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Protein

Terminal uridylyltransferase 4

Gene

ZCCHC11

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

Functioni

Uridylyltransferase that mediates the terminal uridylation of mRNAs with short (less than 25 nucleotides) poly(A) tails, hence facilitating global mRNA decay (PubMed:25480299). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets. Also acts as a suppressor of miRNA biogenesis by mediating the terminal uridylation of some miRNA precursors, including that of let-7 (pre-let-7), miR107, miR-143 and miR-200c. Uridylated miRNAs are not processed by Dicer and undergo degradation. Degradation of pre-let-7 contributes to the maintenance of embryonic stem (ES) cell pluripotency (By similarity). Does not bind RNA directly, but recruited to RNA targets by RNA-binding protein LIN28A. Also catalyzes the 3' uridylation of miR-26A, a miRNA that targets IL6 transcript. This abrogates the silencing of IL6 transcript, hence promoting cytokine expression (By similarity). May also suppress Toll-like receptor-induced NF-kappa-B activation via binding to T2BP. Does not play a role in replication-dependent histone mRNA degradation. Due to functional redundancy between ZCCHC6 and ZCCHC11, the identification of the specific role of each of these proteins is difficult.By similarity3 Publications

Catalytic activityi

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

Cofactori

Mg2+By similarity, Mn2+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

  • poly(A) RNA binding Source: UniProtKB
  • RNA uridylyltransferase activity Source: UniProtKB
  • zinc ion binding Source: InterPro

GO - Biological processi

  • miRNA catabolic process Source: UniProtKB
  • miRNA metabolic process Source: UniProtKB
  • pre-miRNA processing Source: UniProtKB
  • RNA 3'-end processing Source: UniProtKB
  • 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

Enzyme and pathway databases

BRENDAi2.7.7.52. 2681.

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 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:28981. ZCCHC11.

Subcellular locationi

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • extracellular exosome Source: UniProtKB
  • extracellular space Source: UniProtKB
  • 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 and stabilization of pre-let-7 miRNAs. 2 Publications

Organism-specific databases

PharmGKBiPA134918178.

Polymorphism and mutation databases

BioMutaiZCCHC11.
DMDMi116242850.

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

BgeeiQ5TAX3.
CleanExiHS_ZCCHC11.
ExpressionAtlasiQ5TAX3. baseline and differential.
GenevisibleiQ5TAX3. HS.

Organism-specific databases

HPAiHPA027412.
HPA027973.

Interactioni

Subunit structurei

Interacts with LIN28A in the presence of pre-let-7 RNA. Interacts with T2BP.3 Publications

Binary interactionsi

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

Protein-protein interaction databases

BioGridi116909. 10 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.
GeneTreeiENSGT00550000074490.
InParanoidiQ5TAX3.
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. AlignAdd to basket

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

        10         20         30         40         50
MEESKTLKSE NHEPKKNVIC EESKAVQVIG NQTLKARNDK SVKEIENSSP
60 70 80 90 100
NRNSSKKNKQ NDICIEKTEV KSCKVNAANL PGPKDLGLVL RDQSHCKAKK
110 120 130 140 150
FPNSPVKAEK ATISQAKSEK ATSLQAKAEK SPKSPNSVKA EKASSYQMKS
160 170 180 190 200
EKVPSSPAEA EKGPSLLLKD MRQKTELQQI GKKIPSSFTS VDKVNIEAVG
210 220 230 240 250
GEKCALQNSP RSQKQQTCTD NTGDSDDSAS GIEDVSDDLS KMKNDESNKE
260 270 280 290 300
NSSEMDYLEN ATVIDESALT PEQRLGLKQA EERLERDHIF RLEKRSPEYT
310 320 330 340 350
NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE LRSLPPPSPA
360 370 380 390 400
HLAALSVAVI ELAKEHGITD DDLRVRQEIV EEMSKVITTF LPECSLRLYG
410 420 430 440 450
SSLTRFALKS SDVNIDIKFP PKMNHPDLLI KVLGILKKNV LYVDVESDFH
460 470 480 490 500
AKVPVVVCRD RKSGLLCRVS AGNDMACLTT DLLTALGKIE PVFIPLVLAF
510 520 530 540 550
RYWAKLCYID SQTDGGIPSY CFALMVMFFL QQRKPPLLPC LLGSWIEGFD
560 570 580 590 600
PKRMDDFQLK GIVEEKFVKW ECNSSSATEK NSIAEENKAK ADQPKDDTKK
610 620 630 640 650
TETDNQSNAM KEKHGKSPLA LETPNRVSLG QLWLELLKFY TLDFALEEYV
660 670 680 690 700
ICVRIQDILT RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF
710 720 730 740 750
RAAYRYFACP QTKGGNKSTV DFKKREKGKI SNKKPVKSNN MATNGCILLG
760 770 780 790 800
ETTEKINAER EQPVQCDEMD CTSQRCIIDN NNLLVNELDF ADHGQDSSSL
810 820 830 840 850
STSKSSEIEP KLDKKQDDLA PSETCLKKEL SQCNCIDLSK SPDPDKSTGT
860 870 880 890 900
DCRSNLETES SHQSVCTDTS ATSCNCKATE DASDLNDDDN LPTQELYYVF
910 920 930 940 950
DKFILTSGKP PTIVCSICKK DGHSKNDCPE DFRKIDLKPL PPMTNRFREI
960 970 980 990 1000
LDLVCKRCFD ELSPPCSEQH NREQILIGLE KFIQKEYDEK ARLCLFGSSK
1010 1020 1030 1040 1050
NGFGFRDSDL DICMTLEGHE NAEKLNCKEI IENLAKILKR HPGLRNILPI
1060 1070 1080 1090 1100
TTAKVPIVKF EHRRSGLEGD ISLYNTLAQH NTRMLATYAA IDPRVQYLGY
1110 1120 1130 1140 1150
TMKVFAKRCD IGDASRGSLS SYAYILMVLY FLQQRKPPVI PVLQEIFDGK
1160 1170 1180 1190 1200
QIPQRMVDGW NAFFFDKTEE LKKRLPSLGK NTESLGELWL GLLRFYTEEF
1210 1220 1230 1240 1250
DFKEYVISIR QKKLLTTFEK QWTSKCIAIE DPFDLNHNLG AGVSRKMTNF
1260 1270 1280 1290 1300
IMKAFINGRK LFGTPFYPLI GREAEYFFDS RVLTDGELAP NDRCCRVCGK
1310 1320 1330 1340 1350
IGHYMKDCPK RKSLLFRLKK KDSEEEKEGN EEEKDSRDVL DPRDLHDTRD
1360 1370 1380 1390 1400
FRDPRDLRCF ICGDAGHVRR ECPEVKLARQ RNSSVAAAQL VRNLVNAQQV
1410 1420 1430 1440 1450
AGSAQQQGDQ SIRTRQSSEC SESPSYSPQP QPFPQNSSQS AAITQPSSQP
1460 1470 1480 1490 1500
GSQPKLGPPQ QGAQPPHQVQ MPLYNFPQSP PAQYSPMHNM GLLPMHPLQI
1510 1520 1530 1540 1550
PAPSWPIHGP VIHSAPGSAP SNIGLNDPSI IFAQPAARPV AIPNTSHDGH
1560 1570 1580 1590 1600
WPRTVAPNSL VNSGAVGNSE PGFRGLTPPI PWEHAPRPHF PLVPASWPYG
1610 1620 1630 1640
LHQNFMHQGN ARFQPNKPFY TQDRCATRRC RERCPHPPRG NVSE
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. Curated

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:
EMBLi
GenBanki
DDBJi
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

EnsembliENST00000371544; ENSP00000360599; ENSG00000134744.
GeneIDi23318.
KEGGihsa:23318.
UCSCiuc001ctx.2. human. [Q5TAX3-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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.

3D structure databases

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

Protein-protein interaction databases

BioGridi116909. 10 interactions.
IntActiQ5TAX3. 7 interactions.
STRINGi9606.ENSP00000257177.

PTM databases

PhosphoSiteiQ5TAX3.

Polymorphism and mutation databases

BioMutaiZCCHC11.
DMDMi116242850.

Proteomic databases

MaxQBiQ5TAX3.
PaxDbiQ5TAX3.
PRIDEiQ5TAX3.

Protocols and materials databases

DNASUi23318.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371544; ENSP00000360599; ENSG00000134744.
GeneIDi23318.
KEGGihsa:23318.
UCSCiuc001ctx.2. human. [Q5TAX3-1]

Organism-specific databases

CTDi23318.
GeneCardsiGC01M052888.
HGNCiHGNC:28981. ZCCHC11.
HPAiHPA027412.
HPA027973.
MIMi613692. gene.
neXtProtiNX_Q5TAX3.
PharmGKBiPA134918178.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG5260.
GeneTreeiENSGT00550000074490.
InParanoidiQ5TAX3.
KOiK13291.
OrthoDBiEOG7VB2DH.
PhylomeDBiQ5TAX3.
TreeFamiTF315661.

Enzyme and pathway databases

BRENDAi2.7.7.52. 2681.

Miscellaneous databases

ChiTaRSiZCCHC11. human.
GenomeRNAii23318.
NextBioi45208.
PROiQ5TAX3.
SOURCEiSearch...

Gene expression databases

BgeeiQ5TAX3.
CleanExiHS_ZCCHC11.
ExpressionAtlasiQ5TAX3. baseline and differential.
GenevisibleiQ5TAX3. HS.

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]
ProtoNetiSearch...

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, MUTAGENESIS OF ASP-1011.
  10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. "Lin28A and Lin28B inhibit let-7 microRNA biogenesis by distinct mechanisms."
    Piskounova E., Polytarchou C., Thornton J.E., LaPierre R.J., Pothoulakis C., Hagan J.P., Iliopoulos D., Gregory R.I.
    Cell 147:1066-1079(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LIN28A.
  12. "Uridylation by TUT4 and TUT7 marks mRNA for degradation."
    Lim J., Ha M., Chang H., Kwon S.C., Simanshu D.K., Patel D.J., Kim V.N.
    Cell 159:1365-1376(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, MUTAGENESIS OF ASP-1011.

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 22, 2015
This is version 108 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.