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PTMA (prothymosin, alpha)

Written2009-01Koji Tanaka, Masato Kusunoki
Departments of Gastrointestinal & Pediatric Surgery, Division of Reparative Medicine, Institute of Life Sciences, Mie University Graduate School of Medicine, 2-174 Edobashi, Tsu, Mie 514-8507, Japan

(Note : for Links provided by Atlas : click)

Identity

Alias_namesTMSA
prothymosin
Other aliasMGC104802
HGNC (Hugo) PTMA
LocusID (NCBI) 5757
Atlas_Id 44094
Location 2q37.1  [Link to chromosome band 2q37]
Location_base_pair Starts at 232573235 and ends at 232578250 bp from pter ( according to hg19-Feb_2009)  [Mapping PTMA.png]
Fusion genes
(updated 2016)
ANP32E (1q21.2) / PTMA (2q37.1)ATP5B (12q13.3) / PTMA (2q37.1)C6orf48 (6p21.33) / PTMA (2q37.1)
CNOT2 (12q15) / PTMA (2q37.1)HMGB2 (4q34.1) / PTMA (2q37.1)HNRNPA2B1 (7p15.2) / PTMA (2q37.1)
HTATSF1 (Xq26.3) / PTMA (2q37.1)JA040725 () / PTMA (2q37.1)MINOS1 (1p36.13) / PTMA (2q37.1)
MTA2 (11q12.3) / PTMA (2q37.1)NCL (2q37.1) / PTMA (2q37.1)NPM1 (5q35.1) / PTMA (2q37.1)
P4HB (17q25.3) / PTMA (2q37.1)PTMA (2q37.1) / ANKRD28 (3p25.1)PTMA (2q37.1) / ATP6V0B (1p34.1)
PTMA (2q37.1) / CASC3 (17q21.1)PTMA (2q37.1) / CREM (10p11.21)PTMA (2q37.1) / DZIP3 (3q13.13)
PTMA (2q37.1) / PBX3 (9q33.3)PTMA (2q37.1) / PPIE (1p34.2)PTMA (2q37.1) / PPIL2 (22q11.21)
PTMA (2q37.1) / PTMA (2q37.1)PTMA (2q37.1) / PTMS (12p13.31)PTMA (2q37.1) / ZNF236 (18q23)
RRP12 (10q24.1) / PTMA (2q37.1)SF3B2 (11q13.1) / PTMA (2q37.1)SLC39A6 (18q12.2) / PTMA (2q37.1)
SMARCA4 (19p13.2) / PTMA (2q37.1)THSD4 (15q23) / PTMA (2q37.1)TRIM63 (1p36.11) / PTMA (2q37.1)
ZKSCAN5 (7q22.1) / PTMA (2q37.1)
Note Initially, the rat PTMA was isolated from fresh rat thymus, which contains the thymosin-alpha-1 sequence at its NH2 terminus (Haritos et al., 1984). A cDNA library from human spleen mRNA was constructed and screened for clones containing cDNAs coding for human PTMA (Goodall et al., 1986). A cDNA clones for human PTMA was also identified in cDNA libraries from staphylococcal endotoxin A-stimulated normal human lymphocytes (Eschenfeldt et al., 1986). Szabo et al. isolated a genomic clone encoding human PTMA with the 5'-regulatory region (Szabo et al., 1993). They used this 5'-flanking cloned probe, and then confirmed that human genomic PTMA gene was localized to chromosome 2.

DNA/RNA

Description The human PTMA cDNA sequence has an open reading frame that was more than 90% identical to the rat PTMA gene, with significant homology extending into the 5' and 3' flanking regions (Frangou-Lazaridis et al., 1988).
NM_001099285.1, NP_001092755.1 prothymosin, alpha isoform 1; NM_002823.4, NP_002814.3 prothymosin, alpha isoform 2: Two named isoforms [FASTA] produced by alternative splicing.
Pseudogene The six members of the human PTMA gene family have been cloned and sequenced. One gene (PTMA) was functional, and the remaining five genes are processed pseudogenes (Manrow et al., 1992).

Protein

Description PTMA is a small, 12.4 kDa protein. It is a 109-111 amino acid long polypeptide as the precursor of thymosin alpha-1. The encoded human PTMA protein is a highly acidic (54 residues out of 111) and shared over 90% sequence homology with rat PTMA. The primary structure of PTMA is highly conserved and shows a number of important features. The first 28 amino acids of its sequence correspond to those of thymosin-alpha-1. It has a central acidic region (residues 41-85) comprising of glutamic and aspartic residues. Neither type of secondary structure has been detected. Thymosin-alpha-1 appeared at positions 2-29 of the PTMA.
Localisation Subcellular location:
Nucleus: Normally, PTMA protein can be seen in nuclei of normal cells in various mammalian tissues (Haritos et al., 1984; Clinton et al., 1991; Palvimo et al., 1990; Manrow et al., 1991; Watts et al., 1989). PTMA is an abundant mammalian acid nuclear protein. Most intracellular PTMA protein appears in the nucleus, which may correlated with increased proliferation as measured by expression of Ki67 nuclear antigen.
Cytoplasm: PTMA protein is also detected in the cytoplasm. PTMA transports between the nucleus and neighbouring cytoplasm. PTMA is a cytosol protein with functions such as anti-apoptosis (Jiang et al., 2003).
Function Summary
PTMA has been shown to serve essential biological functions. However, its exact physiologic roles remain to be elucidated. In general, PTMA is associated with cellular proliferation and carcinogenesis (Eschenfeldt et al., 1986), cellular and viral transcription (Cotter et al., 2000), protection against apoptosis and chromatin remodelling (Karetsou et al., 1998).
PTMA may have a dual role both intracellulary and extracellulary.
The intracellular roles of PTMA are 1) cell proliferation / differentiation, 2) chromatin remodelling, 3) antiapoptotic activity through inhibition of apoptosome formation, and so on.
The extracellular roles of PTMA are 1) immunoenhancing activity by stimulating immune responses, and so forth.
Intracellularly, PTMA acts both in the nucleus (Manrow et al., 1991) and in the cytoplasm. Both nuclear and cytoplasmic PTMA play central roles in cellular functions due to its subcellular localization.
In the nucleus, PTMA affects the activity of several gene transcriptions. It plays an important role in transcription regulation. PTMA promote transcriptional activity of the estrogen receptor (ER) by sequestering a repressor of ER from the ER complex (Martini et al., 2000). PTMA binds to histone H1 known as a major regulator of chromatin structure (Díaz-Jullien et al., 1996) and cooperates in nucleosome assembly relating to chromatin remodelling (Gomez-Marquez et al., 1998). The effect of PTMA on chromatin remodelling is mediated, at least partially, through histone acetyltransferases.
In the cytoplasm, PTMA is involved in protection against apoptosis. It negatively regulates proapoptotic pathways (Jiang et al., 2003). PTMA has a significant antiapoptotic role in the cytoplasm by directly inhibiting the apoptosome, a complex in the execution of apoptosis. PTMA inhibits caspase 9 activation by blocking apoptosome formation.
Extracellularly, PTMA induces T cell maturation, differentiation and in vitro proliferation in response to soluble and cellular antigens (Baxevanis et al., 1990). PTMA demonstrated to present distinct immunoenhancing activity, stimulating immune responses in vitro and in vivo.
Cell proliferation / differentiation
Many previous reports clearly show that PTMA participates in developmental processes like cell proliferation and/or differentiation (Dosil et al., 1990). PTMA is required for cell division, growth, and survival (Piñeiro et al., 2000). It is also up-regulated in proliferating, transcriptionally active cells. PTMA gene level is elevated in normal proliferating tissue, but repressed in quiescent cells.
PTMA is correlated with increased proliferation as measured by expression of Ki67 nuclear antigen (Bianco et al., 2002) and proliferating cell nuclear antigen (PCNA) (Roson et al., 1993). PTMA is established as a proliferation marker.
Chromatin remodelling
PTMA interacts with histones and affects chromatin remodelling processes. PTMA binds to histone H1 known as a major regulator of chromatin structure (Díaz-Jullien et al., 1996) and cooperates in nucleosome assembly relating to chromatin remodelling (Gomez-Marquez et al., 1998). PTMA is involved in transcriptional regulation of histone acetylation. The effect of PTMA on chromatin remodelling is mediated, at least partially, through histone acetyltransferases.
Structurally, the interaction between PTMA and histones can be explained by the presence of its highly acidic domain (aspartate/glutamate between residues 41 and 85). The first 28 amino acids in the PTMA sequence can also bind core histones with high affinity in vitro.
Anti-apoptosis / Negative regulation of caspase activity
The antiapoptotic activity of PTMA occurs through inhibition of apoptosome formation. PTMA negatively regulated caspase-9 activation by inhibiting apoptosome formation (Jiang et al., 2003). Elimination of PTMA expression by RNA interference sensitized cells to ultraviolet irradiation-induced apoptosis.
Immunoregulatory role of PTMA
PTMA has been reported to exert in vitro immunomodulatory effects on autoimmune diseases. PTMA demonstrated to present distinct immunoenhancing activity, stimulating immune responses in vitro and in vivo.
PTMA induces T cell maturation, differentiation and in vitro proliferation in response to soluble and cellular antigens (Baxevanis et al., 1990). PTMA upregulates MHC class II gene expression in various cell types, including tumor cell lines (Baxevanis et al., 1992). PTMA may also mediate immune function by conferring resistance to certain opportunistic infections.
Radiation resistance
Recently, the association between PTMA expression and radiation resistance has been reported (Ojima et al., 2007). PTMA was significantly up-regulated in radioresistant human colon cancer cell lines. Among rectal cancer patients who treated with preoperative chemoradiotherapy, PTMA expression was significantly higher in non-responders who didn't histologically respond to chemoradiotharapy.
These lines of evidence indicate that PTMA may be a novel marker for predicting radiotherapy response.
Regulation
E2F (Vareli et al., 1996) and c-myc (Eilers et al., 1991) are important transcription factors that positively regulate the PTMA gene promoter.
E2F is one of the important transcription factors known to regulate cell cycle and cell proliferation (Vareli et al., 1996). E2F can activate the PTMA promoter and induces PTMA.
C-myc is one of significant proto-oncogenes implicating in normal proliferation and cell transformation. The transcriptional activation of c-myc leads to an increase in the level of transcription of PTMA. PTMA is a transcriptional target of c-myc. C-myc directly regulates the expression of PTMA gene by binding to the E-box of its promoter (Gaubatz et al., 1994). PTMA mRNA levels vary with c-myc expression during tissue proliferation, viral infection, and heat shock (Vareli et al., 1995). PTMA is considered as a downstream effector of the c-myc signalling pathway.
Oncogenic properties
PTMA has a capability of transforming rodent fibroblast cells like in a manner similar to Ras (Orre et al., 2001). PTMA is capable of inducing significant feature of transformed cells. Increased PTMA expression accelerate cellular proliferation. Because of its proliferative activity and overexpression in human cancers, PTMA may function as a cellular oncogene. Overexpression of c-myc, proto-oncogene stimulates cell cycle progression, cell proliferation, and induces cell transformation. Increased c-myc mRNA leads to an increase in PTMA mRNA. PTMA expression correlated with c-myc expression in human colon (Shiwa et al., 2003; Mori et al., 1993) and hepatocellular carcinoma (Wu et al., 1997). In addition, PTMA inhibits apoptosis by preventing formation of the apoptosose (Jiang et al., 2003). The observation that PTMA is a negative regulator of apoptosis indicates that it is a transforming oncoprotein and that its overexpression is associated with human cancers. Although PTMA does not have sequence homology to any other known oncogenes such as ras, it is considered as a growth-promoting and anti-apoptotic oncoprotein.
Homology PTMA is highly conserved and broadly distributed in mammalian tissues.

Implicated in

Note
Note PTMA has been reported to present in various human malignancies. PTMA expression is higher in human cancer tissues than in adjacent normal tissues. Therefore, it may be considered as an oncoprotein or novel tumor marker. In several human cancers, PTMA expression has been related to cancer development, progression, and survival.
  
  
Entity Breast cancer
Prognosis PTMA expression is higher in breast cancer tissue than in normal breast tissue (Tsitsilonis et al., 1998). It correlates with proliferation status and metastatic potential of breast cancer (Dominguez et al., 1993; Magdalena et al., 2000). PTMA levels correlated with the number of positive axillary lymph nodes, risk of tumor recurrence and survival. PTMA is considered as a prognostic factor in breast cancer (Traub et al., 2006).
  
  
Entity Bladder cancer
Note Increased PTMA expression was found in human bladder cancers compared with the paired normal adjacent bladder tissue (Tsai et al., 2009).
  
  
Entity Lung cancer
Prognosis PTMA mRNA levels in lung cancer tissues were higher than those in normal lung tissues. PTMA overexpression in lung cancer was correlated with a poor prognosis (Sasaki et al., 2001a).
  
  
Entity Gastric cancer
Note PTMA is overexpressed in gastric adenocarcinoma (Wang et al., 2007; Leys et al., 2007).
  
  
Entity Thyroid cancer
Note PTMA mRNA levels were found significantly elevated in well-differentiated carcinomas in relation to adenomas and goitres, an event possibly linked to the proliferation activity of thyroid follicular cells (Letsas et al., 2007).
  
  
Entity Neuroblastoma
Prognosis PTMA mRNA levels were significantly correlated with proto-oncogene, N-myc, which is associated with more malignant behavior of neuroblastoma (Sasaki et al., 2001b).
  
  
Entity Hepatocellular carcinoma
Note PTMA mRNA levels were two- to 9.2-fold higher in tumoral tissues than in adjacent non-tumoral tissues in 14 of 17 patients with HCC (Wu et al., 1997). PTMA mRNA levels were significantly correlated with c-myc mRNA levels suggesting that such correlation is possibly involved in the tumorigenic process.
  
  
Entity Prostate cancer
Note PTMA expression is involved in the differentiation and progression of human prostate cancers (Suzuki et al., 2006).
  
  
Entity Colorectal cancers
Note PTMA was overexpressed in human colorectal cancers compared with adjacent normal tissues. There was a significant correlation between the PTMA expression and c-myc expression (Shiwa et al., 2003; Mori et al., 1993).
  

Bibliography

Prothymosin alpha enhances human and murine MHC class II surface antigen expression and messenger RNA accumulation.
Baxevanis CN, Thanos D, Reclos GJ, Anastasopoulos E, Tsokos GC, Papamatheakis J, Papamichail M.
J Immunol. 1992 Apr 1;148(7):1979-84.
PMID 1545115
 
Regulation of prothymosin alpha by estrogen receptor alpha: molecular mechanisms and relevance in estrogen-mediated breast cell growth.
Bianco NR, Montano MM.
Oncogene. 2002 Aug 8;21(34):5233-44.
PMID 12149645
 
Evidence for nuclear targeting of prothymosin and parathymosin synthesized in situ.
Clinton M, Graeve L, el-Dorry H, Rodriguez-Boulan E, Horecker BL.
Proc Natl Acad Sci U S A. 1991 Aug 1;88(15):6608-12.
PMID 1862085
 
Modulation of histone acetyltransferase activity through interaction of epstein-barr nuclear antigen 3C with prothymosin alpha.
Cotter MA 2nd, Robertson ES.
Mol Cell Biol. 2000 Aug;20(15):5722-35.
PMID 10891508
 
Prothymosin alpha binds histones in vitro and shows activity in nucleosome assembly assay.
Diaz-Jullien C, Perez-Estevez A, Covelo G, Freire M.
Biochim Biophys Acta. 1996 Sep 5;1296(2):219-27.
PMID 8814229
 
Tissue concentrations of prothymosin alpha: a novel proliferation index of primary breast cancer.
Dominguez F, Magdalena C, Cancio E, Roson E, Paredes J, Loidi L, Zalvide J, Fraga M, Forteza J, Regueiro BJ, et al.
Eur J Cancer. 1993;29A(6):893-7.
PMID 8387320
 
Tissue-specific and differential expression of prothymosin alpha gene during rat development.
Dosil M, Freire M, Gomez-Marquez J.
FEBS Lett. 1990 Sep 3;269(2):373-6.
PMID 15452976
 
The MYC protein activates transcription of the alpha-prothymosin gene.
Eilers M, Schirm S, Bishop JM.
EMBO J. 1991 Jan;10(1):133-41.
PMID 1989881
 
The human prothymosin alpha gene is polymorphic and induced upon growth stimulation: evidence using a cloned cDNA.
Eschenfeldt WH, Berger SL.
Proc Natl Acad Sci U S A. 1986 Dec;83(24):9403-7.
PMID 3467312
 
Prothymosin alpha and parathymosin: amino acid sequences deduced from the cloned rat spleen cDNAs.
Frangou-Lazaridis M, Clinton M, Goodall GJ, Horecker BL.
Arch Biochem Biophys. 1988 Jun;263(2):305-10.
PMID 3377505
 
An E-box element localized in the first intron mediates regulation of the prothymosin alpha gene by c-myc.
Gaubatz S, Meichle A, Eilers M.
Mol Cell Biol. 1994 Jun;14(6):3853-62.
PMID 8196628
 
Prothymosin alpha is a chromatin-remodelling protein in mammalian cells.
Gomez-Marquez J, Rodriguez P.
Biochem J. 1998 Jul 1;333 ( Pt 1):1-3.
PMID 9639554
 
Molecular cloning of cDNA for human prothymosin alpha.
Goodall GJ, Dominguez F, Horecker BL.
Proc Natl Acad Sci U S A. 1986 Dec;83(23):8926-8.
PMID 3466166
 
Prothymosin alpha: isolation and properties of the major immunoreactive form of thymosin alpha 1 in rat thymus.
Haritos AA, Goodall GJ, Horecker BL.
Proc Natl Acad Sci U S A. 1984 Feb;81(4):1008-11.
PMID 6583693
 
Distinctive roles of PHAP proteins and prothymosin-alpha in a death regulatory pathway.
Jiang X, Kim HE, Shu H, Zhao Y, Zhang H, Kofron J, Donnelly J, Burns D, Ng SC, Rosenberg S, Wang X.
Science. 2003 Jan 10;299(5604):223-6.
PMID 12522243
 
Prothymosin alpha modulates the interaction of histone H1 with chromatin.
Karetsou Z, Sandaltzopoulos R, Frangou-Lazaridis M, Lai CY, Tsolas O, Becker PB, Papamarcaki T.
Nucleic Acids Res. 1998 Jul 1;26(13):3111-8.
PMID 9628907
 
Fine-needle aspiration biopsy-RT-PCR expression analysis of prothymosin alpha and parathymosin in thyroid: novel proliferation markers?
Letsas KP, Vartholomatos G, Tsepi C, Tsatsoulis A, Frangou-Lazaridis M.
Neoplasma. 2007;54(1):57-62.
PMID 17203893
 
Expression and prognostic significance of prothymosin-alpha and ERp57 in human gastric cancer.
Leys CM, Nomura S, LaFleur BJ, Ferrone S, Kaminishi M, Montgomery E, Goldenring JR.
Surgery. 2007 Jan;141(1):41-50. Epub 2006 Aug 14.
PMID 17188166
 
Tumour prothymosin alpha content, a potential prognostic marker for primary breast cancer.
Magdalena C, Dominguez F, Loidi L, Puente JL.
Br J Cancer. 2000 Feb;82(3):584-90.
PMID 10682670
 
The human prothymosin alpha gene family contains several processed pseudogenes lacking deleterious lesions.
Manrow RE, Leone A, Krug MS, Eschenfeldt WH, Berger SL.
Genomics. 1992 Jun;13(2):319-31.
PMID 1612591
 
Nuclear targeting of prothymosin alpha.
Manrow RE, Sburlati AR, Hanover JA, Berger SL.
J Biol Chem. 1991 Feb 25;266(6):3916-24.
PMID 1899869
 
Prothymosin alpha selectively enhances estrogen receptor transcriptional activity by interacting with a repressor of estrogen receptor activity.
Martini PG, Delage-Mourroux R, Kraichely DM, Katzenellenbogen BS.
Mol Cell Biol. 2000 Sep;20(17):6224-32.
PMID 10938099
 
Prothymosin-alpha mRNA expression correlates with that of c-myc in human colon cancer.
Mori M, Barnard GF, Staniunas RJ, Jessup JM, Steele GD Jr, Chen LB.
Oncogene. 1993 Oct;8(10):2821-6.
PMID 8378090
 
Effectiveness of gene expression profiling for response prediction of rectal cancer to preoperative radiotherapy.
Ojima E, Inoue Y, Miki C, Mori M, Kusunoki M.
J Gastroenterol. 2007 Sep;42(9):730-6. Epub 2007 Sep 25.
PMID 17876542
 
Prothymosin alpha functions as a cellular oncoprotein by inducing transformation of rodent fibroblasts in vitro.
Orre RS, Cotter MA 2nd, Subramanian C, Robertson ES.
J Biol Chem. 2001 Jan 19;276(3):1794-9. Epub 2000 Oct 17.
PMID 11036085
 
Identification of a low-Mr acidic nuclear protein as prothymosin alpha.
Palvimo J, Linnala-Kankkunen A.
FEBS Lett. 1990 Dec 17;277(1-2):257-60.
PMID 2269362
 
Fifteen years of prothymosin alpha: contradictory past and new horizons.
Pineiro A, Cordero OJ, Nogueira M.
Peptides. 2000 Sep;21(9):1433-46.
PMID 11072132
 
Evolution of prothymosin alpha and proliferating cell nuclear antigen (PCNA) immunoreactivity through the development of rat ovarian follicles.
Roson E, Gallego R, Garcia-Caballero T, Fraga M, Dominguez F, Beiras A.
Histochem J. 1993 Jul;25(7):497-501.
PMID 8104916
 
Expression of the prothymosin-a gene as a prognostic factor in lung cancer.
Sasaki H, Nonaka M, Fujii Y, Yamakawa Y, Fukai I, Kiriyama M, Sasaki M.
Surg Today. 2001a;31(10):936-8.
PMID 11759895
 
Expression of the prothymosin alpha mRNA correlated with that of N-myc in neuroblastoma.
Sasaki H, Sato Y, Kondo S, Fukai I, Kiriyama M, Yamakawa Y, Fujii Y.
Cancer Lett. 2001b Jul 26;168(2):191-5.
PMID 11403924
 
Rapid discovery and identification of a tissue-specific tumor biomarker from 39 human cancer cell lines using the SELDI ProteinChip platform.
Shiwa M, Nishimura Y, Wakatabe R, Fukawa A, Arikuni H, Ota H, Kato Y, Yamori T.
Biochem Biophys Res Commun. 2003 Sep 12;309(1):18-25.
PMID 12943657
 
Expression of prothymosin alpha is correlated with development and progression in human prostate cancers.
Suzuki S, Takahashi S, Takahashi S, Takeshita K, Hikosaka A, Wakita T, Nishiyama N, Fujita T, Okamura T, Shirai T.
Prostate. 2006 Apr 1;66(5):463-9.
PMID 16353248
 
Prothymosin alpha gene in humans: organization of its promoter region and localization to chromosome 2.
Szabo P, Panneerselvam C, Clinton M, Frangou-Lazaridis M, Weksler D, Whittington E, Macera MJ, Grzeschik KH, Selvakumar A, Horecker BL.
Hum Genet. 1993 Feb;90(6):629-34.
PMID 7916742
 
Peptidomic analysis of breast cancer reveals a putative surrogate marker for estrogen receptor-negative carcinomas.
Traub F, Jost M, Hess R, Schorn K, Menzel C, Budde P, Schulz-Knappe P, Lamping N, Pich A, Kreipe H, Tammen H.
Lab Invest. 2006 Mar;86(3):246-53.
PMID 16485008
 
Aberrant Prothymosin-alpha Expression in Human Bladder Cancer.
Tsai YS, Jou YC, Lee GF, Chen YC, Shiau AL, Tsai HT, Wu CL, Tzai TS.
Urology. 2009 Jan;73(1):188-92. Epub 2008 Aug 9.
PMID 18692879
 
The prognostic value of alpha-thymosins in breast cancer.
Tsitsilonis OE, Bekris E, Voutsas IF, Baxevanis CN, Markopoulos C, Papadopoulou SA, Kontzoglou K, Stoeva S, Gogas J, Voelter W, Papamichail M.
Anticancer Res. 1998 May-Jun;18(3A):1501-8.
PMID 9673361
 
Prothymosin alpha mRNA levels vary with c-myc expression during tissue proliferation, viral infection and heat shock.
Vareli K, Frangou-Lazaridis M, Tsolas O.
FEBS Lett. 1995 Sep 11;371(3):337-40.
PMID 7556624
 
Regulation of prothymosin alpha during the cell cycle.
Vareli K, Tsolas O, Frangou-Lazaridis M.
Eur J Biochem. 1996 Jun 15;238(3):799-806.
PMID 8706683
 
Altered expression of estrogen receptor alpha and beta in advanced gastric adenocarcinoma: correlation with prothymosin alpha and clinicopathological parameters.
Wang M, Pan JY, Song GR, Chen HB, An LJ, Qu SX.
Eur J Surg Oncol. 2007 Mar;33(2):195-201. Epub 2006 Oct 13.
PMID 17046193
 
Prothymosin alpha is a nuclear protein.
Watts JD, Cary PD, Crane-Robinson C.
FEBS Lett. 1989 Mar 13;245(1-2):17-20.
PMID 2924919
 
Overexpression of hepatic prothymosin alpha, a novel marker for human hepatocellular carcinoma.
Wu CG, Habib NA, Mitry RR, Reitsma PH, van Deventer SJ, Chamuleau RA.
Br J Cancer. 1997;76(9):1199-204.
PMID 9365169
 

Citation

This paper should be referenced as such :
Tanaka, K ; Kusunoki, M
PTMA (prothymosin, alpha)
Atlas Genet Cytogenet Oncol Haematol. 2009;13(12):963-967.
Free journal version : [ pdf ]   [ DOI ]
On line version : http://AtlasGeneticsOncology.org/Genes/PTMAID44094ch2q37.html


Other Solid tumors implicated (Data extracted from papers in the Atlas) [ 1 ]
  Liver tumors: an overview


External links

Nomenclature
HGNC (Hugo)PTMA   9623
Cards
AtlasPTMAID44094ch2q37
Entrez_Gene (NCBI)PTMA  5757  prothymosin, alpha
AliasesTMSA
GeneCards (Weizmann)PTMA
Ensembl hg19 (Hinxton)ENSG00000187514 [Gene_View]  chr2:232573235-232578250 [Contig_View]  PTMA [Vega]
Ensembl hg38 (Hinxton)ENSG00000187514 [Gene_View]  chr2:232573235-232578250 [Contig_View]  PTMA [Vega]
ICGC DataPortalENSG00000187514
TCGA cBioPortalPTMA
AceView (NCBI)PTMA
Genatlas (Paris)PTMA
WikiGenes5757
SOURCE (Princeton)PTMA
Genetics Home Reference (NIH)PTMA
Genomic and cartography
GoldenPath hg19 (UCSC)PTMA  -     chr2:232573235-232578250 +  2q37.1   [Description]    (hg19-Feb_2009)
GoldenPath hg38 (UCSC)PTMA  -     2q37.1   [Description]    (hg38-Dec_2013)
EnsemblPTMA - 2q37.1 [CytoView hg19]  PTMA - 2q37.1 [CytoView hg38]
Mapping of homologs : NCBIPTMA [Mapview hg19]  PTMA [Mapview hg38]
OMIM188390   
Gene and transcription
Genbank (Entrez)AF348514 AF452640 AK223605 AK314106 AY169282
RefSeq transcript (Entrez)NM_001099285 NM_002823
RefSeq genomic (Entrez)NC_000002 NC_018913 NT_005403 NW_004929305
Consensus coding sequences : CCDS (NCBI)PTMA
Cluster EST : UnigeneHs.459927 [ NCBI ]
CGAP (NCI)Hs.459927
Alternative Splicing GalleryENSG00000187514
Gene ExpressionPTMA [ NCBI-GEO ]   PTMA [ EBI - ARRAY_EXPRESS ]   PTMA [ SEEK ]   PTMA [ MEM ]
Gene Expression Viewer (FireBrowse)PTMA [ Firebrowse - Broad ]
SOURCE (Princeton)Expression in : [Datasets]   [Normal Tissue Atlas]  [carcinoma Classsification]  [NCI60]
GenevisibleExpression in : [tissues]  [cell-lines]  [cancer]  [perturbations]  
BioGPS (Tissue expression)5757
GTEX Portal (Tissue expression)PTMA
Protein : pattern, domain, 3D structure
UniProt/SwissProtP06454   [function]  [subcellular_location]  [family_and_domains]  [pathology_and_biotech]  [ptm_processing]  [expression]  [interaction]
NextProtP06454  [Sequence]  [Exons]  [Medical]  [Publications]
With graphics : InterProP06454
Splice isoforms : SwissVarP06454
PhosPhoSitePlusP06454
Domains : Interpro (EBI)Pro/parathymosin   
Domain families : Pfam (Sanger)Prothymosin (PF03247)   
Domain families : Pfam (NCBI)pfam03247   
Conserved Domain (NCBI)PTMA
DMDM Disease mutations5757
Blocks (Seattle)PTMA
PDB (SRS)2L9I    2MNQ   
PDB (PDBSum)2L9I    2MNQ   
PDB (IMB)2L9I    2MNQ   
PDB (RSDB)2L9I    2MNQ   
Structural Biology KnowledgeBase2L9I    2MNQ   
SCOP (Structural Classification of Proteins)2L9I    2MNQ   
CATH (Classification of proteins structures)2L9I    2MNQ   
SuperfamilyP06454
Human Protein AtlasENSG00000187514
Peptide AtlasP06454
HPRD01778
IPIIPI00455510   IPI00917401   IPI00916480   IPI00916962   
Protein Interaction databases
DIP (DOE-UCLA)P06454
IntAct (EBI)P06454
FunCoupENSG00000187514
BioGRIDPTMA
STRING (EMBL)PTMA
ZODIACPTMA
Ontologies - Pathways
QuickGOP06454
Ontology : AmiGOprotein binding  nucleus  nucleoplasm  cytoplasm  transcription, DNA-templated  extracellular exosome  
Ontology : EGO-EBIprotein binding  nucleus  nucleoplasm  cytoplasm  transcription, DNA-templated  extracellular exosome  
Pathways : KEGGEpstein-Barr virus infection   
NDEx NetworkPTMA
Atlas of Cancer Signalling NetworkPTMA
Wikipedia pathwaysPTMA
Orthology - Evolution
OrthoDB5757
GeneTree (enSembl)ENSG00000187514
Phylogenetic Trees/Animal Genes : TreeFamPTMA
HOVERGENP06454
HOGENOMP06454
Homologs : HomoloGenePTMA
Homology/Alignments : Family Browser (UCSC)PTMA
Gene fusions - Rearrangements
Fusion Cancer (Beijing)JA040725 [PTMA]  -  2q37.1 [FUSC000670]  [FUSC000670]  [FUSC000670]  [FUSC000670]  [FUSC000670]  [FUSC000670]
Fusion Cancer (Beijing)NCL [2q37.1]  -  PTMA [2q37.1]  [FUSC001210]
Polymorphisms : SNP and Copy number variants
NCBI Variation ViewerPTMA [hg38]
dbSNP Single Nucleotide Polymorphism (NCBI)PTMA
dbVarPTMA
ClinVarPTMA
1000_GenomesPTMA 
Exome Variant ServerPTMA
ExAC (Exome Aggregation Consortium)PTMA (select the gene name)
Genetic variants : HAPMAP5757
Genomic Variants (DGV)PTMA [DGVbeta]
DECIPHER (Syndromes)2:232573235-232578250  ENSG00000187514
CONAN: Copy Number AnalysisPTMA 
Mutations
ICGC Data PortalPTMA 
TCGA Data PortalPTMA 
Broad Tumor PortalPTMA
OASIS PortalPTMA [ Somatic mutations - Copy number]
Somatic Mutations in Cancer : COSMICPTMA  [overview]  [genome browser]  [tissue]  [distribution]  
Mutations and Diseases : HGMDPTMA
LOVD (Leiden Open Variation Database)Whole genome datasets
LOVD (Leiden Open Variation Database)LOVD 3.0 shared installation
BioMutasearch PTMA
DgiDB (Drug Gene Interaction Database)PTMA
DoCM (Curated mutations)PTMA (select the gene name)
CIViC (Clinical Interpretations of Variants in Cancer)PTMA (select a term)
intoGenPTMA
NCG5 (London)PTMA
Cancer3DPTMA(select the gene name)
Impact of mutations[PolyPhen2] [SIFT Human Coding SNP] [Buck Institute : MutDB] [Mutation Assessor] [Mutanalyser]
Diseases
OMIM188390   
Orphanet
MedgenPTMA
Genetic Testing Registry PTMA
NextProtP06454 [Medical]
TSGene5757
GENETestsPTMA
Huge Navigator PTMA [HugePedia]
snp3D : Map Gene to Disease5757
BioCentury BCIQPTMA
ClinGenPTMA
Clinical trials, drugs, therapy
Chemical/Protein Interactions : CTD5757
Chemical/Pharm GKB GenePA33966
Clinical trialPTMA
Miscellaneous
canSAR (ICR)PTMA (select the gene name)
Probes
Litterature
PubMed100 Pubmed reference(s) in Entrez
GeneRIFsGene References Into Functions (Entrez)
CoreMinePTMA
EVEXPTMA
GoPubMedPTMA
iHOPPTMA
REVIEW articlesautomatic search in PubMed
Last year publicationsautomatic search in PubMed

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