PUS7L_HUMAN
ID PUS7L_HUMAN Reviewed; 701 AA.
AC Q9H0K6; B3KUJ1; Q05CU0; Q6AHZ3; Q6NUP2;
DT 05-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2001, sequence version 1.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Pseudouridylate synthase PUS7L {ECO:0000305};
DE EC=5.4.99.- {ECO:0000269|PubMed:35051350};
DE AltName: Full=Pseudouridylate synthase 7 homolog-like protein {ECO:0000305};
GN Name=PUS7L {ECO:0000303|PubMed:35051350, ECO:0000312|HGNC:HGNC:25276};
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).
RC TISSUE=Testis;
RX PubMed=11230166; DOI=10.1101/gr.gr1547r;
RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S.,
RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J.,
RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W.,
RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B.,
RA Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and analysis of
RT 500 novel complete protein coding human cDNAs.";
RL Genome Res. 11:422-435(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Stomach;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT GLU-264.
RC TISSUE=Seminoma;
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., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16541075; DOI=10.1038/nature04569;
RA Scherer S.E., Muzny D.M., Buhay C.J., Chen R., Cree A., Ding Y.,
RA Dugan-Rocha S., Gill R., Gunaratne P., Harris R.A., Hawes A.C.,
RA Hernandez J., Hodgson A.V., Hume J., Jackson A., Khan Z.M., Kovar-Smith C.,
RA Lewis L.R., Lozado R.J., Metzker M.L., Milosavljevic A., Miner G.R.,
RA Montgomery K.T., Morgan M.B., Nazareth L.V., Scott G., Sodergren E.,
RA Song X.-Z., Steffen D., Lovering R.C., Wheeler D.A., Worley K.C., Yuan Y.,
RA Zhang Z., Adams C.Q., Ansari-Lari M.A., Ayele M., Brown M.J., Chen G.,
RA Chen Z., Clerc-Blankenburg K.P., Davis C., Delgado O., Dinh H.H.,
RA Draper H., Gonzalez-Garay M.L., Havlak P., Jackson L.R., Jacob L.S.,
RA Kelly S.H., Li L., Li Z., Liu J., Liu W., Lu J., Maheshwari M.,
RA Nguyen B.-V., Okwuonu G.O., Pasternak S., Perez L.M., Plopper F.J.H.,
RA Santibanez J., Shen H., Tabor P.E., Verduzco D., Waldron L., Wang Q.,
RA Williams G.A., Zhang J., Zhou J., Allen C.C., Amin A.G., Anyalebechi V.,
RA Bailey M., Barbaria J.A., Bimage K.E., Bryant N.P., Burch P.E.,
RA Burkett C.E., Burrell K.L., Calderon E., Cardenas V., Carter K., Casias K.,
RA Cavazos I., Cavazos S.R., Ceasar H., Chacko J., Chan S.N., Chavez D.,
RA Christopoulos C., Chu J., Cockrell R., Cox C.D., Dang M., Dathorne S.R.,
RA David R., Davis C.M., Davy-Carroll L., Deshazo D.R., Donlin J.E.,
RA D'Souza L., Eaves K.A., Egan A., Emery-Cohen A.J., Escotto M., Flagg N.,
RA Forbes L.D., Gabisi A.M., Garza M., Hamilton C., Henderson N.,
RA Hernandez O., Hines S., Hogues M.E., Huang M., Idlebird D.G., Johnson R.,
RA Jolivet A., Jones S., Kagan R., King L.M., Leal B., Lebow H., Lee S.,
RA LeVan J.M., Lewis L.C., London P., Lorensuhewa L.M., Loulseged H.,
RA Lovett D.A., Lucier A., Lucier R.L., Ma J., Madu R.C., Mapua P.,
RA Martindale A.D., Martinez E., Massey E., Mawhiney S., Meador M.G.,
RA Mendez S., Mercado C., Mercado I.C., Merritt C.E., Miner Z.L., Minja E.,
RA Mitchell T., Mohabbat F., Mohabbat K., Montgomery B., Moore N., Morris S.,
RA Munidasa M., Ngo R.N., Nguyen N.B., Nickerson E., Nwaokelemeh O.O.,
RA Nwokenkwo S., Obregon M., Oguh M., Oragunye N., Oviedo R.J., Parish B.J.,
RA Parker D.N., Parrish J., Parks K.L., Paul H.A., Payton B.A., Perez A.,
RA Perrin W., Pickens A., Primus E.L., Pu L.-L., Puazo M., Quiles M.M.,
RA Quiroz J.B., Rabata D., Reeves K., Ruiz S.J., Shao H., Sisson I.,
RA Sonaike T., Sorelle R.P., Sutton A.E., Svatek A.F., Svetz L.A.,
RA Tamerisa K.S., Taylor T.R., Teague B., Thomas N., Thorn R.D., Trejos Z.Y.,
RA Trevino B.K., Ukegbu O.N., Urban J.B., Vasquez L.I., Vera V.A.,
RA Villasana D.M., Wang L., Ward-Moore S., Warren J.T., Wei X., White F.,
RA Williamson A.L., Wleczyk R., Wooden H.S., Wooden S.H., Yen J., Yoon L.,
RA Yoon V., Zorrilla S.E., Nelson D., Kucherlapati R., Weinstock G.,
RA Gibbs R.A.;
RT "The finished DNA sequence of human chromosome 12.";
RL Nature 440:346-351(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain, and Prostate;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-79, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and 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 [8]
RP FUNCTION, AND CATALYTIC ACTIVITY.
RX PubMed=35051350; DOI=10.1016/j.molcel.2021.12.023;
RA Martinez N.M., Su A., Burns M.C., Nussbacher J.K., Schaening C., Sathe S.,
RA Yeo G.W., Gilbert W.V.;
RT "Pseudouridine synthases modify human pre-mRNA co-transcriptionally and
RT affect pre-mRNA processing.";
RL Mol. Cell 82:645-659(2022).
CC -!- FUNCTION: Pseudouridine synthase that catalyzes pseudouridylation of
CC mRNAs. {ECO:0000269|PubMed:35051350}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a uridine in mRNA = a pseudouridine in mRNA;
CC Xref=Rhea:RHEA:56644, Rhea:RHEA-COMP:14658, Rhea:RHEA-COMP:14659,
CC ChEBI:CHEBI:65314, ChEBI:CHEBI:65315;
CC Evidence={ECO:0000269|PubMed:35051350};
CC -!- INTERACTION:
CC Q9H0K6; P14373: TRIM27; NbExp=7; IntAct=EBI-5464419, EBI-719493;
CC Q9H0K6; Q8WV44: TRIM41; NbExp=3; IntAct=EBI-5464419, EBI-725997;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9H0K6-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H0K6-2; Sequence=VSP_054568;
CC -!- SIMILARITY: Belongs to the pseudouridine synthase TruD family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH20781.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AL136759; CAB66693.1; -; mRNA.
DR EMBL; AK097331; BAG53453.1; -; mRNA.
DR EMBL; AC016143; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC093012; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CR627435; CAH10521.1; -; mRNA.
DR EMBL; BC020781; AAH20781.1; ALT_TERM; mRNA.
DR EMBL; BC033621; AAH33621.1; -; mRNA.
DR EMBL; BC068502; AAH68502.1; -; mRNA.
DR CCDS; CCDS61104.1; -. [Q9H0K6-2]
DR CCDS; CCDS8743.1; -. [Q9H0K6-1]
DR RefSeq; NP_001092084.1; NM_001098614.2. [Q9H0K6-1]
DR RefSeq; NP_001092085.1; NM_001098615.1. [Q9H0K6-1]
DR RefSeq; NP_001258755.1; NM_001271826.1. [Q9H0K6-2]
DR RefSeq; NP_112582.3; NM_031292.4. [Q9H0K6-1]
DR AlphaFoldDB; Q9H0K6; -.
DR SMR; Q9H0K6; -.
DR BioGRID; 123650; 12.
DR IntAct; Q9H0K6; 5.
DR STRING; 9606.ENSP00000415899; -.
DR iPTMnet; Q9H0K6; -.
DR PhosphoSitePlus; Q9H0K6; -.
DR BioMuta; PUS7L; -.
DR DMDM; 74733527; -.
DR EPD; Q9H0K6; -.
DR jPOST; Q9H0K6; -.
DR MassIVE; Q9H0K6; -.
DR MaxQB; Q9H0K6; -.
DR PaxDb; Q9H0K6; -.
DR PeptideAtlas; Q9H0K6; -.
DR PRIDE; Q9H0K6; -.
DR ProteomicsDB; 80292; -. [Q9H0K6-1]
DR Antibodypedia; 25131; 49 antibodies from 14 providers.
DR DNASU; 83448; -.
DR Ensembl; ENST00000344862.10; ENSP00000343081.5; ENSG00000129317.15. [Q9H0K6-1]
DR Ensembl; ENST00000416848.6; ENSP00000415899.2; ENSG00000129317.15. [Q9H0K6-1]
DR Ensembl; ENST00000431332.7; ENSP00000398497.3; ENSG00000129317.15. [Q9H0K6-2]
DR Ensembl; ENST00000551923.5; ENSP00000447706.1; ENSG00000129317.15. [Q9H0K6-1]
DR GeneID; 83448; -.
DR KEGG; hsa:83448; -.
DR MANE-Select; ENST00000344862.10; ENSP00000343081.5; NM_031292.5; NP_112582.3.
DR UCSC; uc001rnq.7; human. [Q9H0K6-1]
DR CTD; 83448; -.
DR DisGeNET; 83448; -.
DR GeneCards; PUS7L; -.
DR HGNC; HGNC:25276; PUS7L.
DR HPA; ENSG00000129317; Low tissue specificity.
DR neXtProt; NX_Q9H0K6; -.
DR OpenTargets; ENSG00000129317; -.
DR PharmGKB; PA143485588; -.
DR VEuPathDB; HostDB:ENSG00000129317; -.
DR eggNOG; KOG2339; Eukaryota.
DR GeneTree; ENSGT00530000063554; -.
DR HOGENOM; CLU_005281_1_1_1; -.
DR InParanoid; Q9H0K6; -.
DR OMA; FEPDGNK; -.
DR OrthoDB; 955294at2759; -.
DR PhylomeDB; Q9H0K6; -.
DR TreeFam; TF314278; -.
DR PathwayCommons; Q9H0K6; -.
DR SignaLink; Q9H0K6; -.
DR BioGRID-ORCS; 83448; 10 hits in 1075 CRISPR screens.
DR ChiTaRS; PUS7L; human.
DR GeneWiki; PUS7L; -.
DR GenomeRNAi; 83448; -.
DR Pharos; Q9H0K6; Tdark.
DR PRO; PR:Q9H0K6; -.
DR Proteomes; UP000005640; Chromosome 12.
DR RNAct; Q9H0K6; protein.
DR Bgee; ENSG00000129317; Expressed in calcaneal tendon and 186 other tissues.
DR ExpressionAtlas; Q9H0K6; baseline and differential.
DR Genevisible; Q9H0K6; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0009982; F:pseudouridine synthase activity; IDA:UniProtKB.
DR GO; GO:0003723; F:RNA binding; IEA:InterPro.
DR GO; GO:0006397; P:mRNA processing; IEA:UniProtKB-KW.
DR GO; GO:1990481; P:mRNA pseudouridine synthesis; IDA:UniProtKB.
DR GO; GO:0001522; P:pseudouridine synthesis; IBA:GO_Central.
DR Gene3D; 3.30.2350.20; -; 2.
DR InterPro; IPR020103; PsdUridine_synth_cat_dom_sf.
DR InterPro; IPR001656; PsdUridine_synth_TruD.
DR InterPro; IPR011760; PsdUridine_synth_TruD_insert.
DR InterPro; IPR042214; TruD_catalytic.
DR PANTHER; PTHR13326; PTHR13326; 1.
DR Pfam; PF01142; TruD; 1.
DR PIRSF; PIRSF037016; Pseudouridin_synth_euk_prd; 1.
DR SUPFAM; SSF55120; SSF55120; 1.
DR TIGRFAMs; TIGR00094; tRNA_TruD_broad; 1.
DR PROSITE; PS50984; TRUD; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Isomerase; mRNA processing; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1..701
FT /note="Pseudouridylate synthase PUS7L"
FT /id="PRO_0000316785"
FT DOMAIN 424..647
FT /note="TRUD"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00342"
FT ACT_SITE 339
FT /note="Nucleophile"
FT /evidence="ECO:0000250|UniProtKB:Q57261"
FT MOD_RES 79
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..313
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054568"
FT VARIANT 92
FT /note="I -> M (in dbSNP:rs33999797)"
FT /id="VAR_038392"
FT VARIANT 264
FT /note="K -> E (in dbSNP:rs1057190)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_038393"
FT VARIANT 343
FT /note="I -> V (in dbSNP:rs34668377)"
FT /id="VAR_038394"
FT CONFLICT 167
FT /note="L -> V (in Ref. 5; AAH68502)"
FT /evidence="ECO:0000305"
FT CONFLICT 206
FT /note="L -> F (in Ref. 5; AAH20781)"
FT /evidence="ECO:0000305"
FT CONFLICT 572
FT /note="P -> Q (in Ref. 5; AAH68502)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 701 AA; 80700 MW; F8DD4478EA1210A0 CRC64;
MEEDTDYRIR FSSLCFFNDH VGFHGTIKSS PSDFIVIEID EQGQLVNKTI DEPIFKISEI
QLEPNNFPKK PKLDLQNLSL EDGRNQEVHT LIKYTDGDQN HQSGSEKEDT IVDGTSKCEE
KADVLSSFLD EKTHELLNNF ACDVREKWLS KTELIGLPPE FSIGRILDKN QRASLHSAIR
QKFPFLVTVG KNSEIVVKPN LEYKELCHLV SEEEAFDFFK YLDAKKENSK FTFKPDTNKD
HRKAVHHFVN KKFGNLVETK SFSKMNCSAG NPNVVVTVRF REKAHKRGKR PLSECQEGKV
IYTAFTLRKE NLEMFEAIGF LAIKLGVIPS DFSYAGLKDK KAITYQAMVV RKVTPERLKN
IEKEIEKKRM NVFNIRSVDD SLRLGQLKGN HFDIVIRNLK KQINDSANLR ERIMEAIENV
KKKGFVNYYG PQRFGKGRKV HTDQIGLALL KNEMMKAIKL FLTPEDLDDP VNRAKKYFLQ
TEDAKGTLSL MPEFKVRERA LLEALHRFGM TEEGCIQAWF SLPHSMRIFY VHAYTSKIWN
EAVSYRLETY GARVVQGDLV CLDEDIDDEN FPNSKIHLVT EEEGSANMYA IHQVVLPVLG
YNIQYPKNKV GQWYHDILSR DGLQTCRFKV PTLKLNIPGC YRQILKHPCN LSYQLMEDHD
IDVKTKGSHI DETALSLLIS FDLDASCYAT VCLKEIMKHD V
