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Protein

Trinucleotide repeat-containing gene 6B protein

Gene

TNRC6B

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

Functioni

Plays a role in RNA-mediated gene silencing by both micro-RNAs (miRNAs) and short interfering RNAs (siRNAs). Required for miRNA-dependent translational repression and siRNA-dependent endonucleolytic cleavage of complementary mRNAs by argonaute family proteins. As scaffoldng protein associates with argonaute proteins bound to partially complementary mRNAs and simultaneously can recruit CCR4-NOT and PAN deadenylase complexes.4 Publications

GO - Molecular functioni

  • nucleotide binding Source: InterPro
  • poly(A) RNA binding Source: UniProtKB

GO - Biological processi

  • gene silencing by RNA Source: UniProtKB
  • phosphatidylinositol-mediated signaling Source: Reactome
  • positive regulation of nuclear-transcribed mRNA catabolic process, deadenylation-dependent decay Source: UniProtKB
  • positive regulation of nuclear-transcribed mRNA poly(A) tail shortening Source: UniProtKB
  • posttranscriptional gene silencing by RNA Source: Reactome
  • regulation of translation Source: UniProtKB-KW
  • Wnt signaling pathway, calcium modulating pathway Source: Reactome
Complete GO annotation...

Keywords - Biological processi

RNA-mediated gene silencing, Translation regulation

Keywords - Ligandi

RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-4086398. Ca2+ pathway.
R-HSA-426496. Post-transcriptional silencing by small RNAs.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5687128. MAPK6/MAPK4 signaling.

Names & Taxonomyi

Protein namesi
Recommended name:
Trinucleotide repeat-containing gene 6B protein
Gene namesi
Name:TNRC6B
Synonyms:KIAA1093
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 22

Organism-specific databases

HGNCiHGNC:29190. TNRC6B.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134992981.

Polymorphism and mutation databases

BioMutaiTNRC6B.
DMDMi229904901.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 18331833Trinucleotide repeat-containing gene 6B proteinPRO_0000072605Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei879 – 8791PhosphoserineCombined sources
Modified residuei1432 – 14321PhosphoserineBy similarity
Modified residuei1449 – 14491PhosphothreonineBy similarity
Modified residuei1461 – 14611PhosphoserineBy similarity
Modified residuei1464 – 14641PhosphothreonineBy similarity
Modified residuei1816 – 18161PhosphoserineCombined sources
Modified residuei1832 – 18321PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ9UPQ9.
MaxQBiQ9UPQ9.
PaxDbiQ9UPQ9.
PRIDEiQ9UPQ9.

PTM databases

iPTMnetiQ9UPQ9.
PhosphoSiteiQ9UPQ9.

Expressioni

Gene expression databases

BgeeiQ9UPQ9.
CleanExiHS_TNRC6B.
ExpressionAtlasiQ9UPQ9. baseline and differential.
GenevisibleiQ9UPQ9. HS.

Organism-specific databases

HPAiHPA003180.

Interactioni

Subunit structurei

Interacts with AGO1, AGO2, AGO3 and AGO4. Interacts with CNOT1; the interaction mediates the association with the CCR4-NOT complex. Interacts with PAN3; the interaction mediates the association with the PAN complex.7 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AGO2Q9UKV812EBI-947158,EBI-528269
CNOT1A5YKK64EBI-947158,EBI-1222758
pAbpP211876EBI-947158,EBI-103658From a different organism.
PABPC1P119403EBI-947158,EBI-81531
PAN3Q58A454EBI-947158,EBI-2513054

Protein-protein interaction databases

BioGridi116735. 72 interactions.
DIPiDIP-29624N.
DIP-44174N.
IntActiQ9UPQ9. 60 interactions.
MINTiMINT-2822586.
STRINGi9606.ENSP00000401946.

Structurei

3D structure databases

ProteinModelPortaliQ9UPQ9.
SMRiQ9UPQ9. Positions 1647-1727.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1648 – 172073RRMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 994994Interaction with argonaute proteinsAdd
BLAST
Regioni1218 – 1723506Silencing domain; interaction with CNOT1 and PAN3Add
BLAST
Regioni1472 – 149019PABPC1-interacting motif-2 (PAM2)Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1 – 3939Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi825 – 88056Pro-richAdd
BLAST
Compositional biasi1150 – 122071Gln-richAdd
BLAST

Sequence similaritiesi

Belongs to the GW182 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IET2. Eukaryota.
ENOG410YDKH. LUCA.
GeneTreeiENSGT00410000025966.
HOGENOMiHOG000049171.
HOVERGENiHBG062594.
InParanoidiQ9UPQ9.
KOiK18412.
OMAiMPRPEGK.
OrthoDBiEOG7353VZ.
PhylomeDBiQ9UPQ9.
TreeFamiTF329702.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR019486. Argonaute_hook_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR032226. TNRC6_PABC-bd.
[Graphical view]
PfamiPF10427. Ago_hook. 1 hit.
PF16608. TNRC6-PABC_bdg. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UPQ9-3) [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
MREKEQEREE QLMEDKKRKK EDKKKKEATQ KVTEQKTKVP EVTKPSLSQP
60 70 80 90 100
TAASPIGSSP SPPVNGGNNA KRVAVPNGQP PSAARYMPRE VPPRFRCQQD
110 120 130 140 150
HKVLLKRGQP PPPSCMLLGG GAGPPPCTAP GANPNNAQVT GALLQSESGT
160 170 180 190 200
APDSTLGGAA ASNYANSTWG SGASSNNGTS PNPIHIWDKV IVDGSDMEEW
210 220 230 240 250
PCIASKDTES SSENTTDNNS ASNPGSEKST LPGSTTSNKG KGSQCQSASS
260 270 280 290 300
GNECNLGVWK SDPKAKSVQS SNSTTENNNG LGNWRNVSGQ DRIGPGSGFS
310 320 330 340 350
NFNPNSNPSA WPALVQEGTS RKGALETDNS NSSAQVSTVG QTSREQQSKM
360 370 380 390 400
ENAGVNFVVS GREQAQIHNT DGPKNGNTNS LNLSSPNPME NKGMPFGMGL
410 420 430 440 450
GNTSRSTDAP SQSTGDRKTG SVGSWGAARG PSGTDTVSGQ SNSGNNGNNG
460 470 480 490 500
KEREDSWKGA SVQKSTGSKN DSWDNNNRST GGSWNFGPQD SNDNKWGEGN
510 520 530 540 550
KMTSGVSQGE WKQPTGSDEL KIGEWSGPNQ PNSSTGAWDN QKGHPLPENQ
560 570 580 590 600
GNAQAPCWGR SSSSTGSEVG GQSTGSNHKA GSSDSHNSGR RSYRPTHPDC
610 620 630 640 650
QAVLQTLLSR TDLDPRVLSN TGWGQTQIKQ DTVWDIEEVP RPEGKSDKGT
660 670 680 690 700
EGWESAATQT KNSGGWGDAP SQSNQMKSGW GELSASTEWK DPKNTGGWND
710 720 730 740 750
YKNNNSSNWG GGRPDEKTPS SWNENPSKDQ GWGGGRQPNQ GWSSGKNGWG
760 770 780 790 800
EEVDQTKNSN WESSASKPVS GWGEGGQNEI GTWGNGGNAS LASKGGWEDC
810 820 830 840 850
KRSPAWNETG RQPNSWNKQH QQQQPPQQPP PPQPEASGSW GGPPPPPPGN
860 870 880 890 900
VRPSNSSWSS GPQPATPKDE EPSGWEEPSP QSISRKMDID DGTSAWGDPN
910 920 930 940 950
SYNYKNVNLW DKNSQGGPAP REPNLPTPMT SKSASVWSKS TPPAPDNGTS
960 970 980 990 1000
AWGEPNESSP GWGEMDDTGA STTGWGNTPA NAPNAMKPNS KSMQDGWGES
1010 1020 1030 1040 1050
DGPVTGARHP SWEEEEDGGV WNTTGSQGSA SSHNSASWGQ GGKKQMKCSL
1060 1070 1080 1090 1100
KGGNNDSWMN PLAKQFSNMG LLSQTEDNPS SKMDLSVGSL SDKKFDVDKR
1110 1120 1130 1140 1150
AMNLGDFNDI MRKDRSGFRP PNSKDMGTTD SGPYFEKLTL PFSNQDGCLG
1160 1170 1180 1190 1200
DEAPCSPFSP SPSYKLSPSG STLPNVSLGA IGTGLNPQNF AARQGGSHGL
1210 1220 1230 1240 1250
FGNSTAQSRG LHTPVQPLNS SPSLRAQVPP QFISPQVSAS MLKQFPNSGL
1260 1270 1280 1290 1300
SPGLFNVGPQ LSPQQIAMLS QLPQIPQFQL ACQLLLQQQQ QQQLLQNQRK
1310 1320 1330 1340 1350
ISQAVRQQQE QQLARMVSAL QQQQQQQQRQ PGMKHSPSHP VGPKPHLDNM
1360 1370 1380 1390 1400
VPNALNVGLP DLQTKGPIPG YGSGFSSGGM DYGMVGGKEA GTESRFKQWT
1410 1420 1430 1440 1450
SMMEGLPSVA TQEANMHKNG AIVAPGKTRG GSPYNQFDII PGDTLGGHTG
1460 1470 1480 1490 1500
PAGDSWLPAK SPPTNKIGSK SSNASWPPEF QPGVPWKGIQ NIDPESDPYV
1510 1520 1530 1540 1550
TPGSVLGGTA TSPIVDTDHQ LLRDNTTGSN SSLNTSLPSP GAWPYSASDN
1560 1570 1580 1590 1600
SFTNVHSTSA KFPDYKSTWS PDPIGHNPTH LSNKMWKNHI SSRNTTPLPR
1610 1620 1630 1640 1650
PPPGLTNPKP SSPWSSTAPR SVRGWGTQDS RLASASTWSD GGSVRPSYWL
1660 1670 1680 1690 1700
VLHNLTPQID GSTLRTICMQ HGPLLTFHLN LTQGTALIRY STKQEAAKAQ
1710 1720 1730 1740 1750
TALHMCVLGN TTILAEFATD DEVSRFLAQA QPPTPAATPS APAAGWQSLE
1760 1770 1780 1790 1800
TGQNQSDPVG PALNLFGGST GLGQWSSSAG GSSGADLAGA SLWGPPNYSS
1810 1820 1830
SLWGVPTVED PHRMGSPAPL LPGDLLGGGS DSI
Length:1,833
Mass (Da):194,002
Last modified:May 5, 2009 - v4
Checksum:iE982B786C97C75D0
GO
Isoform 2 (identifier: Q9UPQ9-1) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     936-989: VWSKSTPPAPDNGTSAWGEPNESSPGWGEMDDTGASTTGWGNTPANAPNAMKPN → D
     1138-1194: Missing.

Show »
Length:1,723
Mass (Da):182,815
Checksum:i80AFD934D6D02FC6
GO
Isoform 3 (identifier: Q9UPQ9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: MR → MQTNEGEVSEESSSKVEQEDFVMEGHGKTPPPGEESKQ
     153-935: Missing.
     1138-1194: Missing.

Show »
Length:1,029
Mass (Da):109,345
Checksum:i4CF58AF70B8973B3
GO

Sequence cautioni

The sequence BAA83045.2 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti1321 – 13211Missing in BAA83045 (PubMed:10470851).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti517 – 5171S → C.
Corresponds to variant rs17001767 [ dbSNP | Ensembl ].
VAR_051452

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22MR → MQTNEGEVSEESSSKVEQED FVMEGHGKTPPPGEESKQ in isoform 3. 1 PublicationVSP_037290
Alternative sequencei153 – 935783Missing in isoform 3. 1 PublicationVSP_037291Add
BLAST
Alternative sequencei936 – 98954VWSKS…AMKPN → D in isoform 2. 1 PublicationVSP_037292Add
BLAST
Alternative sequencei1138 – 119457Missing in isoform 2 and isoform 3. 2 PublicationsVSP_037293Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029016 mRNA. Translation: BAA83045.2. Different initiation.
AK294519 mRNA. Translation: BAG57731.1.
Z93783, AL022238, AL031589 Genomic DNA. Translation: CAQ07207.1.
Z93783, AL022238, AL031589 Genomic DNA. Translation: CAQ07209.1.
AL031589, AL022238, Z93783 Genomic DNA. Translation: CAQ08008.1.
AL031589, AL022238, Z93783 Genomic DNA. Translation: CAQ08010.1.
AL022238, AL031589, Z93783 Genomic DNA. Translation: CAQ08927.1.
AL022238, AL031589, Z93783 Genomic DNA. Translation: CAQ08932.1.
CH471095 Genomic DNA. Translation: EAW60367.1.
BC028626 mRNA. Translation: AAH28626.1.
CCDSiCCDS46712.1. [Q9UPQ9-2]
CCDS46713.1. [Q9UPQ9-1]
CCDS54533.1. [Q9UPQ9-3]
RefSeqiNP_001020014.1. NM_001024843.1. [Q9UPQ9-2]
NP_001155973.1. NM_001162501.1. [Q9UPQ9-3]
NP_055903.2. NM_015088.2. [Q9UPQ9-1]
UniGeneiHs.372082.

Genome annotation databases

EnsembliENST00000301923; ENSP00000306759; ENSG00000100354. [Q9UPQ9-2]
ENST00000335727; ENSP00000338371; ENSG00000100354. [Q9UPQ9-1]
ENST00000402203; ENSP00000384795; ENSG00000100354. [Q9UPQ9-2]
ENST00000454349; ENSP00000401946; ENSG00000100354. [Q9UPQ9-3]
GeneIDi23112.
KEGGihsa:23112.
UCSCiuc003aym.4. human. [Q9UPQ9-3]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB029016 mRNA. Translation: BAA83045.2. Different initiation.
AK294519 mRNA. Translation: BAG57731.1.
Z93783, AL022238, AL031589 Genomic DNA. Translation: CAQ07207.1.
Z93783, AL022238, AL031589 Genomic DNA. Translation: CAQ07209.1.
AL031589, AL022238, Z93783 Genomic DNA. Translation: CAQ08008.1.
AL031589, AL022238, Z93783 Genomic DNA. Translation: CAQ08010.1.
AL022238, AL031589, Z93783 Genomic DNA. Translation: CAQ08927.1.
AL022238, AL031589, Z93783 Genomic DNA. Translation: CAQ08932.1.
CH471095 Genomic DNA. Translation: EAW60367.1.
BC028626 mRNA. Translation: AAH28626.1.
CCDSiCCDS46712.1. [Q9UPQ9-2]
CCDS46713.1. [Q9UPQ9-1]
CCDS54533.1. [Q9UPQ9-3]
RefSeqiNP_001020014.1. NM_001024843.1. [Q9UPQ9-2]
NP_001155973.1. NM_001162501.1. [Q9UPQ9-3]
NP_055903.2. NM_015088.2. [Q9UPQ9-1]
UniGeneiHs.372082.

3D structure databases

ProteinModelPortaliQ9UPQ9.
SMRiQ9UPQ9. Positions 1647-1727.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116735. 72 interactions.
DIPiDIP-29624N.
DIP-44174N.
IntActiQ9UPQ9. 60 interactions.
MINTiMINT-2822586.
STRINGi9606.ENSP00000401946.

PTM databases

iPTMnetiQ9UPQ9.
PhosphoSiteiQ9UPQ9.

Polymorphism and mutation databases

BioMutaiTNRC6B.
DMDMi229904901.

Proteomic databases

EPDiQ9UPQ9.
MaxQBiQ9UPQ9.
PaxDbiQ9UPQ9.
PRIDEiQ9UPQ9.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000301923; ENSP00000306759; ENSG00000100354. [Q9UPQ9-2]
ENST00000335727; ENSP00000338371; ENSG00000100354. [Q9UPQ9-1]
ENST00000402203; ENSP00000384795; ENSG00000100354. [Q9UPQ9-2]
ENST00000454349; ENSP00000401946; ENSG00000100354. [Q9UPQ9-3]
GeneIDi23112.
KEGGihsa:23112.
UCSCiuc003aym.4. human. [Q9UPQ9-3]

Organism-specific databases

CTDi23112.
GeneCardsiTNRC6B.
HGNCiHGNC:29190. TNRC6B.
HPAiHPA003180.
MIMi610740. gene.
neXtProtiNX_Q9UPQ9.
PharmGKBiPA134992981.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiENOG410IET2. Eukaryota.
ENOG410YDKH. LUCA.
GeneTreeiENSGT00410000025966.
HOGENOMiHOG000049171.
HOVERGENiHBG062594.
InParanoidiQ9UPQ9.
KOiK18412.
OMAiMPRPEGK.
OrthoDBiEOG7353VZ.
PhylomeDBiQ9UPQ9.
TreeFamiTF329702.

Enzyme and pathway databases

ReactomeiR-HSA-1257604. PIP3 activates AKT signaling.
R-HSA-1912408. Pre-NOTCH Transcription and Translation.
R-HSA-2559580. Oxidative Stress Induced Senescence.
R-HSA-2559585. Oncogene Induced Senescence.
R-HSA-4086398. Ca2+ pathway.
R-HSA-426496. Post-transcriptional silencing by small RNAs.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
R-HSA-5687128. MAPK6/MAPK4 signaling.

Miscellaneous databases

ChiTaRSiTNRC6B. human.
GeneWikiiTNRC6B.
GenomeRNAii23112.
PROiQ9UPQ9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UPQ9.
CleanExiHS_TNRC6B.
ExpressionAtlasiQ9UPQ9. baseline and differential.
GenevisibleiQ9UPQ9. HS.

Family and domain databases

Gene3Di3.30.70.330. 2 hits.
InterProiIPR019486. Argonaute_hook_dom.
IPR012677. Nucleotide-bd_a/b_plait.
IPR032226. TNRC6_PABC-bd.
[Graphical view]
PfamiPF10427. Ago_hook. 1 hit.
PF16608. TNRC6-PABC_bdg. 1 hit.
[Graphical view]
SUPFAMiSSF54928. SSF54928. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Prediction of the coding sequences of unidentified human genes. XIV. The complete sequences of 100 new cDNA clones from brain which code for large proteins in vitro."
    Kikuno R., Nagase T., Ishikawa K., Hirosawa M., Miyajima N., Tanaka A., Kotani H., Nomura N., Ohara O.
    DNA Res. 6:197-205(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Brain.
  2. "Construction of expression-ready cDNA clones for KIAA genes: manual curation of 330 KIAA cDNA clones."
    Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.
    DNA Res. 9:99-106(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SEQUENCE REVISION.
  3. "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 1).
    Tissue: Amygdala.
  4. "The DNA sequence of human chromosome 22."
    Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M.
    , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
    Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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 3).
    Tissue: Testis.
  7. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH AGO1 AND AGO2, SUBCELLULAR LOCATION.
  8. Cited for: IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH AGO1; AGO2; AGO3 AND AGO4.
  9. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1816, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  10. "Importin 8 is a gene silencing factor that targets argonaute proteins to distinct mRNAs."
    Weinmann L., Hoeck J., Ivacevic T., Ohrt T., Muetze J., Schwille P., Kremmer E., Benes V., Urlaub H., Meister G.
    Cell 136:496-507(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY, FUNCTION, INTERACTION WITH AGO3 AND AGO4, SUBCELLULAR LOCATION.
  11. "Importance of the C-terminal domain of the human GW182 protein TNRC6C for translational repression."
    Zipprich J.T., Bhattacharyya S., Mathys H., Filipowicz W.
    RNA 15:781-793(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH AGO2.
  12. "The C-terminal domains of human TNRC6A, TNRC6B, and TNRC6C silence bound transcripts independently of Argonaute proteins."
    Lazzaretti D., Tournier I., Izaurralde E.
    RNA 15:1059-1066(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH AGO1; AGO2; AGO3 AND AGO4.
  13. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1816, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  14. "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-1816 AND SER-1832, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  16. "GW182 proteins directly recruit cytoplasmic deadenylase complexes to miRNA targets."
    Braun J.E., Huntzinger E., Fauser M., Izaurralde E.
    Mol. Cell 44:120-133(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CNOT1 AND PAN3.
  17. "miRNA-mediated deadenylation is orchestrated by GW182 through two conserved motifs that interact with CCR4-NOT."
    Fabian M.R., Cieplak M.K., Frank F., Morita M., Green J., Srikumar T., Nagar B., Yamamoto T., Raught B., Duchaine T.F., Sonenberg N.
    Nat. Struct. Mol. Biol. 18:1211-1217(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CNOT1.
  18. "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-879, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-879, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.

Entry informationi

Entry nameiTNR6B_HUMAN
AccessioniPrimary (citable) accession number: Q9UPQ9
Secondary accession number(s): B0QY73
, B0QY78, B4DGC0, Q5TH52, Q8TBX2
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 7, 2003
Last sequence update: May 5, 2009
Last modified: June 8, 2016
This is version 133 of the entry and version 4 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 22
    Human chromosome 22: 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.