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UniProtKB/Swiss-Prot entry Q9NWB1


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name FOX1_HUMAN
Primary accession number Q9NWB1
Secondary accession numbers Q7Z7I7 Q8TAE3 Q8TAF2 Q8WYB2 Q9NS20
Integrated into Swiss-Prot on December 1, 2000
Sequence was last modified on February 5, 2008 (Sequence version 2)
Annotations were last modified on    July 22, 2008 (Entry version 67)
Name and origin of the protein
Protein name Fox-1 homolog
Synonyms Ataxin-2-binding protein 1
Hexaribonucleotide-binding protein 1
Gene name
Name: FOX1
Synonyms: A2BP, A2BP1, HRNBP1
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
DOI=10.1093/hmg/9.9.1303; PubMed=10814712 [NCBI, ExPASy, EBI, Israel, Japan]
Shibata H., Huynh D.P., Pulst S.-M.;
"A novel protein with RNA-binding motifs interacts with ataxin-2.";
Hum. Mol. Genet. 9:1303-1313(2000).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA] (ISOFORMS 2; 4 AND 5).
Chen W., Chu Z.-L., Blough R.I., Liu L., Hoppes B., Winkelmann J.C.;
"Molecular cloning and chromosomal localization of a human brain, heart and skeletal muscle specific RNA binding protein gene homologous to fox-1 in Caenorhabditis elegans.";
Submitted (SEP-1998) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
Yu L., Guo J., She X.;
"An alternative splicing of a novel protein with RNA-binding motifs interacts with ataxin-2.";
Submitted (NOV-2001) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
DOI=10.1038/ng1285; PubMed=14702039 [NCBI, ExPASy, EBI, Israel, Japan]
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
FUNCTION.
DOI=10.1074/jbc.M511556200; PubMed=16537540 [NCBI, ExPASy, EBI, Israel, Japan]
Ponthier J.L., Schluepen C., Chen W., Lersch R.A., Gee S.L., Hou V.C., Lo A.J., Short S.A., Chasis J.A., Winkelmann J.C., Conboy J.G.;
"Fox-2 splicing factor binds to a conserved intron motif to promote inclusion of protein 4.1R alternative exon 16.";
J. Biol. Chem. 281:12468-12474(2006).
[7]
STRUCTURE BY NMR OF 109-196 IN COMPLEX WITH RNA, AND MUTAGENESIS OF HIS-120; PHE-126; PHE-158 AND PHE-160.
DOI=10.1038/sj.emboj.7600918; PubMed=16362037 [NCBI, ExPASy, EBI, Israel, Japan]
Auweter S.D., Fasan R., Reymond L., Underwood J.G., Black D.L., Pitsch S., Allain F.H.-T.;
"Molecular basis of RNA recognition by the human alternative splicing factor Fox-1.";
EMBO J. 25:163-173(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
AF107203; AAF78291.1; ALT_INIT; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF229057; AAL71904.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF094849; AAL83405.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109106; AAL83406.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109120; AAL83407.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109107; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109108; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109109; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109110; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109111; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109112; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109113; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109114; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109115; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109116; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109117; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109118; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109119; AAL83407.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109120; AAL83408.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109107; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109108; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109109; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109110; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109111; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109112; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109113; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109114; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109115; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109116; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109117; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109119; AAL83408.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109120; AAL83409.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109107; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109108; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109109; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109110; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109111; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109112; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109113; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109114; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109115; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109116; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109117; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF109119; AAL83409.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF448859; AAP41925.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AK001027; BAA91472.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC113691; AAI13692.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
RefSeq NP_061193.2; -.
NP_665898.1; -.
NP_665899.1; -.
NP_665900.1; -.
UniGene Hs.459842
3D structure databases
PDB
2ERR; NMR; -; A=109-196.[ExPASy / RCSB / EBI]
PDBsum 2ERR; -.
ModBase Q9NWB1.
Protein-protein interaction databases
IntAct Q9NWB1; -.
PTM databases
PhosphoSite Q9NWB1; -.
Organism-specific databases
MIM 605104; gene. [NCBI / EBI]
GeneCards Q9NWB1.
Gene expression databases
ArrayExpress Q9NWB1; -.
GermOnline ENSG00000078328; Homo sapiens.
Ontologies
GO
GO:0005802; Cellular component: trans-Golgi network (inferred from direct assay from UniProtKB).
GO:0008022; Molecular function: protein C-terminus binding (inferred from physical interaction from UniProtKB).
GO:0003723; Molecular function: RNA binding (non-traceable author statement from UniProtKB).
GO:0050658; Biological process: RNA transport (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR012677; a_b_plait_nuc_bd.
IPR017325; RNA-bd_9/Ataxin-2-bd.
IPR000504; RRM_RNP1.
Graphical view of domain structure.
Gene3D G3DSA:3.30.70.330; a_b_plait_nuc_bd; 1.
Pfam PF00076; RRM_1; 1.
Pfam graphical view of domain structure.
PIRSF PIRSF037932; Ataxin_2_bd_A2BP; 1.
SMART SM00360; RRM; 1.
SMART graphical view of domain structure.
PROSITE PS50102; RRM; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q9NWB1.
Genome annotation databases
Ensembl ENSG00000078328; Homo sapiens. [Contig view]
GeneID 54715; -.
KEGG hsa:54715; -.
Phylogenomic databases
HOGENOM Q9NWB1; -.
HOVERGEN Q9NWB1; -.
Other
SOURCE FOX1; Homo sapiens.
ProtoNet Q9NWB1.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Cytoplasm; mRNA processing; mRNA splicing; Nucleus; RNA-binding.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
CHAIN   1   397  397     Fox-1 homolog. PRO_0000081480
DOMAIN   117   193  77     RRM. 
SITE   118   118  1     Interaction with RNA. 
SITE   126   126  1     Interaction with RNA. 
SITE   127   127  1     Interaction with RNA. 
SITE   151   151  1     Interaction with RNA. 
SITE   156   156  1     Interaction with RNA. 
SITE   160   160  1     Interaction with RNA. 
SITE   184   184  1     Interaction with RNA. 
SITE   194   194  1     Interaction with RNA. 
VAR_SEQ   1     9        MNCEREQLR -> MLASQGVLLHPYGVPMIVPAAPYLPGLIQ (in isoform 2, isoform 4 and isoform 5). VSP_030874
VAR_SEQ   226   253        GTVLLCQANQEGSSMYSAPSSLVYTSAM -> V (in isoform 3). VSP_030875
VAR_SEQ   302   310        DGFYGADIY -> EPVYGNKLLQ (in isoform 2, isoform 4 and isoform 5). VSP_030876
VAR_SEQ   332   397        SYGRVYAADPYHHALAPAPTYGVGAMNAFAPLTDAKTRSH ADDVGLVLSSLQASIYRGGYNRFAPY -> RNQFVFVAADEISCNTSAVTDEFMLPTPTTTHLLQPPP TALVP (in isoform 5). VSP_030877
VAR_SEQ   358   383        Missing (in isoform 4). VSP_030878
MUTAGEN   120   120        H->A: Reduces RNA-binding affinity 160-fold. 
MUTAGEN   126   126        F->A,I,R: Reduces RNA-binding affinity 1500-fold. 
MUTAGEN   126   126        F->H,W: Reduces RNA-binding affinity 15-fold. 
MUTAGEN   126   126        F->Y: No effect on RNA-binding. 
MUTAGEN   158   158        F->A: Reduces RNA-binding affinity 700-fold. 
MUTAGEN   160   160        F->A: Reduces RNA-binding affinity 30'000-fold. 
CONFLICT   92    92        T -> A (in Ref. 4; BAA91472). 
STRAND   118   123  6      
HELIX   130   136  7      
HELIX   137   139  3      
STRAND   146   148  3      
STRAND   158   162  5      
HELIX   167   176  10      
STRAND   187   190  4      
Sequence information
Length: 397 AA [This is the length of the unprocessed precursor] Molecular weight: 42784 Da [This is the MW of the unprocessed precursor] CRC64: EA96AA7B6E144D80 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MNCEREQLRG NQEAAAAPDT MAQPYASAQF APPQNGIPAE YTAPHPHPAP EYTGQTTVPE 

        70         80         90        100        110        120 
HTLNLYPPAQ THSEQSPADT SAQTVSGTAT QTDDAAPTDG QPQTQPSENT ENKSQPKRLH 

       130        140        150        160        170        180 
VSNIPFRFRD PDLRQMFGQF GKILDVEIIF NERGSKGFGF VTFENSADAD RAREKLHGTV 

       190        200        210        220        230        240 
VEGRKIEVNN ATARVMTNKK TVNPYTNGWK LNPVVGAVYS PEFYAGTVLL CQANQEGSSM 

       250        260        270        280        290        300 
YSAPSSLVYT SAMPGFPYPA ATAAAAYRGA HLRGRGRTVY NTFRAAAPPP PIPAYGGVVY 

       310        320        330        340        350        360 
QDGFYGADIY GGYAAYRYAQ PTPATAAAYS DSYGRVYAAD PYHHALAPAP TYGVGAMNAF 

       370        380        390 
APLTDAKTRS HADDVGLVLS SLQASIYRGG YNRFAPY 

Q9NWB1 in FASTA format

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