Glutamate rich 5
From Wikipedia, the free encyclopedia
| ERICH5 | |||||||||||||||||||||||||||||||||||||||||||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||||||||||||||||||||||||||||||||||||||||||||
| Aliases | ERICH5, C8orf47, glutamate rich 5 | ||||||||||||||||||||||||||||||||||||||||||||||||||
| External IDs | MGI: 2447772; HomoloGene: 52129; GeneCards: ERICH5; OMA:ERICH5 - orthologs | ||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
| Wikidata | |||||||||||||||||||||||||||||||||||||||||||||||||||
| |||||||||||||||||||||||||||||||||||||||||||||||||||
Glutamate rich protein 5 is a protein in humans encoded by the ERICH5 gene, also known as chromosome 8 open reading frame 47 (C8orf47).
Protein
Isoforms
The ERICH5 protein has two isofroms. The longest isofrom, isofrom 1, spans 1,550 base pairs and is composed of 374 amino acids. The second isoform lacks the third and final exon and is 596 base pairs long.[6]
Domains and motifs
ERICH5 contains one conserved domain, a domain of unknown function called DUF4573.[7] ERICH5 is predicted to contain two highly conserved motifs, an APC/C binding motif and the LIG_FHA_2 motif.[8] The APC/C motif spans amino acid 222-226 and serves as a binding site for the anaphase-promoting complex.[9] The LIG_FHA_2 motif is involved in the cell checkpoint pathway and is found in many proteins localized in the nucleus that regulate cell cycle.[10]
Post-translational modifications
ERICH5 is predicted to undergo several post-translational modifications including phosphorylation, O-glycosylation, and sumoylation.[11][12][13] Many of the phosphorylation sites and O-glycosylation sites were predicted at the same amino acid. The post translational modifications shown are those conserved among ERICH5 orthologs. Several kinases were predicted to phosphorylate ERICH5 including PKC, cdc2, CKI, PKA, DNAPK, ATM, EGFR, and CKII.[11]
| Post-translational modification | Amino acid location |
| Phosphorylation | S4, S5, S27, S32, S49, T50, S58, S100, T101, T104, T138, S169, S227, S234, T239, T248, S274, T289, S307, Y320, T340, T346 |
| O-Glycosylation | S5, S27, S32, S49, T50, S58, S100, T101, T104, T138, S169, S227, S234, T239, T248, S274, T289, S307 |
| Sumoylation | K121, K131, K211, K251, K343, K360 |
Secondary structure
ERICH5 was predicted to contain three alpha helices and two beta sheets as well as regions of random coils.[14]


Sub-cellular localization
ERICH5 was predicted to be localized in the nucleus.[16]
Protein interactions
ERICH5 was predicted to interact with several proteins through yeast two-hybrid screening and affinity chromatography.[15] Several of the proteins ERICH5 was predicted to interact with were also localized in the nucleus.[15]

