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 27-MAR-2024, entry version 201. 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}, ROBPI GN {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. DR RefSeq; XP_016868729.1; XM_017013240.1. 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 PDB; 7Q8A; X-ray; 2.05 A; A/B=114-310. DR PDB; 7Z3X; X-ray; 1.65 A; A/B=114-308. 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 PDBsum; 7Q8A; -. DR PDBsum; 7Z3X; -. DR AlphaFoldDB; Q9UHX1; -. DR BMRB; Q9UHX1; -. DR SMR; Q9UHX1; -. DR BioGRID; 116502; 370. DR CORUM; Q9UHX1; -. DR DIP; DIP-34636N; -. DR ELM; Q9UHX1; -. DR IntAct; Q9UHX1; 90. 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; 9606-ENSP00000434359; -. DR PeptideAtlas; 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 Pumba; Q9UHX1; -. DR TopDownProteomics; Q9UHX1-3; -. [Q9UHX1-3] DR Antibodypedia; 28098; 496 antibodies from 35 providers. DR DNASU; 22827; -. DR Ensembl; ENST00000313352.11; ENSP00000322016.7; ENSG00000179950.15. [Q9UHX1-4] DR Ensembl; ENST00000349157.10; ENSP00000322036.7; ENSG00000179950.15. [Q9UHX1-2] DR Ensembl; ENST00000453551.6; ENSP00000402953.2; ENSG00000179950.15. [Q9UHX1-3] DR Ensembl; ENST00000456095.6; ENSP00000395417.2; ENSG00000179950.15. [Q9UHX1-5] DR Ensembl; ENST00000526683.6; ENSP00000434359.1; ENSG00000179950.15. [Q9UHX1-1] DR Ensembl; ENST00000527197.5; ENSP00000431960.1; ENSG00000179950.15. [Q9UHX1-6] DR Ensembl; ENST00000531951.6; ENSP00000515500.1; ENSG00000179950.15. [Q9UHX1-3] DR Ensembl; ENST00000703846.1; ENSP00000515498.1; ENSG00000179950.15. [Q9UHX1-3] DR Ensembl; ENST00000703849.1; ENSP00000515501.1; ENSG00000179950.15. [Q9UHX1-3] DR Ensembl; ENST00000703866.1; ENSP00000515511.1; ENSG00000179950.15. [Q9UHX1-1] 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 AGR; HGNC:17042; -. 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; 12294at2759; -. DR PhylomeDB; Q9UHX1; -. DR TreeFam; TF313987; -. DR PathwayCommons; Q9UHX1; -. DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway. DR SignaLink; Q9UHX1; -. DR SIGNOR; Q9UHX1; -. DR BioGRID-ORCS; 22827; 843 hits in 1161 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 100 other cell types or tissues. DR ExpressionAtlas; Q9UHX1; baseline and differential. DR GO; GO:0030054; C:cell junction; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:1990904; C:ribonucleoprotein complex; IEA:UniProtKB-KW. 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 recognition; 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 NCBIfam; TIGR01645; half-pint; 1. DR PANTHER; PTHR47330:SF1; POLY(U)-BINDING-SPLICING FACTOR PUF60; 1. DR PANTHER; PTHR47330; POLY(U)-BINDING-SPLICING FACTOR PUF60-B-RELATED; 1. DR Pfam; PF00076; RRM_1; 2. DR SMART; SM00360; RRM; 3. DR SMART; SM00361; RRM_1; 2. DR SUPFAM; SSF54928; RNA-binding domain, RBD; 2. DR PROSITE; PS50102; RRM; 3. DR Genevisible; Q9UHX1; HS. 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 115..128 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 130..134 FT /evidence="ECO:0007829|PDB:7Z3X" FT HELIX 142..149 FT /evidence="ECO:0007829|PDB:7Z3X" FT HELIX 150..152 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 155..160 FT /evidence="ECO:0007829|PDB:7Z3X" FT TURN 164..167 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 173..179 FT /evidence="ECO:0007829|PDB:7Z3X" FT HELIX 180..190 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 194..199 FT /evidence="ECO:0007829|PDB:3UWT" FT STRAND 201..203 FT /evidence="ECO:0007829|PDB:7Z3X" FT HELIX 208..211 FT /evidence="ECO:0007829|PDB:7Z3X" FT HELIX 214..222 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 225..231 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 235..237 FT /evidence="ECO:0007829|PDB:2KXH" FT HELIX 239..246 FT /evidence="ECO:0007829|PDB:7Z3X" FT HELIX 247..249 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 252..259 FT /evidence="ECO:0007829|PDB:7Z3X" FT TURN 261..264 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 266..276 FT /evidence="ECO:0007829|PDB:7Z3X" FT HELIX 277..286 FT /evidence="ECO:0007829|PDB:7Z3X" FT STRAND 293..296 FT /evidence="ECO:0007829|PDB:2QFJ" FT STRAND 298..301 FT /evidence="ECO:0007829|PDB:7Z3X" 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 //