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Q5TAX3 (TUT4_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 98. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Terminal uridylyltransferase 4

Short name=TUTase 4
EC=2.7.7.52
Alternative name(s):
Zinc finger CCHC domain-containing protein 11
Gene names
Name:ZCCHC11
Synonyms:KIAA0191, TUT4
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1644 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.6 Ref.8 Ref.9

Catalytic activity

UTP + RNA(n) = diphosphate + RNA(n+1). Ref.9

Cofactor

Magnesium or manganese By similarity.

Subunit structure

Interacts with LIN28A, LIN28B and T2BP. Ref.6 Ref.9

Subcellular location

Nucleus. Cytoplasm. Note: Translocates into the cytoplasm following treatment of the cell with LPS. Ref.6 Ref.9

Sequence similarities

Belongs to the DNA polymerase type-B-like family.

Contains 3 CCHC-type zinc fingers.

Contains 2 PAP-associated domains.

Sequence caution

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

Ontologies

Keywords
   Biological processRNA-mediated gene silencing
   Cellular componentCytoplasm
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainRepeat
Zinc-finger
   LigandMagnesium
Manganese
Metal-binding
Zinc
   Molecular functionNucleotidyltransferase
Transferase
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processRNA 3'-end processing

Inferred from direct assay Ref.9. Source: UniProtKB

cytokine production

Inferred from electronic annotation. Source: Ensembl

interleukin-6-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

miRNA catabolic process

Inferred from mutant phenotype Ref.9. Source: UniProtKB

miRNA metabolic process

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of NF-kappaB transcription factor activity

Inferred from electronic annotation. Source: Ensembl

positive regulation of interleukin-6 production

Inferred from electronic annotation. Source: Ensembl

pre-miRNA processing

Inferred from mutant phenotype Ref.9. Source: UniProtKB

regulation of lipopolysaccharide-mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

stem cell maintenance

Inferred from mutant phenotype Ref.9. Source: UniProtKB

   Cellular_componentcytoplasm

Inferred from direct assay Ref.9. Source: UniProtKB

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 19056867. Source: UniProt

nucleolus

Inferred from direct assay. Source: HPA

   Molecular_functionRNA uridylyltransferase activity

Inferred from direct assay Ref.9. Source: UniProtKB

poly(A) RNA binding

Inferred from direct assay PubMed 22658674PubMed 22681889. Source: UniProtKB

protein binding

Inferred from physical interaction Ref.6. Source: IntAct

zinc ion binding

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

TIFAQ96CG32EBI-1606425,EBI-740711

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q5TAX3-1)

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.
Isoform 2 (identifier: Q5TAX3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     685-719: RSLNSQLVYEYVVERFRAAYRYFACPQTKGGNKST → LQPGRQEWKLCLKKKKKNSVKYTFIYEIQVSLFVI
     720-1644: Missing.
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 16441644Terminal uridylyltransferase 4
PRO_0000150970

Regions

Domain628 – 67851PAP-associated 1
Domain1184 – 123754PAP-associated 2
Zinc finger913 – 93018CCHC-type 1
Zinc finger1293 – 131018CCHC-type 2
Zinc finger1357 – 137418CCHC-type 3
Compositional bias1398 – 148386Gln-rich
Compositional bias1424 – 1598175Pro-rich

Sites

Metal binding10091Magnesium or manganese; catalytic By similarity
Metal binding10111Magnesium or manganese; catalytic By similarity

Amino acid modifications

Modified residue1341Phosphoserine By similarity

Natural variations

Alternative sequence685 – 71935RSLNS…GNKST → LQPGRQEWKLCLKKKKKNSV KYTFIYEIQVSLFVI in isoform 2.
VSP_038135
Alternative sequence720 – 1644925Missing in isoform 2.
VSP_038136
Natural variant7961D → Y.
Corresponds to variant rs12127732 [ dbSNP | Ensembl ].
VAR_028402

Experimental info

Mutagenesis10111D → A: Loss of nucleotidyltransferase activity. Ref.9
Sequence conflict13131S → SS in AAI31735. Ref.4

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified October 17, 2006. Version 3.
Checksum: B7C88D7DCF0F3356

FASTA1,644185,166
        10         20         30         40         50         60 
MEESKTLKSE NHEPKKNVIC EESKAVQVIG NQTLKARNDK SVKEIENSSP NRNSSKKNKQ 

        70         80         90        100        110        120 
NDICIEKTEV KSCKVNAANL PGPKDLGLVL RDQSHCKAKK FPNSPVKAEK ATISQAKSEK 

       130        140        150        160        170        180 
ATSLQAKAEK SPKSPNSVKA EKASSYQMKS EKVPSSPAEA EKGPSLLLKD MRQKTELQQI 

       190        200        210        220        230        240 
GKKIPSSFTS VDKVNIEAVG GEKCALQNSP RSQKQQTCTD NTGDSDDSAS GIEDVSDDLS 

       250        260        270        280        290        300 
KMKNDESNKE NSSEMDYLEN ATVIDESALT PEQRLGLKQA EERLERDHIF RLEKRSPEYT 

       310        320        330        340        350        360 
NCRYLCKLCL IHIENIQGAH KHIKEKRHKK NILEKQEESE LRSLPPPSPA HLAALSVAVI 

       370        380        390        400        410        420 
ELAKEHGITD DDLRVRQEIV EEMSKVITTF LPECSLRLYG SSLTRFALKS SDVNIDIKFP 

       430        440        450        460        470        480 
PKMNHPDLLI KVLGILKKNV LYVDVESDFH AKVPVVVCRD RKSGLLCRVS AGNDMACLTT 

       490        500        510        520        530        540 
DLLTALGKIE PVFIPLVLAF RYWAKLCYID SQTDGGIPSY CFALMVMFFL QQRKPPLLPC 

       550        560        570        580        590        600 
LLGSWIEGFD PKRMDDFQLK GIVEEKFVKW ECNSSSATEK NSIAEENKAK ADQPKDDTKK 

       610        620        630        640        650        660 
TETDNQSNAM KEKHGKSPLA LETPNRVSLG QLWLELLKFY TLDFALEEYV ICVRIQDILT 

       670        680        690        700        710        720 
RENKNWPKRR IAIEDPFSVK RNVARSLNSQ LVYEYVVERF RAAYRYFACP QTKGGNKSTV 

       730        740        750        760        770        780 
DFKKREKGKI SNKKPVKSNN MATNGCILLG ETTEKINAER EQPVQCDEMD CTSQRCIIDN 

       790        800        810        820        830        840 
NNLLVNELDF ADHGQDSSSL STSKSSEIEP KLDKKQDDLA PSETCLKKEL SQCNCIDLSK 

       850        860        870        880        890        900 
SPDPDKSTGT DCRSNLETES SHQSVCTDTS ATSCNCKATE DASDLNDDDN LPTQELYYVF 

       910        920        930        940        950        960 
DKFILTSGKP PTIVCSICKK DGHSKNDCPE DFRKIDLKPL PPMTNRFREI LDLVCKRCFD 

       970        980        990       1000       1010       1020 
ELSPPCSEQH NREQILIGLE KFIQKEYDEK ARLCLFGSSK NGFGFRDSDL DICMTLEGHE 

      1030       1040       1050       1060       1070       1080 
NAEKLNCKEI IENLAKILKR HPGLRNILPI TTAKVPIVKF EHRRSGLEGD ISLYNTLAQH 

      1090       1100       1110       1120       1130       1140 
NTRMLATYAA IDPRVQYLGY TMKVFAKRCD IGDASRGSLS SYAYILMVLY FLQQRKPPVI 

      1150       1160       1170       1180       1190       1200 
PVLQEIFDGK QIPQRMVDGW NAFFFDKTEE LKKRLPSLGK NTESLGELWL GLLRFYTEEF 

      1210       1220       1230       1240       1250       1260 
DFKEYVISIR QKKLLTTFEK QWTSKCIAIE DPFDLNHNLG AGVSRKMTNF IMKAFINGRK 

      1270       1280       1290       1300       1310       1320 
LFGTPFYPLI GREAEYFFDS RVLTDGELAP NDRCCRVCGK IGHYMKDCPK RKSLLFRLKK 

      1330       1340       1350       1360       1370       1380 
KDSEEEKEGN EEEKDSRDVL DPRDLHDTRD FRDPRDLRCF ICGDAGHVRR ECPEVKLARQ 

      1390       1400       1410       1420       1430       1440 
RNSSVAAAQL VRNLVNAQQV AGSAQQQGDQ SIRTRQSSEC SESPSYSPQP QPFPQNSSQS 

      1450       1460       1470       1480       1490       1500 
AAITQPSSQP GSQPKLGPPQ QGAQPPHQVQ MPLYNFPQSP PAQYSPMHNM GLLPMHPLQI 

      1510       1520       1530       1540       1550       1560 
PAPSWPIHGP VIHSAPGSAP SNIGLNDPSI IFAQPAARPV AIPNTSHDGH WPRTVAPNSL 

      1570       1580       1590       1600       1610       1620 
VNSGAVGNSE PGFRGLTPPI PWEHAPRPHF PLVPASWPYG LHQNFMHQGN ARFQPNKPFY 

      1630       1640 
TQDRCATRRC RERCPHPPRG NVSE 

« Hide

Isoform 2 [UniParc].

Checksum: 51037667A4C3D3A1
Show »

FASTA71981,141

References

« Hide 'large scale' references
[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. expand/collapse author list , 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. expand/collapse author list , 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]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases
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]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
CCDSCCDS30716.1. [Q5TAX3-1]
RefSeqNP_001009881.1. NM_001009881.2.
NP_056084.1. NM_015269.2. [Q5TAX3-1]
UniGeneHs.655407.

3D structure databases

ProteinModelPortalQ5TAX3.
SMRQ5TAX3. Positions 361-705, 961-1269.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116909. 11 interactions.
IntActQ5TAX3. 7 interactions.
STRING9606.ENSP00000257177.

PTM databases

PhosphoSiteQ5TAX3.

Polymorphism databases

DMDM116242850.

Proteomic databases

MaxQBQ5TAX3.
PaxDbQ5TAX3.
PRIDEQ5TAX3.

Protocols and materials databases

DNASU23318.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000257177; ENSP00000257177; ENSG00000134744.
ENST00000371544; ENSP00000360599; ENSG00000134744. [Q5TAX3-1]
GeneID23318.
KEGGhsa:23318.
UCSCuc001ctx.2. human. [Q5TAX3-1]

Organism-specific databases

CTD23318.
GeneCardsGC01M052888.
HGNCHGNC:28981. ZCCHC11.
HPAHPA027412.
HPA027973.
MIM613692. gene.
neXtProtNX_Q5TAX3.
PharmGKBPA134918178.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5260.
KOK13291.
OrthoDBEOG7VB2DH.
PhylomeDBQ5TAX3.
TreeFamTF315661.

Gene expression databases

ArrayExpressQ5TAX3.
BgeeQ5TAX3.
CleanExHS_ZCCHC11.
GenevestigatorQ5TAX3.

Family and domain databases

Gene3D4.10.60.10. 3 hits.
InterProIPR002934. Nucleotidyltransferase.
IPR002058. PAP_assoc.
IPR001878. Znf_CCHC.
[Graphical view]
PfamPF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 2 hits.
PF00098. zf-CCHC. 2 hits.
[Graphical view]
SMARTSM00343. ZnF_C2HC. 3 hits.
[Graphical view]
SUPFAMSSF57756. SSF57756. 2 hits.
PROSITEPS50158. ZF_CCHC. 3 hits.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSZCCHC11. human.
GenomeRNAi23318.
NextBio45208.
PROQ5TAX3.
SOURCESearch...

Entry information

Entry nameTUT4_HUMAN
AccessionPrimary (citable) accession number: Q5TAX3
Secondary accession number(s): A2RRP0 expand/collapse secondary AC list , B7Z8J5, D3DQ35, Q12764, Q5TAX2, Q5TAX4, Q86XZ3
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 1

Human chromosome 1: entries, gene names and cross-references to MIM