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:
PRICKLE1 (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
PRICKLE1 Involved in the planar cell polarity pathway that controls convergent extension during gastrulation and neural tube closure. Convergent extension is a complex morphogenetic process during which cells elongate, move mediolaterally, and intercalate between neighboring cells, leading to convergence toward the mediolateral axis and extension along the anteroposterior axis. Necessary for nuclear localization of REST. May serve as nuclear receptor. Defects in PRICKLE1 are the cause of progressive myoclonic epilepsy type 1B (EPM1B). EPM1B is an autosomal recessive disorder characterized by myoclonus that progresses in severity over time, tonic-clonic seizures and ataxia. Defects in PRICKLE1 may be a cause of susceptibility to neural tube defects (NTD). Congenital malformations of the central nervous system and adjacent structures related to defective neural tube closure during the first trimester of pregnancy. Failure of neural tube closure can occur at any level of the embryonic axis. Common NTD forms include anencephaly, myelomeningocele and spina bifida, which result from the failure of fusion in the cranial and spinal region of the neural tube. NTDs have a multifactorial etiology encompassing both genetic and environmental components. Belongs to the prickle / espinas / testin family. Note: This description may include information from UniProtKB.
Protein type: Unknown function
Cellular Component: nuclear membrane; nucleus; cytosol
Molecular Function: protein binding; zinc ion binding
Biological Process: positive regulation of protein ubiquitination; protein import into nucleus; positive regulation of proteasomal ubiquitin-dependent protein catabolic process; neural tube closure; negative regulation of transcription, DNA-dependent
Reference #:  Q96MT3 (UniProtKB)
Alt. Names/Synonyms: EPM1B; FLJ31627; FLJ31937; MGC138902; MGC138903; PRIC1; prickle homolog 1 (Drosophila); prickle-like 1; Prickle-like protein 1; PRICKLE1; REST (RE-1 silencing transcription factor)/NRSF (neuron-restrictive silencer factor)-interacting LIM domain protein; REST/NRSF-interacting LIM domain protein 1; RILP
Gene Symbols: PRICKLE1
Molecular weight: 94,300 Da
Basal Isoelectric point: 5.84  Predict pI for various phosphorylation states
Select Structure to View Below

PRICKLE1

Protein Structure Not Found.


STRING  |  neXtProt  |  Protein Atlas  |  BioGPS  |  DISEASE  |  Scansite  |  Pfam  |  Phospho.ELM  |  NetworKIN  |  Source  |  GeneCards  |  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 2 T21-p FGCQRSStSDDDSGC
0 1 S315 LGEDVHASDSSDSAF
0 1 S317 EDVHASDSSDSAFQS
0 1 K359 LSPALNYKFPGLSGN
0 1 K394 FASEEFWKGRVEQET
0 1 S445-p RASEHWIsDNMVKsK
0 1 S451-p IsDNMVKsKTELKQN
0 2 S476 SDMYWAQSQDGLGDS
0 1 S493-p GSHPGPAssRRLQEL
0 1 S494-p SHPGPAssRRLQELE
0 4 S591 NSSMLHRSAESLKSL
0 2 S594 MLHRSAESLKSLSSE
0 1 S597 RSAESLKSLSSELCP
0 4 S624 PVLRRSKSQSRPQQV
0 7 Y661 ERTRRRVYNFEERGS
0 2 S681-p RRRRSRKsRsDNALN
0 4 S683-p RRSRKsRsDNALNLV
0 1 T691-p DNALNLVtERKYSPK
0 1 Y731 YIQNADLYGQYAHAT
  mouse

 
T21 FGCQRSSTSDDDSGC
S315-p LGEDIHAsDsSDSAF
S317-p EDIHAsDsSDSAFQS
K359-ub LSPALNYkFPGLSGN
K395-ub FANEEFWkARVEQEA
P446 RASEHWIPDNMVTNK
N452 IPDNMVTNKPEVKPN
S477-p SDMYWAQsQDGLGDS
S494 GSHPGPASSRRLQEL
S495 SHPGPASSRRLQELD
S592-p NSSMLHRsAEsLQsL
S595-p MLHRsAEsLQsLNSG
S598-p RsAEsLQsLNSGLCP
S625-p PVLRRSKsQSRPQQV
Y662 ERTRRRAYHFEERGS
S682-p RHRRSRKsRsDNALN
S684-p RRSRKsRsDNALNLV
T692 DNALNLVTERKYSAK
Y732 YMQNANLYSQYAHAT
  rat

 
T21 FGCQRSSTSDDDSGC
S315 LGEDIHASDSSDSAF
S317 EDIHASDSSDSAFQS
K359 LSPALNYKFPGLSGS
K394 FAHEEFWKARVDQEA
P445 RASEHWIPDNMVTNK
N451 IPDNMVTNKPEAKQN
S476-p SDMYWAQsQDGLGDS
S493 GSHPGPASSRRLQEL
S494 SHPGPASSRRLQELD
S591 NSSMLHRSAESLKSL
S594 MLHRSAESLKSLNSE
S597 RSAESLKSLNSELCP
S624 PVLRRSKSQSRPQQV
Y661-p ERTRRRVyHFEERGS
S681 RHRRSRKSRSDNALN
S683 RRSRKSRSDNALNLV
T691 DNALNLVTERKYSAK
Y731-p YMQNANLyGQYAHTT
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.