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Zinc finger protein 335

NIF-1, NIF-2, NRC-interacting factor 1

The protein encoded by this gene enhances transcriptional activation by ligand-bound nuclear hormone receptors. However, it does this not by direct interaction with the receptor, but by direct interaction with the nuclear hormone receptor transcriptional coactivator NRC. The encoded protein may function by altering local chromatin structure. [provided by RefSeq, Jul 2008] (from NCBI)

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Antibodies online ZNF335 (Human)

Top mentioned proteins: NRC, ACID, CAN, HOXA1, V1a

Papers on NIF-1

NRC-interacting factor directs neurite outgrowth in an activity-dependent manner.

New

Ip et al., Hong Kong, Hong Kong. In Neuroscience, Apr 2015

Nuclear hormone receptor coregulator-interacting factor 1 (NIF-1) is a zinc finger nuclear protein that was initially identified to enhance nuclear hormone receptor transcription via its interaction with nuclear hormone receptor coregulator (NRC).

p35 regulates the CRM1-dependent nucleocytoplasmic shuttling of nuclear hormone receptor coregulator-interacting factor 1 (NIF-1).

Ip et al., Hong Kong, Hong Kong. In Plos One, 2013

Here, we report that a nuclear protein, nuclear hormone receptor coregulator (NRC)-interacting factor 1 (NIF-1), is a new interacting partner of p35.

IMAC fractionation in combination with LC-MS reveals H2B and NIF-1 peptides as potential bladder cancer biomarkers.

Vlahou et al., Athens, Greece. In J Proteome Res, 2013

The differential expression of two candidate biomarkers, histone H2B and NIF-1 (zinc finger 335) in BC, was verified in independent sets of urine samples by ELISA and by immunohistochemical analysis of BC tissue.

Microcephaly gene links trithorax and REST/NRSF to control neural stem cell proliferation and differentiation.

Impact

Walsh et al., Boston, United States. In Cell, 2012

Here, we identify and characterize a nuclear zinc finger protein, ZNF335/NIF-1, as a causative gene for severe microcephaly, small somatic size, and neonatal death.

Loss of Xenopus tropicalis EMSY causes impairment of gastrulation and upregulation of p53.

Smith et al., Cambridge, United Kingdom. In N Biotechnol, 2011

It also interacts with BS69 and HP1b, both of which are involved in chromatin remodelling, and with NIF-1 and DBC-1 in the regulation of nuclear receptor-mediated transcription.

Identification and characterization of a novel nuclear protein complex involved in nuclear hormone receptor-mediated gene regulation.

Samuels et al., New York City, United States. In J Biol Chem, 2009

NRC interacting factor 1 (NIF-1) was cloned as a novel factor that interacts in vivo with NRC.

Components of the CCR4-NOT complex function as nuclear hormone receptor coactivators via association with the NRC-interacting Factor NIF-1.

GeneRIF

Samuels et al., New York City, United States. In J Biol Chem, 2008

CCR4 plays a role in the regulation of certain endogenous RARalpha target genes and RCD1 and CCR4 might mediate their function through their interaction with NIF-1

Nuclear receptor coregulator (NRC): mapping of the dimerization domain, activation of p53 and STAT-2, and identification of the activation domain AD2 necessary for nuclear receptor signaling.

Samuels et al., New York City, United States. In Mol Endocrinol, 2007

Activation of p53 by NRC appears to involve a novel mechanism where NRC interacts indirectly with p53 through Trap80, a member of the mediator complex, which binds NRC interacting factor-1 (NIF-1), which interacts with and potentiates the effect of NRC.

NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC.

GeneRIF

Samuels et al., New York City, United States. In Mol Cell Biol, 2002

NRC-interacting factor 1 is a novel cotransducer that interacts with and regulates the activity of the nuclear hormone receptor coactivator NRC

An N-ethylmaleimide-sensitive cytosolic factor necessary for nuclear protein import: requirement in signal-mediated binding to the nuclear pore.

Forbes et al., Los Angeles, United States. In J Cell Biol, 1990

The effect of NIF-1 is enhanced by a second cytosolic NEM-sensitive factor, NIF-2.

Ionomycin-regulated phosphorylation of the myeloid calcium-binding protein p14.

Impact

Hogg et al., Lincoln, United Kingdom. In Nature, 1989

Part of this sequence is identical to the neutrophil immobilizing factors NIF-1 and NIF-2, indicating that the phosphorylation event could have a role in the generation of NIF activity in the p14 protein.

Isolation of two polypeptides comprising the neutrophil-immobilizing factor of human leucocytes.

Goetzl et al., In Immunology, 1983

The larger (NIF-1) and smaller (NIF-2) of the polypeptides were resolved by filtration on Bio-Gel P6 and purified to homogeneity by sequential reverse-phase high performance liquid chromatography and paper electrophoresis.