ZNF837

ZNF837
Identifiers
Aliases	ZNF837, zinc finger protein 837
External IDs	HomoloGene: 138182 GeneCards: ZNF837
Gene location (Human)
Chr.	Chromosome 19 (human)
End	58,381,030 bp
RNA expression pattern
	Top expressed in
	right uterine tube; ; right lobe of liver; ; left lobe of thyroid gland; ; right lobe of thyroid gland; ; stromal cell of endometrium; ; right adrenal gland; ; left adrenal gland; ; skin of abdomen; ; left uterine tube; ; canal of the cervix;
	n/a
	More reference expression data
	n/a
Gene ontology
Molecular function	DNA binding; metal ion binding; nucleic acid binding; DNA-binding transcription factor activity, RNA polymerase II-specific;
Cellular component	nucleus;
Biological process	transcription, DNA-templated; regulation of transcription, DNA-templated; regulation of transcription by RNA polymerase II;
	Sources:Amigo / QuickGO
Orthologs
	116412
	n/a
	ENSG00000152475
	n/a
	Q96EG3
	n/a
	NM_001129730; NM_138466
	n/a
	NP_612475
	n/a
	Wikidata
View/Edit Human

ZNF837 is a protein that in humans is encoded by the ZNF837 gene,^[3] is located at 19q13.431 with minus strand orientation.^[4] ZNF837 protein is characterized as a C2H2-type zinc finger protein.^[5]

Homology and Evolution[edit]

The human ZNF837 has homologs present in many mammals and seen more distantly. All homologs are chordates. All contain both COG5048 and Zf-C2H2_2 domains. The areas that these domains are found contain the highest conservation rates. In humans, 5 Zf-H2C2 double domains^[6] and 2 COG5048 domains^[7] are present.

The protein sequence is fast evolving among these homologs.

ZNF837 has numerous paralogs in humans, all of which are zinc finger proteins.

Human ZNF837[edit]

In humans, there are no other aliases, and its neighboring genes are MIR4754, A1BG, and RPS5. ZNF837 mRNA that is made into function protein contains 1921 nucleotides, of which 222-1817 are translated to a protein containing 3 exons. The protein consists of 531 amino acids^[8] with a weight of 58,078 Da with an isoelectric point at 9.525.^[9]

Gene Variants[edit]

There are 2 transcript variants. Transcript variant 1, 2050 base pairs in length, is non-coding due to a nonsense-mediated mRNA decay .^[10] Transcript variant 2 is made into the functional protein due to an alternate splice site^[11]

Post Translational[edit]

It is predicted via high conservation to have 4 phosphorylation sites^[12] at T386, T455, S460, Y503.^[13] The internal structure is includes combination of alpha helices, beta sheets and mainly random coils.^[14]

Expression[edit]

ZNF837 has observed in the pancreas, liver, uterus, and muscle cells. In all cases concentration is low.^[15] However, the expression of ZNF837 is seen to have the most impact is when looking at normal vs diseased state. There is a consistent change that is able to be seen.

References[edit]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000152475 – Ensembl, May 2017
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Strausberg, RL; Feingold, EA; Grouse, LH; et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
^ "ZNF837 zinc finger protein 837 [Homo sapiens (human)] - Gene - NCBI".
^ Pieler, T.; Bellefroid, E. (1994). "Perspectives on zinc finger protein function and evolution - an update". Molecular Biology Reports. 20 (1): 1–8. doi:10.1007/bf00999848. PMID 7531280. S2CID 22962225.
^ Iuchi, S (2001). "Three classes of C2H2 zinc finger proteins". Cellular and Molecular Life Sciences. 58 (4): 625–635. doi:10.1007/pl00000885. PMID 11361095. S2CID 6522993.
^ "NCBI Conserved Domain Search".
^ "ZNF837 protein [Homo sapiens] - Protein - NCBI".
^ "ZNF837 (human)".
^ Maquat, Lynne E (2002). "Nonsense-mediated mRNA decay". Current Biology. 12 (6): R196–R197. doi:10.1016/S0960-9822(02)00747-9. PMID 11909543.
^ "ZNF837 (human)".
^ Blom, Nikolaj; Gammeltoft, Steen; Brunak, Søren (1999). "Sequence and structure-based prediction of eukaryotic protein phosphorylation sites 1". Journal of Molecular Biology. 294 (5): 1351–1362. doi:10.1006/jmbi.1999.3310. PMID 10600390.
^ Guo, Ailan et al. Serine, Threonine, and Tyrosine Phosphorylation Sites. Patent US20110045603 A1. 20 Apr. 2010. Print.
^ Kelley, LA; Sternberg, MJE (2009). "Protein structure prediction on the Web: a case study using the Phyre server". Nature Protocols. 4 (3): 363–371. doi:10.1038/nprot.2009.2. hdl:10044/1/18157. PMID 19247286. S2CID 12497300.
^ "EST Profile - Hs.222236".

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000152475 – Ensembl, May 2017

[2] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[3] Strausberg, RL; Feingold, EA; Grouse, LH; et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.

[4] "ZNF837 zinc finger protein 837 [Homo sapiens (human)] - Gene - NCBI".

[5] Pieler, T.; Bellefroid, E. (1994). "Perspectives on zinc finger protein function and evolution - an update". Molecular Biology Reports. 20 (1): 1–8. doi:10.1007/bf00999848. PMID 7531280. S2CID 22962225.

[6] Iuchi, S (2001). "Three classes of C2H2 zinc finger proteins". Cellular and Molecular Life Sciences. 58 (4): 625–635. doi:10.1007/pl00000885. PMID 11361095. S2CID 6522993.

[7] "NCBI Conserved Domain Search".

[8] "ZNF837 protein [Homo sapiens] - Protein - NCBI".

[9] "ZNF837 (human)".

[10] Maquat, Lynne E (2002). "Nonsense-mediated mRNA decay". Current Biology. 12 (6): R196–R197. doi:10.1016/S0960-9822(02)00747-9. PMID 11909543.

[11] "ZNF837 (human)".

[12] Blom, Nikolaj; Gammeltoft, Steen; Brunak, Søren (1999). "Sequence and structure-based prediction of eukaryotic protein phosphorylation sites 1". Journal of Molecular Biology. 294 (5): 1351–1362. doi:10.1006/jmbi.1999.3310. PMID 10600390.

[13] Guo, Ailan et al. Serine, Threonine, and Tyrosine Phosphorylation Sites. Patent US20110045603 A1. 20 Apr. 2010. Print.

[14] Kelley, LA; Sternberg, MJE (2009). "Protein structure prediction on the Web: a case study using the Phyre server". Nature Protocols. 4 (3): 363–371. doi:10.1038/nprot.2009.2. hdl:10044/1/18157. PMID 19247286. S2CID 12497300.

[15] "EST Profile - Hs.222236".

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