BRIP1

BRIP1
Dostupne strukture
PDB	Pretraga ortologa: PDBe RCSB
Spisak PDB ID kodova
	1T15, 1T29, 3AL3
Identifikatori
Aliasi	BRIP1
Vanjski ID-jevi	OMIM: 605882 MGI: 2442836 HomoloGene: 32766 GeneCards: BRIP1
Lokacija gena (čovjek)
Hrom.	Hromosom 17 (čovjek)
Kraj	61,863,559 bp
Lokacija gena (miš)
Hrom.	Hromosom 11 (miš)
Kraj	86,092,019 bp
Obrazac RNK ekspresije
	Više referentnih podataka o ekspresiji
Ontologija gena
Molekularna funkcija	• vezivanje sa DNK; • 4 iron, 4 sulfur cluster binding; • nucleotide binding; • GO:0008026 helicase activity; • iron-sulfur cluster binding; • GO:0004003 DNA helicase activity; • vezivanje iona metala; • GO:0102490, GO:0102491, GO:0102489, GO:0102488, GO:0102487, GO:0102486, GO:0102485 hydrolase activity, acting on acid anhydrides, in phosphorus-containing anhydrides; • GO:0001948, GO:0016582 vezivanje za proteine; • nucleic acid binding; • hydrolase activity; • ATP binding; • chromatin binding;
Ćelijska komponenta	• citoplazma; • Jedarna membrana; • nukleoplazma; • jedro;
Biološki proces	• 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; • DNA damage checkpoint signaling; • cellular response to DNA damage stimulus; • cellular response to vitamin; • nucleobase-containing compound metabolic process; • negative regulation of cell population proliferation; • Replikacija DNK; • DNA duplex unwinding; • double-strand break repair; • GO:0100026 Popravka DNK; • homologous chromosome pairing at meiosis; • Spermatogeneza; • spermatogonial cell division; • spermatid development; • male gonad development; • response to toxic substance; • negative regulation of gene expression; • meiotic DNA double-strand break processing involved in reciprocal meiotic recombination; • chiasma assembly; • cellular response to hypoxia; • seminiferous tubule development; • cellular response to angiotensin; • double-strand break repair involved in meiotic recombination; • Popravak ekscizijom nukleotida; • regulation of signal transduction by p53 class mediator;
	Izvori:Amigo / QuickGO
Ortolozi
	83990
	237911
	ENSG00000136492
	ENSMUSG00000034329
	Q9BX63
	Q5SXJ3
	NM_032043
	NM_178309
	NP_114432
	NP_840094
	Wikipodaci
Pogledaj/uredi – čovjek	Pogledaj/uredi – miš

Protein komplementarne grupe J Fanconijeve anemije jest protein koji je kod ljudi kodiran genom BRIP1 sa hromosoma 17.^[5]^[6]^[7]

Aminokiselinska sekvenca[uredi | uredi izvor]

Dužina polipeptidnog lanca je 1.249 aminokiselina, a molekulska težina 140.878 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
MSSMWSEYTI	GGVKIYFPYK	AYPSQLAMMN	SILRGLNSKQ	HCLLESPTGS
GKSLALLCSA	LAWQQSLSGK	PADEGVSEKA	EVQLSCCCAC	HSKDFTNNDM
NQGTSRHFNY	PSTPPSERNG	TSSTCQDSPE	KTTLAAKLSA	KKQASIYRDE
NDDFQVEKKR	IRPLETTQQI	RKRHCFGTEV	HNLDAKVDSG	KTVKLNSPLE
KINSFSPQKP	PGHCSRCCCS	TKQGNSQESS	NTIKKDHTGK	SKIPKIYFGT
RTHKQIAQIT	RELRRTAYSG	VPMTILSSRD	HTCVHPEVVG	NFNRNEKCME
LLDGKNGKSC	YFYHGVHKIS	DQHTLQTFQG	MCKAWDIEEL	VSLGKKLKAC
PYYTARELIQ	DADIIFCPYN	YLLDAQIRES	MDLNLKEQVV	ILDEAHNIED
CARESASYSV	TEVQLRFARD	ELDSMVNNNI	RKKDHEPLRA	VCCSLINWLE
ANAEYLVERD	YESACKIWSG	NEMLLTLHKM	GITTATFPIL	QGHFSAVLQK
EEKISPIYGK	EEAREVPVIS	ASTQIMLKGL	FMVLDYLFRQ	NSRFADDYKI
AIQQTYSWTN	QIDISDKNGL	LVLPKNKKRS	RQKTAVHVLN	FWCLNPAVAF
SDINGKVQTI	VLTSGTLSPM	KSFSSELGVT	FTIQLEANHI	IKNSQVWVGT
IGSGPKGRNL	CATFQNTETF	EFQDEVGALL	LSVCQTVSQG	ILCFLPSYKL
LEKLKERWLS	TGLWHNLELV	KTVIVEPQGG	EKTNFDELLQ	VYYDAIKYKG
EKDGALLVAV	CRGKVSEGLD	FSDDNARAVI	TIGIPFPNVK	DLQVELKRQY
NDHHSKLRGL	LPGRQWYEIQ	AYRALNQALG	RCIRHRNDWG	ALILVDDRFR
NNPSRYISGL	SKWVRQQIQH	HSTFESALES	LAEFSKKHQK	VLNVSIKDRT
NIQDNESTLE	VTSLKYSTPP	YLLEAASHLS	PENFVEDEAK	ICVQELQCPK
IITKNSPLPS	SIISRKEKND	PVFLEEAGKA	EKIVISRSTS	PTFNKQTKRV
SWSSFNSLGQ	YFTGKIPKAT	PELGSSENSA	SSPPRFKTEK	MESKTVLPFT
DKCESSNLTV	NTSFGSCPQS	ETIISSLKID	ATLTRKNHSE	HPLCSEEALD
PDIELSLVSE	EDKQSTSNRD	FETEAEDESI	YFTPELYDPE	DTDEEKNDLA
ETDRGNRLAN	NSDCILAKDL	FEIRTIKEVD	SAREVKAEDC	IDTKLNGILH
IEESKIDDID	GNVKTTWINE	LELGKTHEIE	IKNFKPSPSK	NKGMFPGFK

Funkcija[uredi | uredi izvor]

Protein kodiran ovim genom je član porodice helikaza RecQ DEAH i stupa u interakciju sa BRCT ponavljanjima raka dojke tipa 1 (BRCA1). Vezani kompleks je važan u normalnoj funkciji popravljanja prekida dvostrukog lanca raka dojke tipa 1 (BRCA1). Ovaj gen može biti meta mutacija koje izazivaju rak zametne linije.^[7]

Čini se da je ovaj protein važan i kod raka jajnika, gdje djeluje kao supresor tumora.^[8] Mutacije u BRIP1 povezane su sa 10-15% rizikom od raka jajnika.^[9]

Čini se da BRIP1 ima važnu ulogu u neuronskim ćelijama, tako što potiskuje oksidativni stres, a ekscitotoksičnost inducira oštećenje DNK i štiti integritet mitohondrija.^[10] Nedostatak BRIP1 uzrokuje povećano oštećenje DNK, mitohondrijske abnormalnosti i smrt neuronske ćelije.

Popravka DNK[uredi | uredi izvor]

BRIP1 protein je DNK helikaza koja se koristi u homolognorekombinacijskoj popravci i u odgovoru ćelije na stres replikacije DNK.^[11] Djelimično, BRIP1 obavlja svoju funkciju interakcijom s drugim ključnim proteinima za popravku DNK, posebno MLH1, BRCA1 i BLM.^[11] Ova grupa proteina pomaže u osiguravanju stabilnosti genoma, a posebno popravlja prekide dvostrukih lanaca DNK tokom profaze 1 mejoze.

Interakcije[uredi | uredi izvor]

Pokazalo se da BRIP1 reaguje sa BRCA1.^[12]^[13]^[14]^[15]^[16]^[17]

Reference[uredi | uredi izvor]

^ ^a ^b ^c GRCh38: Ensembl release 89: ENSG00000136492 - Ensembl, maj 2017
^ ^a ^b ^c GRCm38: Ensembl release 89: ENSMUSG00000034329 - 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.
^ Menichini P, Linial M (novembar 2001). "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutation Research. 487 (1–2): 67–71. doi:10.1016/s0921-8777(01)00104-5. PMID 11595410.
^ Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, et al. (april 2001). "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function". Cell. 105 (1): 149–160. doi:10.1016/S0092-8674(01)00304-X. PMID 11301010. S2CID 15966253.
^ ^a ^b ^c "Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1".
^ Rafnar T, Gudbjartsson DF, Sulem P, Jonasdottir A, Sigurdsson A, Jonasdottir A, et al. (oktobar 2011). "Mutations in BRIP1 confer high risk of ovarian cancer". Nature Genetics. 43 (11): 1104–1107. doi:10.1038/ng.955. hdl:2336/228034. PMID 21964575. S2CID 24535565.
^ Ring KL, Garcia C, Thomas MH, Modesitt SC (novembar 2017). "Current and future role of genetic screening in gynecologic malignancies". American Journal of Obstetrics and Gynecology. 217 (5): 512–521. doi:10.1016/j.ajog.2017.04.011. PMID 28411145. S2CID 29024566.
^ Mani C, Acharya G, Kshirsagar S, Vijayan M, Khan H, Reddy PH, Palle K (2022). "A Novel Role for BRIP1/FANCJ in Neuronal Cells Health and in Resolving Oxidative Stress-Induced DNA Lesions". Journal of Alzheimer's Disease. 85 (1): 207–221. doi:10.3233/JAD-215305. PMID 34776453 Provjerite vrijednost parametra |pmid= (pomoć). S2CID 244078679 Provjerite vrijednost parametra |s2cid= (pomoć).
^ ^a ^b Sun X, Brieño-Enríquez MA, Cornelius A, Modzelewski AJ, Maley TT, Campbell-Peterson KM, et al. (juni 2016). "FancJ (Brip1) loss-of-function allele results in spermatogonial cell depletion during embryogenesis and altered processing of crossover sites during meiotic prophase I in mice". Chromosoma. 125 (2): 237–252. doi:10.1007/s00412-015-0549-2. PMC 5415080. PMID 26490168.
^ Botuyan MV, Nominé Y, Yu X, Juranic N, Macura S, Chen J, Mer G (juli 2004). "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure. 12 (7): 1137–1146. doi:10.1016/j.str.2004.06.002. PMC 3652423. PMID 15242590.
^ Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP (mart 2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development. 16 (5): 583–593. doi:10.1101/gad.959202. PMC 155350. PMID 11877378.
^ Yu X, Chini CC, He M, Mer G, Chen J (oktobar 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–642. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID 14576433. S2CID 29407635.
^ Rodriguez M, Yu X, Chen J, Songyang Z (decembar 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". The Journal of Biological Chemistry. 278 (52): 52914–52918. doi:10.1074/jbc.C300407200. PMID 14578343.
^ Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ (juni 2004). "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nature Structural & Molecular Biology. 11 (6): 512–518. doi:10.1038/nsmb775. PMID 15133502. S2CID 7354915.
^ Wada O, Oishi H, Takada I, Yanagisawa J, Yano T, Kato S (august 2004). "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene. 23 (35): 6000–6005. doi:10.1038/sj.onc.1207786. PMID 15208681.

Dopunska literatura[uredi | uredi izvor]

Kobayashi A, Yamagiwa H, Hoshino H, Muto A, Sato K, Morita M, et al. (mart 2000). "A combinatorial code for gene expression generated by transcription factor Bach2 and MAZR (MAZ-related factor) through the BTB/POZ domain". Molecular and Cellular Biology. 20 (5): 1733–1746. doi:10.1128/MCB.20.5.1733-1746.2000. PMC 85356. PMID 10669750.
Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP (mart 2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development. 16 (5): 583–593. doi:10.1101/gad.959202. PMC 155350. PMID 11877378.
Luo L, Lei H, Du Q, von Wachenfeldt A, Kockum I, Luthman H, et al. (april 2002). "No mutations in the BACH1 gene in BRCA1 and BRCA2 negative breast-cancer families linked to 17q22". International Journal of Cancer. 98 (4): 638–639. doi:10.1002/ijc.10214. PMID 11920628. S2CID 31182390.
Karppinen SM, Vuosku J, Heikkinen K, Allinen M, Winqvist R (februar 2003). "No evidence of involvement of germline BACH1 mutations in Finnish breast and ovarian cancer families". European Journal of Cancer. 39 (3): 366–371. doi:10.1016/S0959-8049(02)00498-7. PMID 12565990.
Rutter JL, Smith AM, Dávila MR, Sigurdson AJ, Giusti RM, Pineda MA, et al. (august 2003). "Mutational analysis of the BRCA1-interacting genes ZNF350/ZBRK1 and BRIP1/BACH1 among BRCA1 and BRCA2-negative probands from breast-ovarian cancer families and among early-onset breast cancer cases and reference individuals". Human Mutation. 22 (2): 121–128. doi:10.1002/humu.10238. PMID 12872252. S2CID 36167584.
Suzuki H, Tashiro S, Sun J, Doi H, Satomi S, Igarashi K (decembar 2003). "Cadmium induces nuclear export of Bach1, a transcriptional repressor of heme oxygenase-1 gene". The Journal of Biological Chemistry. 278 (49): 49246–49253. doi:10.1074/jbc.M306764200. PMID 14504288.
Yu X, Chini CC, He M, Mer G, Chen J (oktobar 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–642. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID 14576433. S2CID 29407635.
Rodriguez M, Yu X, Chen J, Songyang Z (decembar 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". The Journal of Biological Chemistry. 278 (52): 52914–52918. doi:10.1074/jbc.C300407200. PMID 14578343.
Cantor S, Drapkin R, Zhang F, Lin Y, Han J, Pamidi S, Livingston DM (februar 2004). "The BRCA1-associated protein BACH1 is a DNA helicase targeted by clinically relevant inactivating mutations". Proceedings of the National Academy of Sciences of the United States of America. 101 (8): 2357–2362. Bibcode:2004PNAS..101.2357C. doi:10.1073/pnas.0308717101. PMC 356955. PMID 14983014.
Shiozaki EN, Gu L, Yan N, Shi Y (maj 2004). "Structure of the BRCT repeats of BRCA1 bound to a BACH1 phosphopeptide: implications for signaling". Molecular Cell. 14 (3): 405–412. doi:10.1016/S1097-2765(04)00238-2. PMID 15125843.
Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ (juni 2004). "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nature Structural & Molecular Biology. 11 (6): 512–518. doi:10.1038/nsmb775. PMID 15133502. S2CID 7354915.
Wada O, Oishi H, Takada I, Yanagisawa J, Yano T, Kato S (august 2004). "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene. 23 (35): 6000–6005. doi:10.1038/sj.onc.1207786. PMID 15208681.
Botuyan MV, Nominé Y, Yu X, Juranic N, Macura S, Chen J, Mer G (juli 2004). "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure. 12 (7): 1137–1146. doi:10.1016/j.str.2004.06.002. PMC 3652423. PMID 15242590.
Gupta R, Sharma S, Sommers JA, Jin Z, Cantor SB, Brosh RM (juli 2005). "Analysis of the DNA substrate specificity of the human BACH1 helicase associated with breast cancer". The Journal of Biological Chemistry. 280 (27): 25450–25460. doi:10.1074/jbc.M501995200. PMID 15878853.

Vanjski linkovi[uredi | uredi izvor]

Lokacija ljudskog genoma BACH1 i stranica sa detaljima o genu BACH1 u UCSC Genome Browseru.
Lokacija ljudskog genoma BRIP1 i stranica sa detaljima o genu BRIP1 u UCSC Genome Browseru.

[refGRCh38Ensembl-1] GRCh38: Ensembl release 89: ENSG00000136492 - Ensembl, maj 2017

[refGRCm38Ensembl-2] GRCm38: Ensembl release 89: ENSMUSG00000034329 - 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.

[pmid11595410-5] Menichini P, Linial M (novembar 2001). "SUVi and BACH1: a new subfamily of mammalian helicases?". Mutation Research. 487 (1–2): 67–71. doi:10.1016/s0921-8777(01)00104-5. PMID 11595410.

[pmid11301010-6] Cantor SB, Bell DW, Ganesan S, Kass EM, Drapkin R, Grossman S, et al. (april 2001). "BACH1, a novel helicase-like protein, interacts directly with BRCA1 and contributes to its DNA repair function". Cell. 105 (1): 149–160. doi:10.1016/S0092-8674(01)00304-X. PMID 11301010. S2CID 15966253.

[entrez-7] "Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1".

[pmid21964575-8] Rafnar T, Gudbjartsson DF, Sulem P, Jonasdottir A, Sigurdsson A, Jonasdottir A, et al. (oktobar 2011). "Mutations in BRIP1 confer high risk of ovarian cancer". Nature Genetics. 43 (11): 1104–1107. doi:10.1038/ng.955. hdl:2336/228034. PMID 21964575. S2CID 24535565.

[9] Ring KL, Garcia C, Thomas MH, Modesitt SC (novembar 2017). "Current and future role of genetic screening in gynecologic malignancies". American Journal of Obstetrics and Gynecology. 217 (5): 512–521. doi:10.1016/j.ajog.2017.04.011. PMID 28411145. S2CID 29024566.

[Mani_2022-10] Mani C, Acharya G, Kshirsagar S, Vijayan M, Khan H, Reddy PH, Palle K (2022). "A Novel Role for BRIP1/FANCJ in Neuronal Cells Health and in Resolving Oxidative Stress-Induced DNA Lesions". Journal of Alzheimer's Disease. 85 (1): 207–221. doi:10.3233/JAD-215305. PMID 34776453 Provjerite vrijednost parametra |pmid= (pomoć). S2CID 244078679 Provjerite vrijednost parametra |s2cid= (pomoć).

[Sun_2016-11] Sun X, Brieño-Enríquez MA, Cornelius A, Modzelewski AJ, Maley TT, Campbell-Peterson KM, et al. (juni 2016). "FancJ (Brip1) loss-of-function allele results in spermatogonial cell depletion during embryogenesis and altered processing of crossover sites during meiotic prophase I in mice". Chromosoma. 125 (2): 237–252. doi:10.1007/s00412-015-0549-2. PMC 5415080. PMID 26490168.

[pmid15242590-12] Botuyan MV, Nominé Y, Yu X, Juranic N, Macura S, Chen J, Mer G (juli 2004). "Structural basis of BACH1 phosphopeptide recognition by BRCA1 tandem BRCT domains". Structure. 12 (7): 1137–1146. doi:10.1016/j.str.2004.06.002. PMC 3652423. PMID 15242590.

[pmid11877378-13] Joo WS, Jeffrey PD, Cantor SB, Finnin MS, Livingston DM, Pavletich NP (mart 2002). "Structure of the 53BP1 BRCT region bound to p53 and its comparison to the Brca1 BRCT structure". Genes & Development. 16 (5): 583–593. doi:10.1101/gad.959202. PMC 155350. PMID 11877378.

[pmid14576433-14] Yu X, Chini CC, He M, Mer G, Chen J (oktobar 2003). "The BRCT domain is a phospho-protein binding domain". Science. 302 (5645): 639–642. Bibcode:2003Sci...302..639Y. doi:10.1126/science.1088753. PMID 14576433. S2CID 29407635.

[pmid14578343-15] Rodriguez M, Yu X, Chen J, Songyang Z (decembar 2003). "Phosphopeptide binding specificities of BRCA1 COOH-terminal (BRCT) domains". The Journal of Biological Chemistry. 278 (52): 52914–52918. doi:10.1074/jbc.C300407200. PMID 14578343.

[pmid15133502-16] Clapperton JA, Manke IA, Lowery DM, Ho T, Haire LF, Yaffe MB, Smerdon SJ (juni 2004). "Structure and mechanism of BRCA1 BRCT domain recognition of phosphorylated BACH1 with implications for cancer". Nature Structural & Molecular Biology. 11 (6): 512–518. doi:10.1038/nsmb775. PMID 15133502. S2CID 7354915.

[pmid15208681-17] Wada O, Oishi H, Takada I, Yanagisawa J, Yano T, Kato S (august 2004). "BRCA1 function mediates a TRAP/DRIP complex through direct interaction with TRAP220". Oncogene. 23 (35): 6000–6005. doi:10.1038/sj.onc.1207786. PMID 15208681.

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p r u Popravak DNK
Popravak ekscizije	Popravak ekscizije baze/AP-mjesto DNK-glikozilaza Uracil-DNK glikozilaza Poli ADP riboza-polimeraza Popravak ekscizijom nukleotida/ERCC XPA XPB XPC XPD/ERCC2 XPE/DDB1 XPF/DDB1 XPG/ERCC5 ERCC1 RPA RAD23A RAD23B Ekscinukleaza Popravak neusklađenosti DNK MLH1 MSH2
Ostali oblici popravka	Transkripcijski-spregnuti popravak ERCC6 ERCC8 Homologno usmjereni popravak Nehomologno spajanje kraja Ku Mikrohomologno posredovano spajanje kraja Postreplikacijski popravak Fotolijaza CRY1 CRY2
Ostali/negrupirani proteini	Ogt PcrA Proliferirajući ćelijski jedarni antigen Homologna rekombinacija RecA/RAD51 Sgs1 Slx4
Regulacija	SOS-kutija SOS odgovor
Ostali/negrupirani	8-Oksoguanin Adaptivni odgovor Kontrolna tačka mejotske rekombinacije RecF-put DNK helikaza: BLM WRN FANC-proteini: Jezgarni proteinski kompleks FANCA FANCB FANCC FANCE FANCF FANCG FANCL FANCM FANCD1 FANCD2 FANCI FANCJ FANCN