Q15631 (TSN_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Translin
EC=3.1.-.-

Alternative name(s):
Component 3 of promoter of RISC
Short name=C3PO

Gene names

Name:

TSN

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	228 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.7 Ref.12 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. Ref.7 Ref.12
Subunit structure	Ring-shaped heterooctamer of six TSN and two TSNAX subunits, DNA/RNA binding occurs inside the ring. Ref.12
Subcellular location	Cytoplasm. Nucleus Ref.9.
Sequence similarities	Belongs to the translin family.

Ontologies

Keywords
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing
Ligand	DNA-binding RNA-binding
Molecular function	Endonuclease Hydrolase Nuclease
PTM	Acetylation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	DNA recombination Traceable author statement Ref.1. Source: ProtInc nucleic acid phosphodiester bond hydrolysis Inferred from electronic annotation. Source: GOC
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Traceable author statement Ref.1. Source: ProtInc
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc endonuclease activity Inferred from electronic annotation. Source: UniProtKB-KW mRNA binding Inferred from electronic annotation. Source: Compara sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GIT2	Q14161	2	EBI-1044160,EBI-1046878

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: Q15631-1)

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: Q15631-2)

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

Note: No experimental confirmation available.

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 228

228

Translin

PRO_0000191683

Regions

Region

86 – 90

5

DNA/RNA binding

Region

177 – 198

22

Leucine-zipper Potential

Amino acid modifications

Modified residue

187

1

N6-acetyllysine Ref.10

Modified residue

199

1

N6-acetyllysine Ref.10

Natural variations

Alternative sequence

127 – 148

22

PDREK…VLILA → AVCQQRDCWRLLPTPPHLHL HQ in isoform 2.

VSP_044937

Alternative sequence

149 – 228

80

Missing in isoform 2.

VSP_044938

Secondary structure

1

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228

Helix Strand Turn

Details...

Helix

3 – 42

40

Helix

43 – 46

4

Beta strand

47 – 51

5

Helix

54 – 77

24

Helix

81 – 83

3

Helix

84 – 87

4

Helix

88 – 90

3

Helix

92 – 110

19

Helix

116 – 123

8

Beta strand

128 – 133

6

Helix

137 – 160

24

Helix

166 – 181

16

Helix

189 – 195

7

Helix

198 – 213

16

Turn

214 – 216

3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 1, 1996. Version 1. Checksum: 3CAAF20BED7C4939	FASTA	228	26,183
	10 20 30 40 50 60 MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG FQDIPKRCLK 70 80 90 100 110 120 AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLET ETLVTREAVT 130 140 150 160 170 180 EILGIEPDRE KGFHLDVEDY LSGVLILASE LSRLSVNSVT AGDYSRPLHI STFINELDSG 190 200 210 220 FRLLNLKNDS LRKRYDGLKY DVKKVEEVVY DLSIRGFNKE TAAACVEK
	Isoform 2 [UniParc]. Checksum: 475F177A67256825	FASTA	148	17,279
	10 20 30 40 50 60 MSVSEIFVEL QGFLAAEQDI REEIRKVVQS LEQTAREILT LLQGVHQGAG FQDIPKRCLK 70 80 90 100 110 120 AREHFGTVKT HLTSLKTKFP AEQYYRFHEH WRFVLQRLVF LAAFVVYLET ETLVTREAVT 130 140 EILGIEAVCQ QRDCWRLLPT PPHLHLHQ

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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, MASS SPECTROMETRY.
[11]	"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].
[12]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00018768.
IPI00922875.

PIR

S51738.

RefSeq

NP_001248330.1. NM_001261401.1.
NP_004613.1. NM_004622.2.

UniGene

Hs.75066.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1J1J	X-ray	2.20	A/B/C/D	1-228	[»]
3PJA	X-ray	3.00	A/B/C/D/E/F/G/H/I	1-228	[»]
3QB5	X-ray	2.95	A/B/C	1-228	[»]

ProteinModelPortal

Q15631.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-42216N.

IntAct

Q15631. 2 interactions.

MINT

MINT-5002843.

STRING

9606.ENSP00000374332.

PTM databases

PhosphoSite

Q15631.

Polymorphism databases

DMDM

6136060.

Proteomic databases

PaxDb

Q15631.

PeptideAtlas

Q15631.

PRIDE

Q15631.

Protocols and materials databases

DNASU

7247.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000389682; ENSP00000374332; ENSG00000211460.
ENST00000536142; ENSP00000437728; ENSG00000211460.

GeneID

7247.

KEGG

hsa:7247.

UCSC

uc002tnl.3. human.

Organism-specific databases

CTD

7247.

GeneCards

GC02P122419.

HGNC

HGNC:12379. TSN.

MIM

600575. gene.

neXtProt

NX_Q15631.

PharmGKB

PA37047.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG268068.

HOGENOM

HOG000198374.

HOVERGEN

HBG000373.

InParanoid

Q15631.

OMA

VLIMASE.

OrthoDB

EOG4S7JQZ.

PhylomeDB

Q15631.

Gene expression databases

ArrayExpress

Q15631.

Bgee

Q15631.

CleanEx

HS_TSN.

Genevestigator

Q15631.

GermOnline

ENSG00000211460. Homo sapiens.

Family and domain databases

Gene3D

1.20.58.190. 1 hit.
1.20.58.200. 1 hit.

InterPro

IPR002848. Translin.
IPR016069. Translin_C.
IPR016068. Translin_N.
[Graphical view]

PANTHER

PTHR10741. PTHR10741. 1 hit.

Pfam

PF01997. Translin. 1 hit.
[Graphical view]

SUPFAM

SSF74784. Translin. 1 hit.

ProtoNet

Search...

Other

ChiTaRS

TSN. human.

EvolutionaryTrace

Q15631.

GenomeRNAi

7247.

NextBio

28337.

SOURCE

Search...

Entry information

Entry name

TSN_HUMAN

Accession

Primary (citable) accession number: Q15631
Secondary accession number(s): B7Z3X8, Q5U0K7

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	November 1, 1996
Last modified:	May 1, 2013
This is version 113 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.