Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
reelin (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

Overview
reelin 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. Defects in RELN are the cause of lissencephaly type 2 (LIS2); also known as lissencephaly with cerebellar hypoplasia or Norman-Roberts syndrome. LIS2 is a classic type lissencephaly associated with abnormalities of the cerebellum, hippocampus and brainstem. Individuals with LIS2 are severely ataxic, mentally retarded and suffer from epilepsy. Belongs to the reelin family. 3 isoforms of the human protein are produced by alternative splicing. Note: This description may include information from UniProtKB.
Protein type: Protease; EC 3.4.21.-; Cell adhesion; Motility/polarity/chemotaxis; Secreted; Secreted, signal peptide; Cell development/differentiation
Cellular Component: extracellular space; proteinaceous extracellular matrix; dendrite; cytoplasm
Molecular Function: serine-type peptidase activity; metal ion binding; protein serine/threonine/tyrosine kinase activity
Biological Process: axon guidance; cellular morphogenesis during differentiation; peptidyl-tyrosine phosphorylation; central nervous system development; spinal cord patterning; neuron migration; response to pain; proteolysis; positive regulation of synaptic transmission, glutamatergic; glial cell differentiation; dendrite development; cell adhesion; positive regulation of TOR signaling pathway; associative learning; regulation of behavior; regulation of synaptic transmission; cerebral cortex tangential migration; hippocampus development; activation of CREB transcription factor; ventral spinal cord development; positive regulation of phosphoinositide 3-kinase cascade; positive regulation of small GTPase mediated signal transduction; positive regulation of peptidyl-tyrosine phosphorylation; long-term memory; positive regulation of protein kinase activity; brain development
Reference #:  P78509 (UniProtKB)
Alt. Names/Synonyms: PRO1598; Reelin; RELN; RL
Gene Symbols: RELN
Molecular weight: 388,388 Da
Basal Isoelectric point: 5.54  Predict pI for various phosphorylation states
Select Structure to View Below

reelin

Protein Structure Not Found.


STRING  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  ENZYME  |  Phospho.ELM  |  NetworKIN  |  UCSD-Nature  |  UniProtKB  |  Entrez-Gene  |  Ensembl Gene


Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 T10-p RSGWARQtFLLALLL
0 2 Y29-p RARAAAGyyPRFSPF
0 1 Y30-p ARAAAGyyPRFSPFF
0 1 S101 TSTSVQASQSIGGSS
0 1 S278-p GSCRFSYsDPsIIVL
0 1 S281-p RFSYsDPsIIVLyAK
0 1 Y286-p DPsIIVLyAKNNSAD
0 1 K299-ac ADWIQLEkIRAPSNV
0 1 S465-p ERKLCTPsMDtTGyG
0 1 T468-p LCTPsMDtTGyGNLR
0 1 Y471-p PsMDtTGyGNLRFYF
0 1 S735-p SIRGAEVsFGCGVLA
0 1 S743-p FGCGVLAsGKALVFN
0 2 S764-p LITSFLDsSQSRFLQ
0 1 T773-p QSRFLQFtLRLGSkS
0 1 K779-ub FtLRLGSkSVLSTCR
0 1 K833-ub VELPGDAkQFGIQFR
0 1 Y914-p KLASSMRyVETQSMQ
0 1 A1272 KNETFCAATPSAMIF
0 1 S1351-p GKGCEGNsRELsEPT
0 1 S1355-p EGNsRELsEPTMYHT
0 1 Y1915-p FINVPLPytAQtNAT
0 1 T1916-p INVPLPytAQtNATR
0 1 T1919-p PLPytAQtNATRFRL
0 1 Y2154-p KCICDPGysGPTCKI
0 1 S2155-p CICDPGysGPTCKIS
0 1 S2548 TVCGAVASGMALHFS
0 1 Y2821-p KGWKRITyPLPESLV
0 1 K2893 HTLKTFLKERFDSEE
0 1 S3108-p DKTHNALsSRELIIQ
0 1 Y3118-p ELIIQPGyMMQFkIV
0 1 K3123-ac PGyMMQFkIVVGCEA
0 1 T3319-p CQIRQAAtKPLDLTR
  mouse

 
A10 RGCWAPRALVLAVLL
Y30 RARAATGYYPRFSPF
Y31 ARAATGYYPRFSPFF
S102-p TSTSIQSsQSIGGSS
S279 GSCRFSYSDPSITVS
S282 RFSYSDPSITVSYAK
Y287 DPSITVSYAKNNTAD
K300 ADWIQLEKIRAPSNV
Y466 ERKLCTPYMDTTGYG
T469 LCTPYMDTTGYGNLR
Y472 PYMDTTGYGNLRFYF
S736 SIRGAEVSFGCGVLA
S744 FGCGVLASGKALVFN
S765 LITSFLDSSQSRFLQ
T774 QSRFLQFTLRLGSKS
K780 FTLRLGSKSVLSTCR
R834 VELPDDARQFGIQFR
Y915 KLASSMRYVETQSMQ
T1273-p KNDSFCAtTPSAMVF
S1352 GKGCEGNSRELSEPT
S1356 EGNSRELSEPTVYYT
Y1916 FINVPLPYGAQTNAT
G1917 INVPLPYGAQTNATR
T1920 PLPYGAQTNATRFRL
Y2155 KCICDPGYSGPTCKI
S2156 CICDPGYSGPTCKIS
S2549-p TVCGAVAsGLALHFS
Y2822 EGWKRITYPLPESLT
K2894-ub HSLKTFLkERFDSEE
S3109 DKTHNALSSRELIIQ
Y3119 ELIIQPGYMMQFKIV
K3124 PGYMMQFKIVVGCEA
T3320 CQIRQAATKPLDLTR
  rat

 
T10 RGCWAPRTLVLAVLL
Y31 RARAATGYYPRFSPF
Y32 ARAATGYYPRFSPFF
S103 TSTSIQSSQSIGGSS
S280 GSCRFSYSDPSIIVS
S283 RFSYSDPSIIVSYAK
Y288 DPSIIVSYAKNNTAD
K301 ADWIQLEKIRAPSNV
Y467 ERKLCTPYMDTTGYG
T470 LCTPYMDTTGYGNLR
Y473 PYMDTTGYGNLRFYF
S737 SIRGAEVSFGCGVLA
S745 FGCGVLASGKALVFN
S766 LITSFLDSSQSRFLQ
T775 QSRFLQFTLRLGSKS
K781 FTLRLGSKSVLSTCR
K835 VELPDDAKQFGIQFR
Y916 KLASSMRYVETQSMQ
T1274 KNDSFCATTPSAMVF
S1353 GKGCEGNSRELSEPT
S1357 EGNSRELSEPTVYYT
Y1917 FINVPLPYSAQTNAT
S1918 INVPLPYSAQTNATR
T1921 PLPYSAQTNATRFRL
Y2156 KCICDPGYSGPTCKI
S2157 CICDPGYSGPTCKIS
S2550 TVCGAVASGLALHFS
Y2823 KGWKRITYPLPESLM
K2895 HTLKTFLKERFDSEE
S3110 DKTHNALSSRELIIQ
Y3120 ELIIQPGYMMQFKIV
K3125 PGYMMQFKIVVGCEA
T3321 CQIRQAATKPLDLTR
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.