Full text data of NFX1
NFX1
(NFX2)
[Confidence: low (only semi-automatic identification from reviews)]
Transcriptional repressor NF-X1; 6.3.2.- (Nuclear transcription factor, X box-binding protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Transcriptional repressor NF-X1; 6.3.2.- (Nuclear transcription factor, X box-binding protein 1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q12986
ID NFX1_HUMAN Reviewed; 1120 AA.
AC Q12986; A8K6H8; Q5VXW6; Q96EL5; Q9BXI1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-MAY-2008, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Transcriptional repressor NF-X1;
DE EC=6.3.2.-;
DE AltName: Full=Nuclear transcription factor, X box-binding protein 1;
GN Name=NFX1; Synonyms=NFX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Li J.M., Sah J.H., Zhou Z.M.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-1120 (ISOFORM 1).
RX PubMed=7964459; DOI=10.1084/jem.180.5.1763;
RA Song Z., Krishna S., Thanos D., Strominger J.L., Ono S.J.;
RT "A novel cysteine-rich sequence-specific DNA-binding protein interacts
RT with the conserved X-box motif of the human major histocompatibility
RT complex class II genes via a repeated Cys-His domain and functions as
RT a transcriptional repressor.";
RL J. Exp. Med. 180:1763-1774(1994).
RN [7]
RP FUNCTION AS AN E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE.
RX PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S.,
RA Weissman A.M.;
RT "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN [8]
RP INTERACTION WITH HPV16 E6, AND FUNCTION.
RX PubMed=15371341; DOI=10.1101/gad.1214704;
RA Gewin L., Myers H., Kiyono T., Galloway D.A.;
RT "Identification of a novel telomerase repressor that interacts with
RT the human papillomavirus type-16 E6/E6-AP complex.";
RL Genes Dev. 18:2269-2282(2004).
RN [9]
RP FUNCTION, INTERACTION WITH PABPC1 AND PABPC4, AND MUTAGENESIS OF
RP PHE-20.
RX PubMed=17267499; DOI=10.1128/JVI.02007-06;
RA Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C.,
RA Gafken P.R., Galloway D.A.;
RT "NFX1-123 and poly(A) binding proteins synergistically augment
RT activation of telomerase in human papillomavirus type 16 E6-expressing
RT cells.";
RL J. Virol. 81:3786-3796(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Binds to the X-box motif of MHC class II genes and
CC represses their expression. May play an important role in
CC regulating the duration of an inflammatory response by limiting
CC the period in which MHC class II molecules are induced by
CC interferon-gamma. Isoform 3 binds to the X-box motif of TERT
CC promoter and represses its expression. Together with PABPC1 or
CC PABPC4, isoform 1 acts as a coactivator for TERT expression.
CC Mediates E2-dependent ubiquitination.
CC -!- SUBUNIT: Isoform 1 and isoform 3 interact with human
CC papillomavirus (HPV) type-16 E6 oncoprotein. Isoform 1 interacts
CC with PABPC1 and PABPC4.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NFX-123;
CC IsoId=Q12986-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12986-2; Sequence=VSP_033684, VSP_033685;
CC Name=3; Synonyms=NFX-91;
CC IsoId=Q12986-3; Sequence=VSP_033682, VSP_033683;
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an
CC ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.
CC -!- PTM: Isoform 3 is polyubiquitinated in the presence of HPV16 E6
CC protein; which leads to proteasomal degradation. Isoform 1 is not
CC polyubiquitinated.
CC -!- SIMILARITY: Belongs to the NFX1 family.
CC -!- SIMILARITY: Contains 8 NF-X1-type zinc fingers.
CC -!- SIMILARITY: Contains 1 R3H domain.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69517.1; Type=Frameshift; Positions=78, 202, 284;
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DR EMBL; AF332009; AAK16545.1; -; mRNA.
DR EMBL; AK291643; BAF84332.1; -; mRNA.
DR EMBL; AL356472; CAH72745.1; -; Genomic_DNA.
DR EMBL; AL356218; CAH72745.1; JOINED; Genomic_DNA.
DR EMBL; AL356472; CAH72746.1; -; Genomic_DNA.
DR EMBL; AL356218; CAH72746.1; JOINED; Genomic_DNA.
DR EMBL; AL356472; CAH72747.3; -; Genomic_DNA.
DR EMBL; AL356218; CAI13304.1; -; Genomic_DNA.
DR EMBL; AL356472; CAI13304.1; JOINED; Genomic_DNA.
DR EMBL; AL356218; CAI13305.1; -; Genomic_DNA.
DR EMBL; AL356472; CAI13305.1; JOINED; Genomic_DNA.
DR EMBL; CH471071; EAW58510.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58511.1; -; Genomic_DNA.
DR EMBL; BC012151; AAH12151.1; -; mRNA.
DR EMBL; U15306; AAA69517.1; ALT_FRAME; mRNA.
DR PIR; I38869; I38869.
DR RefSeq; NP_002495.2; NM_002504.4.
DR RefSeq; NP_667344.1; NM_147133.2.
DR RefSeq; XP_005251531.1; XM_005251474.1.
DR UniGene; Hs.413074; -.
DR ProteinModelPortal; Q12986; -.
DR IntAct; Q12986; 2.
DR STRING; 9606.ENSP00000368856; -.
DR PhosphoSite; Q12986; -.
DR DMDM; 189047116; -.
DR PaxDb; Q12986; -.
DR PRIDE; Q12986; -.
DR DNASU; 4799; -.
DR Ensembl; ENST00000318524; ENSP00000317695; ENSG00000086102.
DR Ensembl; ENST00000379521; ENSP00000368836; ENSG00000086102.
DR Ensembl; ENST00000379540; ENSP00000368856; ENSG00000086102.
DR GeneID; 4799; -.
DR KEGG; hsa:4799; -.
DR UCSC; uc003zsq.3; human.
DR CTD; 4799; -.
DR GeneCards; GC09P033280; -.
DR HGNC; HGNC:7803; NFX1.
DR MIM; 603255; gene.
DR neXtProt; NX_Q12986; -.
DR PharmGKB; PA31608; -.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000006942; -.
DR HOVERGEN; HBG003827; -.
DR InParanoid; Q12986; -.
DR KO; K12236; -.
DR OMA; SKLSDMQ; -.
DR OrthoDB; EOG7NCV2M; -.
DR PhylomeDB; Q12986; -.
DR ChiTaRS; NFX1; human.
DR GeneWiki; NFX1; -.
DR GenomeRNAi; 4799; -.
DR NextBio; 18492; -.
DR PRO; PR:Q12986; -.
DR Bgee; Q12986; -.
DR CleanEx; HS_NFX1; -.
DR Genevestigator; Q12986; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR001374; R3H_ss-bd.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 5.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00438; ZnF_NFX; 9.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Complete proteome; DNA-binding;
KW Host-virus interaction; Ligase; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 1120 Transcriptional repressor NF-X1.
FT /FTId=PRO_0000055979.
FT DOMAIN 994 1062 R3H.
FT ZN_FING 358 409 RING-type; atypical.
FT ZN_FING 453 471 NF-X1-type 1.
FT ZN_FING 506 525 NF-X1-type 2.
FT ZN_FING 567 586 NF-X1-type 3.
FT ZN_FING 632 655 NF-X1-type 4.
FT ZN_FING 694 713 NF-X1-type 5.
FT ZN_FING 721 740 NF-X1-type 6.
FT ZN_FING 832 854 NF-X1-type 7.
FT ZN_FING 863 884 NF-X1-type 8.
FT REGION 9 26 Interaction with PABPC1 and PABC4.
FT COMPBIAS 1084 1089 Poly-Pro.
FT MOD_RES 50 50 Phosphoserine.
FT VAR_SEQ 809 833 FRSNIPCHLVDISCGLPCSATLPCG -> QSHYWASTQKKR
FT SHYMKKIPAHACL (in isoform 3).
FT /FTId=VSP_033682.
FT VAR_SEQ 834 1120 Missing (in isoform 3).
FT /FTId=VSP_033683.
FT VAR_SEQ 1014 1024 GKNSKKSHSFP -> VEVETSHWTFL (in isoform
FT 2).
FT /FTId=VSP_033684.
FT VAR_SEQ 1025 1120 Missing (in isoform 2).
FT /FTId=VSP_033685.
FT VARIANT 731 731 H -> Y (in dbSNP:rs5017299).
FT /FTId=VAR_043380.
FT VARIANT 760 760 P -> S (in dbSNP:rs2860036).
FT /FTId=VAR_043381.
FT VARIANT 1086 1086 P -> Q (in dbSNP:rs2274866).
FT /FTId=VAR_043382.
FT MUTAGEN 20 20 F->A: Reduces PABPC1 and PABC4 binding.
FT CONFLICT 179 179 G -> A (in Ref. 1; AAA69517).
FT CONFLICT 186 186 G -> E (in Ref. 1; AAA69517).
FT CONFLICT 312 312 Q -> P (in Ref. 1; AAA69517).
FT CONFLICT 419 420 YT -> FS (in Ref. 1; AAA69517).
FT CONFLICT 560 560 I -> T (in Ref. 1; AAA69517).
FT CONFLICT 653 653 C -> V (in Ref. 1; AAA69517).
FT CONFLICT 678 678 E -> EA (in Ref. 2; BAF84332).
FT CONFLICT 714 714 I -> N (in Ref. 1; AAA69517).
FT CONFLICT 786 786 C -> G (in Ref. 1; AAA69517).
SQ SEQUENCE 1120 AA; 124395 MW; F2203BE1DB6437E6 CRC64;
MAEAPPVSGT FKFNTDAAEF IPQEKKNSGL NCGTQRRLDS NRIGRRNYSS PPPCHLSRQV
PYDEISAVHQ HSYHPSGSKP KSQQTSFQSS PCNKSPKSHG LQNQPWQKLR NEKHHIRVKK
AQSLAEQTSD TAGLESSTRS ESGTDLREHS PSESEKEVVG ADPRGAKPKK ATQFVYSYGR
GPKVKGKLKC EWSNRTTPKP EDAGPESTKP VGVFHPDSSE ASSRKGVLDG YGARRNEQRR
YPQKRPPWEV EGARPRPGRN PPKQEGHRHT NAGHRNNMGP IPKDDLNERP AKSTCDSENL
AVINKSSRRV DQEKCTVRRQ DPQVVSPFSR GKQNHVLKNV ETHTGSLIEQ LTTEKYECMV
CCELVRVTAP VWSCQSCYHV FHLNCIKKWA RSPASQADGQ SGWRCPACQN VSAHVPNTYT
CFCGKVKNPE WSRNEIPHSC GEVCRKKQPG QDCPHSCNLL CHPGPCPPCP AFMTKTCECG
RTRHTVRCGQ AVSVHCSNPC ENILNCGQHQ CAELCHGGQC QPCQIILNQV CYCGSTSRDV
LCGTDVGKSD GFGDFSCLKI CGKDLKCGNH TCSQVCHPQP CQQCPRLPQL VRCCPCGQTP
LSQLLELGSS SRKTCMDPVP SCGKVCGKPL PCGSLDFIHT CEKLCHEGDC GPCSRTSVIS
CRCSFRTKEL PCTSLKSEDA TFMCDKRCNK KRLCGRHKCN EICCVDKEHK CPLICGRKLR
CGLHRCEEPC HRGNCQTCWQ ASFDELTCHC GASVIYPPVP CGTRPPECTQ TCARVHECDH
PVYHSCHSEE KCPPCTFLTQ KWCMGKHEFR SNIPCHLVDI SCGLPCSATL PCGMHKCQRL
CHKGECLVDE PCKQPCTTPR ADCGHPCMAP CHTSSPCPVT ACKAKVELQC ECGRRKEMVI
CSEASSTYQR IAAISMASKI TDMQLGGSVE ISKLITKKEV HQARLECDEE CSALERKKRL
AEAFHISEDS DPFNIRSSGS KFSDSLKEDA RKDLKFVSDV EKEMETLVEA VNKGKNSKKS
HSFPPMNRDH RRIIHDLAQV YGLESVSYDS EPKRNVVVTA IRGKSVCPPT TLTGVLEREM
QARPPPPIPH HRHQSDKNPG SSNLQKITKE PIIDYFDVQD
//
ID NFX1_HUMAN Reviewed; 1120 AA.
AC Q12986; A8K6H8; Q5VXW6; Q96EL5; Q9BXI1;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
read moreDT 20-MAY-2008, sequence version 2.
DT 22-JAN-2014, entry version 134.
DE RecName: Full=Transcriptional repressor NF-X1;
DE EC=6.3.2.-;
DE AltName: Full=Nuclear transcription factor, X box-binding protein 1;
GN Name=NFX1; Synonyms=NFX2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RC TISSUE=Testis;
RA Li J.M., Sah J.H., Zhou Z.M.;
RL Submitted (DEC-2000) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E.,
RA Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S.,
RA Babbage A.K., Babbage S., Bagguley C.L., Bailey J., Banerjee R.,
RA Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P.,
RA Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W.,
RA Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G.,
RA Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M.,
RA Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W.,
RA Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A.,
RA Frankland J.A., French L., Fricker D.G., Garner P., Garnett J.,
RA Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M.,
RA Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S.,
RA McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J.,
RA Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R.,
RA Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M.,
RA Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M.,
RA Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A.,
RA Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P.,
RA Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W.,
RA Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S.,
RA Rogers J., Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Eye;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 48-1120 (ISOFORM 1).
RX PubMed=7964459; DOI=10.1084/jem.180.5.1763;
RA Song Z., Krishna S., Thanos D., Strominger J.L., Ono S.J.;
RT "A novel cysteine-rich sequence-specific DNA-binding protein interacts
RT with the conserved X-box motif of the human major histocompatibility
RT complex class II genes via a repeated Cys-His domain and functions as
RT a transcriptional repressor.";
RL J. Exp. Med. 180:1763-1774(1994).
RN [7]
RP FUNCTION AS AN E2-DEPENDENT UBIQUITIN-PROTEIN LIGASE.
RX PubMed=10500182; DOI=10.1073/pnas.96.20.11364;
RA Lorick K.L., Jensen J.P., Fang S., Ong A.M., Hatakeyama S.,
RA Weissman A.M.;
RT "RING fingers mediate ubiquitin-conjugating enzyme (E2)-dependent
RT ubiquitination.";
RL Proc. Natl. Acad. Sci. U.S.A. 96:11364-11369(1999).
RN [8]
RP INTERACTION WITH HPV16 E6, AND FUNCTION.
RX PubMed=15371341; DOI=10.1101/gad.1214704;
RA Gewin L., Myers H., Kiyono T., Galloway D.A.;
RT "Identification of a novel telomerase repressor that interacts with
RT the human papillomavirus type-16 E6/E6-AP complex.";
RL Genes Dev. 18:2269-2282(2004).
RN [9]
RP FUNCTION, INTERACTION WITH PABPC1 AND PABPC4, AND MUTAGENESIS OF
RP PHE-20.
RX PubMed=17267499; DOI=10.1128/JVI.02007-06;
RA Katzenellenbogen R.A., Egelkrout E.M., Vliet-Gregg P., Gewin L.C.,
RA Gafken P.R., Galloway D.A.;
RT "NFX1-123 and poly(A) binding proteins synergistically augment
RT activation of telomerase in human papillomavirus type 16 E6-expressing
RT cells.";
RL J. Virol. 81:3786-3796(2007).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18220336; DOI=10.1021/pr0705441;
RA Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
RA Yates J.R. III;
RT "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
RT efficient phosphoproteomic analysis.";
RL J. Proteome Res. 7:1346-1351(2008).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-50, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [13]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19369195; DOI=10.1074/mcp.M800588-MCP200;
RA Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G.,
RA Mann M., Daub H.;
RT "Large-scale proteomics analysis of the human kinome.";
RL Mol. Cell. Proteomics 8:1751-1764(2009).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
CC -!- FUNCTION: Binds to the X-box motif of MHC class II genes and
CC represses their expression. May play an important role in
CC regulating the duration of an inflammatory response by limiting
CC the period in which MHC class II molecules are induced by
CC interferon-gamma. Isoform 3 binds to the X-box motif of TERT
CC promoter and represses its expression. Together with PABPC1 or
CC PABPC4, isoform 1 acts as a coactivator for TERT expression.
CC Mediates E2-dependent ubiquitination.
CC -!- SUBUNIT: Isoform 1 and isoform 3 interact with human
CC papillomavirus (HPV) type-16 E6 oncoprotein. Isoform 1 interacts
CC with PABPC1 and PABPC4.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1; Synonyms=NFX-123;
CC IsoId=Q12986-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q12986-2; Sequence=VSP_033684, VSP_033685;
CC Name=3; Synonyms=NFX-91;
CC IsoId=Q12986-3; Sequence=VSP_033682, VSP_033683;
CC -!- INDUCTION: By IFNG/IFN-gamma.
CC -!- DOMAIN: The RING-type zinc finger domain interacts with an
CC ubiquitin-conjugating enzyme (E2) and facilitates ubiquitination.
CC -!- PTM: Isoform 3 is polyubiquitinated in the presence of HPV16 E6
CC protein; which leads to proteasomal degradation. Isoform 1 is not
CC polyubiquitinated.
CC -!- SIMILARITY: Belongs to the NFX1 family.
CC -!- SIMILARITY: Contains 8 NF-X1-type zinc fingers.
CC -!- SIMILARITY: Contains 1 R3H domain.
CC -!- SIMILARITY: Contains 1 RING-type zinc finger.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAA69517.1; Type=Frameshift; Positions=78, 202, 284;
CC -----------------------------------------------------------------------
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DR EMBL; AF332009; AAK16545.1; -; mRNA.
DR EMBL; AK291643; BAF84332.1; -; mRNA.
DR EMBL; AL356472; CAH72745.1; -; Genomic_DNA.
DR EMBL; AL356218; CAH72745.1; JOINED; Genomic_DNA.
DR EMBL; AL356472; CAH72746.1; -; Genomic_DNA.
DR EMBL; AL356218; CAH72746.1; JOINED; Genomic_DNA.
DR EMBL; AL356472; CAH72747.3; -; Genomic_DNA.
DR EMBL; AL356218; CAI13304.1; -; Genomic_DNA.
DR EMBL; AL356472; CAI13304.1; JOINED; Genomic_DNA.
DR EMBL; AL356218; CAI13305.1; -; Genomic_DNA.
DR EMBL; AL356472; CAI13305.1; JOINED; Genomic_DNA.
DR EMBL; CH471071; EAW58510.1; -; Genomic_DNA.
DR EMBL; CH471071; EAW58511.1; -; Genomic_DNA.
DR EMBL; BC012151; AAH12151.1; -; mRNA.
DR EMBL; U15306; AAA69517.1; ALT_FRAME; mRNA.
DR PIR; I38869; I38869.
DR RefSeq; NP_002495.2; NM_002504.4.
DR RefSeq; NP_667344.1; NM_147133.2.
DR RefSeq; XP_005251531.1; XM_005251474.1.
DR UniGene; Hs.413074; -.
DR ProteinModelPortal; Q12986; -.
DR IntAct; Q12986; 2.
DR STRING; 9606.ENSP00000368856; -.
DR PhosphoSite; Q12986; -.
DR DMDM; 189047116; -.
DR PaxDb; Q12986; -.
DR PRIDE; Q12986; -.
DR DNASU; 4799; -.
DR Ensembl; ENST00000318524; ENSP00000317695; ENSG00000086102.
DR Ensembl; ENST00000379521; ENSP00000368836; ENSG00000086102.
DR Ensembl; ENST00000379540; ENSP00000368856; ENSG00000086102.
DR GeneID; 4799; -.
DR KEGG; hsa:4799; -.
DR UCSC; uc003zsq.3; human.
DR CTD; 4799; -.
DR GeneCards; GC09P033280; -.
DR HGNC; HGNC:7803; NFX1.
DR MIM; 603255; gene.
DR neXtProt; NX_Q12986; -.
DR PharmGKB; PA31608; -.
DR eggNOG; NOG12793; -.
DR HOGENOM; HOG000006942; -.
DR HOVERGEN; HBG003827; -.
DR InParanoid; Q12986; -.
DR KO; K12236; -.
DR OMA; SKLSDMQ; -.
DR OrthoDB; EOG7NCV2M; -.
DR PhylomeDB; Q12986; -.
DR ChiTaRS; NFX1; human.
DR GeneWiki; NFX1; -.
DR GenomeRNAi; 4799; -.
DR NextBio; 18492; -.
DR PRO; PR:Q12986; -.
DR Bgee; Q12986; -.
DR CleanEx; HS_NFX1; -.
DR Genevestigator; Q12986; -.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0016874; F:ligase activity; IEA:UniProtKB-KW.
DR GO; GO:0003700; F:sequence-specific DNA binding transcription factor activity; TAS:ProtInc.
DR GO; GO:0008270; F:zinc ion binding; IEA:InterPro.
DR GO; GO:0006954; P:inflammatory response; TAS:ProtInc.
DR GO; GO:0019048; P:modulation by virus of host morphology or physiology; IEA:UniProtKB-KW.
DR GO; GO:0045347; P:negative regulation of MHC class II biosynthetic process; IEA:Ensembl.
DR GO; GO:0000122; P:negative regulation of transcription from RNA polymerase II promoter; TAS:ProtInc.
DR GO; GO:0006366; P:transcription from RNA polymerase II promoter; TAS:ProtInc.
DR InterPro; IPR001374; R3H_ss-bd.
DR InterPro; IPR019786; Zinc_finger_PHD-type_CS.
DR InterPro; IPR000967; Znf_NFX1.
DR InterPro; IPR019787; Znf_PHD-finger.
DR InterPro; IPR001841; Znf_RING.
DR Pfam; PF01424; R3H; 1.
DR Pfam; PF01422; zf-NF-X1; 5.
DR SMART; SM00393; R3H; 1.
DR SMART; SM00184; RING; 1.
DR SMART; SM00438; ZnF_NFX; 9.
DR PROSITE; PS51061; R3H; 1.
DR PROSITE; PS00518; ZF_RING_1; FALSE_NEG.
DR PROSITE; PS50089; ZF_RING_2; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; Complete proteome; DNA-binding;
KW Host-virus interaction; Ligase; Metal-binding; Nucleus;
KW Phosphoprotein; Polymorphism; Reference proteome; Repeat; Repressor;
KW Transcription; Transcription regulation; Ubl conjugation;
KW Ubl conjugation pathway; Zinc; Zinc-finger.
FT CHAIN 1 1120 Transcriptional repressor NF-X1.
FT /FTId=PRO_0000055979.
FT DOMAIN 994 1062 R3H.
FT ZN_FING 358 409 RING-type; atypical.
FT ZN_FING 453 471 NF-X1-type 1.
FT ZN_FING 506 525 NF-X1-type 2.
FT ZN_FING 567 586 NF-X1-type 3.
FT ZN_FING 632 655 NF-X1-type 4.
FT ZN_FING 694 713 NF-X1-type 5.
FT ZN_FING 721 740 NF-X1-type 6.
FT ZN_FING 832 854 NF-X1-type 7.
FT ZN_FING 863 884 NF-X1-type 8.
FT REGION 9 26 Interaction with PABPC1 and PABC4.
FT COMPBIAS 1084 1089 Poly-Pro.
FT MOD_RES 50 50 Phosphoserine.
FT VAR_SEQ 809 833 FRSNIPCHLVDISCGLPCSATLPCG -> QSHYWASTQKKR
FT SHYMKKIPAHACL (in isoform 3).
FT /FTId=VSP_033682.
FT VAR_SEQ 834 1120 Missing (in isoform 3).
FT /FTId=VSP_033683.
FT VAR_SEQ 1014 1024 GKNSKKSHSFP -> VEVETSHWTFL (in isoform
FT 2).
FT /FTId=VSP_033684.
FT VAR_SEQ 1025 1120 Missing (in isoform 2).
FT /FTId=VSP_033685.
FT VARIANT 731 731 H -> Y (in dbSNP:rs5017299).
FT /FTId=VAR_043380.
FT VARIANT 760 760 P -> S (in dbSNP:rs2860036).
FT /FTId=VAR_043381.
FT VARIANT 1086 1086 P -> Q (in dbSNP:rs2274866).
FT /FTId=VAR_043382.
FT MUTAGEN 20 20 F->A: Reduces PABPC1 and PABC4 binding.
FT CONFLICT 179 179 G -> A (in Ref. 1; AAA69517).
FT CONFLICT 186 186 G -> E (in Ref. 1; AAA69517).
FT CONFLICT 312 312 Q -> P (in Ref. 1; AAA69517).
FT CONFLICT 419 420 YT -> FS (in Ref. 1; AAA69517).
FT CONFLICT 560 560 I -> T (in Ref. 1; AAA69517).
FT CONFLICT 653 653 C -> V (in Ref. 1; AAA69517).
FT CONFLICT 678 678 E -> EA (in Ref. 2; BAF84332).
FT CONFLICT 714 714 I -> N (in Ref. 1; AAA69517).
FT CONFLICT 786 786 C -> G (in Ref. 1; AAA69517).
SQ SEQUENCE 1120 AA; 124395 MW; F2203BE1DB6437E6 CRC64;
MAEAPPVSGT FKFNTDAAEF IPQEKKNSGL NCGTQRRLDS NRIGRRNYSS PPPCHLSRQV
PYDEISAVHQ HSYHPSGSKP KSQQTSFQSS PCNKSPKSHG LQNQPWQKLR NEKHHIRVKK
AQSLAEQTSD TAGLESSTRS ESGTDLREHS PSESEKEVVG ADPRGAKPKK ATQFVYSYGR
GPKVKGKLKC EWSNRTTPKP EDAGPESTKP VGVFHPDSSE ASSRKGVLDG YGARRNEQRR
YPQKRPPWEV EGARPRPGRN PPKQEGHRHT NAGHRNNMGP IPKDDLNERP AKSTCDSENL
AVINKSSRRV DQEKCTVRRQ DPQVVSPFSR GKQNHVLKNV ETHTGSLIEQ LTTEKYECMV
CCELVRVTAP VWSCQSCYHV FHLNCIKKWA RSPASQADGQ SGWRCPACQN VSAHVPNTYT
CFCGKVKNPE WSRNEIPHSC GEVCRKKQPG QDCPHSCNLL CHPGPCPPCP AFMTKTCECG
RTRHTVRCGQ AVSVHCSNPC ENILNCGQHQ CAELCHGGQC QPCQIILNQV CYCGSTSRDV
LCGTDVGKSD GFGDFSCLKI CGKDLKCGNH TCSQVCHPQP CQQCPRLPQL VRCCPCGQTP
LSQLLELGSS SRKTCMDPVP SCGKVCGKPL PCGSLDFIHT CEKLCHEGDC GPCSRTSVIS
CRCSFRTKEL PCTSLKSEDA TFMCDKRCNK KRLCGRHKCN EICCVDKEHK CPLICGRKLR
CGLHRCEEPC HRGNCQTCWQ ASFDELTCHC GASVIYPPVP CGTRPPECTQ TCARVHECDH
PVYHSCHSEE KCPPCTFLTQ KWCMGKHEFR SNIPCHLVDI SCGLPCSATL PCGMHKCQRL
CHKGECLVDE PCKQPCTTPR ADCGHPCMAP CHTSSPCPVT ACKAKVELQC ECGRRKEMVI
CSEASSTYQR IAAISMASKI TDMQLGGSVE ISKLITKKEV HQARLECDEE CSALERKKRL
AEAFHISEDS DPFNIRSSGS KFSDSLKEDA RKDLKFVSDV EKEMETLVEA VNKGKNSKKS
HSFPPMNRDH RRIIHDLAQV YGLESVSYDS EPKRNVVVTA IRGKSVCPPT TLTGVLEREM
QARPPPPIPH HRHQSDKNPG SSNLQKITKE PIIDYFDVQD
//
MIM
603255
*RECORD*
*FIELD* NO
603255
*FIELD* TI
*603255 NUCLEAR TRANSCRIPTION FACTOR, X BOX-BINDING, 1; NFX1
*FIELD* TX
DESCRIPTION
read more
Expression of class II major histocompatibility complex (MHC) molecules
is usually restricted to cells of the immune system and dysregulated
expression is thought to contribute to the pathogenesis of a severe
combined immunodeficiency syndrome and certain autoimmune diseases. See
RFX5 (601863). MHC class II gene expression is controlled primarily at
the transcriptional level by transcription factors that bind to the X
and Y boxes, 2 highly conserved elements in the proximal promoter of MHC
class II genes. The X box is further subdivided into an upstream X1 box
and an X2 box.
CLONING
Raji cells are an EBV-transformed human B lymphoblastoid cell line that
expresses MHC class II molecules. By screening a Raji cell cDNA
expression library for the ability to bind oligonucleotides that contain
X box sequences, Song et al. (1994) isolated NFX1 cDNAs. The predicted
1,104-amino acid protein has a central cysteine-rich DNA-binding domain
that is subdivided into 7 repeated motifs; the motif is similar to, but
distinct from, LIM (see 601999) and RING finger (see 602045) domains.
Two acidic regions surround the cysteine-rich domain. Northern blot
analysis revealed that NFX1 was expressed as an approximately 4-kb mRNA.
Using RT-PCR and an RNase protection assay, Song et al. (1994) found
NFX1 expression in all cell lines tested, regardless of the MHC class II
phenotype.
Arlotta et al. (2002) cloned the mouse homolog of NFX1. The N and C
termini of the mouse protein share 70% and 88% homology with those of
the human protein, respectively, and mouse Nfx1 contains the conserved
central cysteine-rich DNA-binding motif, which is 95% homologous to that
of the human protein. Arlotta et al. (2002) noted that other studies
identified an important role for NFX1 in neuronal development.
GENE FUNCTION
Song et al. (1994) showed that recombinant NFX1 bound specifically to
the X1 boxes of HLA-DRA (142860) and other MHC class II genes in vitro.
Overexpression of NFX1 specifically repressed transcription of HLA-DRA.
Song et al. (1994) concluded that NFX1 is a potent and biologically
relevant repressor of HLA-DRA transcription.
MAPPING
Arlotta et al. (2002) mapped the mouse Nfx1 gene to the proximal region
of chromosome 4 by interspecific backcross analysis. By homology of
synteny, genomic sequence analysis, and other methods, they mapped the
human NFX1 gene to chromosome 9p13 in close proximity to the CNTFR gene
(118946).
*FIELD* RF
1. Arlotta, P.; Miyazaki, D.; Copeland, N. G.; Gilbert, D. J.; Jenkins,
N. A.; Ono, S. J.: Murine NFX.1: isolation and characterization of
its messenger RNA, mapping of its chromosomal location and assessment
of its developmental expression. Immunology 106: 173-181, 2002.
2. Song, Z.; Krishna, S.; Thanos, D.; Strominger, J. L.; Ono, S. J.
: A novel cysteine-rich sequence-specific DNA-binding protein interacts
with the conserved X-box motif of the human major histocompatibility
complex class II genes via a repeated cys-his domain and functions
as a transcriptional repressor. J. Exp. Med. 180: 1763-1774, 1994.
*FIELD* CN
Paul J. Converse - updated: 9/18/2002
*FIELD* CD
Rebekah S. Rasooly: 11/4/1998
*FIELD* ED
mgross: 09/18/2002
mgross: 9/18/2002
psherman: 11/4/1998
*RECORD*
*FIELD* NO
603255
*FIELD* TI
*603255 NUCLEAR TRANSCRIPTION FACTOR, X BOX-BINDING, 1; NFX1
*FIELD* TX
DESCRIPTION
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Expression of class II major histocompatibility complex (MHC) molecules
is usually restricted to cells of the immune system and dysregulated
expression is thought to contribute to the pathogenesis of a severe
combined immunodeficiency syndrome and certain autoimmune diseases. See
RFX5 (601863). MHC class II gene expression is controlled primarily at
the transcriptional level by transcription factors that bind to the X
and Y boxes, 2 highly conserved elements in the proximal promoter of MHC
class II genes. The X box is further subdivided into an upstream X1 box
and an X2 box.
CLONING
Raji cells are an EBV-transformed human B lymphoblastoid cell line that
expresses MHC class II molecules. By screening a Raji cell cDNA
expression library for the ability to bind oligonucleotides that contain
X box sequences, Song et al. (1994) isolated NFX1 cDNAs. The predicted
1,104-amino acid protein has a central cysteine-rich DNA-binding domain
that is subdivided into 7 repeated motifs; the motif is similar to, but
distinct from, LIM (see 601999) and RING finger (see 602045) domains.
Two acidic regions surround the cysteine-rich domain. Northern blot
analysis revealed that NFX1 was expressed as an approximately 4-kb mRNA.
Using RT-PCR and an RNase protection assay, Song et al. (1994) found
NFX1 expression in all cell lines tested, regardless of the MHC class II
phenotype.
Arlotta et al. (2002) cloned the mouse homolog of NFX1. The N and C
termini of the mouse protein share 70% and 88% homology with those of
the human protein, respectively, and mouse Nfx1 contains the conserved
central cysteine-rich DNA-binding motif, which is 95% homologous to that
of the human protein. Arlotta et al. (2002) noted that other studies
identified an important role for NFX1 in neuronal development.
GENE FUNCTION
Song et al. (1994) showed that recombinant NFX1 bound specifically to
the X1 boxes of HLA-DRA (142860) and other MHC class II genes in vitro.
Overexpression of NFX1 specifically repressed transcription of HLA-DRA.
Song et al. (1994) concluded that NFX1 is a potent and biologically
relevant repressor of HLA-DRA transcription.
MAPPING
Arlotta et al. (2002) mapped the mouse Nfx1 gene to the proximal region
of chromosome 4 by interspecific backcross analysis. By homology of
synteny, genomic sequence analysis, and other methods, they mapped the
human NFX1 gene to chromosome 9p13 in close proximity to the CNTFR gene
(118946).
*FIELD* RF
1. Arlotta, P.; Miyazaki, D.; Copeland, N. G.; Gilbert, D. J.; Jenkins,
N. A.; Ono, S. J.: Murine NFX.1: isolation and characterization of
its messenger RNA, mapping of its chromosomal location and assessment
of its developmental expression. Immunology 106: 173-181, 2002.
2. Song, Z.; Krishna, S.; Thanos, D.; Strominger, J. L.; Ono, S. J.
: A novel cysteine-rich sequence-specific DNA-binding protein interacts
with the conserved X-box motif of the human major histocompatibility
complex class II genes via a repeated cys-his domain and functions
as a transcriptional repressor. J. Exp. Med. 180: 1763-1774, 1994.
*FIELD* CN
Paul J. Converse - updated: 9/18/2002
*FIELD* CD
Rebekah S. Rasooly: 11/4/1998
*FIELD* ED
mgross: 09/18/2002
mgross: 9/18/2002
psherman: 11/4/1998