.
CCDSiCCDS34722.1. [P78509-2]
CCDS47680.1. [P78509-1]
RefSeqiNP_005036.2. NM_005045.3. [P78509-1]
NP_774959.1. NM_173054.2. [P78509-2]
UniGeneiHs.655654.

Genome annotation databases

EnsembliENST00000343529; ENSP00000345694; ENSG00000189056. [P78509-2]
ENST00000428762; ENSP00000392423; ENSG00000189056. [P78509-1]
GeneIDi5649.
KEGGihsa:5649.
UCSCiuc010liz.3. human. [P78509-2]
uc022ajq.1. human. [P78509-1]

Polymorphism databases

DMDMi296452988.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

Wikipedia

Reelin entry

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
U79716 mRNA. Translation: AAC51105.1 .
AC002067 Genomic DNA. Translation: AAM49151.1 .
AC006981 Genomic DNA. No translation available.
AC073208 Genomic DNA. Translation: AAP22355.1 .
AC005101 Genomic DNA. Translation: AAP22330.1 .
AC000121 Genomic DNA. Translation: AAB46357.2 .
AC006316 Genomic DNA. Translation: AAD29127.1 .
AC005064 Genomic DNA. No translation available.
CH236947 Genomic DNA. Translation: EAL24410.1 .
CH236947 Genomic DNA. Translation: EAL24411.1 .
CCDSi CCDS34722.1. [P78509-2 ]
CCDS47680.1. [P78509-1 ]
RefSeqi NP_005036.2. NM_005045.3. [P78509-1 ]
NP_774959.1. NM_173054.2. [P78509-2 ]
UniGenei Hs.655654.

3D structure databases

ProteinModelPortali P78509.
SMRi P78509. Positions 1293-1596, 1955-2661.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 111630. 5 interactions.
MINTi MINT-155986.
STRINGi 9606.ENSP00000392423.

PTM databases

PhosphoSitei P78509.

Polymorphism databases

DMDMi 296452988.

Proteomic databases

MaxQBi P78509.
PaxDbi P78509.
PRIDEi P78509.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000343529 ; ENSP00000345694 ; ENSG00000189056 . [P78509-2 ]
ENST00000428762 ; ENSP00000392423 ; ENSG00000189056 . [P78509-1 ]
GeneIDi 5649.
KEGGi hsa:5649.
UCSCi uc010liz.3. human. [P78509-2 ]
uc022ajq.1. human. [P78509-1 ]

Organism-specific databases

CTDi 5649.
GeneCardsi GC07M103112.
H-InvDB HIX0033998.
HIX0201200.
HGNCi HGNC:9957. RELN.
HPAi CAB004556.
MIMi 257320. phenotype.
600514. gene.
neXtProti NX_P78509.
Orphaneti 89844. Lissencephaly syndrome, Norman-Roberts type.
PharmGKBi PA34323.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG45680.
GeneTreei ENSGT00580000081623.
HOVERGENi HBG023117.
InParanoidi P78509.
KOi K06249.
OMAi NWFFYPG.
OrthoDBi EOG7P2XR4.
PhylomeDBi P78509.
TreeFami TF106479.

Miscellaneous databases

GeneWikii Reelin.
GenomeRNAii 5649.
NextBioi 21946.
PROi P78509.
SOURCEi Search...

Gene expression databases

Bgeei P78509.
CleanExi HS_RELN.
ExpressionAtlasi P78509. baseline and differential.
Genevestigatori P78509.

Family and domain databases

Gene3Di 2.120.10.10. 2 hits.
InterProi IPR000742. EG-like_dom.
IPR013032. EGF-like_CS.
IPR002861. Reeler_dom.
IPR011040. Sialidases.
[Graphical view ]
Pfami PF12661. hEGF. 2 hits.
PF02014. Reeler. 1 hit.
[Graphical view ]
SMARTi SM00181. EGF. 5 hits.
[Graphical view ]
SUPFAMi SSF50939. SSF50939. 17 hits.
PROSITEi PS00022. EGF_1. 7 hits.
PS01186. EGF_2. 6 hits.
PS50026. EGF_3. 5 hits.
PS51019. REELIN. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The human reelin gene: isolation, sequencing, and mapping on chromosome 7."
    DeSilva U., D'Arcangelo G., Braden V.V., Chen J., Miao G.G., Curran T., Green E.D.
    Genome Res. 7:157-164(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "Evolutionarily conserved, alternative splicing of reelin during brain development."
    Lambert de Rouvroit C., Bernier B., Royaux I., de Bergeyck V., Goffinet A.M.
    Exp. Neurol. 156:229-238(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: ALTERNATIVE SPLICING.
  5. Cited for: TISSUE SPECIFICITY.
  6. "Autosomal recessive lissencephaly with cerebellar hypoplasia is associated with human RELN mutations."
    Hong S.E., Shugart Y.Y., Huang D.T., Shahwan S.A., Grant P.E., Hourihane J.O.B., Martin N.D.T., Walsh C.A.
    Nat. Genet. 26:93-96(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN LIS2.
  7. Cited for: POLYMORPHISM.
  8. "Glycoproteomics analysis of human liver tissue by combination of multiple enzyme digestion and hydrazide chemistry."
    Chen R., Jiang X., Sun D., Han G., Wang F., Ye M., Wang L., Zou H.
    J. Proteome Res. 8:651-661(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION [LARGE SCALE ANALYSIS] AT ASN-305; ASN-1920 AND ASN-3015.
    Tissue: Liver.

Entry informationi

Entry nameiRELN_HUMAN
AccessioniPrimary (citable) accession number: P78509
Secondary accession number(s): A4D0P9
, A4D0Q0, Q86UJ0, Q86UJ8, Q8NDV0, Q9UDQ2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: March 27, 2002
Last sequence update: May 18, 2010
Last modified: October 29, 2014
This is version 143 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3