HSPA1B

HSPA1B
PDBに登録されている構造
PDB	オルソログ検索: RCSB PDBe PDBj
PDBのIDコード一覧
	1HJO, 1S3X, 1XQS, 2E88, 2E8A, 2LMG, 3A8Y, 3ATU, 3ATV, 3AY9, 3D2E, 3D2F, 3JXU, 3LOF, 4IO8, 4J8F, 4PO2, 4WV5, 4WV7, 5AR0, 5AQZ, 3Q49,%%s3D2E
識別子
記号	HSPA1B, HSP70-1B, HSP70-2, HSP70.2, heat shock protein family A (Hsp70) member 1B, HSX70, HSPA1, HSP70-1, HSP72, HSP70.1
外部ID	OMIM: 603012 MGI: 96244 HomoloGene: 74294 GeneCards: HSPA1B
遺伝子の位置 (ヒト)
染色体	6番染色体 (ヒト)
終点	31,830,254 bp
遺伝子の位置 (マウス)
染色体	17番染色体 (マウス)
終点	35,191,132 bp
遺伝子オントロジー
分子機能	• ヌクレオチド結合; • 熱ショックタンパク質結合; • 受容体結合; • C3HC4-type RING finger domain binding; • ATPアーゼ活性; • virus receptor activity; • ヒストンデアセチラーゼ結合; • protein folding chaperone activity; • G protein-coupled receptor binding; • ATP binding; • 酵素結合; • ubiquitin protein ligase binding; • 血漿タンパク結合; • transcription corepressor activity; • cadherin binding; • RNA結合; • denatured protein binding; • protein N-terminus binding; • unfolded protein binding; • disordered domain specific binding; • misfolded protein binding;
細胞の構成要素	• blood microparticle; • 中心小体; • 核質; • 封入体; • 焦点接着; • perinuclear region of cytoplasm; • ubiquitin ligase complex; • 細胞質基質; • 細胞外領域; • ficolin-1-rich granule lumen; • 中心体; • 微小管形成中心; • 細胞骨格; • 細胞核; • 細胞質; • ミトコンドリア; • 小胞体; • アグリソーム; • nuclear speck; • 小胞; • エキソソーム; • COP9シグナロソーム; • 高分子複合体; • リボ核タンパク質;
生物学的プロセス	• cellular response to oxidative stress; • regulation of mRNA stability; • negative regulation of endoplasmic reticulum stress-induced intrinsic apoptotic signaling pathway; • positive regulation of NF-kappaB transcription factor activity; • negative regulation of mitochondrial outer membrane permeabilization involved in apoptotic signaling pathway; • cellular heat acclimation; • negative regulation of inclusion body assembly; • positive regulation of tumor necrosis factor-mediated signaling pathway; • negative regulation of cell death; • positive regulation of gene expression; • ウイルス侵入; • regulation of cell death; • ATP metabolic process; • negative regulation of protein ubiquitination; • negative regulation of extrinsic apoptotic signaling pathway in absence of ligand; • positive regulation of endoribonuclease activity; • positive regulation of nucleotide-binding oligomerization domain containing 2 signaling pathway; • regulation of protein ubiquitination; • positive regulation of interleukin-8 production; • regulation of cellular response to heat; • cellular response to heat; • negative regulation of transforming growth factor beta receptor signaling pathway; • positive regulation of proteasomal ubiquitin-dependent protein catabolic process; • 好中球脱顆粒; • negative regulation of transcription from RNA polymerase II promoter in response to stress; • protein refolding; • positive regulation of microtubule nucleation; • regulation of mitotic spindle assembly; • mRNA異化プロセス; • response to unfolded protein; • negative regulation of cell population proliferation; • negative regulation of cell growth; • negative regulation of apoptotic process; • タンパク質の安定化; • chaperone-mediated protein complex assembly; • positive regulation of RNA splicing; • Unfolded Protein Response; • positive regulation of erythrocyte differentiation; • chaperone cofactor-dependent protein refolding; • lysosomal transport; • response to heat; • telomere maintenance; • DNA修復;
	出典:Amigo / QuickGO
オルソログ
	3304
	193740
ENSG00000232804; ENSG00000224501; ENSG00000212866; ENSG00000204388; ENSG00000231555;
	n/a
	ENSMUSG00000091971
	P0DMV8,P0DMV9,A8K5I0
	Q61696
	NM_005346
	NM_010479
	NP_005337; NP_005336; NP_005336; NP_005336.3; NP_005337.2
	NP_034609
	ウィキデータ
閲覧/編集ヒト	閲覧/編集マウス

HSPA1B（heat shock protein family A (Hsp70) member 1B）またはHSP70-2はHsp70ファミリーのタンパク質であり、イントロンを持たないHSPA1B遺伝子にコードされる^[5]。HSPA1B遺伝子は6番染色体（英語版）短腕のMHCクラスIII（英語版）遺伝子領域内に、2つのパラログ遺伝子HSPA1A、HSPA1Lとともにクラスターとして存在する^[6]^[7]^[8]。HSPA1A遺伝子とHSPA1B遺伝子のDNA配列に存在するわずかな差異は、ほぼ同義置換や3' UTRに位置するものであるため、両遺伝子からはほぼ同一なタンパク質HSPA1AとHSPA1Bが産生される^[8]。同領域に位置する3つ目のパラログであるHSPA1Lは、他の2つと90%が相同である^[7]。

概要 PDBに登録されている構造, PDB ...

閉じる

HSPA1Bはシャペロンタンパク質であり、他の熱ショックタンパク質やシャペロンタンパク質と協働して細胞内の他のタンパク質のコンフォメーションを安定化し、ストレスによる凝集から保護することで、プロテオスタシス（英語版）を維持する^[9]。また、Hsp70はタンパク質に対するシャペロン作用とは独立に、アデニンとウラシルに富むmRNAに結合して安定化することが示されている^[10]。Hsp70は結合したATPがADPへ加水分解されることで基質を強固に結合するようになる。この加水分解の促進にはカリウムイオンを必要とする^[11]。

HSPA1Bは雄性生殖細胞系列の減数分裂時に特異的に発現しており、そこではCDC2とサイクリンB1との複合体の形成に必要である^[12]。またその後の段階では、精原細胞に運動性をもたらす特殊なカルシウムイオンチャネルであるCatSper（英語版）複合体へ組み込まれる^[13]。

マウスではHSPA1Bの発現が損なわれた際には、CDC2がサイクリンB1とヘテロ二量体を形成し減数分裂細胞の細胞周期をS期以降へ進行させることができなくなるため、不妊が観察される^[12]。

卵巣がん、膀胱尿路上皮がん、乳がんにおいて、形質転換腫瘍細胞でのHSPA1Bの発現は迅速な増殖、転移、アポトーシス阻害へ関与していることが示唆されている。HSPA1Bのヌクレオチド1267番のSNPは慢性B型肝炎やC型肝炎の患者の肝細胞がん発症リスクを高める^[14]。

HSPA1Bは次に挙げる因子と相互作用することが示されている。

ATF5（英語版）^[15]
BAG1（英語版）^[16]
BAG2（英語版）^[16]
BAG3（英語版）^[16]
CATSPERB^[13]
CDC2^[17]
CHCHD3^[18]
DNAJC7（英語版）^[19]^[20]
DNAJC8^[21]
DNAJC9^[22]^[23]
FOXP3^[24]
HDAC4（英語版）^[25]
HOPX（英語版）^[25]
Hsp40^[25]
Hsp90^[25]
Hsp105（英語版）^[16]
IRAK1BP1^[26]
METTL21A^[27]
NAA10^[25]
NEDD1（英語版）^[28]
NOD2（英語版）^[29]
PPP5C（英語版）^[30]
Parkin（英語版）^[31]
SMAD3^[32]
STUB1（英語版）^[25]
TERT^[33]
TRIM5（英語版）,^[34]
TSC2^[35]

[1]
GRCh38: Ensembl release 89: ENSG00000232804、ENSG00000224501、ENSG00000212866、ENSG00000204388、ENSG00000231555 - Ensembl, May 2017
[2]
GRCm38: Ensembl release 89: ENSMUSG00000091971 - Ensembl, May 2017
[3]
Human PubMed Reference:
[4]
Mouse PubMed Reference:
[5]
“Structure and expression of the three MHC-linked HSP70 genes”. Immunogenetics 32 (4): 242–251. (1990). doi:10.1007/BF00187095. PMID 1700760.
[6]
“Entrez Gene: HSPA1A heat shock 70kDa protein 1B”. 2024年2月29日閲覧。
[7]
“Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man”. Journal of Biochemistry 124 (2): 347–353. (August 1998). doi:10.1093/oxfordjournals.jbchem.a022118. PMID 9685725.
[8]
“Human major histocompatibility complex contains genes for the major heat shock protein HSP70”. Proceedings of the National Academy of Sciences of the United States of America 86 (6): 1968–1972. (March 1989). Bibcode: 1989PNAS...86.1968S. doi:10.1073/pnas.86.6.1968. PMC 286826. PMID 2538825.
[9]
“The Hsp70 chaperone network”. Nature Reviews. Molecular Cell Biology 20 (11): 665–680. (November 2019). doi:10.1038/s41580-019-0133-3. PMID 31253954.
[10]
“Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions” (English). The Journal of Biological Chemistry 292 (34): 14122–14133. (August 2017). doi:10.1074/jbc.M117.785394. PMC 5572911. PMID 28679534.
[11]
“Biochemical and structural studies on the high affinity of Hsp70 for ADP”. Protein Science 20 (8): 1367–1379. (August 2011). doi:10.1002/pro.663. PMC 3189522. PMID 21608060.
[12]
“Role of heat shock protein HSP70-2 in spermatogenesis”. Reviews of Reproduction 4 (1): 23–30. (January 1999). doi:10.1530/ror.0.0040023. PMID 10051099.
[13]
“CatSperbeta, a novel transmembrane protein in the CatSper channel complex” (English). The Journal of Biological Chemistry 282 (26): 18945–18952. (June 2007). doi:10.1074/jbc.M701083200. PMID 17478420.
[14]
“Heat shock protein A1B 1267 polymorphism is highly associated with risk and prognosis of hepatocellular carcinoma: a case-control study”. Medicine 87 (2): 87–98. (March 2008). doi:10.1097/MD.0b013e31816be95c. PMID 18344806.
[15]
“Nucleophosmin (NPM1/B23) interacts with activating transcription factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent ATF5 degradation in hepatocellular carcinoma cells”. The Journal of Biological Chemistry 287 (23): 19599–19609. (June 2012). doi:10.1074/jbc.M112.363622. PMC 3365995. PMID 22528486.
[16]
“Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro”. The Journal of Biological Chemistry 289 (3): 1402–1414. (January 2014). doi:10.1074/jbc.M113.521997. PMC 3894324. PMID 24318877.
[17]
“HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes”. Development 124 (15): 3007–3014. (August 1997). doi:10.1242/dev.124.15.3007. PMID 9247342.
[18]
“ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function” (English). The Journal of Biological Chemistry 286 (4): 2918–2932. (January 2011). doi:10.1074/jbc.M110.171975. PMC 3024787. PMID 21081504.
[19]
“Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system”. The EMBO Journal 22 (14): 3613–3623. (July 2003). doi:10.1093/emboj/cdg362. PMC 165632. PMID 12853476.
[20]
“Role of the cochaperone Tpr2 in Hsp90 chaperoning”. Biochemistry 47 (31): 8203–8213. (August 2008). doi:10.1021/bi800770g. PMID 18620420.
[21]
“A novel nuclear DnaJ protein, DNAJC8, can suppress the formation of spinocerebellar ataxia 3 polyglutamine aggregation in a J-domain independent manner”. Biochemical and Biophysical Research Communications 474 (4): 626–633. (June 2016). doi:10.1016/j.bbrc.2016.03.152. PMID 27133716.
[22]
“HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain”. Biochemical and Biophysical Research Communications 353 (2): 280–285. (February 2007). doi:10.1016/j.bbrc.2006.12.013. PMID 17182002.
[23]
“DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network”. Molecular Cell 81 (12): 2533–2548.e9. (June 2021). doi:10.1016/j.molcel.2021.03.041. PMC 8221569. PMID 33857403.
[24]
“The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3”. Immunity 39 (2): 272–285. (August 2013). doi:10.1016/j.immuni.2013.08.006. PMC 3817295. PMID 23973223.
[25]
“ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation”. Nature Communications 7: 12882. (October 2016). Bibcode: 2016NatCo...712882S. doi:10.1038/ncomms12882. PMC 5059642. PMID 27708256.
[26]
“The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family”. DNA and Cell Biology 25 (12): 704–714. (December 2006). doi:10.1089/dna.2006.25.704. PMID 17233114.
[27]
“Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation”. The Journal of Biological Chemistry 288 (39): 27752–27763. (September 2013). doi:10.1074/jbc.M113.483248. PMC 3784692. PMID 23921388.
[28]
“HSP70 regulates the function of mitotic centrosomes”. Cellular and Molecular Life Sciences 73 (20): 3949–3960. (October 2016). doi:10.1007/s00018-016-2236-8. PMID 27137183.
[29]
“The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease”. The Journal of Biological Chemistry 289 (27): 18987–18998. (July 2014). doi:10.1074/jbc.M114.557686. PMC 4081938. PMID 24790089.
[30]
“Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole”. The Biochemical Journal 385 (Pt 1): 45–56. (January 2005). doi:10.1042/BJ20040690. PMC 1134672. PMID 15383005.
[31]
“High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy”. Nature 504 (7479): 291–295. (December 2013). Bibcode: 2013Natur.504..291H. doi:10.1038/nature12748. PMC 5841086. PMID 24270810.
[32]
“Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1”. Biochemical and Biophysical Research Communications 446 (1): 387–392. (March 2014). doi:10.1016/j.bbrc.2014.02.124. PMID 24613385.
[33]
“Stable association of hsp90 and p23, but Not hsp70, with active human telomerase”. The Journal of Biological Chemistry 276 (19): 15571–15574. (May 2001). doi:10.1074/jbc.C100055200. PMID 11274138.
[34]
“Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha”. The Journal of Biological Chemistry 285 (10): 7827–7837. (March 2010). doi:10.1074/jbc.M109.040618. PMC 2844226. PMID 20053985.
[35]
“Phosphorylation and binding partner analysis of the TSC1-TSC2 complex”. Biochemical and Biophysical Research Communications 333 (3): 818–826. (August 2005). doi:10.1016/j.bbrc.2005.05.175. PMID 15963462.

HSPA1B protein, human - MeSH・アメリカ国立医学図書館・生命科学用語シソーラス（英語）

[refGRCh38Ensembl-1] [1]
GRCh38: Ensembl release 89: ENSG00000232804、ENSG00000224501、ENSG00000212866、ENSG00000204388、ENSG00000231555 - Ensembl, May 2017

[refGRCm38Ensembl-2] [2]
GRCm38: Ensembl release 89: ENSMUSG00000091971 - Ensembl, May 2017

[3] [3]
Human PubMed Reference:

[4] [4]
Mouse PubMed Reference:

[pmid1700760-5] [5]
“Structure and expression of the three MHC-linked HSP70 genes”. Immunogenetics 32 (4): 242–251. (1990). doi:10.1007/BF00187095. PMID 1700760.

[entrez-6] [6]
“Entrez Gene: HSPA1A heat shock 70kDa protein 1B”. 2024年2月29日閲覧。

[pmid9685725-7] [7]
“Genomic structure of the spermatid-specific hsp70 homolog gene located in the class III region of the major histocompatibility complex of mouse and man”. Journal of Biochemistry 124 (2): 347–353. (August 1998). doi:10.1093/oxfordjournals.jbchem.a022118. PMID 9685725.

[Sargent_1989-8] [8]
“Human major histocompatibility complex contains genes for the major heat shock protein HSP70”. Proceedings of the National Academy of Sciences of the United States of America 86 (6): 1968–1972. (March 1989). Bibcode: 1989PNAS...86.1968S. doi:10.1073/pnas.86.6.1968. PMC 286826. PMID 2538825.

[9] [9]
“The Hsp70 chaperone network”. Nature Reviews. Molecular Cell Biology 20 (11): 665–680. (November 2019). doi:10.1038/s41580-019-0133-3. PMID 31253954.

[10] [10]
“Hsp70's RNA-binding and mRNA-stabilizing activities are independent of its protein chaperone functions” (English). The Journal of Biological Chemistry 292 (34): 14122–14133. (August 2017). doi:10.1074/jbc.M117.785394. PMC 5572911. PMID 28679534.

[11] [11]
“Biochemical and structural studies on the high affinity of Hsp70 for ADP”. Protein Science 20 (8): 1367–1379. (August 2011). doi:10.1002/pro.663. PMC 3189522. PMID 21608060.

[Role_of_heat_shock_protein_HSP70-2-12] [12]
“Role of heat shock protein HSP70-2 in spermatogenesis”. Reviews of Reproduction 4 (1): 23–30. (January 1999). doi:10.1530/ror.0.0040023. PMID 10051099.

[CatSperbeta,_a_novel_transmembrane-13] [13]
“CatSperbeta, a novel transmembrane protein in the CatSper channel complex” (English). The Journal of Biological Chemistry 282 (26): 18945–18952. (June 2007). doi:10.1074/jbc.M701083200. PMID 17478420.

[pmid183448062-14] [14]
“Heat shock protein A1B 1267 polymorphism is highly associated with risk and prognosis of hepatocellular carcinoma: a case-control study”. Medicine 87 (2): 87–98. (March 2008). doi:10.1097/MD.0b013e31816be95c. PMID 18344806.

[15] [15]
“Nucleophosmin (NPM1/B23) interacts with activating transcription factor 5 (ATF5) protein and promotes proteasome- and caspase-dependent ATF5 degradation in hepatocellular carcinoma cells”. The Journal of Biological Chemistry 287 (23): 19599–19609. (June 2012). doi:10.1074/jbc.M112.363622. PMC 3365995. PMID 22528486.

[Binding_of_human_nucleotide_exchang-16] [16]
“Binding of human nucleotide exchange factors to heat shock protein 70 (Hsp70) generates functionally distinct complexes in vitro”. The Journal of Biological Chemistry 289 (3): 1402–1414. (January 2014). doi:10.1074/jbc.M113.521997. PMC 3894324. PMID 24318877.

[17] [17]
“HSP70-2 is required for CDC2 kinase activity in meiosis I of mouse spermatocytes”. Development 124 (15): 3007–3014. (August 1997). doi:10.1242/dev.124.15.3007. PMID 9247342.

[18] [18]
“ChChd3, an inner mitochondrial membrane protein, is essential for maintaining crista integrity and mitochondrial function” (English). The Journal of Biological Chemistry 286 (4): 2918–2932. (January 2011). doi:10.1074/jbc.M110.171975. PMC 3024787. PMID 21081504.

[19] [19]
“Cofactor Tpr2 combines two TPR domains and a J domain to regulate the Hsp70/Hsp90 chaperone system”. The EMBO Journal 22 (14): 3613–3623. (July 2003). doi:10.1093/emboj/cdg362. PMC 165632. PMID 12853476.

[20] [20]
“Role of the cochaperone Tpr2 in Hsp90 chaperoning”. Biochemistry 47 (31): 8203–8213. (August 2008). doi:10.1021/bi800770g. PMID 18620420.

[21] [21]
“A novel nuclear DnaJ protein, DNAJC8, can suppress the formation of spinocerebellar ataxia 3 polyglutamine aggregation in a J-domain independent manner”. Biochemical and Biophysical Research Communications 474 (4): 626–633. (June 2016). doi:10.1016/j.bbrc.2016.03.152. PMID 27133716.

[22] [22]
“HDJC9, a novel human type C DnaJ/HSP40 member interacts with and cochaperones HSP70 through the J domain”. Biochemical and Biophysical Research Communications 353 (2): 280–285. (February 2007). doi:10.1016/j.bbrc.2006.12.013. PMID 17182002.

[23] [23]
“DNAJC9 integrates heat shock molecular chaperones into the histone chaperone network”. Molecular Cell 81 (12): 2533–2548.e9. (June 2021). doi:10.1016/j.molcel.2021.03.041. PMC 8221569. PMID 33857403.

[24] [24]
“The ubiquitin ligase Stub1 negatively modulates regulatory T cell suppressive activity by promoting degradation of the transcription factor Foxp3”. Immunity 39 (2): 272–285. (August 2013). doi:10.1016/j.immuni.2013.08.006. PMC 3817295. PMID 23973223.

[ARD1-mediated_Hsp70_acetylation_bal-25] [25]
“ARD1-mediated Hsp70 acetylation balances stress-induced protein refolding and degradation”. Nature Communications 7: 12882. (October 2016). Bibcode: 2016NatCo...712882S. doi:10.1038/ncomms12882. PMC 5059642. PMID 27708256.

[26] [26]
“The disordered amino-terminus of SIMPL interacts with members of the 70-kDa heat-shock protein family”. DNA and Cell Biology 25 (12): 704–714. (December 2006). doi:10.1089/dna.2006.25.704. PMID 17233114.

[27] [27]
“Identification and characterization of a novel human methyltransferase modulating Hsp70 protein function through lysine methylation”. The Journal of Biological Chemistry 288 (39): 27752–27763. (September 2013). doi:10.1074/jbc.M113.483248. PMC 3784692. PMID 23921388.

[28] [28]
“HSP70 regulates the function of mitotic centrosomes”. Cellular and Molecular Life Sciences 73 (20): 3949–3960. (October 2016). doi:10.1007/s00018-016-2236-8. PMID 27137183.

[29] [29]
“The molecular chaperone HSP70 binds to and stabilizes NOD2, an important protein involved in Crohn disease”. The Journal of Biological Chemistry 289 (27): 18987–18998. (July 2014). doi:10.1074/jbc.M114.557686. PMC 4081938. PMID 24790089.

[30] [30]
“Human protein phosphatase 5 dissociates from heat-shock proteins and is proteolytically activated in response to arachidonic acid and the microtubule-depolymerizing drug nocodazole”. The Biochemical Journal 385 (Pt 1): 45–56. (January 2005). doi:10.1042/BJ20040690. PMC 1134672. PMID 15383005.

[31] [31]
“High-content genome-wide RNAi screens identify regulators of parkin upstream of mitophagy”. Nature 504 (7479): 291–295. (December 2013). Bibcode: 2013Natur.504..291H. doi:10.1038/nature12748. PMC 5841086. PMID 24270810.

[32] [32]
“Hsp70 and Hsp90 oppositely regulate TGF-β signaling through CHIP/Stub1”. Biochemical and Biophysical Research Communications 446 (1): 387–392. (March 2014). doi:10.1016/j.bbrc.2014.02.124. PMID 24613385.

[33] [33]
“Stable association of hsp90 and p23, but Not hsp70, with active human telomerase”. The Journal of Biological Chemistry 276 (19): 15571–15574. (May 2001). doi:10.1074/jbc.C100055200. PMID 11274138.

[34] [34]
“Hsp70 interacts with the retroviral restriction factor TRIM5alpha and assists the folding of TRIM5alpha”. The Journal of Biological Chemistry 285 (10): 7827–7837. (March 2010). doi:10.1074/jbc.M109.040618. PMC 2844226. PMID 20053985.

[35] [35]
“Phosphorylation and binding partner analysis of the TSC1-TSC2 complex”. Biochemical and Biophysical Research Communications 333 (3): 818–826. (August 2005). doi:10.1016/j.bbrc.2005.05.175. PMID 15963462.

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[34]

[35]

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