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Q5TAX3

- TUT4_HUMAN

UniProt

Q5TAX3 - TUT4_HUMAN

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Protein

Terminal uridylyltransferase 4

Gene
ZCCHC11, KIAA0191, TUT4
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.3 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; catalytic By similarity
Metal bindingi1011 – 10111Magnesium or manganese; catalytic By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri913 – 93018CCHC-type 1Add
BLAST
Zinc fingeri1293 – 131018CCHC-type 2Add
BLAST
Zinc fingeri1357 – 137418CCHC-type 3Add
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
Complete GO annotation...

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.2 Publications

GO - Cellular componenti

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

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 – 1341Phosphoserine By 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.

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

Zinc finger

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

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. VSP_038135Add
BLAST
Alternative sequencei720 – 1644925Missing in isoform 2. VSP_038136Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1313 – 13131S → SS in AAI31735. 1 Publication

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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 98 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

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