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Q99598

- TSNAX_HUMAN

UniProt

Q99598 - TSNAX_HUMAN

Protein

Translin-associated protein X

Gene

TSNAX

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 120 (01 Oct 2014)
      Sequence version 1 (01 May 1997)
      Previous versions | rss
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    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

    1. DNA binding Source: ProtInc
    2. metal ion binding Source: UniProtKB-KW
    3. poly(A) RNA binding Source: UniProtKB
    4. protein transporter activity Source: ProtInc
    5. sequence-specific DNA binding Source: InterPro

    GO - Biological processi

    1. cell differentiation Source: UniProtKB-KW
    2. multicellular organismal development Source: UniProtKB-KW
    3. protein transport Source: GOC
    4. spermatogenesis Source: UniProtKB-KW

    Keywords - Molecular functioni

    Developmental protein

    Keywords - Biological processi

    Differentiation, Spermatogenesis

    Keywords - Ligandi

    DNA-binding, Magnesium, Metal-binding

    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: Chromosome 1

    Organism-specific databases

    HGNCiHGNC:12380. TSNAX.

    Subcellular locationi

    Cytoplasmperinuclear region. Golgi apparatus By similarity. Nucleus
    Note: Accumulate in the Golgi complex of mid-late pachytene spermatocytes By similarity. Expressed in the cytoplasm in the presence of TSN.By similarity

    GO - Cellular componenti

    1. Golgi apparatus Source: UniProtKB-SubCell
    2. nucleus Source: UniProtKB-SubCell
    3. perinuclear region of cytoplasm Source: UniProtKB-SubCell

    Keywords - Cellular componenti

    Cytoplasm, Golgi apparatus, Nucleus

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA37048.

    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

    ArrayExpressiQ99598.
    BgeeiQ99598.
    CleanExiHS_TSNAX.
    GenevestigatoriQ99598.

    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

    Protein-protein interaction databases

    BioGridi113108. 23 interactions.
    DIPiDIP-29463N.
    IntActiQ99598. 19 interactions.
    MINTiMINT-1347706.
    STRINGi9606.ENSP00000355599.

    Structurei

    Secondary structure

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

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    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.
    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

    MSNKEGSGGF RKRKHDNFPH NQRREGKDVN SSSPVMLAFK SFQQELDARH    50
    DKYERLVKLS RDITVESKRT IFLLHRITSA PDMEDILTES EIKLDGVRQK 100
    IFQVAQELSG EDMHQFHRAI TTGLQEYVEA VSFQHFIKTR SLISMDEINK 150
    QLIFTTEDNG KENKTPSSDA QDKQFGTWRL RVTPVDYLLG VADLTGELMR 200
    MCINSVGNGD IDTPFEVSQF LRQVYDGFSF IGNTGPYEVS KKLYTLKQSL 250
    AKVENACYAL KVRGSEIPKH MLADVFSVKT EMIDQEEGIS 290
    Length:290
    Mass (Da):33,112
    Last modified:May 1, 1997 - v1
    Checksum:iD38B0DD96B50C0B9
    GO

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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.

    Polymorphism databases

    DMDMi6136057.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    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 .
    CCDSi CCDS1596.1.
    RefSeqi NP_005990.1. NM_005999.2.
    UniGenei Hs.13318.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    3PJA X-ray 3.00 J/K/L 1-290 [» ]
    3QB5 X-ray 2.95 K 1-290 [» ]
    ProteinModelPortali Q99598.
    SMRi Q99598. Positions 31-272.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113108. 23 interactions.
    DIPi DIP-29463N.
    IntActi Q99598. 19 interactions.
    MINTi MINT-1347706.
    STRINGi 9606.ENSP00000355599.

    PTM databases

    PhosphoSitei Q99598.

    Polymorphism databases

    DMDMi 6136057.

    Proteomic databases

    MaxQBi Q99598.
    PaxDbi Q99598.
    PeptideAtlasi Q99598.
    PRIDEi Q99598.

    Protocols and materials databases

    DNASUi 7257.
    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000366639 ; ENSP00000355599 ; ENSG00000116918 .
    GeneIDi 7257.
    KEGGi hsa:7257.
    UCSCi uc001huw.3. human.

    Organism-specific databases

    CTDi 7257.
    GeneCardsi GC01P231664.
    HGNCi HGNC:12380. TSNAX.
    HPAi CAB034263.
    HPA031054.
    HPA031055.
    MIMi 602964. gene.
    neXtProti NX_Q99598.
    PharmGKBi PA37048.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG2178.
    HOGENOMi HOG000008075.
    HOVERGENi HBG059067.
    InParanoidi Q99598.
    OMAi CISSVGN.
    OrthoDBi EOG7XWPPR.
    PhylomeDBi Q99598.
    TreeFami TF323633.

    Miscellaneous databases

    ChiTaRSi TSNAX. human.
    GeneWikii TSNAX.
    GenomeRNAii 7257.
    NextBioi 28373.
    PROi Q99598.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q99598.
    Bgeei Q99598.
    CleanExi HS_TSNAX.
    Genevestigatori Q99598.

    Family and domain databases

    Gene3Di 1.20.58.190. 1 hit.
    1.20.58.200. 1 hit.
    InterProi IPR002848. Translin.
    IPR016069. Translin_C.
    IPR016068. Translin_N.
    [Graphical view ]
    PANTHERi PTHR10741. PTHR10741. 1 hit.
    Pfami PF01997. Translin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF74784. SSF74784. 1 hit.
    ProtoNeti Search...

    Publicationsi

    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: October 1, 2014
    This is version 120 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