PUF60_HUMAN
ID PUF60_HUMAN Reviewed; 559 AA.
AC Q9UHX1; A8K8K8; Q969E7; Q96D94; Q96H63; Q99628; Q9NZA0; Q9UJY7;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Poly(U)-binding-splicing factor PUF60 {ECO:0000312|HGNC:HGNC:17042};
DE AltName: Full=60 kDa poly(U)-binding-splicing factor {ECO:0000312|HGNC:HGNC:17042};
DE AltName: Full=FUSE-binding protein-interacting repressor {ECO:0000303|PubMed:16452196};
DE Short=FBP-interacting repressor {ECO:0000303|PubMed:16452196};
DE AltName: Full=Ro-binding protein 1 {ECO:0000312|HGNC:HGNC:17042};
DE Short=RoBP1;
DE AltName: Full=Siah-binding protein 1 {ECO:0000312|HGNC:HGNC:17042};
DE Short=Siah-BP1 {ECO:0000312|HGNC:HGNC:17042};
GN Name=PUF60 {ECO:0000312|HGNC:HGNC:17042};
GN Synonyms=FIR {ECO:0000303|PubMed:16628215},
GN ROBPI {ECO:0000303|PubMed:10668799}, SIAHBP1 {ECO:0000303|Ref.23};
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 [MRNA] (ISOFORM 2), FUNCTION, IDENTIFICATION IN A
RP COMPLEX WITH FUBP1 AND FUSE DNA, AND INTERACTION WITH CDK7; ERCC3; FUBP1
RP AND GTF2H1.
RX PubMed=10882074; DOI=10.1016/s1097-2765(00)80428-1;
RA Liu J., He L., Collins I., Ge H., Libutti D., Li J., Egly J.-M., Levens D.;
RT "The FBP interacting repressor targets TFIIH to inhibit activated
RT transcription.";
RL Mol. Cell 5:331-341(2000).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), ALTERNATIVE SPLICING (ISOFORM 5),
RP IDENTIFICATION IN A COMPLEX WITH RO60 AND Y5 RNA, RNA-BINDING, SUBCELLULAR
RP LOCATION, AND TISSUE SPECIFICITY.
RX PubMed=10668799; DOI=10.1017/s1355838200990277;
RA Bouffard P., Barbar E., Briere F., Boire G.;
RT "Interaction cloning and characterization of RoBPI, a novel protein binding
RT to human Ro ribonucleoproteins.";
RL RNA 6:66-78(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Testis;
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 [5]
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 (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2; 3 AND 4).
RC TISSUE=Brain, Lung, Muscle, and Ovary;
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 [7]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 2-559 (ISOFORM 2).
RA Hu Y., Holloway A.J., Bowtell D.D.L.;
RT "Interaction of sina and siah ring finger proteins with proteins involved
RT in RNA metabolism, detected using the yeast two hybrid system.";
RL Submitted (MAR-1996) to the EMBL/GenBank/DDBJ databases.
RN [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 4-559 (ISOFORM 1), PROTEIN SEQUENCE OF 32-43;
RP 53-69; 72-80; 156-167; 169-185; 227-243; 267-296; 301-313; 332-342; 419-437
RP AND 527-559, FUNCTION, SUBUNIT, RNA-BINDING, INTERACTION WITH SRSF11, AND
RP SUBCELLULAR LOCATION.
RX PubMed=10606266; DOI=10.1017/s1355838299991938;
RA Page-McCaw P.S., Amonlirdviman K., Sharp P.A.;
RT "PUF60: a novel U2AF65-related splicing activity.";
RL RNA 5:1548-1560(1999).
RN [9]
RP FUNCTION, AND INTERACTION WITH ERCC3.
RX PubMed=11239393; DOI=10.1016/s0092-8674(01)00223-9;
RA Liu J., Akoulitchev S., Weber A., Ge H., Chuikov S., Libutti D., Wang X.W.,
RA Conaway J.W., Harris C.C., Conaway R.C., Reinberg D., Levens D.;
RT "Defective interplay of activators and repressors with TFIH in xeroderma
RT pigmentosum.";
RL Cell 104:353-363(2001).
RN [10]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 6), AND TISSUE SPECIFICITY.
RX PubMed=16452196; DOI=10.1158/0008-5472.can-04-4459;
RA Matsushita K., Tomonaga T., Shimada H., Shioya A., Higashi M.,
RA Matsubara H., Harigaya K., Nomura F., Libutti D., Levens D., Ochiai T.;
RT "An essential role of alternative splicing of c-myc suppressor FUSE-binding
RT protein-interacting repressor in carcinogenesis.";
RL Cancer Res. 66:1409-1417(2006).
RN [11]
RP FUNCTION, AND DNA-BINDING.
RX PubMed=16628215; DOI=10.1038/sj.emboj.7601101;
RA Liu J., Kouzine F., Nie Z., Chung H.-J., Elisha-Feil Z., Weber A., Zhao K.,
RA Levens D.;
RT "The FUSE/FBP/FIR/TFIIH system is a molecular machine programming a pulse
RT of c-myc expression.";
RL EMBO J. 25:2119-2130(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=16964243; DOI=10.1038/nbt1240;
RA Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
RT "A probability-based approach for high-throughput protein phosphorylation
RT analysis and site localization.";
RL Nat. Biotechnol. 24:1285-1292(2006).
RN [13]
RP FUNCTION, IDENTIFICATION IN THE SPLICEOSOME COMPLEX, IDENTIFICATION BY MASS
RP SPECTROMETRY, RNA-BINDING, AND SUBCELLULAR LOCATION.
RX PubMed=17579712; DOI=10.1371/journal.pone.0000538;
RA Hastings M.L., Allemand E., Duelli D.M., Myers M.P., Krainer A.R.;
RT "Control of pre-mRNA splicing by the general splicing factors PUF60 and
RT U2AF.";
RL PLoS ONE 2:E538-E538(2007).
RN [14]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [16]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-251 AND LYS-454, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60; SER-112 AND THR-314, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [18]
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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-60, AND IDENTIFICATION BY
RP 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 [20]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [21]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-458, SUMOYLATION [LARGE SCALE
RP ANALYSIS] AT LYS-14 (ISOFORMS 5 AND 6), AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25218447; DOI=10.1038/nsmb.2890;
RA Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
RA Vertegaal A.C.;
RT "Uncovering global SUMOylation signaling networks in a site-specific
RT manner.";
RL Nat. Struct. Mol. Biol. 21:927-936(2014).
RN [22]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-43; LYS-80; LYS-419 AND LYS-458,
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-14 (ISOFORMS 5 AND 6), AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [23]
RP STRUCTURE BY NMR OF 454-559.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the third RNA binding domain of FBP-interacting
RT repressor, SIAHBP1.";
RL Submitted (APR-2007) to the PDB data bank.
RN [24]
RP VARIANT VRJS TYR-169, AND CHARACTERIZATION OF VARIANT VRJS TYR-169.
RX PubMed=24140112; DOI=10.1016/j.ajhg.2013.09.010;
RA Dauber A., Golzio C., Guenot C., Jodelka F.M., Kibaek M., Kjaergaard S.,
RA Leheup B., Martinet D., Nowaczyk M.J., Rosenfeld J.A., Zeesman S.,
RA Zunich J., Beckmann J.S., Hirschhorn J.N., Hastings M.L., Jacquemont S.,
RA Katsanis N.;
RT "SCRIB and PUF60 are primary drivers of the multisystemic phenotypes of the
RT 8q24.3 copy-number variant.";
RL Am. J. Hum. Genet. 93:798-811(2013).
CC -!- FUNCTION: DNA- and RNA-binding protein, involved in several nuclear
CC processes such as pre-mRNA splicing, apoptosis and transcription
CC regulation. In association with FUBP1 regulates MYC transcription at
CC the P2 promoter through the core-TFIIH basal transcription factor. Acts
CC as a transcriptional repressor through the core-TFIIH basal
CC transcription factor. Represses FUBP1-induced transcriptional
CC activation but not basal transcription. Decreases ERCC3 helicase
CC activity. Does not repress TFIIH-mediated transcription in xeroderma
CC pigmentosum complementation group B (XPB) cells. Is also involved in
CC pre-mRNA splicing. Promotes splicing of an intron with weak 3'-splice
CC site and pyrimidine tract in a cooperative manner with U2AF2. Involved
CC in apoptosis induction when overexpressed in HeLa cells. Isoform 6
CC failed to repress MYC transcription and inhibited FIR-induced apoptosis
CC in colorectal cancer. Isoform 6 may contribute to tumor progression by
CC enabling increased MYC expression and greater resistance to apoptosis
CC in tumors than in normal cells. Modulates alternative splicing of
CC several mRNAs. Binds to relaxed DNA of active promoter regions. Binds
CC to the pyrimidine tract and 3'-splice site regions of pre-mRNA; binding
CC is enhanced in presence of U2AF2. Binds to Y5 RNA in association with
CC RO60. Binds to poly(U) RNA. {ECO:0000269|PubMed:10606266,
CC ECO:0000269|PubMed:10882074, ECO:0000269|PubMed:11239393,
CC ECO:0000269|PubMed:16452196, ECO:0000269|PubMed:16628215,
CC ECO:0000269|PubMed:17579712}.
CC -!- SUBUNIT: Homodimer (PubMed:10606266). Associates with the spliceosome
CC (PubMed:17579712). Found in a complex with RO60 and Y5 RNA
CC (PubMed:10668799). Found in a complex with FUBP1 and far upstream
CC element (FUSE) DNA segment (PubMed:10882074). Interacts directly with
CC ERCC3 (PubMed:11239393). Interacts with CDK7 and GTF2H1
CC (PubMed:10882074). Interacts with SRSF11/P54 (PubMed:10606266). Does
CC not interact with ERCC3 in xeroderma pigmentosum complementation group
CC B (XPB) cells (PubMed:11239393). {ECO:0000269|PubMed:10606266,
CC ECO:0000269|PubMed:10668799, ECO:0000269|PubMed:10882074,
CC ECO:0000269|PubMed:11239393, ECO:0000269|PubMed:17579712}.
CC -!- INTERACTION:
CC Q9UHX1; Q96BM9: ARL8A; NbExp=3; IntAct=EBI-1053259, EBI-4401082;
CC Q9UHX1; Q969J3: BORCS5; NbExp=4; IntAct=EBI-1053259, EBI-747707;
CC Q9UHX1; O00555: CACNA1A; NbExp=2; IntAct=EBI-1053259, EBI-766279;
CC Q9UHX1; P24863: CCNC; NbExp=3; IntAct=EBI-1053259, EBI-395261;
CC Q9UHX1; Q9H0B3: IQCN; NbExp=3; IntAct=EBI-1053259, EBI-745878;
CC Q9UHX1; Q7Z7F0: KHDC4; NbExp=3; IntAct=EBI-1053259, EBI-751942;
CC Q9UHX1; Q9H204: MED28; NbExp=6; IntAct=EBI-1053259, EBI-514199;
CC Q9UHX1; Q15365: PCBP1; NbExp=2; IntAct=EBI-1053259, EBI-946095;
CC Q9UHX1; Q96I34: PPP1R16A; NbExp=2; IntAct=EBI-1053259, EBI-710402;
CC Q9UHX1; Q9UHX1: PUF60; NbExp=4; IntAct=EBI-1053259, EBI-1053259;
CC Q9UHX1; Q2TAL8: QRICH1; NbExp=3; IntAct=EBI-1053259, EBI-2798044;
CC Q9UHX1; P54727: RAD23B; NbExp=3; IntAct=EBI-1053259, EBI-954531;
CC Q9UHX1; Q9UHR5: SAP30BP; NbExp=10; IntAct=EBI-1053259, EBI-751683;
CC Q9UHX1; O00560: SDCBP; NbExp=3; IntAct=EBI-1053259, EBI-727004;
CC Q9UHX1; Q8IUQ4: SIAH1; NbExp=7; IntAct=EBI-1053259, EBI-747107;
CC Q9UHX1; Q05519: SRSF11; NbExp=6; IntAct=EBI-1053259, EBI-1051785;
CC Q9UHX1; P26368: U2AF2; NbExp=5; IntAct=EBI-1053259, EBI-742339;
CC Q9UHX1; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-1053259, EBI-10180829;
CC Q9UHX1; Q9HAU5: UPF2; NbExp=3; IntAct=EBI-1053259, EBI-372073;
CC Q9UHX1; O60844: ZG16; NbExp=3; IntAct=EBI-1053259, EBI-746479;
CC Q9UHX1-2; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-11529177, EBI-742054;
CC Q9UHX1-2; Q9BXU8: FTHL17; NbExp=3; IntAct=EBI-11529177, EBI-12156897;
CC Q9UHX1-2; Q96AE4-1: FUBP1; NbExp=2; IntAct=EBI-11529177, EBI-5455665;
CC Q9UHX1-2; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-11529177, EBI-12121668;
CC Q9UHX1-2; P04406: GAPDH; NbExp=3; IntAct=EBI-11529177, EBI-354056;
CC Q9UHX1-2; P42858: HTT; NbExp=6; IntAct=EBI-11529177, EBI-466029;
CC Q9UHX1-2; Q7Z7F0-4: KHDC4; NbExp=10; IntAct=EBI-11529177, EBI-9089060;
CC Q9UHX1-2; P57721-2: PCBP3; NbExp=3; IntAct=EBI-11529177, EBI-11983983;
CC Q9UHX1-2; Q9UHX1-2: PUF60; NbExp=3; IntAct=EBI-11529177, EBI-11529177;
CC Q9UHX1-2; P54727: RAD23B; NbExp=3; IntAct=EBI-11529177, EBI-954531;
CC Q9UHX1-2; Q15637-4: SF1; NbExp=3; IntAct=EBI-11529177, EBI-12223157;
CC Q9UHX1-2; Q05519-2: SRSF11; NbExp=6; IntAct=EBI-11529177, EBI-11975029;
CC Q9UHX1-2; Q6P1X5: TAF2; NbExp=3; IntAct=EBI-11529177, EBI-1560063;
CC Q9UHX1-2; P07101-3: TH; NbExp=3; IntAct=EBI-11529177, EBI-12001016;
CC Q9UHX1-2; P26368-2: U2AF2; NbExp=3; IntAct=EBI-11529177, EBI-11097439;
CC Q9UHX1-2; P0CB47: UBTFL1; NbExp=3; IntAct=EBI-11529177, EBI-17208936;
CC Q9UHX1-2; O60844: ZG16; NbExp=3; IntAct=EBI-11529177, EBI-746479;
CC Q9UHX1-5; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-11526420, EBI-9089060;
CC Q9UHX1-6; P42858: HTT; NbExp=9; IntAct=EBI-11085298, EBI-466029;
CC Q9UHX1-6; Q7Z7F0-4: KHDC4; NbExp=3; IntAct=EBI-11085298, EBI-9089060;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10606266,
CC ECO:0000269|PubMed:10668799, ECO:0000269|PubMed:17579712}.
CC Note=Colocalizes partially with RO60. {ECO:0000269|PubMed:10668799}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=1;
CC IsoId=Q9UHX1-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9UHX1-2; Sequence=VSP_027719;
CC Name=3;
CC IsoId=Q9UHX1-3; Sequence=VSP_027717;
CC Name=4;
CC IsoId=Q9UHX1-4; Sequence=VSP_027717, VSP_027719;
CC Name=5;
CC IsoId=Q9UHX1-5; Sequence=VSP_027718;
CC Name=6;
CC IsoId=Q9UHX1-6; Sequence=VSP_027718, VSP_027719;
CC -!- TISSUE SPECIFICITY: Isoform 2 is expressed in colonic epithelium and
CC colorectal epithelium cancer (at protein level). Isoform 6 is expressed
CC in colorectal epithelial cancer but below detection level in colonic
CC epithelium. Expressed in heart, brain, placenta, lung, liver, skeletal
CC muscle, kidney, pancreas, spleen, thymus, prostate, testis, ovary,
CC small intestine, colon and peripheral blood leukocytes.
CC {ECO:0000269|PubMed:10668799, ECO:0000269|PubMed:16452196}.
CC -!- DOMAIN: The third RNA recognition motif, called PUMP domain, is
CC atypical and may rather mediate homodimerization and/or protein-protein
CC interactions.
CC -!- DISEASE: Verheij syndrome (VRJS) [MIM:615583]: A syndrome characterized
CC by growth retardation, delayed psychomotor development, dysmorphic
CC facial features, and skeletal, mainly vertebral, abnormalities.
CC Additional variable features may include coloboma, renal defects, and
CC cardiac defects. {ECO:0000269|PubMed:24140112}. Note=The disease is
CC caused by variants affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: Does not repress TFIIH-mediated transcription in
CC xeroderma pigmentosum complementation group B (XPB) cells.
CC -!- SIMILARITY: Belongs to the RRM half pint 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; AF217197; AAF27522.2; -; mRNA.
DR EMBL; AF114818; AAF23589.1; -; mRNA.
DR EMBL; AK292373; BAF85062.1; -; mRNA.
DR EMBL; CR457143; CAG33424.1; -; mRNA.
DR EMBL; CH471162; EAW82187.1; -; Genomic_DNA.
DR EMBL; CH471162; EAW82189.1; -; Genomic_DNA.
DR EMBL; BC008875; AAH08875.1; -; mRNA.
DR EMBL; BC009734; AAH09734.1; -; mRNA.
DR EMBL; BC011265; AAH11265.1; -; mRNA.
DR EMBL; BC011979; AAH11979.1; -; mRNA.
DR EMBL; U51586; AAB41656.1; -; mRNA.
DR EMBL; AF190744; AAF05605.1; -; mRNA.
DR CCDS; CCDS47933.1; -. [Q9UHX1-2]
DR CCDS; CCDS47934.1; -. [Q9UHX1-1]
DR CCDS; CCDS47935.1; -. [Q9UHX1-3]
DR CCDS; CCDS59514.1; -. [Q9UHX1-4]
DR CCDS; CCDS59515.1; -. [Q9UHX1-6]
DR CCDS; CCDS59516.1; -. [Q9UHX1-5]
DR RefSeq; NP_001129505.1; NM_001136033.2. [Q9UHX1-3]
DR RefSeq; NP_001258025.1; NM_001271096.1.
DR RefSeq; NP_001258026.1; NM_001271097.1. [Q9UHX1-6]
DR RefSeq; NP_001258027.1; NM_001271098.1.
DR RefSeq; NP_001258028.1; NM_001271099.1. [Q9UHX1-5]
DR RefSeq; NP_001258029.1; NM_001271100.1. [Q9UHX1-4]
DR RefSeq; NP_055096.2; NM_014281.4. [Q9UHX1-2]
DR RefSeq; NP_510965.1; NM_078480.2. [Q9UHX1-1]
DR RefSeq; XP_016868728.1; XM_017013239.1. [Q9UHX1-3]
DR RefSeq; XP_016868729.1; XM_017013240.1. [Q9UHX1-4]
DR PDB; 2DNY; NMR; -; A=454-559.
DR PDB; 2KXF; NMR; -; A=119-314.
DR PDB; 2KXH; NMR; -; A=119-314.
DR PDB; 2QFJ; X-ray; 2.10 A; A/B=118-316.
DR PDB; 3DXB; X-ray; 2.20 A; A/B/C/D/E/F/G/H=460-559.
DR PDB; 3UE2; X-ray; 1.23 A; A=443-559.
DR PDB; 3US5; X-ray; 1.38 A; A=443-559.
DR PDB; 3UWT; X-ray; 2.50 A; A=118-316.
DR PDB; 5KVY; X-ray; 1.95 A; A/B=118-316.
DR PDB; 5KW1; X-ray; 2.10 A; A/B=118-316.
DR PDB; 5KW6; X-ray; 1.91 A; A/B=118-316.
DR PDB; 5KWQ; X-ray; 2.80 A; A/B=118-316.
DR PDB; 6LUR; X-ray; 2.00 A; A/B/C/D/E/F/G/H=460-559.
DR PDB; 6SLO; X-ray; 1.94 A; A/B/C/D=460-559.
DR PDBsum; 2DNY; -.
DR PDBsum; 2KXF; -.
DR PDBsum; 2KXH; -.
DR PDBsum; 2QFJ; -.
DR PDBsum; 3DXB; -.
DR PDBsum; 3UE2; -.
DR PDBsum; 3US5; -.
DR PDBsum; 3UWT; -.
DR PDBsum; 5KVY; -.
DR PDBsum; 5KW1; -.
DR PDBsum; 5KW6; -.
DR PDBsum; 5KWQ; -.
DR PDBsum; 6LUR; -.
DR PDBsum; 6SLO; -.
DR AlphaFoldDB; Q9UHX1; -.
DR BMRB; Q9UHX1; -.
DR SMR; Q9UHX1; -.
DR BioGRID; 116502; 304.
DR CORUM; Q9UHX1; -.
DR DIP; DIP-34636N; -.
DR ELM; Q9UHX1; -.
DR IntAct; Q9UHX1; 84.
DR MINT; Q9UHX1; -.
DR STRING; 9606.ENSP00000434359; -.
DR GlyGen; Q9UHX1; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q9UHX1; -.
DR MetOSite; Q9UHX1; -.
DR PhosphoSitePlus; Q9UHX1; -.
DR SwissPalm; Q9UHX1; -.
DR BioMuta; PUF60; -.
DR DMDM; 74761960; -.
DR EPD; Q9UHX1; -.
DR jPOST; Q9UHX1; -.
DR MassIVE; Q9UHX1; -.
DR MaxQB; Q9UHX1; -.
DR PaxDb; Q9UHX1; -.
DR PeptideAtlas; Q9UHX1; -.
DR PRIDE; Q9UHX1; -.
DR ProteomicsDB; 84428; -. [Q9UHX1-1]
DR ProteomicsDB; 84429; -. [Q9UHX1-2]
DR ProteomicsDB; 84430; -. [Q9UHX1-3]
DR ProteomicsDB; 84431; -. [Q9UHX1-4]
DR ProteomicsDB; 84432; -. [Q9UHX1-5]
DR ProteomicsDB; 84433; -. [Q9UHX1-6]
DR TopDownProteomics; Q9UHX1-3; -. [Q9UHX1-3]
DR Antibodypedia; 28098; 448 antibodies from 35 providers.
DR DNASU; 22827; -.
DR Ensembl; ENST00000313352.11; ENSP00000322016.7; ENSG00000179950.14. [Q9UHX1-4]
DR Ensembl; ENST00000349157.10; ENSP00000322036.7; ENSG00000179950.14. [Q9UHX1-2]
DR Ensembl; ENST00000453551.6; ENSP00000402953.2; ENSG00000179950.14. [Q9UHX1-3]
DR Ensembl; ENST00000456095.6; ENSP00000395417.2; ENSG00000179950.14. [Q9UHX1-5]
DR Ensembl; ENST00000526683.6; ENSP00000434359.1; ENSG00000179950.14. [Q9UHX1-1]
DR Ensembl; ENST00000527197.5; ENSP00000431960.1; ENSG00000179950.14. [Q9UHX1-6]
DR Ensembl; ENST00000612237.3; ENSP00000478495.1; ENSG00000274081.4. [Q9UHX1-2]
DR Ensembl; ENST00000620341.4; ENSP00000484860.1; ENSG00000274081.4. [Q9UHX1-1]
DR Ensembl; ENST00000620953.2; ENSP00000478209.1; ENSG00000274081.4. [Q9UHX1-5]
DR Ensembl; ENST00000632444.1; ENSP00000487945.1; ENSG00000274081.4. [Q9UHX1-3]
DR Ensembl; ENST00000633206.1; ENSP00000487930.1; ENSG00000274081.4. [Q9UHX1-4]
DR GeneID; 22827; -.
DR KEGG; hsa:22827; -.
DR MANE-Select; ENST00000526683.6; ENSP00000434359.1; NM_078480.3; NP_510965.1.
DR UCSC; uc003yzq.5; human. [Q9UHX1-1]
DR CTD; 22827; -.
DR DisGeNET; 22827; -.
DR GeneCards; PUF60; -.
DR HGNC; HGNC:17042; PUF60.
DR HPA; ENSG00000179950; Low tissue specificity.
DR MalaCards; PUF60; -.
DR MIM; 604819; gene.
DR MIM; 615583; phenotype.
DR neXtProt; NX_Q9UHX1; -.
DR OpenTargets; ENSG00000179950; -.
DR Orphanet; 508488; 8q24.3 microdeletion syndrome.
DR Orphanet; 508498; Intellectual disability-cardiac anomalies-short stature-joint laxity syndrome.
DR PharmGKB; PA162400364; -.
DR VEuPathDB; HostDB:ENSG00000179950; -.
DR eggNOG; KOG0124; Eukaryota.
DR GeneTree; ENSGT00940000155594; -.
DR HOGENOM; CLU_020551_3_1_1; -.
DR InParanoid; Q9UHX1; -.
DR OMA; VHTHKGY; -.
DR OrthoDB; 861359at2759; -.
DR PhylomeDB; Q9UHX1; -.
DR TreeFam; TF313987; -.
DR PathwayCommons; Q9UHX1; -.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR SignaLink; Q9UHX1; -.
DR BioGRID-ORCS; 22827; 811 hits in 1085 CRISPR screens.
DR ChiTaRS; PUF60; human.
DR EvolutionaryTrace; Q9UHX1; -.
DR GeneWiki; PUF60; -.
DR GenomeRNAi; 22827; -.
DR Pharos; Q9UHX1; Tbio.
DR PRO; PR:Q9UHX1; -.
DR Proteomes; UP000005640; Chromosome 8.
DR RNAct; Q9UHX1; protein.
DR Bgee; ENSG00000179950; Expressed in ventricular zone and 98 other tissues.
DR ExpressionAtlas; Q9UHX1; baseline and differential.
DR Genevisible; Q9UHX1; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0042802; F:identical protein binding; IPI:IntAct.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000380; P:alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0006376; P:mRNA splice site selection; IBA:GO_Central.
DR GO; GO:0000381; P:regulation of alternative mRNA splicing, via spliceosome; IBA:GO_Central.
DR CDD; cd12370; RRM1_PUF60; 1.
DR CDD; cd12371; RRM2_PUF60; 1.
DR CDD; cd12648; RRM3_UHM_PUF60; 1.
DR Gene3D; 3.30.70.330; -; 3.
DR InterPro; IPR012677; Nucleotide-bd_a/b_plait_sf.
DR InterPro; IPR006532; PUF60-like.
DR InterPro; IPR034209; PUF60_RRM1.
DR InterPro; IPR034211; PUF60_RRM2.
DR InterPro; IPR034212; PUF60_RRM3.
DR InterPro; IPR035979; RBD_domain_sf.
DR InterPro; IPR000504; RRM_dom.
DR InterPro; IPR003954; RRM_dom_euk.
DR Pfam; PF00076; RRM_1; 2.
DR SMART; SM00360; RRM; 3.
DR SMART; SM00361; RRM_1; 2.
DR SUPFAM; SSF54928; SSF54928; 2.
DR TIGRFAMs; TIGR01645; half-pint; 1.
DR PROSITE; PS50102; RRM; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Apoptosis;
KW Direct protein sequencing; Disease variant; DNA-binding; Isopeptide bond;
KW mRNA processing; mRNA splicing; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Repressor; Ribonucleoprotein; RNA-binding;
KW Transcription; Transcription regulation; Ubl conjugation.
FT CHAIN 1..559
FT /note="Poly(U)-binding-splicing factor PUF60"
FT /id="PRO_0000299519"
FT DOMAIN 129..207
FT /note="RRM 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 226..304
FT /note="RRM 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT DOMAIN 462..549
FT /note="RRM 3; atypical"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00176"
FT REGION 1..516
FT /note="Inhibits homodimerization"
FT REGION 77..559
FT /note="Inhibits transcriptional repression, interaction
FT with ERCC3 and apoptosis induction"
FT REGION 416..437
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 416..436
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 60
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 244
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q3UEB3"
FT MOD_RES 251
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 314
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 454
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT CROSSLNK 43
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 80
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 419
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 458
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..43
FT /note="Missing (in isoform 3 and isoform 4)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_027717"
FT VAR_SEQ 9..37
FT /note="Missing (in isoform 5 and isoform 6)"
FT /evidence="ECO:0000305"
FT /id="VSP_027718"
FT VAR_SEQ 101..117
FT /note="Missing (in isoform 2, isoform 4 and isoform 6)"
FT /evidence="ECO:0000303|PubMed:10882074,
FT ECO:0000303|PubMed:15489334, ECO:0000303|Ref.7"
FT /id="VSP_027719"
FT VARIANT 169
FT /note="H -> Y (in VRJS; loss of function mutation; results
FT in altered dosage of different PUF60 protein forms and
FT abnormal splicing profile of several target genes;
FT dbSNP:rs398123001)"
FT /evidence="ECO:0000269|PubMed:24140112"
FT /id="VAR_070939"
FT CONFLICT 3
FT /note="T -> R (in Ref. 7; AAB41656)"
FT /evidence="ECO:0000305"
FT CONFLICT 123
FT /note="R -> G (in Ref. 7; AAB41656)"
FT /evidence="ECO:0000305"
FT HELIX 118..128
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 130..134
FT /evidence="ECO:0007829|PDB:5KW6"
FT HELIX 142..149
FT /evidence="ECO:0007829|PDB:5KW6"
FT HELIX 150..152
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 155..160
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 164..166
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 171..179
FT /evidence="ECO:0007829|PDB:5KW6"
FT HELIX 180..190
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 194..199
FT /evidence="ECO:0007829|PDB:3UWT"
FT STRAND 201..203
FT /evidence="ECO:0007829|PDB:5KW6"
FT HELIX 206..208
FT /evidence="ECO:0007829|PDB:3UWT"
FT HELIX 209..211
FT /evidence="ECO:0007829|PDB:2QFJ"
FT HELIX 212..222
FT /evidence="ECO:0007829|PDB:5KW6"
FT HELIX 223..225
FT /evidence="ECO:0007829|PDB:2KXH"
FT STRAND 227..231
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:2KXH"
FT HELIX 239..246
FT /evidence="ECO:0007829|PDB:5KW6"
FT HELIX 247..249
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 252..259
FT /evidence="ECO:0007829|PDB:5KW6"
FT TURN 261..263
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 266..276
FT /evidence="ECO:0007829|PDB:5KW6"
FT HELIX 277..287
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 293..296
FT /evidence="ECO:0007829|PDB:2QFJ"
FT STRAND 298..301
FT /evidence="ECO:0007829|PDB:5KW6"
FT STRAND 306..309
FT /evidence="ECO:0007829|PDB:3UWT"
FT HELIX 445..448
FT /evidence="ECO:0007829|PDB:3UE2"
FT TURN 449..452
FT /evidence="ECO:0007829|PDB:3UE2"
FT HELIX 453..459
FT /evidence="ECO:0007829|PDB:3UE2"
FT STRAND 463..468
FT /evidence="ECO:0007829|PDB:3UE2"
FT HELIX 472..474
FT /evidence="ECO:0007829|PDB:3UE2"
FT HELIX 479..487
FT /evidence="ECO:0007829|PDB:3UE2"
FT TURN 488..490
FT /evidence="ECO:0007829|PDB:3UE2"
FT STRAND 493..506
FT /evidence="ECO:0007829|PDB:3UE2"
FT STRAND 510..521
FT /evidence="ECO:0007829|PDB:3UE2"
FT HELIX 522..532
FT /evidence="ECO:0007829|PDB:3UE2"
FT STRAND 536..541
FT /evidence="ECO:0007829|PDB:3DXB"
FT STRAND 543..547
FT /evidence="ECO:0007829|PDB:3UE2"
FT HELIX 549..553
FT /evidence="ECO:0007829|PDB:3UE2"
FT STRAND 557..559
FT /evidence="ECO:0007829|PDB:2DNY"
FT CROSSLNK Q9UHX1-5:14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK Q9UHX1-6:14
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:28112733"
SQ SEQUENCE 559 AA; 59875 MW; 619F3C30D1C5951C CRC64;
MATATIALQV NGQQGGGSEP AAAAAVVAAG DKWKPPQGTD SIKMENGQST AAKLGLPPLT
PEQQEALQKA KKYAMEQSIK SVLVKQTIAH QQQQLTNLQM AAVTMGFGDP LSPLQSMAAQ
RQRALAIMCR VYVGSIYYEL GEDTIRQAFA PFGPIKSIDM SWDSVTMKHK GFAFVEYEVP
EAAQLALEQM NSVMLGGRNI KVGRPSNIGQ AQPIIDQLAE EARAFNRIYV ASVHQDLSDD
DIKSVFEAFG KIKSCTLARD PTTGKHKGYG FIEYEKAQSS QDAVSSMNLF DLGGQYLRVG
KAVTPPMPLL TPATPGGLPP AAAVAAAAAT AKITAQEAVA GAAVLGTLGT PGLVSPALTL
AQPLGTLPQA VMAAQAPGVI TGVTPARPPI PVTIPSVGVV NPILASPPTL GLLEPKKEKE
EEELFPESER PEMLSEQEHM SISGSSARHM VMQKLLRKQE STVMVLRNMV DPKDIDDDLE
GEVTEECGKF GAVNRVIIYQ EKQGEEEDAE IIVKIFVEFS IASETHKAIQ ALNGRWFAGR
KVVAEVYDQE RFDNSDLSA
