Lipid Modification Database
Tag Content
LipidDB ID
LipidDB-9606-00013
Entry Name
UniProt Accession
Theoretical PI
5.84
Molecular Weight
94300.26
Genbank Protein ID
Genbank Nucleotide ID
Protein Name
Prickle-like protein 1
Protein Synonyms/Alias
REST/NRSF-interacting LIM domain protein 1;
Gene Name
PRICKLE1
Gene Synonyms/Alias
RILP;
Created Date
01-FEB-2005
 Lipid Modification Sites 
 Position   Sequence Form   Peptide   References   Modification Type 
828
Canonical
KGHKGKNCIIS****
[1][2]
S-Farnesylation
Organism
Homo sapiens (Human)
NCBI Taxa ID
9606
Reference
[1] Shimojo M, Hersh LB. REST/NRSF-interacting LIM domain protein, a putativenuclear translocation receptor. Mol Cell Biol. 2003 Dec;23(24):9025-31. PubMedPMID: 14645515; PubMed Central PMCID: PMC309669.[PMID:14645515]
[2] Maurer-Stroh S, Koranda M, Benetka W, Schneider G, Sirota FL, Eisenhaber F.Towards complete sets of farnesylated and geranylgeranylated proteins. PLoSComput Biol. 2007 Apr 6;3(4):e66. Epub 2007 Feb 23.[PMID:17411337]
Functional Description
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.
Sequence Annotation
Domain: 14 122 PET.
Domain: 124 189 LIM zinc-binding 1.
Domain: 189 249 LIM zinc-binding 2.
Domain: 249 313 LIM zinc-binding 3.
Modified residue: 828 828 Cysteine methyl ester.
Protein Length
831 AA.
Protein Sequence
(Canonical)
MPLEMEPKMS KLAFGCQRSS TSDDDSGCAL EEYAWVPPGL RPEQIQLYFA CLPEEKVPYV  60
NSPGEKHRIK QLLYQLPPHD NEVRYCQSLS EEEKKELQVF SAQRKKEALG RGTIKLLSRA  120
VMHAVCEQCG LKINGGEVAV FASRAGPGVC WHPSCFVCFT CNELLVDLIY FYQDGKIHCG  180
RHHAELLKPR CSACDEIIFA DECTEAEGRH WHMKHFCCLE CETVLGGQRY IMKDGRPFCC  240
GCFESLYAEY CETCGEHIGV DHAQMTYDGQ HWHATEACFS CAQCKASLLG CPFLPKQGQI  300
YCSKTCSLGE DVHASDSSDS AFQSARSRDS RRSVRMGKSS RSADQCRQSL LLSPALNYKF  360
PGLSGNADDT LSRKLDDLSL SRQGTSFASE EFWKGRVEQE TPEDPEEWAD HEDYMTQLLL  420
KFGDKSLFQP QPNEMDIRAS EHWISDNMVK SKTELKQNNQ SLASKKYQSD MYWAQSQDGL  480
GDSAYGSHPG PASSRRLQEL ELDHGASGYN HDETQWYEDS LECLSDLKPE QSVRDSMDSL  540
ALSNITGASV DGENKPRPSL YSLQNFEEME TEDCEKMSNM GTLNSSMLHR SAESLKSLSS  600
ELCPEKILPE EKPVHLPVLR RSKSQSRPQQ VKFSDDVIDN GNYDIEIRQP PMSERTRRRV  660
YNFEERGSRS HHHRRRRSRK SRSDNALNLV TERKYSPKDR LRLYTPDNYE KFIQNKSARE  720
IQAYIQNADL YGQYAHATSD YGLQNPGMNR FLGLYGEDDD SWCSSSSSSS DSEEEGYFLG  780
QPIPQPRPQR FAYYTDDLSS PPSALPTPQF GQRTTKSKKK KGHKGKNCII S           831
FASTA
(Canonical)
>LipidDB-9606-00013|Q96MT3
MPLEMEPKMSKLAFGCQRSSTSDDDSGCALEEYAWVPPGLRPEQIQLYFACLPEEKVPYV
NSPGEKHRIKQLLYQLPPHDNEVRYCQSLSEEEKKELQVFSAQRKKEALGRGTIKLLSRA
VMHAVCEQCGLKINGGEVAVFASRAGPGVCWHPSCFVCFTCNELLVDLIYFYQDGKIHCG
RHHAELLKPRCSACDEIIFADECTEAEGRHWHMKHFCCLECETVLGGQRYIMKDGRPFCC
GCFESLYAEYCETCGEHIGVDHAQMTYDGQHWHATEACFSCAQCKASLLGCPFLPKQGQI
YCSKTCSLGEDVHASDSSDSAFQSARSRDSRRSVRMGKSSRSADQCRQSLLLSPALNYKF
PGLSGNADDTLSRKLDDLSLSRQGTSFASEEFWKGRVEQETPEDPEEWADHEDYMTQLLL
KFGDKSLFQPQPNEMDIRASEHWISDNMVKSKTELKQNNQSLASKKYQSDMYWAQSQDGL
GDSAYGSHPGPASSRRLQELELDHGASGYNHDETQWYEDSLECLSDLKPEQSVRDSMDSL
ALSNITGASVDGENKPRPSLYSLQNFEEMETEDCEKMSNMGTLNSSMLHRSAESLKSLSS
ELCPEKILPEEKPVHLPVLRRSKSQSRPQQVKFSDDVIDNGNYDIEIRQPPMSERTRRRV
YNFEERGSRSHHHRRRRSRKSRSDNALNLVTERKYSPKDRLRLYTPDNYEKFIQNKSARE
IQAYIQNADLYGQYAHATSDYGLQNPGMNRFLGLYGEDDDSWCSSSSSSSDSEEEGYFLG
QPIPQPRPQRFAYYTDDLSSPPSALPTPQFGQRTTKSKKKKGHKGKNCIIS
Gene Ontology
GO:0005829; C:cytosol; IDA:UniProtKB
GO:0031965; C:nuclear membrane; IDA:UniProtKB
GO:0005634; C:nucleus; IDA:UniProtKB
GO:0008270; F:zinc ion binding; IEA:InterPro
GO:0090090; P:negative regulation of canonical Wnt signaling pathway; IDA:BHF-UCL
GO:2000691; P:negative regulation of cardiac muscle cell myoblast differentiation; IDA:UniProtKB
GO:0045892; P:negative regulation of transcription, DNA-templated; IDA:BHF-UCL
GO:0001843; P:neural tube closure; IMP:UniProtKB
GO:0032436; P:positive regulation of proteasomal ubiquitin-dependent protein catabolic process; IDA:BHF-UCL
GO:0031398; P:positive regulation of protein ubiquitination; IDA:BHF-UCL
GO:0006606; P:protein import into nucleus; IDA:UniProtKB
Interpro
InterPro; IPR010442; PET_domain
InterPro; IPR001781; Znf_LIM
Pfam
Pfam; PF00412; LIM;
Pfam; PF06297; PET;
SMART
SMART; SM00132; LIM;
PROSITE
PROSITE; PS00478; LIM_DOMAIN_1;
PROSITE; PS50023; LIM_DOMAIN_2;
PROSITE; PS51303; PET;
PRINTS