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Protein

Terminal uridylyltransferase 7

Gene

ZCCHC6

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:19703396, PubMed:25480299). Involved in microRNA (miRNA)-induced gene silencing through uridylation of deadenylated miRNA targets (PubMed:25480299). 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). Uridylated pre-let-7 RNA is not processed by Dicer and undergo degradation. Pre-let-7 uridylation is strongly enhanced in the presence of LIN28A (PubMed:22898984). Due to functional redundancy between ZCCHC6 and ZCCHC11, the identification of the specific role of each of these proteins is difficult.3 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 bindingi1058 – 10581Magnesium or manganese; catalyticBy similarity
Metal bindingi1060 – 10601Magnesium or manganese; catalyticBy similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Zinc fingeri963 – 98018CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1345 – 136218CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1451 – 146818CCHC-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

  • RNA 3'-end processing Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Nucleotidyltransferase, Transferase

Keywords - Ligandi

Magnesium, Manganese, Metal-binding, Zinc

Enzyme and pathway databases

BRENDAi2.7.7.52. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Terminal uridylyltransferase 7 (EC:2.7.7.52)
Short name:
TUTase 7
Alternative name(s):
Zinc finger CCHC domain-containing protein 6
Gene namesi
Name:ZCCHC6
Synonyms:HS2, KIAA1711, TUT7
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:25817. ZCCHC6.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134971144.

Polymorphism and mutation databases

BioMutaiZCCHC6.
DMDMi67462100.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 14951495Terminal uridylyltransferase 7PRO_0000150957Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei57 – 571PhosphothreonineCombined sources
Modified residuei64 – 641PhosphothreonineCombined sources
Modified residuei132 – 1321PhosphoserineBy similarity
Modified residuei172 – 1721PhosphoserineCombined sources
Modified residuei844 – 8441PhosphoserineCombined sources
Modified residuei893 – 8931PhosphoserineBy similarity
Modified residuei939 – 9391PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ5VYS8.
MaxQBiQ5VYS8.
PaxDbiQ5VYS8.
PRIDEiQ5VYS8.

PTM databases

iPTMnetiQ5VYS8.
PhosphoSiteiQ5VYS8.

Expressioni

Gene expression databases

BgeeiQ5VYS8.
CleanExiHS_ZCCHC6.
ExpressionAtlasiQ5VYS8. baseline and differential.
GenevisibleiQ5VYS8. HS.

Organism-specific databases

HPAiHPA020615.
HPA020620.

Interactioni

Protein-protein interaction databases

BioGridi122795. 25 interactions.
IntActiQ5VYS8. 18 interactions.
MINTiMINT-4718069.
STRINGi9606.ENSP00000365130.

Structurei

3D structure databases

ProteinModelPortaliQ5VYS8.
SMRiQ5VYS8. Positions 299-515, 1010-1308.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini551 – 60050PAP-associated 1Add
BLAST
Domaini1233 – 128654PAP-associated 2Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi20 – 234Poly-Asp
Compositional biasi815 – 936122Glu-richAdd
BLAST
Compositional biasi1367 – 13704Poly-Arg

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 fingeri963 – 98018CCHC-type 1PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1345 – 136218CCHC-type 2PROSITE-ProRule annotationAdd
BLAST
Zinc fingeri1451 – 146818CCHC-type 3PROSITE-ProRule annotationAdd
BLAST

Keywords - Domaini

Repeat, Zinc-finger

Phylogenomic databases

eggNOGiKOG2277. Eukaryota.
COG5260. LUCA.
GeneTreeiENSGT00550000074490.
InParanoidiQ5VYS8.
KOiK13291.
OMAiKYFALPH.
OrthoDBiEOG7VB2DH.
PhylomeDBiQ5VYS8.
TreeFamiTF315661.

Family and domain databases

Gene3Di4.10.60.10. 3 hits.
InterProiIPR002058. PAP_assoc.
IPR002934. Polymerase_NTP_transf_dom.
IPR001878. Znf_CCHC.
IPR003604. Znf_U1.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 2 hits.
PF00098. zf-CCHC. 3 hits.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 3 hits.
SM00451. ZnF_U1. 1 hit.
[Graphical view]
SUPFAMiSSF57756. SSF57756. 3 hits.
PROSITEiPS50158. ZF_CCHC. 3 hits.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q5VYS8-1) [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
MGDTAKPYFV KRTKDRGTMD DDDFRRGHPQ QDYLIIDDHA KGHGSKMEKG
60 70 80 90 100
LQKKKITPGN YGNTPRKGPC AVSSNPYAFK NPIYSQPAWM NDSHKDQSKR
110 120 130 140 150
WLSDEHTGNS DNWREFKPGP RIPVINRQRK DSFQENEDGY RWQDTRGCRT
160 170 180 190 200
VRRLFHKDLT SLETTSEMEA GSPENKKQRS RPRKPRKTRN EENEQDGDLE
210 220 230 240 250
GPVIDESVLS TKELLGLQQA EERLKRDCID RLKRRPRNYP TAKYTCRLCD
260 270 280 290 300
VLIESIAFAH KHIKEKRHKK NIKEKQEEEL LTTLPPPTPS QINAVGIAID
310 320 330 340 350
KVVQEFGLHN ENLEQRLEIK RIMENVFQHK LPDCSLRLYG SSCSRLGFKN
360 370 380 390 400
SDVNIDIQFP AIMSQPDVLL LVQECLKNSD SFIDVDADFH ARVPVVVCRE
410 420 430 440 450
KQSGLLCKVS AGNENACLTT KHLTALGKLE PKLVPLVIAF RYWAKLCSID
460 470 480 490 500
RPEEGGLPPY VFALMAIFFL QQRKEPLLPV YLGSWIEGFS LSKLGNFNLQ
510 520 530 540 550
DIEKDVVIWE HTDSAAGDTG ITKEEAPRET PIKRGQVSLI LDVKHQPSVP
560 570 580 590 600
VGQLWVELLR FYALEFNLAD LVISIRVKEL VSRELKDWPK KRIAIEDPYS
610 620 630 640 650
VKRNVARTLN SQPVFEYILH CLRTTYKYFA LPHKITKSSL LKPLNAITCI
660 670 680 690 700
SEHSKEVINH HPDVQTKDDK LKNSVLAQGP GATSSAANTC KVQPLTLKET
710 720 730 740 750
AESFGSPPKE EMGNEHISVH PENSDCIQAD VNSDDYKGDK VYHPETGRKN
760 770 780 790 800
EKEKVGRKGK HLLTVDQKRG EHVVCGSTRN NESESTLDLE GFQNPTAKEC
810 820 830 840 850
EGLATLDNKA DLDGESTEGT EELEDSLNHF THSVQGQTSE MIPSDEEEED
860 870 880 890 900
DEEEEEEEEP RLTINQREDE DGMANEDELD NTYTGSGDED ALSEEDDELG
910 920 930 940 950
EAAKYEDVKE CGKHVERALL VELNKISLKE ENVCEEKNSP VDQSDFFYEF
960 970 980 990 1000
SKLIFTKGKS PTVVCSLCKR EGHLKKDCPE DFKRIQLEPL PPLTPKFLNI
1010 1020 1030 1040 1050
LDQVCIQCYK DFSPTIIEDQ AREHIRQNLE SFIRQDFPGT KLSLFGSSKN
1060 1070 1080 1090 1100
GFGFKQSDLD VCMTINGLET AEGLDCVRTI EELARVLRKH SGLRNILPIT
1110 1120 1130 1140 1150
TAKVPIVKFF HLRSGLEVDI SLYNTLALHN TRLLSAYSAI DPRVKYLCYT
1160 1170 1180 1190 1200
MKVFTKMCDI GDASRGSLSS YAYTLMVLYF LQQRNPPVIP VLQEIYKGEK
1210 1220 1230 1240 1250
KPEIFVDGWN IYFFDQIDEL PTYWSECGKN TESVGQLWLG LLRFYTEEFD
1260 1270 1280 1290 1300
FKEHVISIRR KSLLTTFKKQ WTSKYIVIED PFDLNHNLGA GLSRKMTNFI
1310 1320 1330 1340 1350
MKAFINGRRV FGIPVKGFPK DYPSKMEYFF DPDVLTEGEL APNDRCCRIC
1360 1370 1380 1390 1400
GKIGHFMKDC PMRRKVRRRR DQEDALNQRY PENKEKRSKE DKEIHNKYTE
1410 1420 1430 1440 1450
REVSTKEDKP IQCTPQKAKP MRAAADLGRE KILRPPVEKW KRQDDKDLRE
1460 1470 1480 1490
KRCFICGREG HIKKECPQFK GSSGSLSSKY MTQGKASAKR TQQES
Length:1,495
Mass (Da):171,229
Last modified:December 7, 2004 - v1
Checksum:i1AAB0F5B37266FF9
GO
Isoform 2 (identifier: Q5VYS8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     597-615: DPYSVKRNVARTLNSQPVF → GISKCLSYSPPLFFLKVPV
     616-1495: Missing.

Note: No experimental confirmation available.
Show »
Length:615
Mass (Da):70,475
Checksum:iE3B7FEE22E438BBD
GO
Isoform 3 (identifier: Q5VYS8-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     538-544: SLILDVK → VSSLLCR
     545-1495: Missing.

Note: No experimental confirmation available.
Show »
Length:544
Mass (Da):62,261
Checksum:iDE285E0532C43340
GO
Isoform 4 (identifier: Q5VYS8-4) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     363-486: MSQPDVLLLV...LLPVYLGSWI → I
     960-1072: Missing.

Note: No experimental confirmation available.
Show »
Length:1,259
Mass (Da):144,656
Checksum:i2DFDA89240222042
GO
Isoform 5 (identifier: Q5VYS8-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     403-412: SGLLCKVSAG → RSHFFKLFIY
     413-1495: Missing.

Note: No experimental confirmation available.
Show »
Length:412
Mass (Da):47,903
Checksum:i73F48669DDBD99CB
GO
Isoform 6 (identifier: Q5VYS8-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1157-1194: Missing.

Note: No experimental confirmation available.
Show »
Length:1,457
Mass (Da):166,970
Checksum:iF5F376C95EF2CEE5
GO

Sequence cautioni

The sequence BAB14584.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence BAB71052.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti157 – 1571K → R in BAB70951 (PubMed:14702039).Curated
Sequence conflicti316 – 3161R → T in CAE46038 (PubMed:17974005).Curated
Sequence conflicti514 – 5141S → N in CAE46038 (PubMed:17974005).Curated
Sequence conflicti900 – 9001G → V in CAI45944 (PubMed:17974005).Curated
Sequence conflicti937 – 9371Missing in CAI45944 (PubMed:17974005).Curated
Sequence conflicti937 – 9371Missing in CAH56219 (PubMed:17974005).Curated
Sequence conflicti1104 – 11041V → M in CAH56219 (PubMed:17974005).Curated
Sequence conflicti1319 – 13191P → S in CAH56219 (PubMed:17974005).Curated
Sequence conflicti1474 – 14741G → D in CAI45944 (PubMed:17974005).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti40 – 401A → V.
Corresponds to variant rs2378695 [ dbSNP | Ensembl ].
VAR_053753

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei363 – 486124MSQPD…LGSWI → I in isoform 4. 1 PublicationVSP_013832Add
BLAST
Alternative sequencei403 – 41210SGLLCKVSAG → RSHFFKLFIY in isoform 5. 1 PublicationVSP_013833
Alternative sequencei413 – 14951083Missing in isoform 5. 1 PublicationVSP_013834Add
BLAST
Alternative sequencei538 – 5447SLILDVK → VSSLLCR in isoform 3. 1 PublicationVSP_013835
Alternative sequencei545 – 1495951Missing in isoform 3. 1 PublicationVSP_013836Add
BLAST
Alternative sequencei597 – 61519DPYSV…SQPVF → GISKCLSYSPPLFFLKVPV in isoform 2. 1 PublicationVSP_013837Add
BLAST
Alternative sequencei616 – 1495880Missing in isoform 2. 1 PublicationVSP_013838Add
BLAST
Alternative sequencei960 – 1072113Missing in isoform 4. 1 PublicationVSP_013839Add
BLAST
Alternative sequencei1157 – 119438Missing in isoform 6. 1 PublicationVSP_013840Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL832026 mRNA. Translation: CAH56219.1.
AL832193 mRNA. Translation: CAH56214.1.
BX641077 mRNA. Translation: CAE46038.1.
CR933643 mRNA. Translation: CAI45944.1.
CR933644 mRNA. Translation: CAI45945.1.
CR936608 mRNA. Translation: CAI56753.1.
AL353678, AL137849 Genomic DNA. Translation: CAH71514.1. Sequence problems.
AL353678, AL137849 Genomic DNA. Translation: CAH71515.1. Sequence problems.
AL353678, AL137849 Genomic DNA. Translation: CAH71518.1.
AL353678, AL137849 Genomic DNA. Translation: CAH71519.1.
AL137849, AL353678 Genomic DNA. Translation: CAI14918.1. Sequence problems.
AL137849, AL353678 Genomic DNA. Translation: CAI14919.1.
AL137849, AL353678 Genomic DNA. Translation: CAI14920.1.
AL137849, AL353678 Genomic DNA. Translation: CAI14921.1.
BC032456 mRNA. Translation: AAH32456.1.
AK023471 mRNA. Translation: BAB14584.1. Different initiation.
AK055546 mRNA. Translation: BAB70951.1.
AK055948 mRNA. Translation: BAB71052.1. Different initiation.
AB051498 mRNA. Translation: BAB21802.1.
CCDSiCCDS35057.1. [Q5VYS8-1]
CCDS55323.1. [Q5VYS8-4]
RefSeqiNP_001171988.1. NM_001185059.1. [Q5VYS8-1]
NP_001172003.1. NM_001185074.1. [Q5VYS8-4]
NP_078893.2. NM_024617.3. [Q5VYS8-1]
UniGeneiHs.597057.

Genome annotation databases

EnsembliENST00000375960; ENSP00000365127; ENSG00000083223. [Q5VYS8-4]
ENST00000375963; ENSP00000365130; ENSG00000083223. [Q5VYS8-1]
GeneIDi79670.
KEGGihsa:79670.
UCSCiuc004aoq.4. human. [Q5VYS8-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL832026 mRNA. Translation: CAH56219.1.
AL832193 mRNA. Translation: CAH56214.1.
BX641077 mRNA. Translation: CAE46038.1.
CR933643 mRNA. Translation: CAI45944.1.
CR933644 mRNA. Translation: CAI45945.1.
CR936608 mRNA. Translation: CAI56753.1.
AL353678, AL137849 Genomic DNA. Translation: CAH71514.1. Sequence problems.
AL353678, AL137849 Genomic DNA. Translation: CAH71515.1. Sequence problems.
AL353678, AL137849 Genomic DNA. Translation: CAH71518.1.
AL353678, AL137849 Genomic DNA. Translation: CAH71519.1.
AL137849, AL353678 Genomic DNA. Translation: CAI14918.1. Sequence problems.
AL137849, AL353678 Genomic DNA. Translation: CAI14919.1.
AL137849, AL353678 Genomic DNA. Translation: CAI14920.1.
AL137849, AL353678 Genomic DNA. Translation: CAI14921.1.
BC032456 mRNA. Translation: AAH32456.1.
AK023471 mRNA. Translation: BAB14584.1. Different initiation.
AK055546 mRNA. Translation: BAB70951.1.
AK055948 mRNA. Translation: BAB71052.1. Different initiation.
AB051498 mRNA. Translation: BAB21802.1.
CCDSiCCDS35057.1. [Q5VYS8-1]
CCDS55323.1. [Q5VYS8-4]
RefSeqiNP_001171988.1. NM_001185059.1. [Q5VYS8-1]
NP_001172003.1. NM_001185074.1. [Q5VYS8-4]
NP_078893.2. NM_024617.3. [Q5VYS8-1]
UniGeneiHs.597057.

3D structure databases

ProteinModelPortaliQ5VYS8.
SMRiQ5VYS8. Positions 299-515, 1010-1308.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi122795. 25 interactions.
IntActiQ5VYS8. 18 interactions.
MINTiMINT-4718069.
STRINGi9606.ENSP00000365130.

PTM databases

iPTMnetiQ5VYS8.
PhosphoSiteiQ5VYS8.

Polymorphism and mutation databases

BioMutaiZCCHC6.
DMDMi67462100.

Proteomic databases

EPDiQ5VYS8.
MaxQBiQ5VYS8.
PaxDbiQ5VYS8.
PRIDEiQ5VYS8.

Protocols and materials databases

DNASUi79670.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000375960; ENSP00000365127; ENSG00000083223. [Q5VYS8-4]
ENST00000375963; ENSP00000365130; ENSG00000083223. [Q5VYS8-1]
GeneIDi79670.
KEGGihsa:79670.
UCSCiuc004aoq.4. human. [Q5VYS8-1]

Organism-specific databases

CTDi79670.
GeneCardsiZCCHC6.
H-InvDBHIX0008144.
HGNCiHGNC:25817. ZCCHC6.
HPAiHPA020615.
HPA020620.
MIMi613467. gene.
neXtProtiNX_Q5VYS8.
PharmGKBiPA134971144.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG2277. Eukaryota.
COG5260. LUCA.
GeneTreeiENSGT00550000074490.
InParanoidiQ5VYS8.
KOiK13291.
OMAiKYFALPH.
OrthoDBiEOG7VB2DH.
PhylomeDBiQ5VYS8.
TreeFamiTF315661.

Enzyme and pathway databases

BRENDAi2.7.7.52. 2681.

Miscellaneous databases

ChiTaRSiZCCHC6. human.
GeneWikiiZCCHC6.
GenomeRNAii79670.
NextBioi68893.
PROiQ5VYS8.
SOURCEiSearch...

Gene expression databases

BgeeiQ5VYS8.
CleanExiHS_ZCCHC6.
ExpressionAtlasiQ5VYS8. baseline and differential.
GenevisibleiQ5VYS8. HS.

Family and domain databases

Gene3Di4.10.60.10. 3 hits.
InterProiIPR002058. PAP_assoc.
IPR002934. Polymerase_NTP_transf_dom.
IPR001878. Znf_CCHC.
IPR003604. Znf_U1.
[Graphical view]
PfamiPF01909. NTP_transf_2. 1 hit.
PF03828. PAP_assoc. 2 hits.
PF00098. zf-CCHC. 3 hits.
[Graphical view]
SMARTiSM00343. ZnF_C2HC. 3 hits.
SM00451. ZnF_U1. 1 hit.
[Graphical view]
SUPFAMiSSF57756. SSF57756. 3 hits.
PROSITEiPS50158. ZF_CCHC. 3 hits.
PS00028. ZINC_FINGER_C2H2_1. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 2; 3 AND 4).
    Tissue: Cervix, Endometrial tumor, Fetal kidney and Skeletal muscle.
  2. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. "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] (ISOFORM 5).
    Tissue: Brain.
  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] OF 1-1385 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1019-1495 (ISOFORM 6).
    Tissue: Placenta.
  5. "Prediction of the coding sequences of unidentified human genes. XIX. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.
    DNA Res. 7:347-355(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 406-1495 (ISOFORM 1).
    Tissue: Brain.
  6. "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.
  7. "Efficient RNA polyuridylation by noncanonical poly(A) polymerases."
    Rissland O.S., Mikulasova A., Norbury C.J.
    Mol. Cell. Biol. 27:3612-3624(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: CATALYTIC ACTIVITY.
  8. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-57; THR-64; SER-172 AND SER-844, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "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].
  10. "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.
  11. "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 SER-939, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-939, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "Lin28-mediated control of let-7 microRNA expression by alternative TUTases Zcchc11 (TUT4) and Zcchc6 (TUT7)."
    Thornton J.E., Chang H.M., Piskounova E., Gregory R.I.
    RNA 18:1875-1885(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION IN PRE-LET-7 URIDYLATION.
  15. "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.
  16. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTUT7_HUMAN
AccessioniPrimary (citable) accession number: Q5VYS8
Secondary accession number(s): Q5H9T0
, Q5VYS5, Q5VYS7, Q658Z9, Q659A2, Q6MZJ3, Q8N5F0, Q96N57, Q96NE8, Q9C0F2, Q9H8M6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 7, 2005
Last sequence update: December 7, 2004
Last modified: May 11, 2016
This is version 108 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

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 9
    Human chromosome 9: 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

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 one 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.