Timopoietin
| edit |
| Timopoietin | |||||||||||
|---|---|---|---|---|---|---|---|---|---|---|---|
 PDB prikaz baziran na 1gjj. | |||||||||||
| Dostupne strukture | |||||||||||
| 1GJJ, 1H9E, 1H9F | |||||||||||
| Identifikatori | |||||||||||
| Simboli | TMPO; CMD1T; LAP2; LEMD4; PRO0868; TP | ||||||||||
| Vanjski ID | OMIM: 188380 MGI: 106920 HomoloGene: 31144 GeneCards: TMPO Gene | ||||||||||
| |||||||||||
| Pregled RNK izražavanja | |||||||||||
 | |||||||||||
 | |||||||||||
 | |||||||||||
| podaci | |||||||||||
| Ortolozi | |||||||||||
| Vrsta | Čovek | Miš | |||||||||
| Entrez | 7112 | 21917 | |||||||||
| Ensembl | ENSG00000120802 | ENSMUSG00000019961 | |||||||||
| UniProt | P42166 | Q61029 | |||||||||
| RefSeq (mRNA) | NM_001032283.2 | NM_001080129.1 | |||||||||
| RefSeq (protein) | NP_001027454.1 | NP_001073598.1 | |||||||||
| Lokacija (UCSC) | Chr 12: 98.91 - 98.94 Mb | Chr 10: 91.15 - 91.17 Mb | |||||||||
| PubMed pretraga | [1] | [2] | |||||||||
Timopoietin (polipeptid vezan za laminu 2, LAP2) je protein koji je kod ljudi kodiran TMPO genom.[1][2] LAP2 je protein unutrašnje membrane jedra.[3]
Timopoietin učestvuje u indukciji CD90 proteina u grudnu žlezdu. Gen timopoetina kodira tri alternativno splajsovane iRNK molekula koji kodiraju proteine sa 75 kDa (alfa), 51 kDa (beta) i 39 kDa (gama). Oni su izraženi u većini ćelijskih tipova. Ljudski TMPO gen se nalazi u hromozomsko opsegu 12q22 i sastoji se od osam eksona.
Interakcije
Timopoietin formira interakcije sa barijerom za autointegracioni faktor 1,[4] AKAP8L,[5][6] LMNB1[7][8] i LMNA.[9][10]
Reference
- ↑ Harris CA, Andryuk PJ, Cline S, Chan HK, Natarajan A, Siekierka JJ, Goldstein G (August 1994). „Three distinct human thymopoietins are derived from alternatively spliced mRNAs”. Proc Natl Acad Sci U S A 91 (14): 6283–7. DOI:10.1073/pnas.91.14.6283. PMC 44185. PMID 7517549.
- ↑ „Entrez Gene: TMPO thymopoietin”.
- ↑ Holmer, L.; Worman, H. J. (2001). „Inner nuclear membrane proteins: Functions and targeting”. Cellular and molecular life sciences : CMLS 58 (12–13): 1741–1747. DOI:10.1007/PL00000813. PMID 11766875. edit
- ↑ Furukawa, K (August 1999). „LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction”. J. Cell. Sci. (ENGLAND) 112 (15): 2485–92. ISSN 0021-9533. PMID 10393804.
- ↑ Martins, S B; Eide T, Steen R L, Jahnsen T, Skålhegg B S, Collas P (November 2000). „HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics”. J. Cell. Sci. (ENGLAND) 113 (21): 3703–13. ISSN 0021-9533. PMID 11034899.
- ↑ Martins, Sandra; Eikvar Sissel, Furukawa Kazuhiro, Collas Philippe (January 2003). „HA95 and LAP2 beta mediate a novel chromatin-nuclear envelope interaction implicated in initiation of DNA replication”. J. Cell Biol. (United States) 160 (2): 177–88. DOI:10.1083/jcb.200210026. ISSN 0021-9525. PMC 2172640. PMID 12538639.
- ↑ Furukawa, K; Kondo T (February 1998). „Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin”. Eur. J. Biochem. (GERMANY) 251 (3): 729–33. DOI:10.1046/j.1432-1327.1998.2510729.x. ISSN 0014-2956. PMID 9490046.
- ↑ Foisner, R; Gerace L (July 1993). „Integral membrane proteins of the nuclear envelope interact with lamins and chromosomes, and binding is modulated by mitotic phosphorylation”. Cell (UNITED STATES) 73 (7): 1267–79. DOI:10.1016/0092-8674(93)90355-T. ISSN 0092-8674. PMID 8324822.
- ↑ Markiewicz, Ewa; Dechat Thomas, Foisner Roland, Quinlan Roy A, Hutchison Christopher J (December 2002). „Lamin A/C binding protein LAP2alpha is required for nuclear anchorage of retinoblastoma protein”. Mol. Biol. Cell (United States) 13 (12): 4401–13. DOI:10.1091/mbc.E02-07-0450. ISSN 1059-1524. PMC 138642. PMID 12475961.
- ↑ Dechat, T; Korbei B, Vaughan O A, Vlcek S, Hutchison C J, Foisner R (October 2000). „Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins”. J. Cell. Sci. (ENGLAND) 113 (19): 3473–84. ISSN 0021-9533. PMID 10984438.
Literatura
- Harris CA, Andryuk PJ, Cline SW, Mathew S, Siekierka JJ, Goldstein G (1995). „Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2”. Genomics 28 (2): 198–205. DOI:10.1006/geno.1995.1131. PMID 8530026.
- Dechat T, Vlcek S, Foisner R (2000). „Review: lamina-associated polypeptide 2 isoforms and related proteins in cell cycle-dependent nuclear structure dynamics.”. J. Struct. Biol. 129 (2-3): 335–45. DOI:10.1006/jsbi.2000.4212. PMID 10806084.
- Twomey JJ, Goldstein G, Lewis VM, et al. (1977). „Bioassay determinations of thymopoietin and thymic hormone levels in human plasma.”. Proc. Natl. Acad. Sci. U.S.A. 74 (6): 2541–5. DOI:10.1073/pnas.74.6.2541. PMC 432209. PMID 302007.
- Heavner GA, Audhya T, Goldstein G (1990). „Peptide analogs of thymopentin distinguish distinct thymopoietin receptor specificities on two human T cell lines.”. Regul. Pept. 27 (2): 257–62. DOI:10.1016/0167-0115(90)90044-W. PMID 2158125.
- Fuccello A, Audhya T, Talle MA, Goldstein G (1984). „Immunoassay for bovine serum thymopoietin: discrimination from splenin by monoclonal antibodies.”. Arch. Biochem. Biophys. 228 (1): 292–8. DOI:10.1016/0003-9861(84)90070-5. PMID 6364989.
- Hara H, Hayashi K, Ohta K, et al. (1995). „A new thymopoietin precursor gene from human thymus.”. Biochem. Mol. Biol. Int. 34 (5): 927–33. PMID 7703909.
- Goldstein G, Schlesinger DH, Audhya T (1994). „Isolation and complete amino acid sequence of human thymopoietin and splenin.”. Proc. Natl. Acad. Sci. U.S.A. 91 (13): 6249. DOI:10.1073/pnas.91.13.6249. PMC 44176. PMID 8016147.
- Harris CA, Andryuk PJ, Cline SW, et al. (1996). „Structure and mapping of the human thymopoietin (TMPO) gene and relationship of human TMPO beta to rat lamin-associated polypeptide 2.”. Genomics 28 (2): 198–205. DOI:10.1006/geno.1995.1131. PMID 8530026.
- Andersson B, Wentland MA, Ricafrente JY, et al. (1996). „A "double adaptor" method for improved shotgun library construction.”. Anal. Biochem. 236 (1): 107–13. DOI:10.1006/abio.1996.0138. PMID 8619474.
- Berger R, Theodor L, Shoham J, et al. (1996). „The characterization and localization of the mouse thymopoietin/lamina-associated polypeptide 2 gene and its alternatively spliced products.”. Genome Res. 6 (5): 361–70. DOI:10.1101/gr.6.5.361. PMID 8743987.
- Yu W, Andersson B, Worley KC, et al. (1997). „Large-scale concatenation cDNA sequencing.”. Genome Res. 7 (4): 353–8. DOI:10.1101/gr.7.4.353. PMC 139146. PMID 9110174.
- Furukawa K, Fritze CE, Gerace L (1998). „The major nuclear envelope targeting domain of LAP2 coincides with its lamin binding region but is distinct from its chromatin interaction domain.”. J. Biol. Chem. 273 (7): 4213–9. DOI:10.1074/jbc.273.7.4213. PMID 9461618.
- Furukawa K, Kondo T (1998). „Identification of the lamina-associated-polypeptide-2-binding domain of B-type lamin.”. Eur. J. Biochem. 251 (3): 729–33. DOI:10.1046/j.1432-1327.1998.2510729.x. PMID 9490046.
- Dechat T, Gotzmann J, Stockinger A, et al. (1998). „Detergent-salt resistance of LAP2alpha in interphase nuclei and phosphorylation-dependent association with chromosomes early in nuclear assembly implies functions in nuclear structure dynamics.”. EMBO J. 17 (16): 4887–902. DOI:10.1093/emboj/17.16.4887. PMC 1170818. PMID 9707448.
- Furukawa K (1999). „LAP2 binding protein 1 (L2BP1/BAF) is a candidate mediator of LAP2-chromatin interaction.”. J. Cell. Sci. 112 (15): 2485–92. PMID 10393804.
- Weber PJ, Eckhard CP, Gonser S, et al. (1999). „On the role of thymopoietins in cell proliferation. Immunochemical evidence for new members of the human thymopoietin family.”. Biol. Chem. 380 (6): 653–60. DOI:10.1515/BC.1999.081. PMID 10430029.
- Dechat T, Korbei B, Vaughan OA, et al. (2000). „Lamina-associated polypeptide 2alpha binds intranuclear A-type lamins.”. J. Cell. Sci. 113 (19): 3473–84. PMID 10984438.
- Martins SB, Eide T, Steen RL, et al. (2001). „HA95 is a protein of the chromatin and nuclear matrix regulating nuclear envelope dynamics.”. J. Cell. Sci. 113 (21): 3703–13. PMID 11034899.
Spoljašnje veze
- MeSH Thymopoietins
- p
- r
- u
PDB Galerija
|
