Polyamine-modulated factor 1

PMF1
Identifiers
Aliases	PMF1 , polyamine modulated factor 1
External IDs	OMIM: 609176 MGI: 1914287 HomoloGene: 5224 GeneCards: PMF1
Gene location (Human)
Chr.	Chromosome 1 (human)
End	156,240,042 bp
Gene location (Mouse)
Chr.	Chromosome 3 (mouse)
End	88,317,638 bp
RNA expression pattern
	Top expressed in
	right lobe of thyroid gland; ; left lobe of thyroid gland; ; gastrocnemius muscle; ; left ventricle; ; skin of abdomen; ; monocyte; ; right lobe of liver; ; canal of the cervix; ; right uterine tube; ; body of stomach;
	Top expressed in
	yolk sac; ; internal carotid artery; ; lip; ; morula; ; thymus; ; Paneth cell; ; secondary oocyte; ; blood; ; external carotid artery; ; duodenum;
	More reference expression data
	n/a
Gene ontology
Molecular function	transcription coactivator activity ; leucine zipper domain binding ; protein binding ;
Cellular component	chromosome ; cytosol ; MIS12/MIND type complex ; chromosome, centromeric region ; nucleus ; kinetochore ; transcription regulator complex ; nucleoplasm ; Golgi apparatus ; intracellular membrane-bounded organelle ; nuclear MIS12/MIND complex ;
Biological process	chromosome segregation ; cell division ; cell cycle ; regulation of transcription, DNA-templated ; transcription by RNA polymerase II ; transcription, DNA-templated ; positive regulation of nucleic acid-templated transcription ;
	Sources:Amigo / QuickGO
Orthologs
	11243
	67037
	ENSG00000160783
	ENSMUSG00000028066
	Q6P1K2
	Q9CPV5
	NM_007221 ; NM_001199653 ; NM_001199654
	NM_025928 ; NM_001310605
	NP_001186582 ; NP_001186583 ; NP_009152
	NP_001297534 ; NP_080204
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated March 04, 2023

Polyamine-modulated factor 1 is a protein that in humans is encoded by the PMF1 gene.^[5]^[6]

Interactions

Polyamine-modulated factor 1 has been shown to interact with MIS12.^[7]^[8]

Related Research Articles

<span class="mw-page-title-main">Kinetochore</span> Protein complex that allows microtubules to attach to chromosomes during cell division

A kinetochore is a disc-shaped protein structure associated with duplicated chromatids in eukaryotic cells where the spindle fibers attach during cell division to pull sister chromatids apart. The kinetochore assembles on the centromere and links the chromosome to microtubule polymers from the mitotic spindle during mitosis and meiosis. The term kinetochore was first used in a footnote in a 1934 Cytology book by Lester W. Sharp and commonly accepted in 1936. Sharp's footnote reads: "The convenient term kinetochore has been suggested to the author by J. A. Moore", likely referring to John Alexander Moore who had joined Columbia University as a freshman in 1932.

<span class="mw-page-title-main">Spermidine</span> Chemical compound

Spermidine is a polyamine compound found in ribosomes and living tissues and having various metabolic functions within organisms. It was originally isolated from semen.

Diamine acetyltransferase 1 is an enzyme that in humans is encoded by the SAT1 gene found on the X chromosome.

Kinetochore protein NDC80 homolog is a protein that in humans is encoded by the NDC80 gene.

Kinetochore protein Nuf2 is a protein that in humans is encoded by the NUF2 gene.

COP9 signalosome complex subunit 7a is a protein that in humans is encoded by the COPS7A gene.

ZW10 interactor (Zwint-1) is a protein that in humans is encoded by the ZWINT gene.

Centromere protein H is a protein that in humans is encoded by the CENPH gene.

Centromere protein I is a protein that in humans is encoded by the CENPI gene.

Chromobox protein homolog 5 is a protein that in humans is encoded by the CBX5 gene. It is a highly conserved, non-histone protein part of the heterochromatin family. The protein itself is more commonly called HP1α. Heterochromatin protein-1 (HP1) has an N-terminal domain that acts on methylated lysines residues leading to epigenetic repression. The C-terminal of this protein has a chromo shadow-domain (CSD) that is responsible for homodimerizing, as well as interacting with a variety of chromatin-associated, non-histone proteins.

KNL1 is a protein that is encoded by the KNL1 gene in humans.

Kinetochore-associated protein NSL1 homolog is a protein that in humans is encoded by the NSL1 gene.

Protein MIS12 homolog is a protein that in humans is encoded by the MIS12 gene.

Kinetochore protein Spc24 is a protein that in humans is encoded by the SPC24 gene.

DSN1, MIND kinetochore complex component, homolog , also known as DSN1 or MIS13, is a protein which in humans encoded by the DSN1 gene.

Iain Cheeseman investigates the role of the kinetochore, a group of proteins required for cell division and chromosome segregation. This core network of proteins facilitates the attachment of chromosomes to microtubule polymers—the spindle structures that attach to the ends of cells, pulling and dividing them during cell division. The kinetochore is critical to ensuring duplication without loss or damage to the genetic material. Cheeseman is also investigating the activities of the individual molecular machines that make up this structure and how these proteins are controlled and regulated.

MIS18 binding protein 1 is a protein that in humans is encoded by the MIS18BP1 gene. The gene is also known as LKNL2, M18BP1, C14orf106, and HSA242977.

A polyamine is an organic compound having more than two amino groups. Alkyl polyamines occur naturally, but some are synthetic. Alkylpolyamines are colorless, hygroscopic, and water soluble. Near neutral pH, they exist as the ammonium derivatives. Most aromatic polyamines are crystalline solids at room temperature.

Spermine oxidase (EC 1.5.3.16, PAOh1/SMO, AtPAO1, AtPAO4, SMO) is an enzyme with systematic name spermidine:oxygen oxidoreductase (spermidine-forming). This enzyme catalyses the following chemical reaction

Karen Oegema is a molecular cell biologist at the Ludwig Institute for Cancer Research and a professor of cellular and molecular medicine at the University of California, San Diego. She is best known for her research with Caenorhabditis elegans, which her lab uses as a model system in their mission to dissect the molecular mechanics of cytokinesis. She was given the Women in Cell Biology Mid-Career Award for Excellence in Research in 2017, as well as the Women in Cell Biology Junior Award for Excellence in Research in 2006.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000160783 - Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000028066 - Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ Wang Y, Devereux W, Stewart TM, Casero RA (July 1999). "Cloning and characterization of human polyamine-modulated factor-1, a transcriptional cofactor that regulates the transcription of the spermidine/spermine N(1)-acetyltransferase gene". The Journal of Biological Chemistry. 274 (31): 22095–101. doi: 10.1074/jbc.274.31.22095 . PMID 10419538.
↑ "Entrez Gene: PMF1 polyamine-modulated factor 1".
↑ Cheeseman IM, Niessen S, Anderson S, Hyndman F, Yates JR, Oegema K, Desai A (September 2004). "A conserved protein network controls assembly of the outer kinetochore and its ability to sustain tension". Genes & Development. 18 (18): 2255–68. doi:10.1101/gad.1234104. PMC 517519 . PMID 15371340.
↑ Obuse C, Iwasaki O, Kiyomitsu T, Goshima G, Toyoda Y, Yanagida M (November 2004). "A conserved Mis12 centromere complex is linked to heterochromatic HP1 and outer kinetochore protein Zwint-1". Nature Cell Biology. 6 (11): 1135–41. doi:10.1038/ncb1187. PMID 15502821. S2CID 39408000.

Polyamine-modulated factor 1

Contents

Interactions

Related Research Articles

References

Further reading