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BRIP1

S Wikipedije, slobodne enciklopedije
BRIP1
Dostupne strukture
PDBPretraga ortologa: PDBe RCSB
Spisak PDB ID kodova

1T15, 1T29, 3AL3

Identifikatori
AliasiBRIP1
Vanjski ID-jeviOMIM: 605882 MGI: 2442836 HomoloGene: 32766 GeneCards: BRIP1
Lokacija gena (čovjek)
Hromosom 17 (čovjek)
Hrom.Hromosom 17 (čovjek)[1]
Hromosom 17 (čovjek)
Genomska lokacija za BRIP1
Genomska lokacija za BRIP1
Bend17q23.2Početak61,679,139 bp[1]
Kraj61,863,559 bp[1]
Lokacija gena (miš)
Hromosom 11 (miš)
Hrom.Hromosom 11 (miš)[2]
Hromosom 11 (miš)
Genomska lokacija za BRIP1
Genomska lokacija za BRIP1
Bend11|11 CPočetak85,948,964 bp[2]
Kraj86,092,019 bp[2]
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
VrsteČovjekMiš
Entrez
Ensembl
UniProt
RefSeq (mRNK)

NM_032043

NM_178309

RefSeq (bjelančevina)

NP_114432

NP_840094

Lokacija (UCSC)Chr 17: 61.68 – 61.86 MbChr 11: 85.95 – 86.09 Mb
PubMed pretraga[3][4]
Wikipodaci
Pogledaj/uredi – čovjekPogledaj/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

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Dužina polipeptidnog lanca je 1.249 aminokiselina, a molekulska težina 140.878 Da.[7]

1020304050
MSSMWSEYTIGGVKIYFPYKAYPSQLAMMNSILRGLNSKQHCLLESPTGS
GKSLALLCSALAWQQSLSGKPADEGVSEKAEVQLSCCCACHSKDFTNNDM
NQGTSRHFNYPSTPPSERNGTSSTCQDSPEKTTLAAKLSAKKQASIYRDE
NDDFQVEKKRIRPLETTQQIRKRHCFGTEVHNLDAKVDSGKTVKLNSPLE
KINSFSPQKPPGHCSRCCCSTKQGNSQESSNTIKKDHTGKSKIPKIYFGT
RTHKQIAQITRELRRTAYSGVPMTILSSRDHTCVHPEVVGNFNRNEKCME
LLDGKNGKSCYFYHGVHKISDQHTLQTFQGMCKAWDIEELVSLGKKLKAC
PYYTARELIQDADIIFCPYNYLLDAQIRESMDLNLKEQVVILDEAHNIED
CARESASYSVTEVQLRFARDELDSMVNNNIRKKDHEPLRAVCCSLINWLE
ANAEYLVERDYESACKIWSGNEMLLTLHKMGITTATFPILQGHFSAVLQK
EEKISPIYGKEEAREVPVISASTQIMLKGLFMVLDYLFRQNSRFADDYKI
AIQQTYSWTNQIDISDKNGLLVLPKNKKRSRQKTAVHVLNFWCLNPAVAF
SDINGKVQTIVLTSGTLSPMKSFSSELGVTFTIQLEANHIIKNSQVWVGT
IGSGPKGRNLCATFQNTETFEFQDEVGALLLSVCQTVSQGILCFLPSYKL
LEKLKERWLSTGLWHNLELVKTVIVEPQGGEKTNFDELLQVYYDAIKYKG
EKDGALLVAVCRGKVSEGLDFSDDNARAVITIGIPFPNVKDLQVELKRQY
NDHHSKLRGLLPGRQWYEIQAYRALNQALGRCIRHRNDWGALILVDDRFR
NNPSRYISGLSKWVRQQIQHHSTFESALESLAEFSKKHQKVLNVSIKDRT
NIQDNESTLEVTSLKYSTPPYLLEAASHLSPENFVEDEAKICVQELQCPK
IITKNSPLPSSIISRKEKNDPVFLEEAGKAEKIVISRSTSPTFNKQTKRV
SWSSFNSLGQYFTGKIPKATPELGSSENSASSPPRFKTEKMESKTVLPFT
DKCESSNLTVNTSFGSCPQSETIISSLKIDATLTRKNHSEHPLCSEEALD
PDIELSLVSEEDKQSTSNRDFETEAEDESIYFTPELYDPEDTDEEKNDLA
ETDRGNRLANNSDCILAKDLFEIRTIKEVDSAREVKAEDCIDTKLNGILH
IEESKIDDIDGNVKTTWINELELGKTHEIEIKNFKPSPSKNKGMFPGFK

Funkcija

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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.

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

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

Reference

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  1. ^ a b c GRCh38: Ensembl release 89: ENSG00000136492 - Ensembl, maj 2017
  2. ^ a b c 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.
  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.
  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.
  7. ^ a b c "Entrez Gene: BRIP1 BRCA1 interacting protein C-terminal helicase 1".
  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.
  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).
  11. ^ 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.
  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.
  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.
  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.
  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.
  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.
  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.

Dopunska literatura

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Vanjski linkovi

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