이κBα

NFKBIA
사용 가능한 구조물
PDB	직교 검색: PDBe RCSB
PDB ID 코드 목록
	1IKN, 1NFI
식별자
별칭	NFKBIA, IKBA, MAD-3, NFKBI, NFKB 억제제 알파, EDAID2
외부 ID	OMIM: 164008 MGI: 104741 호몰로진: 7863 GeneCard: NFKBIA
유전자 위치(인간)
쳇.	14번 염색체(인간)
끝	35,404,749 bp
유전자 위치(마우스)
쳇.	12번 염색체(쥐)
끝	55,539,432 bp
RNA 표현 패턴
	표현된 상단
	정맥; ; 심막염; ; 폐하엽; ; 난모세포; ; 젖꼭지; ; 수혈정맥; ; 방광 점막; ; 단모세포; ; 폐상엽; ; 오른쪽 폐;
	추가 참조 표현식 데이터
	추가 참조 표현식 데이터
유전자 온톨로지
분자함수	전사 계수 바인딩; GO:0001948 단백질 결합; 핵 국산화 시퀀스 바인딩; 동일한 단백질 결합; 효소 결합; 유비퀴틴 단백질 리가제 결합; 열충격 단백질 결합; GO:0032403 단백질 함유 복합 결합; NF-kappaB 바인딩;
셀룰러 컴포넌트	세포질; I-카파B/NF-카파B 복합체; 플라즈마 막; 핵의; 시토솔; 세포내 해부학적 구조; 단백질 함유 복합체; 핵종의;
생물학적 과정	근육 스트레칭에 대한 반응; 세포단백질대사과정의 양성규제; 외생 dsRNA에 대한 대응; 전사 인자의 세포질 분리; DNA 결합에 대한 부정적 규제; 유기 순환 화합물에 대한 세포 반응; NF-kappaB의 세포질 분리; 무라밀 디펩타이드에 대한 반응; 세포핵 과정에 대한 부정적인 규제; 사이토카인 자극에 대한 세포 반응; 전사의 양성적 조절, DNA-템플링; 지용성당류에 대한 반응; 감기에 대한 세포 반응; 세포 인구증식 규제; 콜레스테롤 유출에 대한 양성 규제; 2개의 신호 경로를 포함하는 뉴클레오티드-알고르기 도메인; 유전자 발현 조절; 지질 저장소의 부정적인 규제; GO:0022415 바이러스 처리; NF-kappaB 전사 계수 활성의 음수 조절; 골수 세포 분화에 대한 부정적인 규제; 대식세포 유도 폼세포 분화의 부정적 규제; 1개의 신호 경로를 포함하는 뉴클레오티드-알고르기 도메인; 지혈당 매개 신호 경로; 노치 신호 경로에 대한 부정적 규제; RNA 중합효소 II에 의한 전사의 양성 조절; 사멸적 과정; 간 재생; 유료 수용체 4 신호 경로; 단백질 분해; I-kappaB kinase/NF-kappaB 신호; 종양 괴사 인자 매개 신호 경로; 염증 반응의 양성 규제; 종양 괴사 인자에 대한 세포 반응; 인터루킨-1 매개 신호 경로; NIK/NF-kappaB 신호 규제; 핵으로 단백질을 수입하다;
	출처:아미고 / 퀵고
직교체
	4792
	18035
	ENSG00000100906
	ENSMUSG00000021025
	P25963
	Q9Z1E3
	NM_020529
	NM_010907
	NP_065390
	NP_035037
	위키다타
인간 보기/편집	마우스 보기/편집

IκBα(B세포 억제제, 알파에 있는 카파 경량 폴리펩타이드 유전자의 핵 인자)는 NF-fB 전사 인자를 억제하는 기능을 하는 세포단백질 계열의 한 구성원이다.IκBα는 NF-κB 단백질의 핵 국산화 신호(NLS)를 가려 세포질에서 비활성 상태로 격리시켜 NF-κB를 억제한다.^[5]또한 IκBα는 NF-κB 전사 인자가 DNA에 결합하는 능력을 차단하는데, 이는 NF-bB의 적절한 기능에 필요하다.^[6]

질병연계

IκBα 단백질을 인코딩하는 유전자는 일부 호지킨의 림프종 세포에서 돌연변이를 일으키는데, 그러한 돌연변이는 IαBα 단백질을 활성화시키지 못하여 NF-κB가 림프종종양 세포에서 만성적으로 활동하게 하고, 이러한 활동은 이러한 종양 세포의 악성 상태에 기여한다.^[7]

상호작용

IκBα는 다음과 상호작용하는 것으로 나타났다.

참조

^ ^a ^b ^c GRCh38: 앙상블 릴리스 89: ENSG00000100906 - 앙상블, 2017년 5월
^ ^a ^b ^c GRCm38: 앙상블 릴리스 89: ENSMUSG000021025 - 앙상블, 2017년 5월
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Jacobs MD, Harrison SC (1998). "Structure of an IkappaBalpha/NF-kappaB complex". Cell. 95 (6): 749–58. doi:10.1016/S0092-8674(00)81698-0. PMID 9865693. S2CID 7003353.
^ Verma IM, Stevenson JK, Schwarz EM, Van Antwerp D, Miyamoto S (1995). "Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation". Genes Dev. 9 (22): 2723–35. doi:10.1101/gad.9.22.2723. PMID 7590248.
^ Cabannes E, Khan G, Aillet F, Jarrett RF, Hay RT (1999). "Mutations in the IkBa gene in Hodgkin's disease suggest a tumour suppressor role for IkappaBalpha". Oncogene. 18 (20): 3063–70. doi:10.1038/sj.onc.1202893. PMID 10340377.
^ Suzuki H, Chiba T, Suzuki T, Fujita T, Ikenoue T, Omata M, Furuichi K, Shikama H, Tanaka K (January 2000). "Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination". J. Biol. Chem. 275 (4): 2877–84. doi:10.1074/jbc.275.4.2877. PMID 10644755.
^ ^a ^b Spencer E, Jiang J, Chen ZJ (February 1999). "Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP". Genes Dev. 13 (3): 284–94. doi:10.1101/gad.13.3.284. PMC 316434. PMID 9990853.
^ "Molecular Interaction Database". Archived from the original on 2006-05-06. Retrieved 2012-05-08.
^ ^a ^b ^c Cohen L, Henzel WJ, Baeuerle PA (September 1998). "IKAP is a scaffold protein of the IkappaB kinase complex". Nature. 395 (6699): 292–6. doi:10.1038/26254. PMID 9751059. S2CID 4327300.
^ ^a ^b Woronicz JD, Gao X, Cao Z, Rothe M, Goeddel DV (October 1997). "IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK". Science. 278 (5339): 866–9. doi:10.1126/science.278.5339.866. PMID 9346485.
^ DiDonato JA, Hayakawa M, Rothwarf DM, Zandi E, Karin M (August 1997). "A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB". Nature. 388 (6642): 548–54. doi:10.1038/41493. PMID 9252186. S2CID 4354442.
^ Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K (March 1999). "The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway". Nature. 398 (6724): 252–6. doi:10.1038/18465. PMID 10094049. S2CID 4421236.
^ Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J (December 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Mol. Cell. Biol. 17 (12): 7375–85. doi:10.1128/MCB.17.12.7375. PMC 232593. PMID 9372968.
^ Prigent M, Barlat I, Langen H, Dargemont C (November 2000). "IkappaBalpha and IkappaBalpha /NF-kappa B complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2". J. Biol. Chem. 275 (46): 36441–9. doi:10.1074/jbc.M004751200. PMID 10969074.
^ ^a ^b ^c Hay DC, Kemp GD, Dargemont C, Hay RT (May 2001). "Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription". Mol. Cell. Biol. 21 (10): 3482–90. doi:10.1128/MCB.21.10.3482-3490.2001. PMC 100270. PMID 11313474.
^ Mercurio F, Murray BW, Shevchenko A, Bennett BL, Young DB, Li JW, Pascual G, Motiwala A, Zhu H, Mann M, Manning AM (February 1999). "IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex". Mol. Cell. Biol. 19 (2): 1526–38. doi:10.1128/mcb.19.2.1526. PMC 116081. PMID 9891086.
^ ^a ^b Malek S, Huxford T, Ghosh G (September 1998). "Ikappa Balpha functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-kappaB". J. Biol. Chem. 273 (39): 25427–35. doi:10.1074/jbc.273.39.25427. PMID 9738011.
^ Chang NS (March 2002). "The non-ankyrin C terminus of Ikappa Balpha physically interacts with p53 in vivo and dissociates in response to apoptotic stress, hypoxia, DNA damage, and transforming growth factor-beta 1-mediated growth suppression". J. Biol. Chem. 277 (12): 10323–31. doi:10.1074/jbc.M106607200. PMID 11799106.
^ Fischle W, Verdin E, Greene WC (August 2001). "Duration of nuclear NF-kappaB action regulated by reversible acetylation". Science. 293 (5535): 1653–7. doi:10.1126/science.1062374. hdl:11858/00-001M-0000-002C-9FF1-A. PMID 11533489. S2CID 45796404.
^ Kiernan R, Brès V, Ng RW, Coudart MP, El Messaoudi S, Sardet C, Jin DY, Emiliani S, Benkirane M (January 2003). "Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65". J. Biol. Chem. 278 (4): 2758–66. doi:10.1074/jbc.M209572200. PMID 12419806.
^ Hansen SK, Baeuerle PA, Blasi F (April 1994). "Purification, reconstitution, and I kappa B association of the c-Rel-p65 (RelA) complex, a strong activator of transcription". Mol. Cell. Biol. 14 (4): 2593–603. doi:10.1128/mcb.14.4.2593. PMC 358627. PMID 8139561.
^ Schouten GJ, Vertegaal AC, Whiteside ST, Israël A, Toebes M, Dorsman JC, van der Eb AJ, Zantema A (June 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". EMBO J. 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. PMC 1169932. PMID 9214631.
^ Guo D, Li M, Zhang Y, Yang P, Eckenrode S, Hopkins D, Zheng W, Purohit S, Podolsky RH, Muir A, Wang J, Dong Z, Brusko T, Atkinson M, Pozzilli P, Zeidler A, Raffel LJ, Jacob CO, Park Y, Serrano-Rios M, Larrad MT, Zhang Z, Garchon HJ, Bach JF, Rotter JI, She JX, Wang CY (August 2004). "A functional variant of SUMO4, a new I kappa B alpha modifier, is associated with type 1 diabetes". Nat. Genet. 36 (8): 837–41. doi:10.1038/ng1391. PMID 15247916. S2CID 41123857.
^ Dai RM, Chen E, Longo DL, Gorbea CM, Li CC (February 1998). "Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha". J. Biol. Chem. 273 (6): 3562–73. doi:10.1074/jbc.273.6.3562. PMID 9452483.

추가 읽기

Roulston A, Lin R, Beauparlant P, Wainberg MA, Hiscott J (1995). "Regulation of human immunodeficiency virus type 1 and cytokine gene expression in myeloid cells by NF-kappa B/Rel transcription factors". Microbiol. Rev. 59 (3): 481–505. doi:10.1128/MMBR.59.3.481-505.1995. PMC 239370. PMID 7565415.
Hay RT, Vuillard L, Desterro JM, Rodriguez MS (2000). "Control of NF-kappa B transcriptional activation by signal induced proteolysis of I kappa B alpha". Philos. Trans. R. Soc. Lond. B Biol. Sci. 354 (1389): 1601–9. doi:10.1098/rstb.1999.0504. PMC 1692667. PMID 10582246.
Muthumani K, Desai BM, Hwang DS, Choo AY, Laddy DJ, Thieu KP, Rao RG, Weiner DB (2004). "HIV-1 Vpr and anti-inflammatory activity". DNA Cell Biol. 23 (4): 239–47. doi:10.1089/104454904773819824. PMID 15142381.
Caraglia M, Marra M, Pelaia G, Maselli R, Caputi M, Marsico SA, Abbruzzese A (2005). "Alpha-interferon and its effects on signal transduction pathways". J. Cell. Physiol. 202 (2): 323–35. doi:10.1002/jcp.20137. PMID 15389589.
Le Rouzic E, Benichou S (2006). "The Vpr protein from HIV-1: distinct roles along the viral life cycle". Retrovirology. 2 (1): 11. doi:10.1186/1742-4690-2-11. PMC 554975. PMID 15725353.
Zhao RY, Bukrinsky M, Elder RT (2005). "HIV-1 viral protein R (Vpr) & host cellular responses". Indian J. Med. Res. 121 (4): 270–86. PMID 15817944.
Sun XF, Zhang H (2007). "NFKB and NFKBI polymorphisms in relation to susceptibility of tumour and other diseases". Histol. Histopathol. 22 (12): 1387–98. PMID 17701919.

외부 링크

T세포 면역 결핍증을 가진 Anhidrotic, Ectodermal Displasia에 대한 OMIM 항목
NFKBIA+단백질,+인간, 미국 국립 의학 도서관의 의학 과목 제목(MSH)
미국 국립 의학 도서관의 NF-kappaB+inhibitor+alpha(MeSH) 제목
PDBe-KB에서 UniProt: P25963(NF-kappa-B 억제제 알파)에 대한 PDB의 모든 구조 정보 개요.

[refGRCh38Ensembl-1] GRCh38: 앙상블 릴리스 89: ENSG00000100906 - 앙상블, 2017년 5월

[refGRCm38Ensembl-2] GRCm38: 앙상블 릴리스 89: ENSMUSG000021025 - 앙상블, 2017년 5월

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[pmid9865693-5] Jacobs MD, Harrison SC (1998). "Structure of an IkappaBalpha/NF-kappaB complex". Cell. 95 (6): 749–58. doi:10.1016/S0092-8674(00)81698-0. PMID 9865693. S2CID 7003353.

[pmid7590248-6] Verma IM, Stevenson JK, Schwarz EM, Van Antwerp D, Miyamoto S (1995). "Rel/NF-kappa B/I kappa B family: intimate tales of association and dissociation". Genes Dev. 9 (22): 2723–35. doi:10.1101/gad.9.22.2723. PMID 7590248.

[pmid10340377-7] Cabannes E, Khan G, Aillet F, Jarrett RF, Hay RT (1999). "Mutations in the IkBa gene in Hodgkin's disease suggest a tumour suppressor role for IkappaBalpha". Oncogene. 18 (20): 3063–70. doi:10.1038/sj.onc.1202893. PMID 10340377.

[pmid10644755-8] Suzuki H, Chiba T, Suzuki T, Fujita T, Ikenoue T, Omata M, Furuichi K, Shikama H, Tanaka K (January 2000). "Homodimer of two F-box proteins betaTrCP1 or betaTrCP2 binds to IkappaBalpha for signal-dependent ubiquitination". J. Biol. Chem. 275 (4): 2877–84. doi:10.1074/jbc.275.4.2877. PMID 10644755.

[pmid9990853-9] Spencer E, Jiang J, Chen ZJ (February 1999). "Signal-induced ubiquitination of IkappaBalpha by the F-box protein Slimb/beta-TrCP". Genes Dev. 13 (3): 284–94. doi:10.1101/gad.13.3.284. PMC 316434. PMID 9990853.

[10] "Molecular Interaction Database". Archived from the original on 2006-05-06. Retrieved 2012-05-08.

[pmid9751059-11] Cohen L, Henzel WJ, Baeuerle PA (September 1998). "IKAP is a scaffold protein of the IkappaB kinase complex". Nature. 395 (6699): 292–6. doi:10.1038/26254. PMID 9751059. S2CID 4327300.

[pmid9346485-12] Woronicz JD, Gao X, Cao Z, Rothe M, Goeddel DV (October 1997). "IkappaB kinase-beta: NF-kappaB activation and complex formation with IkappaB kinase-alpha and NIK". Science. 278 (5339): 866–9. doi:10.1126/science.278.5339.866. PMID 9346485.

[pmid9252186-13] DiDonato JA, Hayakawa M, Rothwarf DM, Zandi E, Karin M (August 1997). "A cytokine-responsive IkappaB kinase that activates the transcription factor NF-kappaB". Nature. 388 (6642): 548–54. doi:10.1038/41493. PMID 9252186. S2CID 4354442.

[pmid10094049-14] Ninomiya-Tsuji J, Kishimoto K, Hiyama A, Inoue J, Cao Z, Matsumoto K (March 1999). "The kinase TAK1 can activate the NIK-I kappaB as well as the MAP kinase cascade in the IL-1 signalling pathway". Nature. 398 (6724): 252–6. doi:10.1038/18465. PMID 10094049. S2CID 4421236.

[pmid9372968-15] Crépieux P, Kwon H, Leclerc N, Spencer W, Richard S, Lin R, Hiscott J (December 1997). "I kappaB alpha physically interacts with a cytoskeleton-associated protein through its signal response domain". Mol. Cell. Biol. 17 (12): 7375–85. doi:10.1128/MCB.17.12.7375. PMC 232593. PMID 9372968.

[pmid10969074-16] Prigent M, Barlat I, Langen H, Dargemont C (November 2000). "IkappaBalpha and IkappaBalpha /NF-kappa B complexes are retained in the cytoplasm through interaction with a novel partner, RasGAP SH3-binding protein 2". J. Biol. Chem. 275 (46): 36441–9. doi:10.1074/jbc.M004751200. PMID 10969074.

[pmid11313474-17] Hay DC, Kemp GD, Dargemont C, Hay RT (May 2001). "Interaction between hnRNPA1 and IkappaBalpha is required for maximal activation of NF-kappaB-dependent transcription". Mol. Cell. Biol. 21 (10): 3482–90. doi:10.1128/MCB.21.10.3482-3490.2001. PMC 100270. PMID 11313474.

[pmid9891086-18] Mercurio F, Murray BW, Shevchenko A, Bennett BL, Young DB, Li JW, Pascual G, Motiwala A, Zhu H, Mann M, Manning AM (February 1999). "IkappaB kinase (IKK)-associated protein 1, a common component of the heterogeneous IKK complex". Mol. Cell. Biol. 19 (2): 1526–38. doi:10.1128/mcb.19.2.1526. PMC 116081. PMID 9891086.

[pmid9738011-19] Malek S, Huxford T, Ghosh G (September 1998). "Ikappa Balpha functions through direct contacts with the nuclear localization signals and the DNA binding sequences of NF-kappaB". J. Biol. Chem. 273 (39): 25427–35. doi:10.1074/jbc.273.39.25427. PMID 9738011.

[pmid11799106-20] Chang NS (March 2002). "The non-ankyrin C terminus of Ikappa Balpha physically interacts with p53 in vivo and dissociates in response to apoptotic stress, hypoxia, DNA damage, and transforming growth factor-beta 1-mediated growth suppression". J. Biol. Chem. 277 (12): 10323–31. doi:10.1074/jbc.M106607200. PMID 11799106.

[pmid11533489-21] Fischle W, Verdin E, Greene WC (August 2001). "Duration of nuclear NF-kappaB action regulated by reversible acetylation". Science. 293 (5535): 1653–7. doi:10.1126/science.1062374. hdl:11858/00-001M-0000-002C-9FF1-A. PMID 11533489. S2CID 45796404.

[pmid12419806-22] Kiernan R, Brès V, Ng RW, Coudart MP, El Messaoudi S, Sardet C, Jin DY, Emiliani S, Benkirane M (January 2003). "Post-activation turn-off of NF-kappa B-dependent transcription is regulated by acetylation of p65". J. Biol. Chem. 278 (4): 2758–66. doi:10.1074/jbc.M209572200. PMID 12419806.

[pmid8139561-23] Hansen SK, Baeuerle PA, Blasi F (April 1994). "Purification, reconstitution, and I kappa B association of the c-Rel-p65 (RelA) complex, a strong activator of transcription". Mol. Cell. Biol. 14 (4): 2593–603. doi:10.1128/mcb.14.4.2593. PMC 358627. PMID 8139561.

[pmid9214631-24] Schouten GJ, Vertegaal AC, Whiteside ST, Israël A, Toebes M, Dorsman JC, van der Eb AJ, Zantema A (June 1997). "IkappaB alpha is a target for the mitogen-activated 90 kDa ribosomal S6 kinase". EMBO J. 16 (11): 3133–44. doi:10.1093/emboj/16.11.3133. PMC 1169932. PMID 9214631.

[pmid15247916-25] Guo D, Li M, Zhang Y, Yang P, Eckenrode S, Hopkins D, Zheng W, Purohit S, Podolsky RH, Muir A, Wang J, Dong Z, Brusko T, Atkinson M, Pozzilli P, Zeidler A, Raffel LJ, Jacob CO, Park Y, Serrano-Rios M, Larrad MT, Zhang Z, Garchon HJ, Bach JF, Rotter JI, She JX, Wang CY (August 2004). "A functional variant of SUMO4, a new I kappa B alpha modifier, is associated with type 1 diabetes". Nat. Genet. 36 (8): 837–41. doi:10.1038/ng1391. PMID 15247916. S2CID 41123857.

[pmid9452483-26] Dai RM, Chen E, Longo DL, Gorbea CM, Li CC (February 1998). "Involvement of valosin-containing protein, an ATPase Co-purified with IkappaBalpha and 26 S proteasome, in ubiquitin-proteasome-mediated degradation of IkappaBalpha". J. Biol. Chem. 273 (6): 3562–73. doi:10.1074/jbc.273.6.3562. PMID 9452483.

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