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FAKD2_MOUSE
ID   FAKD2_MOUSE             Reviewed;         689 AA.
AC   Q922E6; Q3TLQ2; Q3U526; Q3UFY6; Q8BT79; Q8C3T6;
DT   07-FEB-2006, integrated into UniProtKB/Swiss-Prot.
DT   01-MAR-2004, sequence version 2.
DT   03-AUG-2022, entry version 133.
DE   RecName: Full=FAST kinase domain-containing protein 2, mitochondrial;
DE   Flags: Precursor;
GN   Name=Fastkd2;
OS   Mus musculus (Mouse).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC   Murinae; Mus; Mus.
OX   NCBI_TaxID=10090;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=C57BL/6J, and NOD;
RC   TISSUE=Embryo, Fetal lung, Mammary gland, and Thymus;
RX   PubMed=16141072; DOI=10.1126/science.1112014;
RA   Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA   Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA   Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA   Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA   Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA   Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA   Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA   Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA   Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA   Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA   Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA   Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA   Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA   Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA   Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA   Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA   Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA   Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA   Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA   Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA   Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA   Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA   Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA   Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA   Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA   van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA   Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA   Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA   Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA   Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA   Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA   Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA   Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA   Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT   "The transcriptional landscape of the mammalian genome.";
RL   Science 309:1559-1563(2005).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   STRAIN=FVB/N, and NMRI; TISSUE=Embryo, and Mammary tumor;
RX   PubMed=15489334; DOI=10.1101/gr.2596504;
RG   The MGC Project Team;
RT   "The status, quality, and expansion of the NIH full-length cDNA project:
RT   the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [3]
RP   TISSUE SPECIFICITY.
RX   PubMed=18771761; DOI=10.1016/j.ajhg.2008.08.009;
RA   Ghezzi D., Saada A., D'Adamo P., Fernandez-Vizarra E., Gasparini P.,
RA   Tiranti V., Elpeleg O., Zeviani M.;
RT   "FASTKD2 nonsense mutation in an infantile mitochondrial encephalomyopathy
RT   associated with cytochrome c oxidase deficiency.";
RL   Am. J. Hum. Genet. 83:415-423(2008).
RN   [4]
RP   TISSUE SPECIFICITY.
RX   PubMed=20869947; DOI=10.1016/j.bbrc.2010.09.075;
RA   Simarro M., Gimenez-Cassina A., Kedersha N., Lazaro J.B., Adelmant G.O.,
RA   Marto J.A., Rhee K., Tisdale S., Danial N., Benarafa C., Orduna A.,
RA   Anderson P.;
RT   "Fast kinase domain-containing protein 3 is a mitochondrial protein
RT   essential for cellular respiration.";
RL   Biochem. Biophys. Res. Commun. 401:440-446(2010).
CC   -!- FUNCTION: Plays an important role in assembly of the mitochondrial
CC       large ribosomal subunit. As a component of a functional protein-RNA
CC       module, consisting of RCC1L, NGRN, RPUSD3, RPUSD4, TRUB2, FASTKD2 and
CC       16S mitochondrial ribosomal RNA (16S mt-rRNA), controls 16S mt-rRNA
CC       abundance and is required for intra-mitochondrial translation. May play
CC       a role in mitochondrial apoptosis. {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- SUBUNIT: Monomer. Found in a complex with GRSF1, DDX28, DHX30 and
CC       FASTKD5. Associates with the 16S mitochondrial rRNA (16S mt-rRNA).
CC       Forms a regulatory protein-RNA complex, consisting of RCC1L, NGRN,
CC       RPUSD3, RPUSD4, TRUB2, FASTKD2 and 16S mt-rRNA.
CC       {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- SUBCELLULAR LOCATION: Mitochondrion matrix
CC       {ECO:0000250|UniProtKB:Q9NYY8}. Mitochondrion matrix, mitochondrion
CC       nucleoid {ECO:0000250|UniProtKB:Q9NYY8}. Note=Localizes to
CC       mitochondrial RNA granules found in close proximity to the
CC       mitochondrial nucleoids. {ECO:0000250|UniProtKB:Q9NYY8}.
CC   -!- TISSUE SPECIFICITY: Ubiquitously expressed (PubMed:18771761).
CC       Expression detected in spleen, testis, colon, heart, smooth muscle,
CC       kidney, brain, lung, liver, brown and white adipose tissue with highest
CC       expression in testis, heart and smooth muscle.
CC       {ECO:0000269|PubMed:18771761, ECO:0000269|PubMed:20869947}.
CC   -!- SIMILARITY: Belongs to the FAST kinase family. {ECO:0000305}.
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DR   EMBL; AK013125; BAC25392.1; -; mRNA.
DR   EMBL; AK084971; BAC39325.1; -; mRNA.
DR   EMBL; AK148224; BAE28423.1; -; mRNA.
DR   EMBL; AK153916; BAE32254.1; -; mRNA.
DR   EMBL; AK166378; BAE38740.1; -; mRNA.
DR   EMBL; BC008271; AAH08271.2; -; mRNA.
DR   EMBL; BC057208; AAH57208.1; -; mRNA.
DR   EMBL; BC080813; AAH80813.1; -; mRNA.
DR   CCDS; CCDS15001.1; -.
DR   RefSeq; NP_766010.1; NM_172422.3.
DR   AlphaFoldDB; Q922E6; -.
DR   SMR; Q922E6; -.
DR   BioGRID; 217621; 5.
DR   STRING; 10090.ENSMUSP00000027103; -.
DR   iPTMnet; Q922E6; -.
DR   PhosphoSitePlus; Q922E6; -.
DR   EPD; Q922E6; -.
DR   MaxQB; Q922E6; -.
DR   PaxDb; Q922E6; -.
DR   PeptideAtlas; Q922E6; -.
DR   PRIDE; Q922E6; -.
DR   ProteomicsDB; 271551; -.
DR   Antibodypedia; 34183; 239 antibodies from 25 providers.
DR   DNASU; 75619; -.
DR   Ensembl; ENSMUST00000027103; ENSMUSP00000027103; ENSMUSG00000025962.
DR   GeneID; 75619; -.
DR   KEGG; mmu:75619; -.
DR   UCSC; uc007bgl.2; mouse.
DR   CTD; 22868; -.
DR   MGI; MGI:1922869; Fastkd2.
DR   VEuPathDB; HostDB:ENSMUSG00000025962; -.
DR   eggNOG; ENOG502QVSD; Eukaryota.
DR   GeneTree; ENSGT01030000234607; -.
DR   HOGENOM; CLU_025270_0_0_1; -.
DR   InParanoid; Q922E6; -.
DR   OMA; FDIWKLK; -.
DR   OrthoDB; 952682at2759; -.
DR   PhylomeDB; Q922E6; -.
DR   TreeFam; TF352875; -.
DR   BioGRID-ORCS; 75619; 1 hit in 72 CRISPR screens.
DR   ChiTaRS; Fastkd2; mouse.
DR   PRO; PR:Q922E6; -.
DR   Proteomes; UP000000589; Chromosome 1.
DR   RNAct; Q922E6; protein.
DR   Bgee; ENSMUSG00000025962; Expressed in paneth cell and 257 other tissues.
DR   Genevisible; Q922E6; MM.
DR   GO; GO:0005759; C:mitochondrial matrix; IBA:GO_Central.
DR   GO; GO:0042645; C:mitochondrial nucleoid; ISS:UniProtKB.
DR   GO; GO:0005739; C:mitochondrion; HDA:MGI.
DR   GO; GO:0035770; C:ribonucleoprotein granule; ISS:UniProtKB.
DR   GO; GO:0003723; F:RNA binding; IBA:GO_Central.
DR   GO; GO:0019843; F:rRNA binding; ISS:UniProtKB.
DR   GO; GO:0006915; P:apoptotic process; ISS:UniProtKB.
DR   GO; GO:1902775; P:mitochondrial large ribosomal subunit assembly; ISS:UniProtKB.
DR   GO; GO:0000963; P:mitochondrial RNA processing; IBA:GO_Central.
DR   GO; GO:0032543; P:mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0070131; P:positive regulation of mitochondrial translation; ISS:UniProtKB.
DR   GO; GO:0044528; P:regulation of mitochondrial mRNA stability; IBA:GO_Central.
DR   GO; GO:0006396; P:RNA processing; ISS:UniProtKB.
DR   InterPro; IPR010622; FAST_Leu-rich.
DR   InterPro; IPR013584; RAP.
DR   Pfam; PF06743; FAST_1; 1.
DR   Pfam; PF08373; RAP; 1.
DR   SMART; SM00952; RAP; 1.
DR   PROSITE; PS51286; RAP; 1.
PE   2: Evidence at transcript level;
KW   Mitochondrion; Mitochondrion nucleoid; Phosphoprotein; Reference proteome;
KW   Ribosome biogenesis; RNA-binding; rRNA-binding; Transit peptide.
FT   TRANSIT         1..?
FT                   /note="Mitochondrion"
FT                   /evidence="ECO:0000305"
FT   CHAIN           ?..689
FT                   /note="FAST kinase domain-containing protein 2,
FT                   mitochondrial"
FT                   /id="PRO_0000050784"
FT   DOMAIN          617..674
FT                   /note="RAP"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00619"
FT   MOD_RES         113
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYY8"
FT   MOD_RES         126
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0000250|UniProtKB:Q9NYY8"
FT   CONFLICT        55
FT                   /note="G -> V (in Ref. 1; BAE32254)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        172..173
FT                   /note="LA -> FS (in Ref. 1; BAE38740)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        361
FT                   /note="H -> N (in Ref. 1; BAE38740)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        554
FT                   /note="A -> V (in Ref. 1; BAE28423)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        593
FT                   /note="M -> V (in Ref. 1; BAE32254)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        606
FT                   /note="V -> I (in Ref. 1; BAE38740)"
FT                   /evidence="ECO:0000305"
SQ   SEQUENCE   689 AA;  78948 MW;  290D866BC4AAD659 CRC64;
     MNSKARSLLW TIRRFSTLLP RSRALRIDPL GTCRPEVIHS KWNPRNHRLN VFDEGLQPSV
     RYLFQDIFIS KSVDGCIQTK GISHSAVFKP DRLLCPRRLS FDAKHSFVSD GTSDHDLKKI
     NFHHTSSEDV FTKKVRPTPV NYKKLAQECN SLSDVLDTFS KAPTFPGSNY FLAMWIIAKR
     ISEDKRRFER QLMFSHPAFN QLCEQMMREA KIMHYDHLLF SLNAIVKLGI PQNTLMVQTL
     LRTIQERINE CDERCLSILS TALVSMEPCM NVNALRAGLR ILVDQQVWNI KHVFTLQTVM
     KCIGKDAPSA LKKKLEMKAL KELGRFSILN SQHMFEVLAA MDLRSVVLLN ECSKVVIDNV
     HGCPFKVLIS ILQSCRDLRY QNEDLFKSIA EYVATTFDIW KLKQVIFFLL LFETLGFRPP
     GLMDKLMEKV VQEPGSLNVK NIVSILHVYS SLNHVHKIHN REFLEALASA LTGCLHHISS
     ESLLNAVHSF CMMNYFPLAP INQLIKENII NELLTSGDTE KNIHKLHVLN TCLKLDESTY
     KSVHIPLPQL PLSASQPNEK LAEVLSRLLE GEGRFSRNVP LPHNYHIDFE IRMDTNRTQV
     FSFSDVDASS ATNMQRVAVL CVPKSVYCLN SCHPRGLMAM KIRHLNVMGF HVILIHNWEL
     KKLKMEDAVT FVRKKIYSDE VLPTADTTV
 
 
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