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Description:
Non-POU domain-containing octamer-binding protein (NonO protein) (54kDa nuclear RNA- and DNA-binding protein) (p54(nrb)) (p54nrb) (55 kDanuclear protein) (NMT55) (DNA-binding p52/p100 complex, 52 kDasubunit).
Molecular weight: 54232
View which proteins in this organism that is involved with DNA Repair;
classified after biological processes (using data from the GOA project):
DNA repair( GO:0006281 )
Important dates:
15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
05-JUL-2005, sequence version 4.
07-MAR-2006, entry version 53.
Phylogenetic order:
Eukaryota Metazoa Chordata Craniata Vertebrata Euteleostomi Mammalia Eutheria Euarchontoglires Primates Catarrhini Hominidae Homo.
To calculate the pI (Isoelectric point - the pH where a protein has a neutral charge),
go to this page and enter the protein ID (e.g 3MG_ECOLI): http://us.expasy.org/tools/pi_tool.html
Links to references in other databases for protein NONO_HUMAN:
| Database | Pointer | Add. info#1 | Add. info#2 |
| EMBL | L14599 | AAC37578.1 | - |
| EMBL | U89867 | AAC51852.1 | - |
| EMBL | Y11289 | CAA72157.1 | - |
| EMBL | Y11290 | CAA72157.1 | JOINED |
| EMBL | Y11291 | CAA72157.1 | JOINED |
| EMBL | Y11292 | CAA72157.1 | JOINED |
| EMBL | Y11293 | CAA72157.1 | JOINED |
| EMBL | Y11294 | CAA72157.1 | JOINED |
| EMBL | Y11295 | CAA72157.1 | JOINED |
| EMBL | Y11296 | CAA72157.1 | JOINED |
| EMBL | Y11297 | CAA72157.1 | JOINED |
| EMBL | Y11298 | CAA72157.1 | JOINED |
| EMBL | U02493 | AAA03427.1 | - |
| EMBL | CR456761 | CAG33042.1 | - |
| EMBL | BC002364 | AAH02364.1 | - |
| EMBL | BC003129 | AAH03129.1 | - |
| EMBL | BC012141 | AAH12141.1 | - |
| EMBL | BC028299 | AAH28299.1 | - |
| EMBL | BC069616 | AAH69616.1 | - |
| EMBL | BC069639 | AAH69639.1 | - |
| PIR | S29769 | S29769. | |
| HSSP | P19339 | 3SXL | |
| IntAct | Q15233 | -.1 | |
| SWISS-2DPAGE | Q15233 | HUMAN. | |
| Ensembl | ENSG00000147140 | Homo sapiens.1 | |
| H-InvDB | HIX0016862 | -.1 | |
| HGNC | HGNC:7871 | NONO.1 | |
| MIM | 300084 | gene. | |
| LinkHub | Q15233 | -.1 | |
| GO | GO:0005634 | C:nucleus | TAS. |
| GO | GO:0005515 | F:protein binding | IPI. |
| GO | GO:0006397 | P:mRNA processing | TAS. |
| GO | GO:0008380 | P:RNA splicing | TAS. |
| InterPro | IPR012677 | a_b_plait_nuc_bd. | |
| InterPro | IPR012975 | NOPS. | |
| InterPro | IPR000504 | RNP1_RNA_bd. | |
| Pfam | PF08075 | NOPS | 1. |
| Pfam | PF00076 | RRM_1 | 2. |
| SMART | SM00360 | RRM | 2. |
| PROSITE | PS50102 | RRM | 2. |
Keywords:
Activator; Chromosomal translocation; Coiled coil; Direct protein sequencing; DNA damage; DNA recombination; DNA repair; DNA-binding; mRNA processing; mRNA splicing; Nuclear protein; Repeat; RNA-binding; Transcription; Transcription regulation.
References:
RN [1]
RP NUCLEOTIDE SEQUENCE, AND PROTEIN SEQUENCE OF 252-267; 273-279 AND
RP 283-289.
RX MEDLINE=93382787; PubMed=8371983;
RA Dong B., Horowitz D.S., Kobayashi R., Krainer A.R.;
RT "Purification and cDNA cloning of HeLa cell p54nrb, a nuclear protein
RT with two RNA recognition motifs and extensive homology to human
RT splicing factor PSF and Drosophila NONA/BJ6.";
RL Nucleic Acids Res. 21:4085-4092(1993).
RN [2]
RP NUCLEOTIDE SEQUENCE.
RC TISSUE=Mammary carcinoma;
RX MEDLINE=98025317; PubMed=9360842;
RX DOI=10.1097/00019606-199708000-00005;
RA Traish A.M., Huang Y.-H., Ashba J., Pronovost M., Pavao M.,
RA McAneny D.B., Moreland R.B.;
RT "Loss of expression of a 55 kDa nuclear protein (nmt55) in estrogen
RT receptor-negative human breast cancer.";
RL Diagn. Mol. Pathol. 6:209-221(1997).
RN [3]
RP NUCLEOTIDE SEQUENCE, AND TISSUE SPECIFICITY.
RC TISSUE=Blood;
RX MEDLINE=98001080; PubMed=9341872; DOI=10.1007/s004390050553;
RA Peters U., Haberhausen G., Kostrzewa M., Nolte D., Mueller U.;
RT "AFX1 and p54nrb: fine mapping, genomic structure, and exclusion as
RT candidate genes of X-linked dystonia parkinsonism.";
RL Hum. Genet. 100:569-572(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [MRNA].
RA Honore B., Rasmussen H.H., Celis J.E.;
RT "54 kDa human protein.";
RL Submitted (JAN-1994) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Cervix, Kidney, Muscle, and Skin;
RX MEDLINE=22388257; PubMed=12477932; DOI=10.1073/pnas.242603899;
RA Strausberg R.L., Feingold E.A., Grouse L.H., Derge J.G.,
RA Klausner R.D., Collins F.S., Wagner L., Shenmen C.M., Schuler G.D.,
RA Altschul S.F., Zeeberg B., Buetow K.H., Schaefer C.F., Bhat N.K.,
RA Hopkins R.F., Jordan H., Moore T., Max S.I., Wang J., Hsieh F.,
RA Diatchenko L., Marusina K., Farmer A.A., Rubin G.M., Hong L.,
RA Stapleton M., Soares M.B., Bonaldo M.F., Casavant T.L., Scheetz T.E.,
RA Brownstein M.J., Usdin T.B., Toshiyuki S., Carninci P., Prange C.,
RA Raha S.S., Loquellano N.A., Peters G.J., Abramson R.D., Mullahy S.J.,
RA Bosak S.A., McEwan P.J., McKernan K.J., Malek J.A., Gunaratne P.H.,
RA Richards S., Worley K.C., Hale S., Garcia A.M., Gay L.J., Hulyk S.W.,
RA Villalon D.K., Muzny D.M., Sodergren E.J., Lu X., Gibbs R.A.,
RA Fahey J., Helton E., Ketteman M., Madan A., Rodrigues S., Sanchez A.,
RA Whiting M., Madan A., Young A.C., Shevchenko Y., Bouffard G.G.,
RA Blakesley R.W., Touchman J.W., Green E.D., Dickson M.C.,
RA Rodriguez A.C., Grimwood J., Schmutz J., Myers R.M.,
RA Butterfield Y.S.N., Krzywinski M.I., Skalska U., Smailus D.E.,
RA Schnerch A., Schein J.E., Jones S.J.M., Marra M.A.;
RT "Generation and initial analysis of more than 15,000 full-length human
RT and mouse cDNA sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:16899-16903(2002).
RN [7]
RP PROTEIN SEQUENCE OF 2-21 AND 133-153, BLOCKAGE OF THE N-TERMINUS, AND
RP SUBUNIT.
RX MEDLINE=93176127; PubMed=8439294;
RA Zhang W.-W., Zhang L.-X., Busch R.K., Farres J., Busch H.;
RT "Purification and characterization of a DNA-binding heterodimer of 52
RT and 100 kDa from HeLa cells.";
RL Biochem. J. 290:267-272(1993).
RN [8]
RP CHROMOSOMAL TRANSLOCATION.
RX MEDLINE=98054131; PubMed=9393982; DOI=10.1038/sj.onc.1201394;
RA Clark J., Lu Y.-J., Sidhar S.K., Parker C., Gill S., Smedley D.,
RA Hamoudi R., Linehan W.M., Shipley J., Cooper C.S.;
RT "Fusion of splicing factor genes PSF and NonO (p54nrb) to the TFE3
RT gene in papillary renal cell carcinoma.";
RL Oncogene 15:2233-2239(1997).
RN [9]
RP IDENTIFICATION IN A COMPLEX WITH SFPQ AND TOP1.
RX MEDLINE=98434520; PubMed=9756848; DOI=10.1074/jbc.273.41.26261;
RA Straub T., Grue P., Uhse A., Lisby M., Knudsen B.R., Tange T.O.,
RA Westergaard O., Boege F.;
RT "The RNA-splicing factor PSF/p54 controls DNA-topoisomerase I activity
RT by a direct interaction.";
RL J. Biol. Chem. 273:26261-26264(1998).
RN [10]
RP FUNCTION IN DNA UNWINDING.
RX PubMed=10858305; DOI=10.1021/bi992898e;
RA Straub T., Knudsen B.R., Boege F.;
RT "PSF/p54(nrb) stimulates 'jumping' of DNA topoisomerase I between
RT separate DNA helices.";
RL Biochemistry 39:7552-7558(2000).
RN [11]
RP FUNCTION IN NUCLEAR RETENTION OF A-TO-I EDITED RNAS, AND
RP IDENTIFICATION IN A COMPLEX WITH NONO AND MATR3.
RX MEDLINE=21417141; PubMed=11525732; DOI=10.1016/S0092-8674(01)00466-4;
RA Zhang Z., Carmichael G.G.;
RT "The fate of dsRNA in the nucleus: a p54(nrb)-containing complex
RT mediates the nuclear retention of promiscuously A-to-I edited RNAs.";
RL Cell 106:465-475(2001).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION IN TRANSCRIPTION
RP REGULATION, AND IDENTIFICATION IN A COMPLEX WITH SFPQ AND NR5A1.
RX MEDLINE=21895433; PubMed=11897684; DOI=10.1210/en.143.4.1280;
RA Sewer M.B., Nguyen V.Q., Huang C.J., Tucker P.W., Kagawa N.,
RA Waterman M.R.;
RT "Transcriptional activation of human CYP17 in H295R adrenocortical
RT cells depends on complex formation among p54(nrb)/NonO, protein-
RT associated splicing factor, and SF-1, a complex that also participates
RT in repression of transcription.";
RL Endocrinology 143:1280-1290(2002).
RN [13]
RP INTERACTIONS WITH PSQF AND U5 SNRNA, AND IDENTIFICATION IN IN U5/4/6
RP SNRNP SND SPLICEOSOME COMPLEXES.
RX MEDLINE=22290639; PubMed=12403470; DOI=10.1017/S1355838202022070;
RA Peng R., Dye B.T., Perez I., Barnard D.C., Thompson A.B., Patton J.G.;
RT "PSF and p54nrb bind a conserved stem in U5 snRNA.";
RL RNA 8:1334-1347(2002).
RN [14]
RP FUNCTION IN DNA REPAIR, IDENTIFICATION BY MASS-SPECTROMETRY,
RP DNA-BINDING, AND SUBUNIT.
RX PubMed=15590677; DOI=10.1074/jbc.M412758200;
RA Bladen C.L., Udayakumar D., Takeda Y., Dynan W.S.;
RT "Identification of the polypyrimidine tract binding protein-associated
RT splicing factor.p54(nrb) complex as a candidate DNA double-strand
RT break rejoining factor.";
RL J. Biol. Chem. 280:5205-5210(2005).
Feature:
CHAIN 1 471 Non-POU domain-containing octamer-binding
protein.
/FTId=PRO_0000081683.
DOMAIN 74 141 RRM 1.
DOMAIN 148 229 RRM 2.
REGION 54 373 DBHS.
COILED 268 372 Potential.
COMPBIAS 30 35 Poly-Gln.
COMPBIAS 36 42 Poly-Pro.
COMPBIAS 348 351 Poly-Arg.
SITE 377 378 Breakpoint for translocation to form
NONO-TFE3.
CONFLICT 19 19 H -> K (in Ref. 5).
CONFLICT 151 151 T -> H (in Ref. 1).
CONFLICT 358 359 QQ -> HE (in Ref. 3 and 4).
CONFLICT 366 367 QQ -> HE (in Ref. 3 and 4).
Comments:
-!- FUNCTION: DNA- and RNA binding protein, involved in several
nuclear processes. Binds the conventional octamer sequence in
double stranded DNA. Also binds single-stranded DNA and RNA at a
site independent of the duplex site (By similarity). Involved in
pre-mRNA splicing, probably as an heterodimer with SFPQ. Interacts
with U5 snRNA, probably by binding to a purine-rich sequence
located on the 3' side of U5 snRNA stem 1b. The SFPQ-NONO
heteromer associated with MATR3 may play a role in nuclear
retention of defective RNAs. The SFPQ-NONO heteromer may be
involved in DNA unwinding by modulating the function of
topoisomerase I/TOP1. The SFPQ-NONO heteromer may be involved in
DNA nonhomologous end joining (NHEJ) required for double-strand
break repair and V(D)J recombination and may stabilize paired DNA
ends. In vitro, the complex strongly stimulates DNA end joining,
binds directly to the DNA substrates and cooperates with the
Ku70/G22P1-Ku80/XRCC5 (Ku) dimer to establish a functional
preligation complex. Nono is involved in transcriptional
regulation. The SFPQ-NONO-NR5A1/SF-1 complex binds to the CYP17
promoter and regulates basal and cAMP-dependent transcriptional
avtivity. NONO binds to an enhancer element in long terminal
repeats of endogenous intracisternal A particles (IAPs) and
activates transcription (By similarity).
-!- SUBUNIT: Monomer and component of the SFPQ-NONO complex, which is
probably a heterotetramer of two 52 kDa (NONO) and two 100 kDa
(SFPQ) subunits. NONO is a component of spliceosome and U5.4/6
snRNP complexes. Interacts with SNRPA/U1A. Part of complex
consisiting of SFPQ, NONO and MATR3. Part of a complex consisting
of SFPQ, NONO and NR5A1/SF-1. Part of a complex consisting of
SFPQ, NONO and TOP1. Interacts with SPI1 (By similarity).
-!- INTERACTION:
P28700:Rxra (xeno); NbExp=1; IntAct=EBI-350527, EBI-346715;
P23246-1:SFPQ; NbExp=1; IntAct=EBI-350527, EBI-355463;
-!- SUBCELLULAR LOCATION: Nucleus.
-!- TISSUE SPECIFICITY: Heart, brain, placenta, lung, liver, skeletal
muscle, kidney and pancreas. Also found in a number of breast
tumor cell lines.
-!- PTM: The N-terminus is blocked.
-!- DISEASE: A chromosomal aberration involving NONO may be a cause of
papillary renal cell carcinoma (PRCC). Translocation
t(X;X)(p11.2;q13.1) with TFE3.
-!- SIMILARITY: Contains 2 RRM (RNA recognition motif) domains.
-!- DATABASE: NAME=Atlas Genet. Cytogenet. Oncol. Haematol.;
WWW="http://www.infobiogen.fr/services/chromcancer/Genes/NONOID168.html".
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Sequence length: 471
MQSNKTFNLE KQNHTPRKHH QHHHQQQHHQ QQQQQPPPPP IPANGQQASS QNEGLTIDLK
NFRKPGEKTF TQRSRLFVGN LPPDITEEEM RKLFEKYGKA GEVFIHKDKG FGFIRLETRT
LAEIAKVELD NMPLRGKQLR VRFACHSASL TVRNLPQYVS NELLEEAFSV FGQVERAVVI
VDDRGRPSGK GIVEFSGKPA ARKALDRCSE GSFLLTTFPR PVTVEPMDQL DDEEGLPEKL
VIKNQQFHKE REQPPRFAQP GSFEYEYAMR WKALIEMEKQ QQDQVDRNIK EAREKLEMEM
EAARHEHQVM LMRQDLMRRQ EELRRMEELH NQEVQKRKQL ELRQEEERRR REEEMRRQQE
EMMRRQQEGF KGTFPDAREQ EIRMGQMAMG GAMGINNRGA MPPAPVPAGT PAPPGPATMM
PDGTLGLTPP TTERFGQAAT MEGIGAIGGT PPAFNRAAPG AEFAPNKRRR Y