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Protein

Translin

Gene

TSN

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

Functioni

DNA-binding protein that specifically recognizes consensus sequences at the breakpoint junctions in chromosomal translocations, mostly involving immunoglobulin (Ig)/T-cell receptor gene segments. Seems to recognize single-stranded DNA ends generated by staggered breaks occurring at recombination hot spots.
Exhibits both single-stranded and double-stranded endoribonuclease activity. May act as an activator of RNA-induced silencing complex (RISC) by facilitating endonucleolytic cleavage of the siRNA passenger strand.

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • endonuclease activity Source: UniProtKB-KW
  • mRNA binding Source: Ensembl
  • sequence-specific DNA binding Source: InterPro

GO - Biological processi

  • DNA recombination Source: ProtInc
  • gene silencing by RNA Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Endonuclease, Hydrolase, Nuclease

Keywords - Ligandi

DNA-binding, RNA-binding

Enzyme and pathway databases

ReactomeiR-HSA-426486. Small interfering RNA (siRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Translin (EC:3.1.-.-)
Alternative name(s):
Component 3 of promoter of RISC
Short name:
C3PO
Gene namesi
Name:TSN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 2

Organism-specific databases

HGNCiHGNC:12379. TSN.

Subcellular locationi

  • Cytoplasm 1 Publication
  • Nucleus 1 Publication

GO - Cellular componenti

  • cytosol Source: Reactome
  • nucleus Source: ProtInc
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37047.

Polymorphism and mutation databases

BioMutaiTSN.
DMDMi6136060.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 228228TranslinPRO_0000191683Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei187 – 1871N6-acetyllysineCombined sources
Modified residuei199 – 1991N6-acetyllysineCombined sources

Keywords - PTMi

Acetylation

Proteomic databases

EPDiQ15631.
MaxQBiQ15631.
PaxDbiQ15631.
PeptideAtlasiQ15631.
PRIDEiQ15631.
TopDownProteomicsiQ15631-1. [Q15631-1]

PTM databases

iPTMnetiQ15631.
PhosphoSiteiQ15631.

Expressioni

Gene expression databases

BgeeiQ15631.
CleanExiHS_TSN.
ExpressionAtlasiQ15631. baseline and differential.
GenevisibleiQ15631. HS.

Organism-specific databases

HPAiHPA059561.

Interactioni

Subunit structurei

Ring-shaped heterooctamer of six TSN and two TSNAX subunits, DNA/RNA binding occurs inside the ring.1 Publication

Binary interactionsi

WithEntry#Exp.IntActNotes
GIT2Q141612EBI-1044160,EBI-1046878

Protein-protein interaction databases

BioGridi113098. 31 interactions.
DIPiDIP-42216N.
IntActiQ15631. 3 interactions.
MINTiMINT-5002843.
STRINGi9606.ENSP00000374332.

Structurei

Secondary structure

1
228
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi3 – 4240Combined sources
Helixi43 – 464Combined sources
Beta strandi47 – 515Combined sources
Helixi54 – 7724Combined sources
Helixi81 – 833Combined sources
Helixi84 – 874Combined sources
Helixi88 – 903Combined sources
Helixi92 – 11019Combined sources
Helixi116 – 1238Combined sources
Beta strandi128 – 1336Combined sources
Helixi137 – 16024Combined sources
Helixi166 – 18116Combined sources
Helixi189 – 1957Combined sources
Helixi198 – 21316Combined sources
Turni214 – 2163Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J1JX-ray2.20A/B/C/D1-228[»]
3PJAX-ray3.00A/B/C/D/E/F/G/H/I1-228[»]
3QB5X-ray2.95A/B/C1-228[»]
4WYVX-ray3.00A/B/C/D/E/F/G/H1-228[»]
ProteinModelPortaliQ15631.
SMRiQ15631. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ15631.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni86 – 905DNA/RNA binding
Regioni177 – 19822Leucine-zipperSequence analysisAdd
BLAST

Sequence similaritiesi

Belongs to the translin family.Curated

Phylogenomic databases

eggNOGiKOG3067. Eukaryota.
ENOG410XR87. LUCA.
GeneTreeiENSGT00390000014517.
HOGENOMiHOG000198374.
HOVERGENiHBG000373.
InParanoidiQ15631.
OMAiCGLARKQ.
PhylomeDBiQ15631.
TreeFamiTF323690.

Family and domain databases

Gene3Di1.20.58.190. 1 hit.
1.20.58.200. 1 hit.
InterProiIPR002848. Translin.
IPR016069. Translin_C.
IPR016068. Translin_N.
[Graphical view]
PANTHERiPTHR10741. PTHR10741. 1 hit.
PfamiPF01997. Translin. 1 hit.
[Graphical view]
SUPFAMiSSF74784. SSF74784. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q15631-1) [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
MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG
60 70 80 90 100
FQDIPKRCLK AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF
110 120 130 140 150
LAAFVVYLET ETLVTREAVT EILGIEPDRE KGFHLDVEDY LSGVLILASE
160 170 180 190 200
LSRLSVNSVT AGDYSRPLHI STFINELDSG FRLLNLKNDS LRKRYDGLKY
210 220
DVKKVEEVVY DLSIRGFNKE TAAACVEK
Length:228
Mass (Da):26,183
Last modified:November 1, 1996 - v1
Checksum:i3CAAF20BED7C4939
GO
Isoform 2 (identifier: Q15631-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     127-148: PDREKGFHLDVEDYLSGVLILA → AVCQQRDCWRLLPTPPHLHLHQ
     149-228: Missing.

Note: No experimental confirmation available.
Show »
Length:148
Mass (Da):17,279
Checksum:i475F177A67256825
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei127 – 14822PDREK…VLILA → AVCQQRDCWRLLPTPPHLHL HQ in isoform 2. 1 PublicationVSP_044937Add
BLAST
Alternative sequencei149 – 22880Missing in isoform 2. 1 PublicationVSP_044938Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78627 mRNA. Translation: CAA55341.1.
BT019490 mRNA. Translation: AAV38297.1.
BT019491 mRNA. Translation: AAV38298.1.
AK296469 mRNA. Translation: BAH12364.1.
AC018737 Genomic DNA. Translation: AAY14831.1.
BC002359 mRNA. Translation: AAH02359.1.
Y12563
, Y12564, Y12565, Y12566, Y12567 Genomic DNA. Translation: CAA73150.1.
CCDSiCCDS33284.1. [Q15631-1]
CCDS58723.1. [Q15631-2]
PIRiS51738.
RefSeqiNP_001248330.1. NM_001261401.1. [Q15631-2]
NP_004613.1. NM_004622.2. [Q15631-1]
UniGeneiHs.75066.

Genome annotation databases

EnsembliENST00000389682; ENSP00000374332; ENSG00000211460. [Q15631-1]
ENST00000536142; ENSP00000437728; ENSG00000211460. [Q15631-2]
GeneIDi7247.
KEGGihsa:7247.
UCSCiuc002tnl.4. human. [Q15631-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X78627 mRNA. Translation: CAA55341.1.
BT019490 mRNA. Translation: AAV38297.1.
BT019491 mRNA. Translation: AAV38298.1.
AK296469 mRNA. Translation: BAH12364.1.
AC018737 Genomic DNA. Translation: AAY14831.1.
BC002359 mRNA. Translation: AAH02359.1.
Y12563
, Y12564, Y12565, Y12566, Y12567 Genomic DNA. Translation: CAA73150.1.
CCDSiCCDS33284.1. [Q15631-1]
CCDS58723.1. [Q15631-2]
PIRiS51738.
RefSeqiNP_001248330.1. NM_001261401.1. [Q15631-2]
NP_004613.1. NM_004622.2. [Q15631-1]
UniGeneiHs.75066.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1J1JX-ray2.20A/B/C/D1-228[»]
3PJAX-ray3.00A/B/C/D/E/F/G/H/I1-228[»]
3QB5X-ray2.95A/B/C1-228[»]
4WYVX-ray3.00A/B/C/D/E/F/G/H1-228[»]
ProteinModelPortaliQ15631.
SMRiQ15631. Positions 1-217.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113098. 31 interactions.
DIPiDIP-42216N.
IntActiQ15631. 3 interactions.
MINTiMINT-5002843.
STRINGi9606.ENSP00000374332.

PTM databases

iPTMnetiQ15631.
PhosphoSiteiQ15631.

Polymorphism and mutation databases

BioMutaiTSN.
DMDMi6136060.

Proteomic databases

EPDiQ15631.
MaxQBiQ15631.
PaxDbiQ15631.
PeptideAtlasiQ15631.
PRIDEiQ15631.
TopDownProteomicsiQ15631-1. [Q15631-1]

Protocols and materials databases

DNASUi7247.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000389682; ENSP00000374332; ENSG00000211460. [Q15631-1]
ENST00000536142; ENSP00000437728; ENSG00000211460. [Q15631-2]
GeneIDi7247.
KEGGihsa:7247.
UCSCiuc002tnl.4. human. [Q15631-1]

Organism-specific databases

CTDi7247.
GeneCardsiTSN.
HGNCiHGNC:12379. TSN.
HPAiHPA059561.
MIMi600575. gene.
neXtProtiNX_Q15631.
PharmGKBiPA37047.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3067. Eukaryota.
ENOG410XR87. LUCA.
GeneTreeiENSGT00390000014517.
HOGENOMiHOG000198374.
HOVERGENiHBG000373.
InParanoidiQ15631.
OMAiCGLARKQ.
PhylomeDBiQ15631.
TreeFamiTF323690.

Enzyme and pathway databases

ReactomeiR-HSA-426486. Small interfering RNA (siRNA) biogenesis.

Miscellaneous databases

ChiTaRSiTSN. human.
EvolutionaryTraceiQ15631.
GeneWikiiTSN_(gene).
GenomeRNAii7247.
PROiQ15631.
SOURCEiSearch...

Gene expression databases

BgeeiQ15631.
CleanExiHS_TSN.
ExpressionAtlasiQ15631. baseline and differential.
GenevisibleiQ15631. HS.

Family and domain databases

Gene3Di1.20.58.190. 1 hit.
1.20.58.200. 1 hit.
InterProiIPR002848. Translin.
IPR016069. Translin_C.
IPR016068. Translin_N.
[Graphical view]
PANTHERiPTHR10741. PTHR10741. 1 hit.
PfamiPF01997. Translin. 1 hit.
[Graphical view]
SUPFAMiSSF74784. SSF74784. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "A novel gene, Translin, encodes a recombination hotspot binding protein associated with chromosomal translocations."
    Aoki K., Suzuki K., Sugano T., Tasaka T., Nakahara K., Kuge O., Omori A., Kasai M.
    Nat. Genet. 10:167-174(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
  2. "Cloning of human full-length CDSs in BD Creator(TM) system donor vector."
    Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A.
    Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  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 2).
    Tissue: Thalamus.
  4. "Generation and annotation of the DNA sequences of human chromosomes 2 and 4."
    Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., Du H.
    , Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., Wilson R.K.
    Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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 1).
    Tissue: Lung.
  6. "Genomic structure and chromosomal localization of the gene encoding translin, a recombination hotspot binding protein."
    Aoki K., Inazawa J., Takahashi T., Nakahara K., Kasai M.
    Genomics 43:237-241(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 23-215.
  7. "The translin ring specifically recognizes DNA ends at recombination hot spots in the human genome."
    Kasai M., Matsuzaki T., Katayanagi K., Omori A., Maziarz R.T., Strominger J.L., Aoki K., Suzuki K.
    J. Biol. Chem. 272:11402-11407(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  8. "The DNA binding activity of Translin is mediated by a basic region in the ring-shaped structure conserved in evolution."
    Aoki K., Suzuki K., Ishida R., Kasai M.
    FEBS Lett. 443:363-366(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA/RNA-BINDING REGION.
  9. "DNA damage-dependent interaction of the nuclear matrix protein C1D with Translin-associated factor X (TRAX)."
    Erdemir T., Bilican B., Oncel D., Goding C.R., Yavuzer U.
    J. Cell Sci. 115:207-216(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION, INTERACTION WITH TSNAX.
  10. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-187 AND LYS-199, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Structure of C3PO and mechanism of human RISC activation."
    Ye X., Huang N., Liu Y., Paroo Z., Huerta C., Li P., Chen S., Liu Q., Zhang H.
    Nat. Struct. Mol. Biol. 18:650-657(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.95 ANGSTROMS) IN COMPLEX WITH TSNAX, FUNCTION IN RISC ACTIVATION, SUBUNIT.

Entry informationi

Entry nameiTSN_HUMAN
AccessioniPrimary (citable) accession number: Q15631
Secondary accession number(s): B7Z3X8, Q5U0K7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: November 1, 1996
Last modified: June 8, 2016
This is version 143 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

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 2
    Human chromosome 2: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. 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.