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ProteomicsAn increase of NPY1 expression leads to inhibitory phosphorylation of PIN-FORMED (PIN) proteins and suppression of pinoid (pid) null mutants
The PINOID (PID) protein kinase is required for flower initiation in Arabidopsis. The pid mutants fail to initiate flowers on inflorescences, a phenotype that is mimicked by disrupting either the NAKED PINS IN YUC MUTANTS (NPY) gene family or PIN FORMED 1 (PIN1). Both PID and NPY1 have been reported...
ORGANISM(S): Arabidopsis Thaliana (ncbitaxon:3702) 
2025-06-17 | MSV000098241 | MassIVE
ProteomicsSubstrate selectivity for semisynthetic CK2 proteins with Pin1
Protein Ser/Thr kinase CK2 is involved in a myriad of cellular processes including cell growth and proliferation by phosphorylating hundreds of substrates, yet the regulation process of CK2 function is poorly understood. The CK2 catalytic subunit, CK2α, is phosphorylated at Thr344 and phosphorylati...
ORGANISM(S): synthetic construct 
2011-10-24 | E-GEOD-33150 | biostudies-arrayexpress
TranscriptomicsPIN6 and MYB57 in Arabidopsis thaliana nectaries
Transcriptome of three genotypes of Arabidopsis thaliana lateral nectaries from stage 14-15 flowering - one wild type, one pin-6 mutant, and one myb-57 mutant.
ORGANISM(S): Arabidopsis thaliana 
2012-07-30 | E-MTAB-4376 | biostudies-arrayexpress
ProteomicsSubstrate selectivity for semisynthetic CK2 proteins
This SuperSeries is composed of the following subset Series: GSE33149: Substrate selectivity for semisynthetic CK2 proteins with various posttranslational modifications GSE33150: Substrate selectivity for semisynthetic CK2 proteins with Pin1 Refer to individual Series
ORGANISM(S): synthetic construct 
2011-10-24 | E-GEOD-33151 | biostudies-arrayexpress
TranscriptomicsSCBI Wild type and mutant Expression data
Purpose: To compare RNASeq data of wild type and mutants under standard growth conditions (Stationary Phase)28C for 18 h. The mutants were found defective in genes encoding the following proteins: an alkaline metalloprotease secretion protein AprE, GidA, and a PIN domain protein. RNA-seq analysis...
ORGANISM(S): Serratia sp. SCBI 
2014-10-20 | E-GEOD-60476 | biostudies-arrayexpress
UnknownParalogous radiations of PIN proteins with multiple origins of noncanonical PIN structure.
Not available
S-EPMC4104312 | biostudies-literature
ProteomicsTransport properties of canonical PIN proteins and the role of the loop in auxin transport
Auxin is a pivotal plant hormone that controls virtually all aspects of plant growth and development. Auxin is transported in plants in a polar fashion and PIN-FORMED (PIN) transporters are the key players in this process. Canonical PINs possess a long cytosolic loop that is subject to regulation by...
ORGANISM(S): Xenopus laevis (African clawed frog) 
2024-08-23 | PXD044850 | Pride
Phosphoproteomics Pin proteins Auxin transport 
UnknownPlasma membrane-targeted PIN proteins drive shoot development in a moss.
Not available
S-EPMC4251699 | biostudies-literature
UnknownAGC kinases and MAB4/MEL proteins maintain PIN polarity by limiting lateral diffusion in plant cells.
Not available
S-EPMC8112251 | biostudies-literature
UnknownSystems approaches reveal that ABCB and PIN proteins mediate co-dependent auxin efflux.
Not available
S-EPMC9134068 | biostudies-literature
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