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Q9UHX1

- PUF60_HUMAN

UniProt

Q9UHX1 - PUF60_HUMAN

Protein

Poly(U)-binding-splicing factor PUF60

Gene

PUF60

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 126 (01 Oct 2014)
      Sequence version 1 (01 May 2000)
      Previous versions | rss
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    Functioni

    DNA- and RNA-binding protein, involved in several nuclear processes such as pre-mRNA splicing, apoptosis and transcription regulation. In association with FUBP1 regulates MYC transcription at the P2 promoter through the core-TFIIH basal transcription factor. Acts as a transcriptional repressor through the core-TFIIH basal transcription factor. Represses FUBP1-induced transcriptional activation but not basal transcription. Decreases ERCC3 helicase activity. Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells. Is also involved in pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice site and pyrimidine tract in a cooperative manner with U2AF2. Involved in apoptosis induction when overexpressed in HeLa cells. Isoform 6 failed to repress MYC transcription and inhibited FIR-induced apoptosis in colorectal cancer. Isoform 6 may contribute to tumor progression by enabling increased MYC expression and greater resistance to apoptosis in tumors than in normal cells. Modulates alternative splicing of several mRNAs. Binds to relaxed DNA of active promoter regions. Binds to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding is enhanced in presence of U2AF2. Binds to Y5 RNA in association with TROVE2. Binds to poly(U) RNA.6 Publications

    GO - Molecular functioni

    1. DNA binding Source: UniProtKB-KW
    2. identical protein binding Source: IntAct
    3. nucleotide binding Source: InterPro
    4. poly(A) RNA binding Source: UniProtKB
    5. protein binding Source: IntAct

    GO - Biological processi

    1. apoptotic process Source: UniProtKB-KW
    2. mRNA processing Source: UniProtKB-KW
    3. regulation of transcription, DNA-templated Source: UniProtKB-KW
    4. RNA splicing Source: UniProtKB-KW
    5. transcription, DNA-templated Source: UniProtKB-KW

    Keywords - Molecular functioni

    Repressor, Ribonucleoprotein

    Keywords - Biological processi

    Apoptosis, mRNA processing, mRNA splicing, Transcription, Transcription regulation

    Keywords - Ligandi

    DNA-binding, RNA-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Poly(U)-binding-splicing factor PUF60
    Alternative name(s):
    60 kDa poly(U)-binding-splicing factor
    FUSE-binding protein-interacting repressor
    Short name:
    FBP-interacting repressor
    Ro-binding protein 1
    Short name:
    RoBP1
    Siah-binding protein 1
    Short name:
    Siah-BP1
    Gene namesi
    Name:PUF60
    Synonyms:FIR, ROBPI, SIAHBP1
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 8

    Organism-specific databases

    HGNCiHGNC:17042. PUF60.

    Subcellular locationi

    Nucleus 2 Publications
    Note: Colocalizes partially with TROVE2.

    GO - Cellular componenti

    1. nucleus Source: UniProtKB-SubCell
    2. ribonucleoprotein complex Source: UniProtKB-KW

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Involvement in diseasei

    Verheij syndrome (VRJS) [MIM:615583]: A syndrome characterized by growth retardation, delayed psychomotor development, dysmorphic facial features, and skeletal, mainly vertebral, abnormalities. Additional variable features may include coloboma, renal defects, and cardiac defects.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti169 – 1691H → Y in VRJS; loss of function mutation; results in altered dosage of dfferent PUF60 protein forms and abnormal splicing profile of several target genes. 1 Publication
    VAR_070939

    Keywords - Diseasei

    Disease mutation

    Organism-specific databases

    MIMi615583. phenotype.
    PharmGKBiPA162400364.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 559559Poly(U)-binding-splicing factor PUF60PRO_0000299519Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei60 – 601Phosphothreonine2 Publications
    Modified residuei112 – 1121Phosphoserine1 Publication
    Modified residuei251 – 2511N6-acetyllysine1 Publication
    Modified residuei314 – 3141Phosphothreonine1 Publication
    Modified residuei454 – 4541N6-acetyllysine1 Publication

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiQ9UHX1.
    PaxDbiQ9UHX1.
    PRIDEiQ9UHX1.

    PTM databases

    PhosphoSiteiQ9UHX1.

    Expressioni

    Tissue specificityi

    Isoform 2 is expressed in colonic epithelium and colorectal epithelium cancer (at protein level). Isoform 6 is expressed in colorectal epithelial cancer but below detection level in colonic epithelium. Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary, small intestine, colon and peripheral blood leukocytes.2 Publications

    Gene expression databases

    ArrayExpressiQ9UHX1.
    BgeeiQ9UHX1.
    CleanExiHS_PUF60.
    GenevestigatoriQ9UHX1.

    Organism-specific databases

    HPAiHPA045733.

    Interactioni

    Subunit structurei

    Homodimer. Associates with the spliceosome. Found in a complex with TROVE2 and Y5 RNA. Found in a complex with FUBP1 and far upstream element (FUSE) DNA segment. Interacts directly with ERCC3. Interacts with CDK7, GTF2H1 and SFRS11. Does not interact with ERCC3 in xeroderma pigmentosum complementation group B (XPB) cells.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    itself3EBI-1053259,EBI-1053259
    CACNA1AO005552EBI-1053259,EBI-766279
    PCBP1Q153652EBI-1053259,EBI-946095
    PPP1R16AQ96I342EBI-1053259,EBI-710402
    SAP30BPQ9UHR56EBI-1053259,EBI-751683

    Protein-protein interaction databases

    BioGridi116502. 88 interactions.
    DIPiDIP-34636N.
    IntActiQ9UHX1. 30 interactions.
    MINTiMINT-1374433.
    STRINGi9606.ENSP00000322016.

    Structurei

    Secondary structure

    1
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi118 – 12811
    Beta strandi130 – 1345
    Helixi142 – 1498
    Helixi150 – 1523
    Beta strandi155 – 1606
    Turni164 – 1663
    Beta strandi171 – 1799
    Helixi180 – 19011
    Beta strandi194 – 1996
    Beta strandi201 – 2033
    Helixi206 – 2083
    Helixi209 – 2113
    Helixi212 – 22211
    Helixi223 – 2253
    Beta strandi227 – 2315
    Beta strandi235 – 2373
    Helixi239 – 2468
    Beta strandi252 – 2598
    Turni261 – 2633
    Beta strandi266 – 27611
    Helixi277 – 28711
    Beta strandi293 – 2964
    Beta strandi298 – 3014
    Beta strandi306 – 3094
    Helixi445 – 4484
    Turni449 – 4524
    Helixi453 – 4597
    Beta strandi463 – 4686
    Helixi472 – 4743
    Helixi479 – 4879
    Turni488 – 4903
    Beta strandi493 – 50614
    Beta strandi510 – 52112
    Helixi522 – 53211
    Beta strandi543 – 5475
    Helixi549 – 5535
    Beta strandi557 – 5593

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DNYNMR-A454-559[»]
    2KXFNMR-A119-314[»]
    2KXHNMR-A119-314[»]
    2QFJX-ray2.10A/B118-316[»]
    3DXBX-ray2.20A/B/C/D/E/F/G/H460-499[»]
    3UE2X-ray1.23A443-559[»]
    3US5X-ray1.38A443-559[»]
    3UWTX-ray2.50A118-316[»]
    ProteinModelPortaliQ9UHX1.
    SMRiQ9UHX1. Positions 118-313, 443-559.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ9UHX1.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini129 – 20779RRM 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini226 – 30479RRM 2PROSITE-ProRule annotationAdd
    BLAST
    Domaini462 – 54988RRM 3; atypicalPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 516516Inhibits homodimerizationAdd
    BLAST
    Regioni77 – 559483Inhibits transcriptional repression, interaction with ERCC3 and apoptosis inductionAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi321 – 34323Ala-richAdd
    BLAST

    Domaini

    The third RNA recognition motif, called PUMP domain, is atypical and may rather mediate homodimerization and/or protein-protein interactions.

    Sequence similaritiesi

    Belongs to the RRM half pint family.Curated
    Contains 3 RRM (RNA recognition motif) domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Repeat

    Phylogenomic databases

    eggNOGiCOG0724.
    HOVERGENiHBG055622.
    InParanoidiQ9UHX1.
    KOiK12838.
    OMAiAFVEYDV.
    PhylomeDBiQ9UHX1.
    TreeFamiTF313987.

    Family and domain databases

    Gene3Di3.30.70.330. 3 hits.
    InterProiIPR012677. Nucleotide-bd_a/b_plait.
    IPR006532. PolyU-bd.
    IPR000504. RRM_dom.
    IPR003954. RRM_dom_euk.
    [Graphical view]
    PfamiPF00076. RRM_1. 2 hits.
    [Graphical view]
    SMARTiSM00360. RRM. 2 hits.
    SM00361. RRM_1. 1 hit.
    [Graphical view]
    TIGRFAMsiTIGR01645. half-pint. 1 hit.
    PROSITEiPS50102. RRM. 3 hits.
    [Graphical view]

    Sequences (6)i

    Sequence statusi: Complete.

    This entry describes 6 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q9UHX1-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MATATIALQV NGQQGGGSEP AAAAAVVAAG DKWKPPQGTD SIKMENGQST    50
    AAKLGLPPLT PEQQEALQKA KKYAMEQSIK SVLVKQTIAH QQQQLTNLQM 100
    AAVTMGFGDP LSPLQSMAAQ RQRALAIMCR VYVGSIYYEL GEDTIRQAFA 150
    PFGPIKSIDM SWDSVTMKHK GFAFVEYEVP EAAQLALEQM NSVMLGGRNI 200
    KVGRPSNIGQ AQPIIDQLAE EARAFNRIYV ASVHQDLSDD DIKSVFEAFG 250
    KIKSCTLARD PTTGKHKGYG FIEYEKAQSS QDAVSSMNLF DLGGQYLRVG 300
    KAVTPPMPLL TPATPGGLPP AAAVAAAAAT AKITAQEAVA GAAVLGTLGT 350
    PGLVSPALTL AQPLGTLPQA VMAAQAPGVI TGVTPARPPI PVTIPSVGVV 400
    NPILASPPTL GLLEPKKEKE EEELFPESER PEMLSEQEHM SISGSSARHM 450
    VMQKLLRKQE STVMVLRNMV DPKDIDDDLE GEVTEECGKF GAVNRVIIYQ 500
    EKQGEEEDAE IIVKIFVEFS IASETHKAIQ ALNGRWFAGR KVVAEVYDQE 550
    RFDNSDLSA 559
    Length:559
    Mass (Da):59,875
    Last modified:May 1, 2000 - v1
    Checksum:i619F3C30D1C5951C
    GO
    Isoform 2 (identifier: Q9UHX1-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         101-117: Missing.

    Show »
    Length:542
    Mass (Da):58,171
    Checksum:i2C67EBE529A0922E
    GO
    Isoform 3 (identifier: Q9UHX1-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: Missing.

    Show »
    Length:516
    Mass (Da):55,729
    Checksum:iF52D8C619E874B55
    GO
    Isoform 4 (identifier: Q9UHX1-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-43: Missing.
         101-117: Missing.

    Show »
    Length:499
    Mass (Da):54,025
    Checksum:i77881512A09C3EFD
    GO
    Isoform 5 (identifier: Q9UHX1-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         9-37: Missing.

    Show »
    Length:530
    Mass (Da):57,103
    Checksum:i850251A390ECD30C
    GO
    Isoform 6 (identifier: Q9UHX1-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         9-37: Missing.
         101-117: Missing.

    Show »
    Length:513
    Mass (Da):55,399
    Checksum:i2A5BA6848E391E3A
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti3 – 31T → R in AAB41656. 1 PublicationCurated
    Sequence conflicti123 – 1231R → G in AAB41656. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti169 – 1691H → Y in VRJS; loss of function mutation; results in altered dosage of dfferent PUF60 protein forms and abnormal splicing profile of several target genes. 1 Publication
    VAR_070939

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4343Missing in isoform 3 and isoform 4. 1 PublicationVSP_027717Add
    BLAST
    Alternative sequencei9 – 3729Missing in isoform 5 and isoform 6. CuratedVSP_027718Add
    BLAST
    Alternative sequencei101 – 11717Missing in isoform 2, isoform 4 and isoform 6. 3 PublicationsVSP_027719Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF217197 mRNA. Translation: AAF27522.2.
    AF114818 mRNA. Translation: AAF23589.1.
    AK292373 mRNA. Translation: BAF85062.1.
    CR457143 mRNA. Translation: CAG33424.1.
    CH471162 Genomic DNA. Translation: EAW82187.1.
    CH471162 Genomic DNA. Translation: EAW82189.1.
    BC008875 mRNA. Translation: AAH08875.1.
    BC009734 mRNA. Translation: AAH09734.1.
    BC011265 mRNA. Translation: AAH11265.1.
    BC011979 mRNA. Translation: AAH11979.1.
    U51586 mRNA. Translation: AAB41656.1.
    AF190744 mRNA. Translation: AAF05605.1.
    CCDSiCCDS47933.1. [Q9UHX1-2]
    CCDS47934.1. [Q9UHX1-1]
    CCDS47935.1. [Q9UHX1-3]
    CCDS59514.1. [Q9UHX1-4]
    CCDS59515.1. [Q9UHX1-6]
    CCDS59516.1. [Q9UHX1-5]
    RefSeqiNP_001129505.1. NM_001136033.2. [Q9UHX1-3]
    NP_001258025.1. NM_001271096.1.
    NP_001258026.1. NM_001271097.1. [Q9UHX1-6]
    NP_001258027.1. NM_001271098.1.
    NP_001258028.1. NM_001271099.1. [Q9UHX1-5]
    NP_001258029.1. NM_001271100.1. [Q9UHX1-4]
    NP_055096.2. NM_014281.4. [Q9UHX1-2]
    NP_510965.1. NM_078480.2. [Q9UHX1-1]
    UniGeneiHs.521924.

    Genome annotation databases

    EnsembliENST00000313352; ENSP00000322016; ENSG00000179950. [Q9UHX1-4]
    ENST00000349157; ENSP00000322036; ENSG00000179950. [Q9UHX1-2]
    ENST00000453551; ENSP00000402953; ENSG00000179950. [Q9UHX1-3]
    ENST00000456095; ENSP00000395417; ENSG00000179950. [Q9UHX1-5]
    ENST00000526683; ENSP00000434359; ENSG00000179950. [Q9UHX1-1]
    ENST00000527197; ENSP00000431960; ENSG00000179950. [Q9UHX1-6]
    GeneIDi22827.
    KEGGihsa:22827.
    UCSCiuc003yzq.4. human. [Q9UHX1-1]
    uc003yzr.4. human. [Q9UHX1-4]
    uc003yzt.4. human. [Q9UHX1-2]
    uc031tcp.1. human. [Q9UHX1-5]
    uc031tcq.1. human. [Q9UHX1-6]

    Polymorphism databases

    DMDMi74761960.

    Keywords - Coding sequence diversityi

    Alternative splicing

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF217197 mRNA. Translation: AAF27522.2 .
    AF114818 mRNA. Translation: AAF23589.1 .
    AK292373 mRNA. Translation: BAF85062.1 .
    CR457143 mRNA. Translation: CAG33424.1 .
    CH471162 Genomic DNA. Translation: EAW82187.1 .
    CH471162 Genomic DNA. Translation: EAW82189.1 .
    BC008875 mRNA. Translation: AAH08875.1 .
    BC009734 mRNA. Translation: AAH09734.1 .
    BC011265 mRNA. Translation: AAH11265.1 .
    BC011979 mRNA. Translation: AAH11979.1 .
    U51586 mRNA. Translation: AAB41656.1 .
    AF190744 mRNA. Translation: AAF05605.1 .
    CCDSi CCDS47933.1. [Q9UHX1-2 ]
    CCDS47934.1. [Q9UHX1-1 ]
    CCDS47935.1. [Q9UHX1-3 ]
    CCDS59514.1. [Q9UHX1-4 ]
    CCDS59515.1. [Q9UHX1-6 ]
    CCDS59516.1. [Q9UHX1-5 ]
    RefSeqi NP_001129505.1. NM_001136033.2. [Q9UHX1-3 ]
    NP_001258025.1. NM_001271096.1.
    NP_001258026.1. NM_001271097.1. [Q9UHX1-6 ]
    NP_001258027.1. NM_001271098.1.
    NP_001258028.1. NM_001271099.1. [Q9UHX1-5 ]
    NP_001258029.1. NM_001271100.1. [Q9UHX1-4 ]
    NP_055096.2. NM_014281.4. [Q9UHX1-2 ]
    NP_510965.1. NM_078480.2. [Q9UHX1-1 ]
    UniGenei Hs.521924.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DNY NMR - A 454-559 [» ]
    2KXF NMR - A 119-314 [» ]
    2KXH NMR - A 119-314 [» ]
    2QFJ X-ray 2.10 A/B 118-316 [» ]
    3DXB X-ray 2.20 A/B/C/D/E/F/G/H 460-499 [» ]
    3UE2 X-ray 1.23 A 443-559 [» ]
    3US5 X-ray 1.38 A 443-559 [» ]
    3UWT X-ray 2.50 A 118-316 [» ]
    ProteinModelPortali Q9UHX1.
    SMRi Q9UHX1. Positions 118-313, 443-559.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116502. 88 interactions.
    DIPi DIP-34636N.
    IntActi Q9UHX1. 30 interactions.
    MINTi MINT-1374433.
    STRINGi 9606.ENSP00000322016.

    PTM databases

    PhosphoSitei Q9UHX1.

    Polymorphism databases

    DMDMi 74761960.

    Proteomic databases

    MaxQBi Q9UHX1.
    PaxDbi Q9UHX1.
    PRIDEi Q9UHX1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000313352 ; ENSP00000322016 ; ENSG00000179950 . [Q9UHX1-4 ]
    ENST00000349157 ; ENSP00000322036 ; ENSG00000179950 . [Q9UHX1-2 ]
    ENST00000453551 ; ENSP00000402953 ; ENSG00000179950 . [Q9UHX1-3 ]
    ENST00000456095 ; ENSP00000395417 ; ENSG00000179950 . [Q9UHX1-5 ]
    ENST00000526683 ; ENSP00000434359 ; ENSG00000179950 . [Q9UHX1-1 ]
    ENST00000527197 ; ENSP00000431960 ; ENSG00000179950 . [Q9UHX1-6 ]
    GeneIDi 22827.
    KEGGi hsa:22827.
    UCSCi uc003yzq.4. human. [Q9UHX1-1 ]
    uc003yzr.4. human. [Q9UHX1-4 ]
    uc003yzt.4. human. [Q9UHX1-2 ]
    uc031tcp.1. human. [Q9UHX1-5 ]
    uc031tcq.1. human. [Q9UHX1-6 ]

    Organism-specific databases

    CTDi 22827.
    GeneCardsi GC08M144898.
    HGNCi HGNC:17042. PUF60.
    HPAi HPA045733.
    MIMi 604819. gene.
    615583. phenotype.
    neXtProti NX_Q9UHX1.
    PharmGKBi PA162400364.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG0724.
    HOVERGENi HBG055622.
    InParanoidi Q9UHX1.
    KOi K12838.
    OMAi AFVEYDV.
    PhylomeDBi Q9UHX1.
    TreeFami TF313987.

    Miscellaneous databases

    EvolutionaryTracei Q9UHX1.
    GeneWikii PUF60.
    GenomeRNAii 22827.
    NextBioi 43236.
    PROi Q9UHX1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q9UHX1.
    Bgeei Q9UHX1.
    CleanExi HS_PUF60.
    Genevestigatori Q9UHX1.

    Family and domain databases

    Gene3Di 3.30.70.330. 3 hits.
    InterProi IPR012677. Nucleotide-bd_a/b_plait.
    IPR006532. PolyU-bd.
    IPR000504. RRM_dom.
    IPR003954. RRM_dom_euk.
    [Graphical view ]
    Pfami PF00076. RRM_1. 2 hits.
    [Graphical view ]
    SMARTi SM00360. RRM. 2 hits.
    SM00361. RRM_1. 1 hit.
    [Graphical view ]
    TIGRFAMsi TIGR01645. half-pint. 1 hit.
    PROSITEi PS50102. RRM. 3 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "The FBP interacting repressor targets TFIIH to inhibit activated transcription."
      Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.
      Mol. Cell 5:331-341(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION IN A COMPLEX WITH FUBP1 AND FUSE DNA, INTERACTION WITH CDK7; ERCC3; FUBP1 AND GTF2H1.
    2. "Interaction cloning and characterization of RoBPI, a novel protein binding to human Ro ribonucleoproteins."
      Bouffard P., Barbar E., Briere F., Boire G.
      RNA 6:66-78(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 5), IDENTIFICATION IN A COMPLEX WITH TROVE2 AND Y5 RNA, RNA-BINDING, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
    3. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
      Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
      Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      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.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
      Tissue: Testis.
    5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
      Tissue: Brain, Lung, Muscle and Ovary.
    7. "Interaction of sina and siah ring finger proteins with proteins involved in RNA metabolism, detected using the yeast two hybrid system."
      Hu Y., Holloway A.J., Bowtell D.D.L.
      Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-559 (ISOFORM 2).
    8. "PUF60: a novel U2AF65-related splicing activity."
      Page-McCaw P.S., Amonlirdviman K., Sharp P.A.
      RNA 5:1548-1560(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 4-559 (ISOFORM 1), PROTEIN SEQUENCE OF 32-43; 53-69; 72-80; 156-167; 169-185; 227-243; 267-296; 301-313; 332-342; 419-437 AND 527-559, FUNCTION, SUBUNIT, RNA-BINDING, INTERACTION WITH SFRS11.
    9. "Defective interplay of activators and repressors with TFIH in xeroderma pigmentosum."
      Liu J., Akoulitchev S., Weber A., Ge H., Chuikov S., Libutti D., Wang X.W., Conaway J.W., Harris C.C., Conaway R.C., Reinberg D., Levens D.
      Cell 104:353-363(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ERCC3.
    10. "An essential role of alternative splicing of c-myc suppressor FUSE-binding protein-interacting repressor in carcinogenesis."
      Matsushita K., Tomonaga T., Shimada H., Shioya A., Higashi M., Matsubara H., Harigaya K., Nomura F., Libutti D., Levens D., Ochiai T.
      Cancer Res. 66:1409-1417(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, ALTERNATIVE SPLICING (ISOFORM 6), TISSUE SPECIFICITY.
    11. "The FUSE/FBP/FIR/TFIIH system is a molecular machine programming a pulse of c-myc expression."
      Liu J., Kouzine F., Nie Z., Chung H.-J., Elisha-Feil Z., Weber A., Zhao K., Levens D.
      EMBO J. 25:2119-2130(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, DNA-BINDING.
    12. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    13. "Control of pre-mRNA splicing by the general splicing factors PUF60 and U2AF."
      Hastings M.L., Allemand E., Duelli D.M., Myers M.P., Krainer A.R.
      PLoS ONE 2:E538-E538(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE SPLICEOSOME COMPLEX, IDENTIFICATION BY MASS SPECTROMETRY, RNA-BINDING, SUBCELLULAR LOCATION.
    14. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    16. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
      Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
      Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-251 AND LYS-454, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    17. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60; SER-112 AND THR-314, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    18. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    19. "Solution structure of the third RNA binding domain of FBP-interacting repressor, SIAHBP1."
      RIKEN structural genomics initiative (RSGI)
      Submitted (APR-2007) to the PDB data bank
      Cited for: STRUCTURE BY NMR OF 454-559.
    20. Cited for: VARIANT VRJS TYR-169, CHARACTERIZATION OF VARIANT VRJS TYR-169.

    Entry informationi

    Entry nameiPUF60_HUMAN
    AccessioniPrimary (citable) accession number: Q9UHX1
    Secondary accession number(s): A8K8K8
    , Q969E7, Q96D94, Q96H63, Q99628, Q9NZA0, Q9UJY7
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: September 11, 2007
    Last sequence update: May 1, 2000
    Last modified: October 1, 2014
    This is version 126 of the entry and version 1 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Miscellaneous

    Does not repress TFIIH-mediated transcription in xeroderma pigmentosum complementation group B (XPB) cells.

    Keywords - Technical termi

    3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. Human chromosome 8
      Human chromosome 8: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3