Property Summary

NCBI Gene PubMed Count 42
Grant Count 40
R01 Count 36
Funding $4,131,714.2
PubMed Score 124.91
PubTator Score 53.51

Knowledge Summary

Patent

No data available

Expression

  Differential Expression (7)

Disease log2 FC p
ependymoma 1.100 0.000
medulloblastoma -1.300 0.001
atypical teratoid / rhabdoid tumor 1.500 0.000
medulloblastoma, large-cell -2.400 0.000
interstitial cystitis -1.100 0.000
ulcerative colitis -1.200 0.000
ovarian cancer -1.900 0.000

Gene RIF (13)

PMID Text
25760605 Removal of this side chain enhances the binding affinity by more than fivefold, suggesting that access of Crb to Pals1 may be regulated by intradomain contacts or by protein-protein interaction.
24488012 The unique in-frame MPP5-FAM71D fusion product is important for proliferation of PC346C cells.
22337881 the crystal structure of a 4-L27 domain-containing heterotrimer derived from the tripartite complex Patj/Pals1/Mals2
22114289 Small irregularly shaped spots are detected throughout the Pals1-deficient retina of conditional knockdown mice by confocal scanning laser ophthalmoscopy and spectral domain optical coherence tomography.
22102253 Crystals of tripartite complex 1 of L27(PATJ)-(L27N,L27C)(Pals1)-L27(MALS) diffracted to 2.05 A resolution
21479189 The cell polarity protein PALS1 is expressed in T lymphocytes and participates to the optimal activation of NF-kappaB following TCR stimulation.
20861307 Data suggest that hijacking of PALS1 by SARS-CoV E plays a determinant role in the disruption of the lung epithelium in SARS patients.
20833712 Polycystin-2 activity is controlled by transcriptional coactivator with PDZ binding motif and PALS1-associated tight junction protein
20237282 Polarity protein associated with lin seven 1 (Pals1) plays an essential role in radical and longitudinal extension of the myelin sheath in peripheral nerves, likely involving membrane protein trafficking.
17920587 the importance of a conserved Crumbs-MPP5-EPB41L5 polarity complex in mammals for separation of the apical and basolateral domains through specialized cell-cell junctions
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AA Sequence

MTTSHMNGHVTEESDSEVKNVDLASPEEHQKHREMAVDCPGDLGTRMMPIRRSAQLERIRQQQEDMRRRR      1 - 70
EEEGKKQELDLNSSMRLKKLAQIPPKTGIDNPMFDTEEGIVLESPHYAVKILEIEDLFSSLKHIQHTLVD     71 - 140
SQSQEDISLLLQLVQNKDFQNAFKIHNAITVHMNKASPPFPLISNAQDLAQEVQTVLKPVHHKEGQELTA    141 - 210
LLNTPHIQALLLAHDKVAEQEMQLEPITDERVYESIGQYGGETVKIVRIEKARDIPLGATVRNEMDSVII    211 - 280
SRIVKGGAAEKSGLLHEGDEVLEINGIEIRGKDVNEVFDLLSDMHGTLTFVLIPSQQIKPPPAKETVIHV    281 - 350
KAHFDYDPSDDPYVPCRELGLSFQKGDILHVISQEDPNWWQAYREGDEDNQPLAGLVPGKSFQQQREAMK    351 - 420
QTIEEDKEPEKSGKLWCAKKNKKKRKKVLYNANKNDDYDNEEILTYEEMSLYHQPANRKRPIILIGPQNC    421 - 490
GQNELRQRLMNKEKDRFASAVPHTTRSRRDQEVAGRDYHFVSRQAFEADIAAGKFIEHGEFEKNLYGTSI    491 - 560
DSVRQVINSGKICLLSLRTQSLKTLRNSDLKPYIIFIAPPSQERLRALLAKEGKNPKPEELREIIEKTRE    561 - 630
MEQNNGHYFDTAIVNSDLDKAYQELLRLINKLDTEPQWVPSTWLR                             631 - 675
//

Text Mined References (47)

PMID Year Title
25760605 2015 Structures of the human Pals1 PDZ domain with and without ligand suggest gated access of Crb to the PDZ peptide-binding groove.
25416956 2014 A proteome-scale map of the human interactome network.
24488012 2015 Next-generation sequencing reveals novel rare fusion events with functional implication in prostate cancer.
24366813 2013 Interaction proteome of human Hippo signaling: modular control of the co-activator YAP1.
24275569 2014 An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.
23533145 2013 In-depth proteomic analyses of exosomes isolated from expressed prostatic secretions in urine.
23376485 2013 Proteomic analysis of podocyte exosome-enriched fraction from normal human urine.
23201090 2013 miR-199a-5p regulates urothelial permeability and may play a role in bladder pain syndrome.
23186163 2013 Toward a comprehensive characterization of a human cancer cell phosphoproteome.
22337881 2012 Structure of an L27 domain heterotrimer from cell polarity complex Patj/Pals1/Mals2 reveals mutually independent L27 domain assembly mode.
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