FAM83H
| FAM83H | |||
|---|---|---|---|
| Identifiers | |||
Gene ontology | |||
| Molecular function | |||
| Cellular component | |||
| Biological process | |||
| Sources:Amigo / QuickGO | |||
Ensembl | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| UniProt | |||||||||
| RefSeq (mRNA) | |||||||||
| RefSeq (protein) | |||||||||
| Location (UCSC) | Chr 8: 143.72 – 143.74 Mb | Chr 15: 75.87 – 75.89 Mb | |||||||
| PubMed search | [3] | [4] | |||||||
| View/Edit Human | View/Edit Mouse |
FAM83H is a protein, which in humans is encoded by the FAM83H gene. The protein is also known as uncharacterized protein FAM83H. FAM83H is targeted for the nucleus. It is predicted to play a role in the structural development and calcification of tooth enamel.
Gene
Location
FAM83H is located on the long arm of chromosome 8 (8q24.3), starting at 143723933 and ending at 143738030. The FAM83H gene spans 14097 base pairs and is orientated on the—strand. The coding region is made up of 5,604 base pairs and 5 exons.[5]
Expression
FAM83H is ubiquitously expressed throughout the human body at relatively low levels.[6][7]
Transcript Variants
In humans, there is only one known major product of the FAM83H gene.[8][9][10]
Homology
Paralogs
There are no
Orthologs
Below is a table of
Orthologs of the human protein FAM83H are listed above in descending order or date of divergence and then ascending order of percent identity. FAM83H is highly conserved throughout all orthologs, demonstrated by a 40% identity in the least similar ortholog. FAM83H has evolved slowly and evenly over time.[12][13]
Protein
General Properties
The
Composition
FAM83H is proline rich, being 10.32% protein, and is asparagine deficient with only 1.1%. The percent composition of each amino acid is fairly consistent throughout the orthologs of the protein. The most distant ortholog displays the most variance in amino acid composition.
Domains
FAM83H has two known domains. The PLDc_FAM83H (phospholipase like domain) domain stretches from 17-281 on FAM83H. It lacks the functionally important histidine, so while it may share similar structure it most likely lacks PLD activity. The MIP-T3 microtubule binding domain stretches from 909-1176.[15]
Post-translational modifications
FAM83H is highly phosphorylated post modification. There are 11 predicted phosphorylated sites. There are two motifs with high probability of post translational modification
Fam83H is primarily composed of
Subcellular Localization
Protein FAM83H is targeted to the nucleus.[18]
Interacting Proteins
FAM83H was found to interact with
Clinical Significance
Disease Association
People who suffer from amelogenesis imperfecta have lost function in FAM83H.[20][21]
References
- ^ a b c ENSG00000273889 GRCh38: Ensembl release 89: ENSG00000180921, ENSG00000273889 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000046761 – 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.
- ^ "NCBI gene database". NCBI.
- ^ "GEO profiles". NCBI geo profiles.
- ^ "EST profiles". NCBI EST profiles.
- ^ "Emsembl". Vega.
- ^ "Genecards". The Gene Human Database.
- ^ "Aceview". NCBI.
- ^ "Genecards". The Gene Human Database.
- ^ "BLAST". NCBI.
- ^ Hedges SB. "TimeTree". Bioinformatics.
- ^ "SAPS". Statistical Analysis of Protein Sequence, Biology Workbench.[permanent dead link]
- ^ "NCBI Structure". The Gene Human Database.
- ^ "PELE". San Diego Supercomputer Center.
- ^ "CHOFAS (Predict Secondary Structure of PS". Chou-Fasman. Archived from the original on 2003-08-11. Retrieved 2015-05-09.
- ^ "PSORT II". Expasy.
- ^ "IntAct". EMNL-EBI.
- ^ "NCBI gene database". NCBI.
- ^ "Genecards". The Gene Human Database.
Further reading
- Kim JW, Lee SK, Lee ZH, et al. (2008). "FAM83H mutations in families with autosomal-dominant hypocalcified amelogenesis imperfecta". Am. J. Hum. Genet. 82 (2): 489–94. PMID 18252228.
- Ding Y, Estrella MR, Hu YY, et al. (2009). "Fam83h is associated with intracellular vesicles and ADHCAI". J. Dent. Res. 88 (11): 991–6. PMID 19828885.
- Hart PS, Becerik S, Cogulu D, et al. (2009). "Novel FAM83H mutations in Turkish families with autosomal dominant hypocalcified amelogenesis imperfecta". Clin. Genet. 75 (4): 401–4. PMID 19220331.
- Bonaldo MF, Lennon G, Soares MB (1996). "Normalization and subtraction: two approaches to facilitate gene discovery". Genome Res. 6 (9): 791–806. PMID 8889548.
- Lee SK, Hu JC, Bartlett JD, et al. (2008). "Mutational spectrum of FAM83H: the C-terminal portion is required for tooth enamel calcification". Hum. Mutat. 29 (8): E95–9. PMID 18484629.
- El-Sayed W, Shore RC, Parry DA, et al. (2010). "Ultrastructural analyses of deciduous teeth affected by hypocalcified amelogenesis imperfecta from a family with a novel Y458X FAM83H nonsense mutation". Cells Tissues Organs (Print). 191 (3): 235–9. PMID 20160442.
- Strausberg RL, Feingold EA, Grouse LH, et al. (2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. PMID 12477932.
- Brandenberger R, Wei H, Zhang S, et al. (2004). "Transcriptome characterization elucidates signaling networks that control human ES cell growth and differentiation". Nat. Biotechnol. 22 (6): 707–16. S2CID 27764390.
- Wright JT, Frazier-Bowers S, Simmons D, et al. (2009). "Phenotypic variation in FAM83H-associated amelogenesis imperfecta". J. Dent. Res. 88 (4): 356–60. PMID 19407157.
- Hyun HK, Lee SK, Lee KE, et al. (2009). "Identification of a novel FAM83H mutation and microhardness of an affected molar in autosomal dominant hypocalcified amelogenesis imperfecta". International Endodontic Journal. 42 (11): 1039–43. PMID 19825039.