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Q5TAX3

- TUT4_HUMAN

UniProt

Q5TAX3 - TUT4_HUMAN

Protein

Terminal uridylyltransferase 4

Gene

ZCCHC11

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 99 (01 Oct 2014)
      Sequence version 3 (17 Oct 2006)
      Previous versions | rss
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    Functioni

    Uridylyltransferase that acts as a suppressor of microRNA (miRNA) biogenesis by specifically mediating the terminal uridylation of some miRNAs. Catalyzes the 3' uridylation of precursor let-7 (pre-let-7), a miRNA precursor. Uridylated pre-let-7 miRNAs fail to be processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cells and is required for ES cells to maintain pluripotency. Does not bind RNA by itself, recruited to pre-let-7 miRNAs via its interaction with LIN28A and LIN28B. Also catalyzes the 3' uridylation of miR-26A, a miRNA that represses IL6 transcript, leading to abrogate IL6 transcript repression and promote cytokine expression. May also suppress Toll-like receptor-induced NF-kappa-B activity via binding to T2BP. Does not play a role in replication-dependent histone mRNA degradation.2 Publications

    Catalytic activityi

    UTP + RNA(n) = diphosphate + RNA(n+1).1 Publication

    Cofactori

    Magnesium or manganese.By similarity

    Sites

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Metal bindingi1009 – 10091Magnesium or manganese; catalyticBy similarity
    Metal bindingi1011 – 10111Magnesium or manganese; catalyticBy similarity

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri913 – 93018CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1293 – 131018CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1357 – 137418CCHC-type 3PROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. poly(A) RNA binding Source: UniProtKB
    2. protein binding Source: IntAct
    3. RNA uridylyltransferase activity Source: UniProtKB
    4. zinc ion binding Source: InterPro

    GO - Biological processi

    1. cytokine production Source: Ensembl
    2. interleukin-6-mediated signaling pathway Source: Ensembl
    3. miRNA catabolic process Source: UniProtKB
    4. miRNA metabolic process Source: UniProtKB
    5. negative regulation of NF-kappaB transcription factor activity Source: Ensembl
    6. positive regulation of interleukin-6 production Source: Ensembl
    7. pre-miRNA processing Source: UniProtKB
    8. regulation of lipopolysaccharide-mediated signaling pathway Source: Ensembl
    9. RNA 3'-end processing Source: UniProtKB
    10. stem cell maintenance Source: UniProtKB

    Keywords - Molecular functioni

    Nucleotidyltransferase, Transferase

    Keywords - Biological processi

    RNA-mediated gene silencing

    Keywords - Ligandi

    Magnesium, Manganese, Metal-binding, Zinc

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Terminal uridylyltransferase 4 (EC:2.7.7.52)
    Short name:
    TUTase 4
    Alternative name(s):
    Zinc finger CCHC domain-containing protein 11
    Gene namesi
    Name:ZCCHC11
    Synonyms:KIAA0191, TUT4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:28981. ZCCHC11.

    Subcellular locationi

    Nucleus. Cytoplasm
    Note: Translocates into the cytoplasm following treatment of the cell with LPS.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. extracellular space Source: UniProt
    3. extracellular vesicular exosome Source: UniProt
    4. nucleolus Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1011 – 10111D → A: Loss of nucleotidyltransferase activity. 1 Publication

    Organism-specific databases

    PharmGKBiPA134918178.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 16441644Terminal uridylyltransferase 4PRO_0000150970Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei134 – 1341PhosphoserineBy similarity

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ5TAX3.
    PaxDbiQ5TAX3.
    PRIDEiQ5TAX3.

    PTM databases

    PhosphoSiteiQ5TAX3.

    Expressioni

    Gene expression databases

    ArrayExpressiQ5TAX3.
    BgeeiQ5TAX3.
    CleanExiHS_ZCCHC11.
    GenevestigatoriQ5TAX3.

    Organism-specific databases

    HPAiHPA027412.
    HPA027973.

    Interactioni

    Subunit structurei

    Interacts with LIN28A, LIN28B and T2BP.2 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    TIFAQ96CG32EBI-1606425,EBI-740711

    Protein-protein interaction databases

    BioGridi116909. 11 interactions.
    IntActiQ5TAX3. 7 interactions.
    STRINGi9606.ENSP00000257177.

    Structurei

    3D structure databases

    ProteinModelPortaliQ5TAX3.
    SMRiQ5TAX3. Positions 361-705, 961-1269.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini628 – 67851PAP-associated 1Add
    BLAST
    Domaini1184 – 123754PAP-associated 2Add
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1398 – 148386Gln-richAdd
    BLAST
    Compositional biasi1424 – 1598175Pro-richAdd
    BLAST

    Sequence similaritiesi

    Belongs to the DNA polymerase type-B-like family.Curated
    Contains 3 CCHC-type zinc fingers.PROSITE-ProRule annotation
    Contains 2 PAP-associated domains.Curated

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri913 – 93018CCHC-type 1PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1293 – 131018CCHC-type 2PROSITE-ProRule annotationAdd
    BLAST
    Zinc fingeri1357 – 137418CCHC-type 3PROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Repeat, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5260.
    KOiK13291.
    OrthoDBiEOG7VB2DH.
    PhylomeDBiQ5TAX3.
    TreeFamiTF315661.

    Family and domain databases

    Gene3Di4.10.60.10. 3 hits.
    InterProiIPR002934. Nucleotidyltransferase.
    IPR002058. PAP_assoc.
    IPR001878. Znf_CCHC.
    [Graphical view]
    PfamiPF01909. NTP_transf_2. 1 hit.
    PF03828. PAP_assoc. 2 hits.
    PF00098. zf-CCHC. 2 hits.
    [Graphical view]
    SMARTiSM00343. ZnF_C2HC. 3 hits.
    [Graphical view]
    SUPFAMiSSF57756. SSF57756. 2 hits.
    PROSITEiPS50158. ZF_CCHC. 3 hits.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view]

    Sequences (2)i

    Sequence statusi: Complete.

    This entry describes 2 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q5TAX3-1) [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

    MEESKTLKSE NHEPKKNVIC EESKAVQVIG NQTLKARNDK SVKEIENSSP     50
    NRNSSKKNKQ NDICIEKTEV KSCKVNAANL PGPKDLGLVL RDQSHCKAKK 100
    FPNSPVKAEK ATISQAKSEK ATSLQAKAEK SPKSPNSVKA EKASSYQMKS 150
    EKVPSSPAEA EKGPSLLLKD MRQKTELQQI GKKIPSSFTS VDKVNIEAVG 200
    GEKCALQNSP RSQKQQTCTD NTGDSDDSAS GIEDVSDDLS KMKNDESNKE 250
    NSSEMDYLEN ATVIDESALT PEQRLGLKQA EERLERDHIF RLEKRSPEYT 300
    NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE LRSLPPPSPA 350
    HLAALSVAVI ELAKEHGITD DDLRVRQEIV EEMSKVITTF LPECSLRLYG 400
    SSLTRFALKS SDVNIDIKFP PKMNHPDLLI KVLGILKKNV LYVDVESDFH 450
    AKVPVVVCRD RKSGLLCRVS AGNDMACLTT DLLTALGKIE PVFIPLVLAF 500
    RYWAKLCYID SQTDGGIPSY CFALMVMFFL QQRKPPLLPC LLGSWIEGFD 550
    PKRMDDFQLK GIVEEKFVKW ECNSSSATEK NSIAEENKAK ADQPKDDTKK 600
    TETDNQSNAM KEKHGKSPLA LETPNRVSLG QLWLELLKFY TLDFALEEYV 650
    ICVRIQDILT RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF 700
    RAAYRYFACP QTKGGNKSTV DFKKREKGKI SNKKPVKSNN MATNGCILLG 750
    ETTEKINAER EQPVQCDEMD CTSQRCIIDN NNLLVNELDF ADHGQDSSSL 800
    STSKSSEIEP KLDKKQDDLA PSETCLKKEL SQCNCIDLSK SPDPDKSTGT 850
    DCRSNLETES SHQSVCTDTS ATSCNCKATE DASDLNDDDN LPTQELYYVF 900
    DKFILTSGKP PTIVCSICKK DGHSKNDCPE DFRKIDLKPL PPMTNRFREI 950
    LDLVCKRCFD ELSPPCSEQH NREQILIGLE KFIQKEYDEK ARLCLFGSSK 1000
    NGFGFRDSDL DICMTLEGHE NAEKLNCKEI IENLAKILKR HPGLRNILPI 1050
    TTAKVPIVKF EHRRSGLEGD ISLYNTLAQH NTRMLATYAA IDPRVQYLGY 1100
    TMKVFAKRCD IGDASRGSLS SYAYILMVLY FLQQRKPPVI PVLQEIFDGK 1150
    QIPQRMVDGW NAFFFDKTEE LKKRLPSLGK NTESLGELWL GLLRFYTEEF 1200
    DFKEYVISIR QKKLLTTFEK QWTSKCIAIE DPFDLNHNLG AGVSRKMTNF 1250
    IMKAFINGRK LFGTPFYPLI GREAEYFFDS RVLTDGELAP NDRCCRVCGK 1300
    IGHYMKDCPK RKSLLFRLKK KDSEEEKEGN EEEKDSRDVL DPRDLHDTRD 1350
    FRDPRDLRCF ICGDAGHVRR ECPEVKLARQ RNSSVAAAQL VRNLVNAQQV 1400
    AGSAQQQGDQ SIRTRQSSEC SESPSYSPQP QPFPQNSSQS AAITQPSSQP 1450
    GSQPKLGPPQ QGAQPPHQVQ MPLYNFPQSP PAQYSPMHNM GLLPMHPLQI 1500
    PAPSWPIHGP VIHSAPGSAP SNIGLNDPSI IFAQPAARPV AIPNTSHDGH 1550
    WPRTVAPNSL VNSGAVGNSE PGFRGLTPPI PWEHAPRPHF PLVPASWPYG 1600
    LHQNFMHQGN ARFQPNKPFY TQDRCATRRC RERCPHPPRG NVSE 1644
    Length:1,644
    Mass (Da):185,166
    Last modified:October 17, 2006 - v3
    Checksum:iB7C88D7DCF0F3356
    GO
    Isoform 2 (identifier: Q5TAX3-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         685-719: RSLNSQLVYEYVVERFRAAYRYFACPQTKGGNKST → LQPGRQEWKLCLKKKKKNSVKYTFIYEIQVSLFVI
         720-1644: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:719
    Mass (Da):81,141
    Checksum:i51037667A4C3D3A1
    GO

    Sequence cautioni

    The sequence CAI23477.1 differs from that shown. Reason: Erroneous gene model prediction.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti1313 – 13131S → SS in AAI31735. (PubMed:15489334)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti796 – 7961D → Y.
    Corresponds to variant rs12127732 [ dbSNP | Ensembl ].
    VAR_028402

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei685 – 71935RSLNS…GNKST → LQPGRQEWKLCLKKKKKNSV KYTFIYEIQVSLFVI in isoform 2. 1 PublicationVSP_038135Add
    BLAST
    Alternative sequencei720 – 1644925Missing in isoform 2. 1 PublicationVSP_038136Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK303532 mRNA. Translation: BAH13981.1.
    AL138849 Genomic DNA. Translation: CAI23476.1.
    AL138849 Genomic DNA. Translation: CAI23477.1. Sequence problems.
    AL138849 Genomic DNA. Translation: CAI23478.1.
    CH471059 Genomic DNA. Translation: EAX06778.1.
    CH471059 Genomic DNA. Translation: EAX06780.1.
    BC131734 mRNA. Translation: AAI31735.1.
    D83776 mRNA. Translation: BAA12105.1.
    CCDSiCCDS30716.1. [Q5TAX3-1]
    RefSeqiNP_001009881.1. NM_001009881.2.
    NP_056084.1. NM_015269.2. [Q5TAX3-1]
    UniGeneiHs.655407.

    Genome annotation databases

    EnsembliENST00000257177; ENSP00000257177; ENSG00000134744.
    ENST00000371544; ENSP00000360599; ENSG00000134744. [Q5TAX3-1]
    GeneIDi23318.
    KEGGihsa:23318.
    UCSCiuc001ctx.2. human. [Q5TAX3-1]

    Polymorphism databases

    DMDMi116242850.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AK303532 mRNA. Translation: BAH13981.1 .
    AL138849 Genomic DNA. Translation: CAI23476.1 .
    AL138849 Genomic DNA. Translation: CAI23477.1 . Sequence problems.
    AL138849 Genomic DNA. Translation: CAI23478.1 .
    CH471059 Genomic DNA. Translation: EAX06778.1 .
    CH471059 Genomic DNA. Translation: EAX06780.1 .
    BC131734 mRNA. Translation: AAI31735.1 .
    D83776 mRNA. Translation: BAA12105.1 .
    CCDSi CCDS30716.1. [Q5TAX3-1 ]
    RefSeqi NP_001009881.1. NM_001009881.2.
    NP_056084.1. NM_015269.2. [Q5TAX3-1 ]
    UniGenei Hs.655407.

    3D structure databases

    ProteinModelPortali Q5TAX3.
    SMRi Q5TAX3. Positions 361-705, 961-1269.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116909. 11 interactions.
    IntActi Q5TAX3. 7 interactions.
    STRINGi 9606.ENSP00000257177.

    PTM databases

    PhosphoSitei Q5TAX3.

    Polymorphism databases

    DMDMi 116242850.

    Proteomic databases

    MaxQBi Q5TAX3.
    PaxDbi Q5TAX3.
    PRIDEi Q5TAX3.

    Protocols and materials databases

    DNASUi 23318.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000257177 ; ENSP00000257177 ; ENSG00000134744 .
    ENST00000371544 ; ENSP00000360599 ; ENSG00000134744 . [Q5TAX3-1 ]
    GeneIDi 23318.
    KEGGi hsa:23318.
    UCSCi uc001ctx.2. human. [Q5TAX3-1 ]

    Organism-specific databases

    CTDi 23318.
    GeneCardsi GC01M052888.
    HGNCi HGNC:28981. ZCCHC11.
    HPAi HPA027412.
    HPA027973.
    MIMi 613692. gene.
    neXtProti NX_Q5TAX3.
    PharmGKBi PA134918178.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5260.
    KOi K13291.
    OrthoDBi EOG7VB2DH.
    PhylomeDBi Q5TAX3.
    TreeFami TF315661.

    Miscellaneous databases

    ChiTaRSi ZCCHC11. human.
    GenomeRNAii 23318.
    NextBioi 45208.
    PROi Q5TAX3.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q5TAX3.
    Bgeei Q5TAX3.
    CleanExi HS_ZCCHC11.
    Genevestigatori Q5TAX3.

    Family and domain databases

    Gene3Di 4.10.60.10. 3 hits.
    InterProi IPR002934. Nucleotidyltransferase.
    IPR002058. PAP_assoc.
    IPR001878. Znf_CCHC.
    [Graphical view ]
    Pfami PF01909. NTP_transf_2. 1 hit.
    PF03828. PAP_assoc. 2 hits.
    PF00098. zf-CCHC. 2 hits.
    [Graphical view ]
    SMARTi SM00343. ZnF_C2HC. 3 hits.
    [Graphical view ]
    SUPFAMi SSF57756. SSF57756. 2 hits.
    PROSITEi PS50158. ZF_CCHC. 3 hits.
    PS00028. ZINC_FINGER_C2H2_1. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "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 2).
      Tissue: Thymus.
    2. "The DNA sequence and biological annotation of human chromosome 1."
      Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
      , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
      Nature 441:315-321(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    4. "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].
    5. "Prediction of the coding sequences of unidentified human genes. V. The coding sequences of 40 new genes (KIAA0161-KIAA0200) deduced by analysis of cDNA clones from human cell line KG-1."
      Nagase T., Seki N., Ishikawa K., Tanaka A., Nomura N.
      DNA Res. 3:17-24(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 129-1644.
      Tissue: Bone marrow.
    6. "A novel Zinc finger protein, ZCCHC11, interacts with TIFA and modulates TLR signaling."
      Minoda Y., Saeki K., Aki D., Takaki H., Sanada T., Koga K., Kobayashi T., Takaesu G., Yoshimura A.
      Biochem. Biophys. Res. Commun. 344:1023-1030(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH T2BP, SUBCELLULAR LOCATION.
    7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic kidney.
    8. "Degradation of histone mRNA requires oligouridylation followed by decapping and simultaneous degradation of the mRNA both 5' to 3' and 3' to 5'."
      Mullen T.E., Marzluff W.F.
      Genes Dev. 22:50-65(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: ABSENCE OF FUNCTION IN HISTONE MRNA DEGRADATION ACTIVITY.
    9. "TUT4 in concert with Lin28 suppresses MicroRNA biogenesis through pre-microRNA uridylation."
      Heo I., Joo C., Kim Y.-K., Ha M., Yoon M.-J., Cho J., Yeom K.-H., Han J., Kim V.N.
      Cell 138:696-708(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, INTERACTION WITH LIN28A AND LIN28B, MUTAGENESIS OF ASP-1011.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiTUT4_HUMAN
    AccessioniPrimary (citable) accession number: Q5TAX3
    Secondary accession number(s): A2RRP0
    , B7Z8J5, D3DQ35, Q12764, Q5TAX2, Q5TAX4, Q86XZ3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: May 10, 2005
    Last sequence update: October 17, 2006
    Last modified: October 1, 2014
    This is version 99 of the entry and version 3 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

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 1
      Human chromosome 1: 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. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3