TSAP1_HUMAN
ID TSAP1_HUMAN Reviewed; 287 AA.
AC Q9NX07; Q86SU7;
DT 02-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-2000, sequence version 1.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=tRNA selenocysteine 1-associated protein 1;
DE AltName: Full=SECp43;
DE AltName: Full=tRNA selenocysteine-associated protein 1;
GN Name=TRNAU1AP; Synonyms=SECP43, TRSPAP1;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain, and Colon;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5]
RP FUNCTION, AND IDENTIFICATION IN A COMPLEX WITH EEFSEC; SECISBP2 AND
RP TRNA(SEC).
RX PubMed=16508009; DOI=10.1128/mcb.26.6.2337-2346.2006;
RA Small-Howard A., Morozova N., Stoytcheva Z., Forry E.P., Mansell J.B.,
RA Harney J.W., Carlson B.A., Xu X.M., Hatfield D.L., Berry M.J.;
RT "Supramolecular complexes mediate selenocysteine incorporation in vivo.";
RL Mol. Cell. Biol. 26:2337-2346(2006).
RN [6]
RP STRUCTURE BY NMR OF 1-184.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the RRM domain and of the C-terminal RNA recognition
RT motif of tRNA selenocysteine associated protein.";
RL Submitted (SEP-2006) to the PDB data bank.
CC -!- FUNCTION: Involved in the early steps of selenocysteine biosynthesis
CC and tRNA(Sec) charging to the later steps resulting in the
CC cotranslational incorporation of selenocysteine into selenoproteins.
CC Stabilizes the SECISBP2, EEFSEC and tRNA(Sec) complex. May be involved
CC in the methylation of tRNA(Sec). Enhances efficiency of selenoproteins
CC synthesis (By similarity). {ECO:0000250, ECO:0000269|PubMed:16508009}.
CC -!- SUBUNIT: Component of the tRNA(Sec) complex composed at least of
CC EEFSEC, SECISBP2, SEPHS1, SEPSECS, TRNAU1AP and tRNA(Sec). Found in a
CC complex with tRNA(Sec). Interacts with SEPSECS. Associates with mRNP
CC and/or polysomes (By similarity). Found in a complex with EEFSEC,
CC SECISBP2, TRNAU1AP and tRNA(Sec). {ECO:0000250,
CC ECO:0000269|PubMed:16508009}.
CC -!- INTERACTION:
CC Q9NX07; P27797: CALR; NbExp=3; IntAct=EBI-12581310, EBI-1049597;
CC Q9NX07; P36957: DLST; NbExp=3; IntAct=EBI-12581310, EBI-351007;
CC Q9NX07; Q92876: KLK6; NbExp=3; IntAct=EBI-12581310, EBI-2432309;
CC Q9NX07; Q8TDX7: NEK7; NbExp=3; IntAct=EBI-12581310, EBI-1055945;
CC Q9NX07-2; P50570-2: DNM2; NbExp=3; IntAct=EBI-21894090, EBI-10968534;
CC Q9NX07-2; Q16637: SMN2; NbExp=3; IntAct=EBI-21894090, EBI-395421;
CC Q9NX07-2; O14656-2: TOR1A; NbExp=3; IntAct=EBI-21894090, EBI-25847109;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}. Cytoplasm {ECO:0000250}.
CC Note=Abundant in the nucleus. {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9NX07-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9NX07-2; Sequence=VSP_028130;
CC -!- SIMILARITY: Belongs to the RRM TRSPAP family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AK000510; BAA91217.1; -; mRNA.
DR EMBL; AL513497; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471059; EAX07689.1; -; Genomic_DNA.
DR EMBL; BC000680; AAH00680.1; -; mRNA.
DR EMBL; BC039879; AAH39879.1; -; mRNA.
DR CCDS; CCDS324.1; -. [Q9NX07-1]
DR RefSeq; NP_060316.1; NM_017846.4. [Q9NX07-1]
DR RefSeq; XP_016857031.1; XM_017001542.1.
DR PDB; 2DHG; NMR; -; A=94-184.
DR PDB; 2DIV; NMR; -; A=1-86.
DR PDBsum; 2DHG; -.
DR PDBsum; 2DIV; -.
DR AlphaFoldDB; Q9NX07; -.
DR SMR; Q9NX07; -.
DR BioGRID; 120290; 41.
DR IntAct; Q9NX07; 12.
DR MINT; Q9NX07; -.
DR STRING; 9606.ENSP00000362936; -.
DR iPTMnet; Q9NX07; -.
DR PhosphoSitePlus; Q9NX07; -.
DR BioMuta; TRNAU1AP; -.
DR DMDM; 74761781; -.
DR EPD; Q9NX07; -.
DR jPOST; Q9NX07; -.
DR MassIVE; Q9NX07; -.
DR MaxQB; Q9NX07; -.
DR PaxDb; Q9NX07; -.
DR PeptideAtlas; Q9NX07; -.
DR PRIDE; Q9NX07; -.
DR ProteomicsDB; 83017; -. [Q9NX07-1]
DR ProteomicsDB; 83018; -. [Q9NX07-2]
DR Antibodypedia; 30961; 151 antibodies from 23 providers.
DR DNASU; 54952; -.
DR Ensembl; ENST00000373830.4; ENSP00000362936.3; ENSG00000180098.9. [Q9NX07-1]
DR GeneID; 54952; -.
DR KEGG; hsa:54952; -.
DR MANE-Select; ENST00000373830.4; ENSP00000362936.3; NM_017846.5; NP_060316.1.
DR UCSC; uc001bqi.4; human. [Q9NX07-1]
DR CTD; 54952; -.
DR GeneCards; TRNAU1AP; -.
DR HGNC; HGNC:30813; TRNAU1AP.
DR HPA; ENSG00000180098; Low tissue specificity.
DR MIM; 619597; gene.
DR neXtProt; NX_Q9NX07; -.
DR OpenTargets; ENSG00000180098; -.
DR PharmGKB; PA164727240; -.
DR VEuPathDB; HostDB:ENSG00000180098; -.
DR eggNOG; KOG0118; Eukaryota.
DR GeneTree; ENSGT00940000156139; -.
DR HOGENOM; CLU_016304_3_0_1; -.
DR InParanoid; Q9NX07; -.
DR OMA; LKICNAV; -.
DR OrthoDB; 775799at2759; -.
DR PhylomeDB; Q9NX07; -.
DR TreeFam; TF313275; -.
DR PathwayCommons; Q9NX07; -.
DR SignaLink; Q9NX07; -.
DR BioGRID-ORCS; 54952; 207 hits in 1092 CRISPR screens.
DR ChiTaRS; TRNAU1AP; human.
DR EvolutionaryTrace; Q9NX07; -.
DR GenomeRNAi; 54952; -.
DR Pharos; Q9NX07; Tbio.
DR PRO; PR:Q9NX07; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9NX07; protein.
DR Bgee; ENSG00000180098; Expressed in granulocyte and 165 other tissues.
DR Genevisible; Q9NX07; HS.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0005634; C:nucleus; ISS:HGNC-UCL.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000049; F:tRNA binding; IBA:GO_Central.
DR GO; GO:0001514; P:selenocysteine incorporation; ISS:HGNC-UCL.
DR CDD; cd12612; RRM2_SECp43; 1.
DR Gene3D; 3.30.70.330; -; 2.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR034510; SECp43_RRM2.
DR InterPro; IPR040434; TSAP1.
DR InterPro; IPR041085; TSAP1_C.
DR PANTHER; PTHR37457; PTHR37457; 1.
DR Pfam; PF00076; RRM_1; 2.
DR Pfam; PF17654; Trnau1ap; 1.
DR SMART; SM00360; RRM; 2.
DR SUPFAM; SSF54928; SSF54928; 1.
DR PROSITE; PS50102; RRM; 2.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Cytoplasm; Nucleus;
KW Protein biosynthesis; Reference proteome; Repeat; RNA-binding.
FT CHAIN 1..287
FT /note="tRNA selenocysteine 1-associated protein 1"
FT /id="PRO_0000304917"
FT DOMAIN 3..86
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 96..175
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT VAR_SEQ 1..110
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_028130"
FT STRAND 1..7
FT /evidence="ECO:0007829|PDB:2DIV"
FT HELIX 16..25
FT /evidence="ECO:0007829|PDB:2DIV"
FT STRAND 32..37
FT /evidence="ECO:0007829|PDB:2DIV"
FT STRAND 39..41
FT /evidence="ECO:0007829|PDB:2DIV"
FT STRAND 44..51
FT /evidence="ECO:0007829|PDB:2DIV"
FT HELIX 55..63
FT /evidence="ECO:0007829|PDB:2DIV"
FT TURN 64..67
FT /evidence="ECO:0007829|PDB:2DIV"
FT STRAND 68..72
FT /evidence="ECO:0007829|PDB:2DIV"
FT STRAND 81..83
FT /evidence="ECO:0007829|PDB:2DIV"
FT STRAND 98..101
FT /evidence="ECO:0007829|PDB:2DHG"
FT HELIX 109..119
FT /evidence="ECO:0007829|PDB:2DHG"
FT STRAND 123..130
FT /evidence="ECO:0007829|PDB:2DHG"
FT STRAND 136..145
FT /evidence="ECO:0007829|PDB:2DHG"
FT HELIX 147..156
FT /evidence="ECO:0007829|PDB:2DHG"
FT TURN 157..159
FT /evidence="ECO:0007829|PDB:2DHG"
FT STRAND 162..166
FT /evidence="ECO:0007829|PDB:2DHG"
SQ SEQUENCE 287 AA; 32499 MW; 4F85AA839FF256F5 CRC64;
MAASLWMGDL EPYMDENFIS RAFATMGETV MSVKIIRNRL TGIPAGYCFV EFADLATAEK
CLHKINGKPL PGATPAKRFK LNYATYGKQP DNSPEYSLFV GDLTPDVDDG MLYEFFVKVY
PSCRGGKVVL DQTGVSKGYG FVKFTDELEQ KRALTECQGA VGLGSKPVRL SVAIPKASRV
KPVEYSQMYS YSYNQYYQQY QNYYAQWGYD QNTGSYSYSY PQYGYTQSTM QTYEEVGDDA
LEDPMPQLDV TEANKEFMEQ SEELYDALMD CHWQPLDTVS SEIPAMM
