Oxidoreductase HTATIP2 (HTATIP2)
The protein contains 242 amino acids for an estimated molecular weight of 27049 Da.
Oxidoreductase required for tumor suppression. NAPDH-bound form inhibits nuclear import by competing with nuclear import substrates for binding to a subset of nuclear transport receptors. May act as a redox sensor linked to transcription through regulation of nuclear import. Isoform 1 is a metastasis suppressor with proapoptotic as well as antiangiogenic properties. Isoform 2 has an antiapoptotic effect. (updated: Jan. 7, 2015)
Protein identification was indicated in the following studies:
- Goodman and co-workers. (2013) The proteomics and interactomics of human erythrocytes. Exp Biol Med (Maywood) 238(5), 509-518.
- Lange and co-workers. (2014) Annotating N termini for the human proteome project: N termini and Nα-acetylation status differentiate stable cleaved protein species from degradation remnants in the human erythrocyte proteome. J Proteome Res. 13(4), 2028-2044.
- Hegedűs and co-workers. (2015) Inconsistencies in the red blood cell membrane proteome analysis: generation of a database for research and diagnostic applications. Database (Oxford) 1-8.
- Bryk and co-workers. (2017) Quantitative Analysis of Human Red Blood Cell Proteome. J Proteome Res. 16(8), 2752-2761.
- D'Alessandro and co-workers. (2017) Red blood cell proteomics update: is there more to discover? Blood Transfus. 15(2), 182-187.
Methods
The following articles were analysed to gather the proteome content of erythrocytes.
The gene or protein list provided in the studies were processed using the ID mapping API of Uniprot in September 2018. The number of proteins identified and mapped without ambiguity in these studies is indicated below.
Only Swiss-Prot entries (reviewed) were considered for protein evidence assignation.
| Publication | Identification 1 | Uniprot mapping 2 | Not mapped / Obsolete | TrEMBL | Swiss-Prot |
|---|---|---|---|---|---|
| Goodman (2013) | 2289 (gene list) | 2278 | 53 | 20599 | 2269 |
| Lange (2014) | 1234 | 1234 | 7 | 28 | 1224 |
| Hegedus (2015) | 2638 | 2622 | 0 | 235 | 2387 |
| Wilson (2016) | 1658 | 1528 | 170 | 291 | 1068 |
| d'Alessandro (2017) | 1826 | 1817 | 2 | 0 | 1815 |
| Bryk (2017) | 2090 | 2060 | 10 | 108 | 1942 |
| Chu (2018) | 1853 | 1804 | 55 | 362 | 1387 |
1 as available in the article and/or in supplementary material
2 uniprot mapping returns all protein isoforms as one entry
The compilation of older studies can be retrieved from the Red Blood Cell Collection database.
The data and differentiation stages presented below come from the proteomic study and analysis performed by our partners of the GReX consortium, more details are available in their published work.
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Biological Process
Angiogenesis
Apoptotic process
Cell differentiation
Import into nucleus
Negative regulation of apoptotic process
Positive regulation of programmed cell death
Positive regulation of transcription by RNA polymerase II
Protein autophosphorylation
Regulation of angiogenesis
Regulation of transcription by RNA polymerase II
Viral process
The reference OMIM entry for this protein is 605628
Hiv-1 tat-interacting protein 2, 30-kd; htatip2
Tip30
Cc3
CLONING
Small cell lung carcinoma (SCLC), which accounts for 25% of all lung cancers, has the poorest survival rate of all histologic types of lung cancer. Relapses and aggressive metastasis commonly occur after favorable initial responses to therapy. By differential display of mRNA from classic SCLC (c-SCLC) and variant SCLC (v-SCLC) cell lines, followed by EST database searching, cDNA library screening, and 5-prime RACE, Shtivelman (1997) identified a cDNA encoding CC3. The deduced 242-amino acid protein is evolutionarily conserved and lacks known protein domains. Northern blot analysis revealed ubiquitous expression of a 1.6-kb transcript in normal tissues and tumor cell lines except for v-SCLC and neuroblastoma. Introduction of CC3 into v-SCLC cells resulted in a significant suppression of metastasis in a SCID-hu mouse model, as well as massive and rapid cell death in vitro through apoptosis. The author suggested that loss of CC3 in SCLC cells might render them resistant to death-inducing signals. Using affinity chromatography with the human immunodeficiency virus-1 (HIV-1) Tat protein (see 601409) to screen HeLa cell extracts, followed by SDS-PAGE analysis, Xiao et al. (1998) identified 2 Tat-interacting proteins, TIP30 and TIP56. By micropeptide sequence analysis and EST database searching, Xiao et al. (1998) identified a cDNA encoding TIP30. Western blot analysis determined that the translated 242-amino acid protein and the native protein have a molecular mass of 30 kD. Coexpression of TIP30 specifically enhanced transcription of Tat in transfected cells. Immunodepletion of TIP30 from nuclear extracts abolished Tat-activated transcription while leaving Tat-independent transcription unimpaired.GENE FUNCTION
Whitman et al. (2000) identified a splice variant of CC3, which they termed TC3, that encodes a 133-amino acid protein. TC3 shares its N-terminal domain with CC3 but has a short, unique C terminus. Northern blot analysis detected a 0.8-kb TC3 transcript in some but not all tumor cell lines. Western blot analysis detected CC3 predominantly in membrane and nuclear fractions but not in the cytoplasm, whereas TC3 was predominantly in membrane fractions. The authors determined that the potent proapoptotic activity of CC3 resides in the N-terminal domain; however, the short C terminus of TC3 confers upon it antiapoptotic properties capable of inhibiting apoptosis induced by CC3 and other death stimuli.BIOCHEMICAL FEATURES
Baker et al. (2000) pointed out that the sequences of CC3 and TIP30 are identical. Sequence analysis indicated that TIP30/CC3 is a member of the short-chain dehydrogenase/reductase (SDR) family. The authors created a 3-dimensional model of the TIP30/CC3 protein, which showed that like other SDR proteins, TIP30/CC3 contains several well-conserved features. These include a beta-alpha-beta fold at the N terminus, which Baker et al. (2000) predicted binds to NADP(H). The N terminus also contains a unique 20-amino acid alpha-helical stretch that may enable docking to other proteins.MAPPING
The International Radiation Hybrid Mapping Consortium mapped the HTATIP2 gene to chromosome 11 (TMAP SGC34227). ... More on the omim web site
Feb. 2, 2018: Protein entry updated
Automatic update: Uniprot description updated
Dec. 19, 2017: Protein entry updated
Automatic update: Uniprot description updated
Nov. 23, 2017: Protein entry updated
Automatic update: Uniprot description updated
March 16, 2016: Protein entry updated
Automatic update: OMIM entry 605628 was added.
Jan. 28, 2016: Protein entry updated
Automatic update: model status changed
Jan. 24, 2016: Protein entry updated
Automatic update: model status changed