KTN1

KTN1
식별자
에일리어스	KTN1, CG1, KNT, MU-RMS-40.19, 키넥틴 1
외부 ID	OMIM : 600381 HomoloGene : 135663 GenCard : KTN1
유전자 위치(인간)
크르.	14번 염색체(인간)
끝.	55,701,526 bp
RNA발현패턴
	상단 표시 위치:
	정자; ; 상완 이두근; ; 신장수질; ; 외측 광대근; ; 설체; ; 아킬레스건; ; 위근; ; 삼각근; ; 시신경; ; 뇌량;
	추가 참조 표현식 데이터
	; ; ; ;
	추가 참조 표현식 데이터
유전자 존재론
분자 함수	GO:0001948, GO:0016582 단백질 결합; 키네신 결합; RNA결합; 카드헤린 결합;
셀룰러 컴포넌트	막의 적분 성분; 혈장막의 적분 성분; 소포체막; 소포체; 막; 소포체내강;
생물학적 과정	미소관에 의한 운동; 발육 후 단백질 수식;
	출처:아미고 / QuickGO
맞춤법
	3895
	없음
	ENSG00000126777
	없음
	Q86UP2
	없음
	NM_001079521; NM_001079522; NM_001271014; NM_004986; NM_182926
	없음
	NP_001072989; NP_001072990; NP_001257943; NP_004977
	없음
	위키데이터
인간 보기/편집

키넥틴은 KTN1 ^[3]^[4]유전자에 의해 인간에게 암호화되는 단백질이다.

기능.

세포질 내 미세관을 따라 다양한 세포소기관 및 소포가 운반된다.마찬가지로 소포체(ER)의 막 재활용, 미소관 조직 중심에서의 골지 조립, 미소관에 따른 리소좀의 정렬 등도 모두 관련된 과정이다.소기관 운반에는 특별한 종류의 미세관 관련 단백질(MAPs)이 필요하다.이들 중 하나는 분자 모터 키네신(MIM 148760 및 MIM 600025 참조)으로, 소포를 미소관의 플러스 끝을 향해 단방향으로 이동하는 ATP 효소이다.또 다른 그러한 MAP은 큰 일체형 ER막 단백질인 키넥틴이다.키넥틴에 대한 항체는 키넥틴에 대한 결합을 억제하는 것으로 나타났다.[OMIM ^[4]제공]

상호 작용

KTN1은 EEF1D,^[5] RhoG^[6]^[7] 및 ^[6]^[7]^[8]^[9]RHOA와 상호 작용하는 것으로 나타났습니다.

레퍼런스

^ ^a ^b ^c GRCh38: 앙상블 릴리즈 89: ENSG00000126777 - 앙상블, 2017년 5월
^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
^ Rao PN, Yu H, Hodge R, Pettenati MJ, Sheetz MP (1997). "Assignment of the human kinectin gene (KTN1), encoding a kinesin-binding protein, to chromosome 14 band q22.1 by in situ hybridization". Cytogenet. Cell Genet. 79 (3–4): 196–7. doi:10.1159/000134719. PMID 9605849.
^ ^a ^b "Entrez Gene: KTN1 kinectin 1 (kinesin receptor)".
^ Ong LL, Er CP, Ho A, Aung MT, Yu H (Aug 2003). "Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum". J. Biol. Chem. 278 (34): 32115–23. doi:10.1074/jbc.M210917200. PMID 12773547.
^ ^a ^b Neudauer CL, Joberty G, Macara IG (Jan 2001). "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10". Biochem. Biophys. Res. Commun. 280 (2): 541–7. doi:10.1006/bbrc.2000.4160. PMID 11162552.
^ ^a ^b Vignal E, Blangy A, Martin M, Gauthier-Rouvière C, Fort P (Dec 2001). "Kinectin is a key effector of RhoG microtubule-dependent cellular activity". Mol. Cell. Biol. 21 (23): 8022–34. doi:10.1128/MCB.21.23.8022-8034.2001. PMC 99969. PMID 11689693.
^ Riento K, Guasch RM, Garg R, Jin B, Ridley AJ (Jun 2003). "RhoE binds to ROCK I and inhibits downstream signaling". Mol. Cell. Biol. 23 (12): 4219–29. doi:10.1128/MCB.23.12.4219-4229.2003. PMC 156133. PMID 12773565.
^ Hotta K, Tanaka K, Mino A, Kohno H, Takai Y (Aug 1996). "Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor". Biochem. Biophys. Res. Commun. 225 (1): 69–74. doi:10.1006/bbrc.1996.1132. PMID 8769096.

추가 정보

Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S (1994). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1". DNA Res. 1 (1): 27–35. doi:10.1093/dnares/1.1.27. PMID 7584026.
Nomura N, Miyajima N, Sazuka T, Tanaka A, Kawarabayasi Y, Sato S, Nagase T, Seki N, Ishikawa K, Tabata S (1994). "Prediction of the coding sequences of unidentified human genes. I. The coding sequences of 40 new genes (KIAA0001-KIAA0040) deduced by analysis of randomly sampled cDNA clones from human immature myeloid cell line KG-1 (supplement)". DNA Res. 1 (1): 47–56. doi:10.1093/dnares/1.1.47. PMID 7584028.
Fütterer A, Kruppa G, Krämer B, Lemke H, Krönke M (1995). "Molecular cloning and characterization of human kinectin". Mol. Biol. Cell. 6 (2): 161–70. doi:10.1091/mbc.6.2.161. PMC 275826. PMID 7787243.
Yu H, Nicchitta CV, Kumar J, Becker M, Toyoshima I, Sheetz MP (1995). "Characterization of kinectin, a kinesin-binding protein: primary sequence and N-terminal topogenic signal analysis". Mol. Biol. Cell. 6 (2): 171–83. doi:10.1091/mbc.6.2.171. PMC 275827. PMID 7787244.
Print CG, Leung E, Harrison JE, Watson JD, Krissansen GW (1994). "Cloning of a gene encoding a human leukocyte protein characterised by extensive heptad repeats". Gene. 144 (2): 221–8. doi:10.1016/0378-1119(94)90381-6. PMID 8039706.
Print CG, Morris CM, Spurr NK, Rooke L, Krissansen GW (1996). "The CG-1 gene, a member of the kinectin and ES/130 family, maps to human chromosome band 14q22". Immunogenetics. 43 (4): 227–9. doi:10.1007/s002510050050. PMID 8575822.
Hotta K, Tanaka K, Mino A, Kohno H, Takai Y (1996). "Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor". Biochem. Biophys. Res. Commun. 225 (1): 69–74. doi:10.1006/bbrc.1996.1132. PMID 8769096.
Alberts AS, Bouquin N, Johnston LH, Treisman R (1998). "Analysis of RhoA-binding proteins reveals an interaction domain conserved in heterotrimeric G protein beta subunits and the yeast response regulator protein Skn7". J. Biol. Chem. 273 (15): 8616–22. doi:10.1074/jbc.273.15.8616. PMID 9535835.
Vancoillie G, Lambert J, Mulder A, Koerten HK, Mommaas AM, Van Oostveldt P, Naeyaert JM (2000). "Kinesin and kinectin can associate with the melanosomal surface and form a link with microtubules in normal human melanocytes". J. Invest. Dermatol. 114 (3): 421–9. doi:10.1046/j.1523-1747.2000.00896.x. PMID 10692099.
Salassidis K, Bruch J, Zitzelsberger H, Lengfelder E, Kellerer AM, Bauchinger M (2000). "Translocation t(10;14)(q11.2:q22.1) fusing the kinetin to the RET gene creates a novel rearranged form (PTC8) of the RET proto-oncogene in radiation-induced childhood papillary thyroid carcinoma". Cancer Res. 60 (11): 2786–9. PMID 10850414.
Ong LL, Lim AP, Er CP, Kuznetsov SA, Yu H (2000). "Kinectin-kinesin binding domains and their effects on organelle motility". J. Biol. Chem. 275 (42): 32854–60. doi:10.1074/jbc.M005650200. PMID 10913441.
Harrington JJ, Sherf B, Rundlett S, Jackson PD, Perry R, Cain S, Leventhal C, Thornton M, Ramachandran R, Whittington J, Lerner L, Costanzo D, McElligott K, Boozer S, Mays R, Smith E, Veloso N, Klika A, Hess J, Cothren K, Lo K, Offenbacher J, Danzig J, Ducar M (2001). "Creation of genome-wide protein expression libraries using random activation of gene expression". Nat. Biotechnol. 19 (5): 440–5. doi:10.1038/88107. PMID 11329013.
Vignal E, Blangy A, Martin M, Gauthier-Rouvière C, Fort P (2001). "Kinectin is a key effector of RhoG microtubule-dependent cellular activity". Mol. Cell. Biol. 21 (23): 8022–34. doi:10.1128/MCB.21.23.8022-8034.2001. PMC 99969. PMID 11689693.
Tran H, Pankov R, Tran SD, Hampton B, Burgess WH, Yamada KM (2002). "Integrin clustering induces kinectin accumulation". J. Cell Sci. 115 (Pt 10): 2031–40. PMID 11973345.
Ong LL, Er CP, Ho A, Aung MT, Yu H (2003). "Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum". J. Biol. Chem. 278 (34): 32115–23. doi:10.1074/jbc.M210917200. PMID 12773547.
Bouwmeester T, Bauch A, Ruffner H, Angrand PO, Bergamini G, Croughton K, Cruciat C, Eberhard D, Gagneur J, Ghidelli S, Hopf C, Huhse B, Mangano R, Michon AM, Schirle M, Schlegl J, Schwab M, Stein MA, Bauer A, Casari G, Drewes G, Gavin AC, Jackson DB, Joberty G, Neubauer G, Rick J, Kuster B, Superti-Furga G (2004). "A physical and functional map of the human TNF-alpha/NF-kappa B signal transduction pathway". Nat. Cell Biol. 6 (2): 97–105. doi:10.1038/ncb1086. PMID 14743216.

인간 염색체 14번 유전자에 대한 이 기사는 짧은 글이다.위키피디아를 확장함으로써 위키피디아를 도울 수 있습니다.

[refGRCh38Ensembl-1] GRCh38: 앙상블 릴리즈 89: ENSG00000126777 - 앙상블, 2017년 5월

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

[pmid9605849-3] Rao PN, Yu H, Hodge R, Pettenati MJ, Sheetz MP (1997). "Assignment of the human kinectin gene (KTN1), encoding a kinesin-binding protein, to chromosome 14 band q22.1 by in situ hybridization". Cytogenet. Cell Genet. 79 (3–4): 196–7. doi:10.1159/000134719. PMID 9605849.

[entrez-4] "Entrez Gene: KTN1 kinectin 1 (kinesin receptor)".

[pmid12773547-5] Ong LL, Er CP, Ho A, Aung MT, Yu H (Aug 2003). "Kinectin anchors the translation elongation factor-1 delta to the endoplasmic reticulum". J. Biol. Chem. 278 (34): 32115–23. doi:10.1074/jbc.M210917200. PMID 12773547.

[pmid11162552-6] Neudauer CL, Joberty G, Macara IG (Jan 2001). "PIST: a novel PDZ/coiled-coil domain binding partner for the rho-family GTPase TC10". Biochem. Biophys. Res. Commun. 280 (2): 541–7. doi:10.1006/bbrc.2000.4160. PMID 11162552.

[pmid11689693-7] Vignal E, Blangy A, Martin M, Gauthier-Rouvière C, Fort P (Dec 2001). "Kinectin is a key effector of RhoG microtubule-dependent cellular activity". Mol. Cell. Biol. 21 (23): 8022–34. doi:10.1128/MCB.21.23.8022-8034.2001. PMC 99969. PMID 11689693.

[pmid12773565-8] Riento K, Guasch RM, Garg R, Jin B, Ridley AJ (Jun 2003). "RhoE binds to ROCK I and inhibits downstream signaling". Mol. Cell. Biol. 23 (12): 4219–29. doi:10.1128/MCB.23.12.4219-4229.2003. PMC 156133. PMID 12773565.

[pmid8769096-9] Hotta K, Tanaka K, Mino A, Kohno H, Takai Y (Aug 1996). "Interaction of the Rho family small G proteins with kinectin, an anchoring protein of kinesin motor". Biochem. Biophys. Res. Commun. 225 (1): 69–74. doi:10.1006/bbrc.1996.1132. PMID 8769096.

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KTN1

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기능.

상호 작용

레퍼런스

추가 정보