TBX1

TBX1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	4A04
Identifikatori
Aliasi	TBX1
Vanjski ID-jevi	OMIM: 602054 MGI: 98493 HomoloGene: 7966 GeneCards: TBX1
Lokacija gena (čovjek)
Hrom.	Hromosom 22 (čovjek)
Kraj	19,783,593 bp
Lokacija gena (miš)
Hrom.	Hromosom 16 (miš)
Kraj	18,409,421 bp
Ontologija gena
Molekularna funkcija	• sequence-specific DNA binding; • protein dimerization activity; • protein homodimerization activity; • GO:0001131, GO:0001151, GO:0001130, GO:0001204 DNA-binding transcription factor activity; • vezivanje sa DNK; • GO:0001200, GO:0001133, GO:0001201 DNA-binding transcription factor activity, RNA polymerase II-specific;
Ćelijska komponenta	• jedro;
Biološki proces	• pattern specification process; • negative regulation of mesenchymal cell apoptotic process; • cellular response to retinoic acid; • positive regulation of protein phosphorylation; • semicircular canal morphogenesis; • GO:0009373 regulation of transcription, DNA-templated; • epithelial cell differentiation; • blood vessel morphogenesis; • muscle organ morphogenesis; • tongue morphogenesis; • positive regulation of tongue muscle cell differentiation; • positive regulation of epithelial cell proliferation; • thymus development; • mesenchymal cell apoptotic process; • cell fate specification; • negative regulation of cell differentiation; • soft palate development; • muscle cell fate commitment; • coronary artery morphogenesis; • muscle organ development; • heart morphogenesis; • outflow tract morphogenesis; • vagus nerve morphogenesis; • outer ear morphogenesis; • sluh; • cellular response to fibroblast growth factor stimulus; • aorta morphogenesis; • lymph vessel development; • transcription, DNA-templated; • outflow tract septum morphogenesis; • ear morphogenesis; • odontogenesis of dentin-containing tooth; • multicellular organism development; • heart development; • thyroid gland development; • determination of left/right symmetry; • retinoic acid receptor signaling pathway; • blood vessel development; • positive regulation of mesenchymal cell proliferation; • parathyroid gland development; • inner ear morphogenesis; • muscle tissue morphogenesis; • cochlea morphogenesis; • Angiogeneza; • neural crest cell migration; • positive regulation of cell population proliferation; • artery morphogenesis; • middle ear morphogenesis; • socijalno ponašanje; • embryonic cranial skeleton morphogenesis; • embryonic viscerocranium morphogenesis; • enamel mineralization; • mesoderm development; • Ćelijska proliferacija; • face morphogenesis; • anterior/posterior pattern specification; • positive regulation of MAPK cascade; • GO:0003257, GO:0010735, GO:1901228, GO:1900622, GO:1904488 positive regulation of transcription by RNA polymerase II; • pharyngeal system development; • regulation of animal organ morphogenesis; • GO:0044324, GO:0003256, GO:1901213, GO:0046019, GO:0046020, GO:1900094, GO:0061216, GO:0060994, GO:1902064, GO:0003258, GO:0072212 regulation of transcription by RNA polymerase II; • GO:0060469, GO:0009371 positive regulation of transcription, DNA-templated;
	Izvori:Amigo / QuickGO
Ortolozi
	6899
	21380
	ENSG00000184058
	ENSMUSG00000009097
	O43435
	P70323
	NM_005992; NM_080646; NM_080647; NM_001379200
	NM_001285472; NM_001285476; NM_011532; NM_001373938
	NP_005983; NP_542377; NP_542378; NP_001366129
	NP_001272401; NP_001272405; NP_035662
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

RING-kutijski protein 1 jest protein koji je kod ljudi kodiran genom RBX1 sa hromosoma 22.^[5]^[6]

Aminokiselinska sekvenca

Dužina polipeptidnog lanca je aminokiselina, a molekulska težina 108 12.274 Da.^[7]

C: Cistein

D: Asparaginska kiselina

E: Glutaminska kiselina

F: Fenilalanin

G: Glicin

H: Histidin

I: Izoleucin

K: Lizin

L: Leucin

M: Metionin

N: Asparagin

P: Prolin

Q: Glutamin

R: Arginin

S: Serin

T: Treonin

V: Valin

W: Triptofan

Y: Tirozin

10	20	30	40	50
MAAAMDVDTP	SGTNSGAGKK	RFEVKKWNAV	ALWAWDIVVD	NCAICRNHIM
DLCIECQANQ	ASATSEECTV	AWGVCNHAFH	FHCISRWLKT	RQVCPLDNRE
WEFQKYGH

Funkcija

Ovaj gen kodira evolucijski konzervirani protein koji je u interakciji sa kulinima. Protein ima jedinstvenu ulogu u reakciji ubikvitinacije heterodimerizacijom sa kulinom-1, da bi katalizirao polimerizaciju ubikvitina. Također može biti uključen i u regulaciju prometa proteina.^[7]

Interakcije

Pokazalo se da je RBX1 u interakciji sa:

Reference

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000184058 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000009097 - Ensembl, maj 2017
^ "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.
^ Kamura T, Koepp DM, Conrad MN, Skowyra D, Moreland RJ, Iliopoulos O, Lane WS, Kaelin WG, Elledge SJ, Conaway RC, Harper JW, Conaway JW (Apr 1999). "Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase". Science. 284 (5414): 657–61. doi:10.1126/science.284.5414.657. PMID 10213691.
^ ^a ^b ^c ^d ^e Ohta T, Michel JJ, Schottelius AJ, Xiong Y (Apr 1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Molecular Cell. 3 (4): 535–41. doi:10.1016/S1097-2765(00)80482-7. PMID 10230407.
^ ^a ^b "Entrez Gene: RBX1 ring-box 1".
^ ^a ^b Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". The Journal of Biological Chemistry. 278 (18): 15905–10. doi:10.1074/jbc.M213070200. PMID 12609982.
^ ^a ^b ^c Kim AY, Bommeljé CC, Lee BE, Yonekawa Y, Choi L, Morris LG, Huang G, Kaufman A, Ryan RJ, Hao B, Ramanathan Y, Singh B (Nov 2008). "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation". The Journal of Biological Chemistry. 283 (48): 33211–20. doi:10.1074/jbc.M804440200. PMC 2586271. PMID 18826954.
^ ^a ^b ^c ^d Dias DC, Dolios G, Wang R, Pan ZQ (Dec 2002). "CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16601–6. doi:10.1073/pnas.252646399. PMC 139190. PMID 12481031.
^ Kim J, Kim JH, Lee SH, Kim DH, Kang HY, Bae SH, Pan ZQ, Seo YS (Jul 2002). "The novel human DNA helicase hFBH1 is an F-box protein". The Journal of Biological Chemistry. 277 (27): 24530–7. doi:10.1074/jbc.M201612200. PMID 11956208.
^ Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP (Apr 2002). "Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex". Nature. 416 (6882): 703–9. doi:10.1038/416703a. PMID 11961546. S2CID 4423882.
^ Guerrero-Santoro J, Kapetanaki MG, Hsieh CL, Gorbachinsky I, Levine AS, Rapić-Otrin V (Jul 2008). "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A". Cancer Research. 68 (13): 5014–22. doi:10.1158/0008-5472.CAN-07-6162. PMID 18593899.
^ Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA (Sep 2008). "Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation". Cell. 134 (6): 995–1006. doi:10.1016/j.cell.2008.07.022. PMC 2628631. PMID 18805092.
^ Panasyuk G, Nemazanyy I, Filonenko V, Gout I (May 2008). "Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1". Biochemical and Biophysical Research Communications. 369 (2): 339–43. doi:10.1016/j.bbrc.2008.02.016. PMID 18279656.

Dopunska literatura

Skowyra D, Koepp DM, Kamura T, Conrad MN, Conaway RC, Conaway JW, Elledge SJ, Harper JW (Apr 1999). "Reconstitution of G1 cyclin ubiquitination with complexes containing SCFGrr1 and Rbx1". Science. 284 (5414): 662–5. doi:10.1126/science.284.5414.662. PMID 10213692.
Tan P, Fuchs SY, Chen A, Wu K, Gomez C, Ronai Z, Pan ZQ (Apr 1999). "Recruitment of a ROC1-CUL1 ubiquitin ligase by Skp1 and HOS to catalyze the ubiquitination of I kappa B alpha". Molecular Cell. 3 (4): 527–33. doi:10.1016/S1097-2765(00)80481-5. PMID 10230406.
Winston JT, Koepp DM, Zhu C, Elledge SJ, Harper JW (Oct 1999). "A family of mammalian F-box proteins". Current Biology. 9 (20): 1180–2. doi:10.1016/S0960-9822(00)80021-4. PMID 10531037.
Kamura T, Conrad MN, Yan Q, Conaway RC, Conaway JW (Nov 1999). "The Rbx1 subunit of SCF and VHL E3 ubiquitin ligase activates Rub1 modification of cullins Cdc53 and Cul2". Genes & Development. 13 (22): 2928–33. doi:10.1101/gad.13.22.2928. PMC 317157. PMID 10579999.
Dunham I, Shimizu N, Roe BA, Chissoe S, Hunt AR, Collins JE, Bruskiewich R, Beare DM, Clamp M, Smink LJ, Ainscough R, Almeida JP, Babbage A, Bagguley C, Bailey J, Barlow K, Bates KN, Beasley O, Bird CP, Blakey S, Bridgeman AM, Buck D, Burgess J, Burrill WD, O'Brien KP (Dec 1999). "The DNA sequence of human chromosome 22". Nature. 402 (6761): 489–95. doi:10.1038/990031. PMID 10591208.
Seddiqi N, Charbonnier F, Goudou D, Belkadi L, Rieger F, Alliel PM (Dec 1999). "Genomic organization and expression of the ubiquitin-proteasome complex-associated protein Rbx1/ROC1/Hrt1". Cellular and Molecular Biology. 45 (8): 1131–7. PMID 10643962.
Read MA, Brownell JE, Gladysheva TB, Hottelet M, Parent LA, Coggins MB, Pierce JW, Podust VN, Luo RS, Chau V, Palombella VJ (Apr 2000). "Nedd8 modification of cul-1 activates SCF(beta(TrCP))-dependent ubiquitination of IkappaBalpha". Molecular and Cellular Biology. 20 (7): 2326–33. doi:10.1128/MCB.20.7.2326-2333.2000. PMC 85397. PMID 10713156.
Furukawa M, Zhang Y, McCarville J, Ohta T, Xiong Y (Nov 2000). "The CUL1 C-terminal sequence and ROC1 are required for efficient nuclear accumulation, NEDD8 modification, and ubiquitin ligase activity of CUL1". Molecular and Cellular Biology. 20 (21): 8185–97. doi:10.1128/MCB.20.21.8185-8197.2000. PMC 86428. PMID 11027288.
Maeda I, Ohta T, Koizumi H, Fukuda M (Apr 2001). "In vitro ubiquitination of cyclin D1 by ROC1-CUL1 and ROC1-CUL3". FEBS Letters. 494 (3): 181–5. doi:10.1016/S0014-5793(01)02343-2. PMID 11311237.
Lyapina S, Cope G, Shevchenko A, Serino G, Tsuge T, Zhou C, Wolf DA, Wei N, Shevchenko A, Deshaies RJ (May 2001). "Promotion of NEDD-CUL1 conjugate cleavage by COP9 signalosome". Science. 292 (5520): 1382–5. doi:10.1126/science.1059780. PMID 11337588. S2CID 14224920.
Fukuchi M, Imamura T, Chiba T, Ebisawa T, Kawabata M, Tanaka K, Miyazono K (May 2001). "Ligand-dependent degradation of Smad3 by a ubiquitin ligase complex of ROC1 and associated proteins". Molecular Biology of the Cell. 12 (5): 1431–43. doi:10.1091/mbc.12.5.1431. PMC 34595. PMID 11359933.
Kamura T, Burian D, Yan Q, Schmidt SL, Lane WS, Querido E, Branton PE, Shilatifard A, Conaway RC, Conaway JW (Aug 2001). "Muf1, a novel Elongin BC-interacting leucine-rich repeat protein that can assemble with Cul5 and Rbx1 to reconstitute a ubiquitin ligase". The Journal of Biological Chemistry. 276 (32): 29748–53. doi:10.1074/jbc.M103093200. PMID 11384984.
Wu K, Chen A, Tan P, Pan ZQ (Jan 2002). "The Nedd8-conjugated ROC1-CUL1 core ubiquitin ligase utilizes Nedd8 charged surface residues for efficient polyubiquitin chain assembly catalyzed by Cdc34". The Journal of Biological Chemistry. 277 (1): 516–27. doi:10.1074/jbc.M108008200. PMID 11675391.
Gomes MD, Lecker SH, Jagoe RT, Navon A, Goldberg AL (Dec 2001). "Atrogin-1, a muscle-specific F-box protein highly expressed during muscle atrophy". Proceedings of the National Academy of Sciences of the United States of America. 98 (25): 14440–5. doi:10.1073/pnas.251541198. PMC 64700. PMID 11717410.
Kim J, Kim JH, Lee SH, Kim DH, Kang HY, Bae SH, Pan ZQ, Seo YS (Jul 2002). "The novel human DNA helicase hFBH1 is an F-box protein". The Journal of Biological Chemistry. 277 (27): 24530–7. doi:10.1074/jbc.M201612200. PMID 11956208.
Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP (Apr 2002). "Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex". Nature. 416 (6882): 703–9. doi:10.1038/416703a. PMID 11961546. S2CID 4423882.
Yoshida Y, Chiba T, Tokunaga F, Kawasaki H, Iwai K, Suzuki T, Ito Y, Matsuoka K, Yoshida M, Tanaka K, Tai T (Jul 2002). "E3 ubiquitin ligase that recognizes sugar chains". Nature. 418 (6896): 438–42. doi:10.1038/nature00890. PMID 12140560. S2CID 4424996.
Brower CS, Sato S, Tomomori-Sato C, Kamura T, Pause A, Stearman R, Klausner RD, Malik S, Lane WS, Sorokina I, Roeder RG, Conaway JW, Conaway RC (Aug 2002). "Mammalian mediator subunit mMED8 is an Elongin BC-interacting protein that can assemble with Cul2 and Rbx1 to reconstitute a ubiquitin ligase". Proceedings of the National Academy of Sciences of the United States of America. 99 (16): 10353–8. doi:10.1073/pnas.162424199. PMC 124918. PMID 12149480.

Vanjski linkovi

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000184058 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000009097 - Ensembl, maj 2017

[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.

[pmid10213691-5] Kamura T, Koepp DM, Conrad MN, Skowyra D, Moreland RJ, Iliopoulos O, Lane WS, Kaelin WG, Elledge SJ, Conaway RC, Harper JW, Conaway JW (Apr 1999). "Rbx1, a component of the VHL tumor suppressor complex and SCF ubiquitin ligase". Science. 284 (5414): 657–61. doi:10.1126/science.284.5414.657. PMID 10213691.

[pmid10230407-6] Ohta T, Michel JJ, Schottelius AJ, Xiong Y (Apr 1999). "ROC1, a homolog of APC11, represents a family of cullin partners with an associated ubiquitin ligase activity". Molecular Cell. 3 (4): 535–41. doi:10.1016/S1097-2765(00)80482-7. PMID 10230407.

[entrez-7] "Entrez Gene: RBX1 ring-box 1".

[pmid12609982-8] Min KW, Hwang JW, Lee JS, Park Y, Tamura TA, Yoon JB (May 2003). "TIP120A associates with cullins and modulates ubiquitin ligase activity". The Journal of Biological Chemistry. 278 (18): 15905–10. doi:10.1074/jbc.M213070200. PMID 12609982.

[pmid18826954-9] Kim AY, Bommeljé CC, Lee BE, Yonekawa Y, Choi L, Morris LG, Huang G, Kaufman A, Ryan RJ, Hao B, Ramanathan Y, Singh B (Nov 2008). "SCCRO (DCUN1D1) is an essential component of the E3 complex for neddylation". The Journal of Biological Chemistry. 283 (48): 33211–20. doi:10.1074/jbc.M804440200. PMC 2586271. PMID 18826954.

[pmid12481031-10] Dias DC, Dolios G, Wang R, Pan ZQ (Dec 2002). "CUL7: A DOC domain-containing cullin selectively binds Skp1.Fbx29 to form an SCF-like complex". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16601–6. doi:10.1073/pnas.252646399. PMC 139190. PMID 12481031.

[pmid11956208-11] Kim J, Kim JH, Lee SH, Kim DH, Kang HY, Bae SH, Pan ZQ, Seo YS (Jul 2002). "The novel human DNA helicase hFBH1 is an F-box protein". The Journal of Biological Chemistry. 277 (27): 24530–7. doi:10.1074/jbc.M201612200. PMID 11956208.

[pmid11961546-12] Zheng N, Schulman BA, Song L, Miller JJ, Jeffrey PD, Wang P, Chu C, Koepp DM, Elledge SJ, Pagano M, Conaway RC, Conaway JW, Harper JW, Pavletich NP (Apr 2002). "Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex". Nature. 416 (6882): 703–9. doi:10.1038/416703a. PMID 11961546. S2CID 4423882.

[pmid18593899-13] Guerrero-Santoro J, Kapetanaki MG, Hsieh CL, Gorbachinsky I, Levine AS, Rapić-Otrin V (Jul 2008). "The cullin 4B-based UV-damaged DNA-binding protein ligase binds to UV-damaged chromatin and ubiquitinates histone H2A". Cancer Research. 68 (13): 5014–22. doi:10.1158/0008-5472.CAN-07-6162. PMID 18593899.

[pmid18805092-14] Duda DM, Borg LA, Scott DC, Hunt HW, Hammel M, Schulman BA (Sep 2008). "Structural insights into NEDD8 activation of cullin-RING ligases: conformational control of conjugation". Cell. 134 (6): 995–1006. doi:10.1016/j.cell.2008.07.022. PMC 2628631. PMID 18805092.

[pmid18279656-15] Panasyuk G, Nemazanyy I, Filonenko V, Gout I (May 2008). "Ribosomal protein S6 kinase 1 interacts with and is ubiquitinated by ubiquitin ligase ROC1". Biochemical and Biophysical Research Communications. 369 (2): 339–43. doi:10.1016/j.bbrc.2008.02.016. PMID 18279656.

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