Entry sw:PUS10_HUMAN

ID   PUS10_HUMAN             Reviewed;         529 AA.
AC   Q3MIT2; Q5JPJ5; Q96MI8;
DT   11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT   25-OCT-2005, sequence version 1.
DT   30-NOV-2016, entry version 96.
DE   RecName: Full=Putative tRNA pseudouridine synthase Pus10;
DE            EC=5.4.99.-;
DE   AltName: Full=Coiled-coil domain-containing protein 139;
DE   AltName: Full=tRNA pseudouridine 55 synthase;
DE            Short=Psi55 synthase;
DE   AltName: Full=tRNA pseudouridylate synthase;
DE   AltName: Full=tRNA-uridine isomerase;
GN   Name=PUS10; Synonyms=CCDC139, DOBI;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC   Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC   Catarrhini; Hominidae; Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Prostate;
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.,
RA   Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA   Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA   Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA   Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA   Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA   Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA   Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA   Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA   Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA   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.,
RA   Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA   Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA   Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA   Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA   Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA   Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA   Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA   Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA   Nakai K., Yada T., Nakamura Y., Ohara O., 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 MRNA].
RC   TISSUE=Cervix;
RX   PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA   Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA   Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA   Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT   "The full-ORF clone resource of the German cDNA consortium.";
RL   BMC Genomics 8:399-399(2007).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA   Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA   Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA   Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA   Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA   Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA   Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA   Venter J.C.;
RL   Submitted (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain;
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
RT   project: the Mammalian Gene Collection (MGC).";
RL   Genome Res. 14:2121-2127(2004).
RN   [5]
RP   FUNCTION.
RX   PubMed=14527409; DOI=10.1016/S1097-2765(03)00348-4;
RA   Aza-Blanc P., Cooper C.L., Wagner K., Batalov S., Deveraux Q.L.,
RA   Cooke M.P.;
RT   "Identification of modulators of TRAIL-induced apoptosis via RNAi-
RT   based phenotypic screening.";
RL   Mol. Cell 12:627-637(2003).
RN   [6]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79 AND SER-84, AND
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Embryonic kidney;
RX   PubMed=17525332; DOI=10.1126/science.1140321;
RA   Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III,
RA   Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N.,
RA   Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.;
RT   "ATM and ATR substrate analysis reveals extensive protein networks
RT   responsive to DNA damage.";
RL   Science 316:1160-1166(2007).
RN   [7]
RP   PROTEOLYTIC CLEAVAGE, AND FUNCTION.
RX   PubMed=19712588; DOI=10.5483/BMBRep.2009.42.8.511;
RA   Park S.Y., Shin J.N., Woo H.N., Piya S., Moon A.R., Seo Y.W.,
RA   Seol D.W., Kim T.H.;
RT   "DOBI is cleaved by caspases during TRAIL-induced apoptotic cell
RT   death.";
RL   BMB Rep. 42:511-515(2009).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-84, AND IDENTIFICATION
RP   BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Erythroleukemia;
RX   PubMed=23186163; DOI=10.1021/pr300630k;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [9]
RP   X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
RX   PubMed=17900615; DOI=10.1016/j.jmb.2007.08.053;
RA   McCleverty C.J., Hornsby M., Spraggon G., Kreusch A.;
RT   "Crystal structure of human Pus10, a novel pseudouridine synthase.";
RL   J. Mol. Biol. 373:1243-1254(2007).
RN   [10]
RP   VARIANT [LARGE SCALE ANALYSIS] ILE-484.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
RA   Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
RA   Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
RA   Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
RA   Vogelstein B., Kinzler K.W., Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal
RT   cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Pseudouridylate synthases catalyze pseudouridination of
CC       structural RNAs, including transfer, ribosomal, and splicing RNAs.
CC       PUS10 catalyzes the formation of the universal psi55 in the GC
CC       loop of transfer RNAs (Probable). Modulator of TRAIL-induced cell
CC       death via activation of procaspase 8 and BID cleavage. Required
CC       for the progression of the apoptotic signal through intrinsic
CC       mitochondrial cell death. {ECO:0000269|PubMed:14527409,
CC       ECO:0000269|PubMed:19712588, ECO:0000305}.
CC   -!- CATALYTIC ACTIVITY: tRNA uridine = tRNA pseudouridine.
CC   -!- INTERACTION:
CC       Q9NX38:FAM206A; NbExp=4; IntAct=EBI-11983583, EBI-9105722;
CC   -!- PTM: Proteolytically cleaved during TRAIL-induced cell death.
CC       Cleaved, in vitro, either by caspase-3 or caspase-8.
CC       {ECO:0000269|PubMed:19712588}.
CC   -!- SIMILARITY: Belongs to the pseudouridine synthase Pus10 family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=CAI46123.1; Type=Miscellaneous discrepancy; Note=Partially unspliced pre-RNA.; Evidence={ECO:0000305};
DR   EMBL; AK056874; BAB71300.1; -; mRNA.
DR   EMBL; AL832208; CAI46123.1; ALT_SEQ; Transcribed_RNA.
DR   EMBL; CH471053; EAX00024.1; -; Genomic_DNA.
DR   EMBL; BC101680; AAI01681.1; -; mRNA.
DR   EMBL; BC101706; AAI01707.1; -; mRNA.
DR   CCDS; CCDS1865.1; -.
DR   RefSeq; NP_001309052.1; NM_001322123.1.
DR   RefSeq; NP_001309053.1; NM_001322124.1.
DR   RefSeq; NP_653310.2; NM_144709.3.
DR   RefSeq; XP_011530870.1; XM_011532568.2.
DR   RefSeq; XP_011530872.1; XM_011532570.1.
DR   RefSeq; XP_011530873.1; XM_011532571.1.
DR   RefSeq; XP_011530874.1; XM_011532572.1.
DR   RefSeq; XP_011530875.1; XM_011532573.2.
DR   RefSeq; XP_011530876.1; XM_011532574.2.
DR   RefSeq; XP_011530878.1; XM_011532576.2.
DR   UniGene; Hs.368348; -.
DR   PDB; 2V9K; X-ray; 2.00 A; A=1-529.
DR   PDBsum; 2V9K; -.
DR   ProteinModelPortal; Q3MIT2; -.
DR   SMR; Q3MIT2; -.
DR   BioGrid; 127335; 1.
DR   IntAct; Q3MIT2; 4.
DR   STRING; 9606.ENSP00000326003; -.
DR   iPTMnet; Q3MIT2; -.
DR   PhosphoSitePlus; Q3MIT2; -.
DR   BioMuta; PUS10; -.
DR   DMDM; 121942830; -.
DR   EPD; Q3MIT2; -.
DR   MaxQB; Q3MIT2; -.
DR   PaxDb; Q3MIT2; -.
DR   PeptideAtlas; Q3MIT2; -.
DR   PRIDE; Q3MIT2; -.
DR   Ensembl; ENST00000316752; ENSP00000326003; ENSG00000162927.
DR   Ensembl; ENST00000407787; ENSP00000386074; ENSG00000162927.
DR   GeneID; 150962; -.
DR   KEGG; hsa:150962; -.
DR   UCSC; uc002sao.4; human.
DR   CTD; 150962; -.
DR   DisGeNET; 150962; -.
DR   GeneCards; PUS10; -.
DR   HGNC; HGNC:26505; PUS10.
DR   HPA; HPA044736; -.
DR   HPA; HPA049582; -.
DR   MIM; 612787; gene.
DR   neXtProt; NX_Q3MIT2; -.
DR   OpenTargets; ENSG00000162927; -.
DR   PharmGKB; PA162400393; -.
DR   eggNOG; KOG2364; Eukaryota.
DR   eggNOG; COG1258; LUCA.
DR   GeneTree; ENSGT00390000007529; -.
DR   HOGENOM; HOG000030855; -.
DR   HOVERGEN; HBG056180; -.
DR   InParanoid; Q3MIT2; -.
DR   KO; K07583; -.
DR   OMA; IKKVCQK; -.
DR   OrthoDB; EOG091G06K1; -.
DR   PhylomeDB; Q3MIT2; -.
DR   TreeFam; TF106109; -.
DR   BioCyc; ZFISH:HS14989-MONOMER; -.
DR   ChiTaRS; PUS10; human.
DR   EvolutionaryTrace; Q3MIT2; -.
DR   GenomeRNAi; 150962; -.
DR   PRO; PR:Q3MIT2; -.
DR   Proteomes; UP000005640; Chromosome 2.
DR   Bgee; ENSG00000162927; -.
DR   CleanEx; HS_PUS10; -.
DR   ExpressionAtlas; Q3MIT2; baseline and differential.
DR   Genevisible; Q3MIT2; HS.
DR   GO; GO:0009982; F:pseudouridine synthase activity; IBA:GO_Central.
DR   GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR   GO; GO:0031119; P:tRNA pseudouridine synthesis; IBA:GO_Central.
DR   InterPro; IPR020103; PsdUridine_synth_cat_dom.
DR   SUPFAM; SSF55120; SSF55120; 1.
PE   1: Evidence at protein level;
KW   3D-structure; Coiled coil; Complete proteome; Isomerase;
KW   Phosphoprotein; Polymorphism; Reference proteome; tRNA processing.
FT   CHAIN         1    529       Putative tRNA pseudouridine synthase
FT                                Pus10.
FT                                /FTId=PRO_0000299022.
FT   REGION      304    317       RNA binding forefinger loop.
FT                                {ECO:0000255}.
FT   REGION      442    457       RNA binding thumb loop. {ECO:0000255}.
FT   COILED       42     89       {ECO:0000255}.
FT   ACT_SITE    344    344       Nucleophile. {ECO:0000255}.
FT   BINDING     414    414       Substrate. {ECO:0000255}.
FT   BINDING     485    485       Substrate. {ECO:0000255}.
FT   MOD_RES      79     79       Phosphoserine.
FT                                {ECO:0000244|PubMed:17525332}.
FT   MOD_RES      84     84       Phosphoserine.
FT                                {ECO:0000244|PubMed:17525332,
FT                                ECO:0000244|PubMed:23186163}.
FT   VARIANT     484    484       T -> I (in a colorectal cancer sample;
FT                                somatic mutation).
FT                                {ECO:0000269|PubMed:16959974}.
FT                                /FTId=VAR_035617.
FT   CONFLICT    208    208       F -> L (in Ref. 1; BAB71300).
FT                                {ECO:0000305}.
FT   HELIX         6      8       {ECO:0000244|PDB:2V9K}.
FT   HELIX         9     18       {ECO:0000244|PDB:2V9K}.
FT   HELIX        22     28       {ECO:0000244|PDB:2V9K}.
FT   HELIX        35     38       {ECO:0000244|PDB:2V9K}.
FT   HELIX        41     52       {ECO:0000244|PDB:2V9K}.
FT   TURN        110    117       {ECO:0000244|PDB:2V9K}.
FT   HELIX       118    120       {ECO:0000244|PDB:2V9K}.
FT   HELIX       122    134       {ECO:0000244|PDB:2V9K}.
FT   STRAND      142    147       {ECO:0000244|PDB:2V9K}.
FT   HELIX       152    169       {ECO:0000244|PDB:2V9K}.
FT   HELIX       176    178       {ECO:0000244|PDB:2V9K}.
FT   HELIX       182    198       {ECO:0000244|PDB:2V9K}.
FT   STRAND      207    215       {ECO:0000244|PDB:2V9K}.
FT   HELIX       217    220       {ECO:0000244|PDB:2V9K}.
FT   HELIX       221    227       {ECO:0000244|PDB:2V9K}.
FT   HELIX       246    255       {ECO:0000244|PDB:2V9K}.
FT   HELIX       258    264       {ECO:0000244|PDB:2V9K}.
FT   STRAND      277    285       {ECO:0000244|PDB:2V9K}.
FT   STRAND      288    296       {ECO:0000244|PDB:2V9K}.
FT   STRAND      307    315       {ECO:0000244|PDB:2V9K}.
FT   HELIX       318    323       {ECO:0000244|PDB:2V9K}.
FT   HELIX       326    330       {ECO:0000244|PDB:2V9K}.
FT   STRAND      333    341       {ECO:0000244|PDB:2V9K}.
FT   STRAND      348    362       {ECO:0000244|PDB:2V9K}.
FT   HELIX       370    381       {ECO:0000244|PDB:2V9K}.
FT   STRAND      385    395       {ECO:0000244|PDB:2V9K}.
FT   HELIX       398    409       {ECO:0000244|PDB:2V9K}.
FT   STRAND      412    422       {ECO:0000244|PDB:2V9K}.
FT   HELIX       426    429       {ECO:0000244|PDB:2V9K}.
FT   HELIX       430    434       {ECO:0000244|PDB:2V9K}.
FT   STRAND      437    443       {ECO:0000244|PDB:2V9K}.
FT   HELIX       446    448       {ECO:0000244|PDB:2V9K}.
FT   TURN        449    451       {ECO:0000244|PDB:2V9K}.
FT   STRAND      456    470       {ECO:0000244|PDB:2V9K}.
FT   STRAND      473    480       {ECO:0000244|PDB:2V9K}.
FT   HELIX       486    491       {ECO:0000244|PDB:2V9K}.
FT   TURN        493    496       {ECO:0000244|PDB:2V9K}.
FT   STRAND      497    499       {ECO:0000244|PDB:2V9K}.
FT   HELIX       501    505       {ECO:0000244|PDB:2V9K}.
FT   STRAND      509    519       {ECO:0000244|PDB:2V9K}.
SQ   SEQUENCE   529 AA;  60244 MW;  44E7BD6ED9C9864E CRC64;
     MFPLTEENKH VAQLLLNTGT CPRCIFRFCG VDFHAPYKLP YKELLNELQK FLETEKDELI
     LEVMNPPPKK IRLQELEDSI DNLSQNGEGR ISVSHVGSTA SKNSNLNVCN VCLGILQEFC
     EKDFIKKVCQ KVEASGFEFT SLVFSVSFPP QLSVREHAAW LLVKQEMGKQ SLSLGRDDIV
     QLKEAYKWIT HPLFSEELGV PIDGKSLFEV SVVFAHPETV EDCHFLAAIC PDCFKPAKNK
     QSVFTRMAVM KALNKIKEED FLKQFPCPPN SPKAVCAVLE IECAHGAVFV AGRYNKYSRN
     LPQTPWIIDG ERKLESSVEE LISDHLLAVF KAESFNFSSS GREDVDVRTL GNGRPFAIEL
     VNPHRVHFTS QEIKELQQKI NNSSNKIQVR DLQLVTREAI GHMKEGEEEK TKTYSALIWT
     NKAIQKKDIE FLNDIKDLKI DQKTPLRVLH RRPLAVRARV IHFMETQYVD EHHFRLHLKT
     QAGTYIKEFV HGDFGRTKPN IGSLMNVTAD ILELDVESVD VDWPPALDD
//