TRIM7 (Kr.5q35,3), GNIP, RNF90,Glykogeniinin kanssa interaktion tekeevä proteiini (glykogeenisynteesin aloitusjärjestelmän proteiini)

https://www.ncbi.nlm.nih.gov/gene/81786
Tästä TRIM7 proteiinista ja geenistä on aivan tuoretta uutta tietoa:
(Vuosi 2013) Tämän TRIM7 proteiinin rakenteessa  on  2 sinkkiä sitovaa domeenia, RING domeeni, B-box1 ja B-box2 sekä CC-domeeni. Proteiinia on tumassa ja sytoplasmassa ja se lienee osallisena glykogeenisynteesin alkamisessa . Sitä esiintyy ihossa, ruokatorvessa ja 8 muussa kudoksessa.
Domeeni 130-166, BBox (CHC3H2) , sitoo sinkkiä.
Domeeni 29-82. RING  Zn finger  ( tässä on 40-60 kohtaa, jotka voivat sitoa sinkkiä)
https://www.ncbi.nlm.nih.gov/Structure/cdd/cddsrv.cgi?uid=302633;
välittää proteiini-proteiini-interaktioita. identifioitu  virusreplikaatioon, signaalin transduktioon ja kehitykseen kuuluvien proteiinien yhteydessä.
Jakso 159- 211 on ATP_synth_B, ATP-syntaasi B/B´CF.
*RAKENNE:  https://www.ncbi.nlm.nih.gov/protein/Q9C029.2
Tässä *on paljon mielenkiintoista. Jatkan pääsiäisen jälkeen!
(Linkki lisätty 24.4. 2018:) 
http://www.jbc.org/content/277/22/19331.full

The protein encoded by this gene is a member of the tripartite motif (TRIM) family. The TRIM motif includes three zinc-binding domains, a RING, a B-box type 1, a B-box type 2, and a coiled-coil region. The protein localizes to both the nucleus and the cytoplasm, and may represent a participant in the initiation of glycogen synthesis. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Jul 2013] Expression

Biased expression in skin (RPKM 5.6), esophagus (RPKM 2.8) and 8 other tissues See more

GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?

1. GNIP, a novel protein that binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis.... The largest isoform GNIP1 contains, from NH(2)- to COOH-terminal, a RING finger, a B box, a putative coiled-coil region, and a B30.2-like motif. The previously identified protein TRIM7 (tripartite motif containing protein 7) is also derived from the GNIP gene and is composed of the RING finger, B box, and coiled-coil regions. The GNIP2 and GNIP3 isoforms consist of the coiled-coil region and B30.2-like domain. Physical interaction between GNIP2 and glycogenin was confirmed by co-immunoprecipitation, and in addition GNIP2 was shown to stimulate glycogenin self-glucosylation 3-4-fold. GNIPs may represent a novel participant in the initiation of glycogen synthesis.

Related articles in PubMed

1. Structure-function analysis of GNIP, the glycogenin-interacting protein. Zhai L, et al. Arch Biochem Biophys, 2004 Jan 15. PMID 14984203
2. GNIP, a novel protein that binds and activates glycogenin, the self-glucosylating initiator of glycogen biosynthesis. Skurat AV, et al. J Biol Chem, 2002 May 31. PMID 11916970Abstract BACKGROUND: Glycogenin-interacting protein 1 (GNIP1) is a tripartite motif (TRIM) protein with E3 ubiquitin ligase activity that interacts with glycogenin. These data suggest that GNIP1 could play a major role in the control of glycogen metabolism. However, direct evidence based on functional analysis remains to be obtained.  OBJECTIVES: The aim of this study was 1) to define the expression pattern of glycogenin-interacting protein/Tripartite motif containing protein 7 (GNIP/TRIM7) isoforms in humans, 2) to test their ubiquitin E3 ligase activity, and 3) to analyze the functional effects of GNIP1 on muscle glucose/glycogen metabolism both in human cultured cells and in vivo in mice.  RESULTS:
   We show that GNIP1 was the most abundant GNIP/TRIM7 isoform in human skeletal muscle, whereas in cardiac muscle only TRIM7 was expressed. GNIP1 and TRIM7 had autoubiquitination activity in vitro and were localized in the Golgi apparatus and cytosol respectively in LHCN-M2 myoblasts. GNIP1 overexpression increased glucose uptake in LHCN-M2 myotubes. Overexpression of GNIP1 in mouse muscle in vivo increased glycogen content, glycogen synthase (GS) activity and phospho-GSK-3α/β (Ser21/9) and phospho-Akt (Ser473) content, whereas decreased GS phosphorylation in Ser640. These modifications led to decreased blood glucose levels, lactate levels and body weight, without changing whole-body insulin or glucose tolerance in mouse. CONCLUSION: GNIP1 is an ubiquitin ligase with a markedly glycogenic effect in skeletal muscle.