Q99598 (TSNAX_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Translin-associated protein X

Alternative name(s):
Translin-associated factor X

Gene names

Name:	TSNAX
Synonyms:	TRAX

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	290 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Acts in combination with TSN as an endonuclease involved in the activation of the RNA-induced silencing complex (RISC). Possible role in spermatogenesis. Ref.7 Ref.17
Subunit structure	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. Ref.1 Ref.7 Ref.8 Ref.9 Ref.17
Subcellular location	Cytoplasm › perinuclear 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. Ref.7 Ref.8
Post-translational modification	Sumoylated with SUMO1. Ref.10
Sequence similarities	Belongs to the translin family.

Ontologies

Keywords
Biological process	Differentiation Spermatogenesis
Cellular component	Cytoplasm Golgi apparatus Nucleus
Ligand	DNA-binding Magnesium Metal-binding
Molecular function	Developmental protein
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cell differentiation Inferred from electronic annotation. Source: UniProtKB-KW multicellular organismal development Inferred from electronic annotation. Source: UniProtKB-KW spermatogenesis Inferred from electronic annotation. Source: UniProtKB-KW
Cellular_component	Golgi apparatus Inferred from electronic annotation. Source: UniProtKB-SubCell nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell perinuclear region of cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	DNA binding Traceable author statement Ref.1. Source: ProtInc metal ion binding Inferred from electronic annotation. Source: UniProtKB-KW protein transporter activity Traceable author statement Ref.1. Source: ProtInc sequence-specific DNA binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 290

290

Translin-associated protein X

PRO_0000191686

Regions

Region

73 – 208

136

Interaction with C1D

Sites

Metal binding

129

1

Magnesium

Metal binding

197

1

Magnesium

Amino acid modifications

Modified residue

33

1

Phosphoserine Ref.11 Ref.12 Ref.14 Ref.16

Modified residue

68

1

N6-acetyllysine Ref.13

Modified residue

237

1

Phosphotyrosine By similarity

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

290

Helix Strand Turn

Details...

Helix

34 – 75

42

Helix

83 – 108

26

Beta strand

109 – 111

3

Turn

114 – 116

3

Helix

117 – 119

3

Helix

121 – 139

19

Helix

145 – 150

6

Helix

184 – 207

24

Helix

213 – 231

19

Helix

232 – 234

3

Helix

237 – 263

27

Sequences

	Sequence		Length	Mass (Da)
	Q99598 [UniParc]. Last modified May 1, 1997. Version 1. Checksum: D38B0DD96B50C0B9	FASTA	290	33,112
	10 20 30 40 50 60 MSNKEGSGGF RKRKHDNFPH NQRREGKDVN SSSPVMLAFK SFQQELDARH DKYERLVKLS 70 80 90 100 110 120 RDITVESKRT IFLLHRITSA PDMEDILTES EIKLDGVRQK IFQVAQELSG EDMHQFHRAI 130 140 150 160 170 180 TTGLQEYVEA VSFQHFIKTR SLISMDEINK QLIFTTEDNG KENKTPSSDA QDKQFGTWRL 190 200 210 220 230 240 RVTPVDYLLG VADLTGELMR MCINSVGNGD IDTPFEVSQF LRQVYDGFSF IGNTGPYEVS 250 260 270 280 290 KKLYTLKQSL AKVENACYAL KVRGSEIPKH MLADVFSVKT EMIDQEEGIS

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases 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]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[12]	"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-33, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[13]	"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-68, MASS SPECTROMETRY.
[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-33, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"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].
[16]	"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-33, MASS SPECTROMETRY.
[17]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.

IPI

IPI00293350.

RefSeq

NP_005990.1. NM_005999.2.

UniGene

Hs.13318.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

Q99598.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-29463N.

IntAct

Q99598. 19 interactions.

MINT

MINT-1347706.

STRING

9606.ENSP00000355599.

PTM databases

PhosphoSite

Q99598.

Polymorphism databases

DMDM

6136057.

Proteomic databases

PaxDb

Q99598.

PeptideAtlas

Q99598.

PRIDE

Q99598.

Protocols and materials databases

DNASU

7257.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000366639; ENSP00000355599; ENSG00000116918.

GeneID

7257.

KEGG

hsa:7257.

UCSC

uc001huw.3. human.

Organism-specific databases

CTD

7257.

GeneCards

GC01P231664.

HGNC

HGNC:12380. TSNAX.

HPA

CAB034263.
HPA031054.
HPA031055.

MIM

602964. gene.

neXtProt

NX_Q99598.

PharmGKB

PA37048.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG2178.

HOGENOM

HOG000008075.

HOVERGEN

HBG059067.

InParanoid

Q99598.

OMA

CISSVGN.

OrthoDB

EOG49GKHF.

PhylomeDB

Q99598.

Gene expression databases

ArrayExpress

Q99598.

Bgee

Q99598.

CleanEx

HS_TSNAX.

Genevestigator

Q99598.

GermOnline

ENSG00000116918. 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

TSNAX. human.

GenomeRNAi

7257.

NextBio

28373.

SOURCE

Search...

Entry information

Entry name

TSNAX_HUMAN

Accession

Primary (citable) accession number: Q99598
Secondary accession number(s): B1APC6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 15, 1999
Last sequence update:	May 1, 1997
Last modified:	May 1, 2013
This is version 110 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.