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Protein

Translin-associated protein X

Gene

TSNAX

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

Functioni

Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis.2 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Metal bindingi129 – 1291Magnesium
Metal bindingi197 – 1971Magnesium

GO - Molecular functioni

  • DNA binding Source: ProtInc
  • endoribonuclease activity Source: GO_Central
  • metal ion binding Source: UniProtKB-KW
  • poly(A) RNA binding Source: UniProtKB
  • protein transporter activity Source: ProtInc
  • sequence-specific DNA binding Source: GO_Central
  • single-stranded DNA binding Source: GO_Central

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Differentiation, Spermatogenesis

Keywords - Ligandi

DNA-binding, Magnesium, Metal-binding

Enzyme and pathway databases

ReactomeiREACT_118560. Small interfering RNA (siRNA) biogenesis.

Names & Taxonomyi

Protein namesi
Recommended name:
Translin-associated protein X
Alternative name(s):
Translin-associated factor X
Gene namesi
Name:TSNAX
Synonyms:TRAX
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:12380. TSNAX.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Golgi apparatus, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA37048.

Polymorphism and mutation databases

BioMutaiTSNAX.
DMDMi6136057.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 290290Translin-associated protein XPRO_0000191686Add
BLAST

Post-translational modificationi

Sumoylated with SUMO1.1 Publication

Keywords - PTMi

Ubl conjugation

Proteomic databases

MaxQBiQ99598.
PaxDbiQ99598.
PeptideAtlasiQ99598.
PRIDEiQ99598.

PTM databases

PhosphoSiteiQ99598.

Expressioni

Gene expression databases

BgeeiQ99598.
CleanExiHS_TSNAX.
ExpressionAtlasiQ99598. baseline and differential.
GenevisibleiQ99598. HS.

Organism-specific databases

HPAiCAB034263.
HPA031054.
HPA031055.

Interactioni

Subunit structurei

Ring-shaped heterooctamer of six TSN and two TSNAX subunits. Interacts with GOLGA3, TSNAXIP1, SUN1 and AKAP9. Interacts with the homodimeric form of C1D following gamma-radiation. Interacts with TSN and C1D in a mutually exclusive manner.5 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
AIMP1Q129043EBI-742638,EBI-1045802
BLOC1S5Q8TDH93EBI-742638,EBI-465861
CARD9Q9H2575EBI-742638,EBI-751319
KLC3Q6P5975EBI-742638,EBI-1643885
LZTS2Q9BRK43EBI-742638,EBI-741037
TCF12Q990813EBI-742638,EBI-722877

Protein-protein interaction databases

BioGridi113108. 40 interactions.
DIPiDIP-29463N.
IntActiQ99598. 25 interactions.
MINTiMINT-1347706.
STRINGi9606.ENSP00000355599.

Structurei

Secondary structure

1
290
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi34 – 7542Combined sources
Helixi83 – 10826Combined sources
Beta strandi109 – 1113Combined sources
Turni114 – 1163Combined sources
Helixi117 – 1193Combined sources
Helixi121 – 13919Combined sources
Helixi145 – 1506Combined sources
Helixi184 – 20724Combined sources
Helixi213 – 23119Combined sources
Helixi232 – 2343Combined sources
Helixi237 – 26327Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PJAX-ray3.00J/K/L1-290[»]
3QB5X-ray2.95K1-290[»]
ProteinModelPortaliQ99598.
SMRiQ99598. Positions 31-272.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni73 – 208136Interaction with C1DAdd
BLAST

Sequence similaritiesi

Belongs to the translin family.Curated

Phylogenomic databases

eggNOGiCOG2178.
GeneTreeiENSGT00390000014716.
HOGENOMiHOG000008075.
HOVERGENiHBG059067.
InParanoidiQ99598.
OMAiCISSVGN.
OrthoDBiEOG7XWPPR.
PhylomeDBiQ99598.
TreeFamiTF323633.

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.

Sequencei

Sequence statusi: Complete.

Q99598-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSNKEGSGGF RKRKHDNFPH NQRREGKDVN SSSPVMLAFK SFQQELDARH
60 70 80 90 100
DKYERLVKLS RDITVESKRT IFLLHRITSA PDMEDILTES EIKLDGVRQK
110 120 130 140 150
IFQVAQELSG EDMHQFHRAI TTGLQEYVEA VSFQHFIKTR SLISMDEINK
160 170 180 190 200
QLIFTTEDNG KENKTPSSDA QDKQFGTWRL RVTPVDYLLG VADLTGELMR
210 220 230 240 250
MCINSVGNGD IDTPFEVSQF LRQVYDGFSF IGNTGPYEVS KKLYTLKQSL
260 270 280 290
AKVENACYAL KVRGSEIPKH MLADVFSVKT EMIDQEEGIS
Length:290
Mass (Da):33,112
Last modified:May 1, 1997 - v1
Checksum:iD38B0DD96B50C0B9
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95073 mRNA. Translation: CAA64469.1.
AF271269, AF271267, AF271268 Genomic DNA. Translation: AAK58640.1.
AK313068 mRNA. Translation: BAG35896.1.
AL626763, AL445524 Genomic DNA. Translation: CAH70959.1.
AL445524, AL626763 Genomic DNA. Translation: CAH72107.1.
CH471098 Genomic DNA. Translation: EAW69963.1.
BC010376 mRNA. Translation: AAH10376.1.
BC011797 mRNA. Translation: AAH11797.1.
CCDSiCCDS1596.1.
RefSeqiNP_005990.1. NM_005999.2.
UniGeneiHs.13318.

Genome annotation databases

EnsembliENST00000366639; ENSP00000355599; ENSG00000116918.
GeneIDi7257.
KEGGihsa:7257.
UCSCiuc001huw.3. human.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X95073 mRNA. Translation: CAA64469.1.
AF271269, AF271267, AF271268 Genomic DNA. Translation: AAK58640.1.
AK313068 mRNA. Translation: BAG35896.1.
AL626763, AL445524 Genomic DNA. Translation: CAH70959.1.
AL445524, AL626763 Genomic DNA. Translation: CAH72107.1.
CH471098 Genomic DNA. Translation: EAW69963.1.
BC010376 mRNA. Translation: AAH10376.1.
BC011797 mRNA. Translation: AAH11797.1.
CCDSiCCDS1596.1.
RefSeqiNP_005990.1. NM_005999.2.
UniGeneiHs.13318.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
3PJAX-ray3.00J/K/L1-290[»]
3QB5X-ray2.95K1-290[»]
ProteinModelPortaliQ99598.
SMRiQ99598. Positions 31-272.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113108. 40 interactions.
DIPiDIP-29463N.
IntActiQ99598. 25 interactions.
MINTiMINT-1347706.
STRINGi9606.ENSP00000355599.

PTM databases

PhosphoSiteiQ99598.

Polymorphism and mutation databases

BioMutaiTSNAX.
DMDMi6136057.

Proteomic databases

MaxQBiQ99598.
PaxDbiQ99598.
PeptideAtlasiQ99598.
PRIDEiQ99598.

Protocols and materials databases

DNASUi7257.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000366639; ENSP00000355599; ENSG00000116918.
GeneIDi7257.
KEGGihsa:7257.
UCSCiuc001huw.3. human.

Organism-specific databases

CTDi7257.
GeneCardsiGC01P231664.
HGNCiHGNC:12380. TSNAX.
HPAiCAB034263.
HPA031054.
HPA031055.
MIMi602964. gene.
neXtProtiNX_Q99598.
PharmGKBiPA37048.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG2178.
GeneTreeiENSGT00390000014716.
HOGENOMiHOG000008075.
HOVERGENiHBG059067.
InParanoidiQ99598.
OMAiCISSVGN.
OrthoDBiEOG7XWPPR.
PhylomeDBiQ99598.
TreeFamiTF323633.

Enzyme and pathway databases

ReactomeiREACT_118560. Small interfering RNA (siRNA) biogenesis.

Miscellaneous databases

ChiTaRSiTSNAX. human.
GeneWikiiTSNAX.
GenomeRNAii7257.
NextBioi28373.
PROiQ99598.
SOURCEiSearch...

Gene expression databases

BgeeiQ99598.
CleanExiHS_TSNAX.
ExpressionAtlasiQ99598. baseline and differential.
GenevisibleiQ99598. 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. "Isolation and characterization of a cDNA encoding a translin-like protein, TRAX."
    Aoki K., Ishida R., Kasai M.
    FEBS Lett. 401:109-112(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], INTERACTION WITH TSN.
    Tissue: Spleen.
  2. "Genomic structure of human translin-associated factor X (TRAX) gene."
    Guyonnet Duperat V., Dupuy D., Stef M., Arveiler B.
    Submitted (MAY-2000) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  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].
    Tissue: Caudate nucleus.
  4. "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.
    , 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].
  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].
    Tissue: Brain and Muscle.
  7. "Identification and characterization of cDNAs encoding four novel proteins that interact with translin associated factor-X."
    Bray J.D., Chennathukuzhi V.M., Hecht N.B.
    Genomics 79:799-808(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH TSN; GOLGA3; TSNAXIP1; SUN1 AND AKAP9.
    Tissue: Testis.
  8. "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 C1D AND TSN.
  9. "Co-expressed recombinant human Translin-Trax complex binds DNA."
    Gupta G.D., Makde R.D., Kamdar R.P., D'Souza J.S., Kulkarni M.G., Kumar V., Rao B.J.
    FEBS Lett. 579:3141-3146(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: DNA-BINDING, SUBUNIT.
  10. "Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates."
    Gocke C.B., Yu H., Kang J.
    J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION.
  11. "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: 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), SUBUNIT, MAGNESIUM-BINDING SITES, FUNCTION.

Entry informationi

Entry nameiTSNAX_HUMAN
AccessioniPrimary (citable) accession number: Q99598
Secondary accession number(s): B1APC6
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: May 1, 1997
Last modified: July 22, 2015
This is version 128 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 1
    Human chromosome 1: 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

External Data

Dasty 3

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 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.