PRP4B_HUMAN
ID PRP4B_HUMAN Reviewed; 1007 AA.
AC Q13523; A8K5C9; Q5D0F6; Q5TAY8; Q8IVC3; Q8TDP2; Q96QT7; Q9UEE6;
DT 15-JUL-1998, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 3.
DT 03-AUG-2022, entry version 222.
DE RecName: Full=Serine/threonine-protein kinase PRP4 homolog;
DE EC=2.7.11.1;
DE AltName: Full=PRP4 kinase;
DE AltName: Full=PRP4 pre-mRNA-processing factor 4 homolog;
GN Name=PRPF4B; Synonyms=KIAA0536, PRP4, PRP4H, PRP4K;
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], CHARACTERIZATION, AND VARIANT VAL-83.
RX PubMed=11418604; DOI=10.1074/jbc.m103790200;
RA Kojima T., Zama T., Wada K., Onogi H., Hagiwara M.;
RT "Cloning of human PRP4 reveals interaction with Clk1.";
RL J. Biol. Chem. 276:32247-32256(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA], AND VARIANT VAL-83.
RX PubMed=12077342; DOI=10.1128/mcb.22.14.5141-5156.2002;
RA Dellaire G., Makarov E.M., Cowger J.J.M., Longman D., Sutherland H.G.E.,
RA Luehrmann R., Torchia J., Bickmore W.A.;
RT "Mammalian PRP4 kinase copurifies and interacts with components of both the
RT U5 snRNP and the N-CoR deacetylase complexes.";
RL Mol. Cell. Biol. 22:5141-5156(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-83.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT VAL-83.
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].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain, and Lung;
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 [8]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 512-1007.
RX PubMed=9102632; DOI=10.1093/nar/25.5.1028;
RA Gross T., Lutzelberger M., Wiegmann H., Klingenhoff A., Shenoy S.,
RA Kaeufer N.F.;
RT "Functional analysis of the fission yeast Prp4 protein kinase involved in
RT pre-mRNA splicing and isolation of a putative mammalian homologue.";
RL Nucleic Acids Res. 25:1028-1035(1997).
RN [9]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN THE SPLICEOSOMAL
RP C COMPLEX.
RX PubMed=11991638; DOI=10.1017/s1355838202021088;
RA Jurica M.S., Licklider L.J., Gygi S.P., Grigorieff N., Moore M.J.;
RT "Purification and characterization of native spliceosomes suitable for
RT three-dimensional structural analysis.";
RL RNA 8:426-439(2002).
RN [10]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=15592455; DOI=10.1038/nbt1046;
RA Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H.,
RA Zha X.-M., Polakiewicz R.D., Comb M.J.;
RT "Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.";
RL Nat. Biotechnol. 23:94-101(2005).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-23; SER-32; SER-87; SER-93;
RP SER-277; SER-366 AND SER-368, VARIANT [LARGE SCALE ANALYSIS] VAL-83, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; TYR-140;
RP SER-142; SER-144; SER-257; SER-277; SER-427; SER-431; SER-437; SER-569;
RP SER-578; SER-580 AND TYR-849, VARIANT [LARGE SCALE ANALYSIS] VAL-83, AND
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, VARIANT [LARGE SCALE ANALYSIS]
RP VAL-83, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], AND
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 [14]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; TYR-140;
RP SER-142; SER-144; SER-518; SER-578 AND SER-580, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [15]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-717, AND IDENTIFICATION BY MASS
RP 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 [16]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-87;
RP SER-93; SER-239; SER-241; SER-257; SER-277; SER-283; SER-366; SER-368;
RP SER-431; SER-518; SER-519; SER-520; SER-565; SER-578; SER-580 AND TYR-849,
RP VARIANT [LARGE SCALE ANALYSIS] VAL-83, AND IDENTIFICATION BY MASS
RP 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 [17]
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 [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-32; SER-87;
RP SER-93; SER-142; SER-144; SER-277; SER-294; SER-328; SER-354; SER-356;
RP SER-366; SER-368; THR-385; SER-387; SER-431; SER-518; SER-519; SER-520;
RP SER-578; SER-580 AND TYR-849, VARIANT [LARGE SCALE ANALYSIS] VAL-83, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [20]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [21]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-20; SER-23; SER-87; SER-93;
RP SER-166; SER-277; SER-292; SER-294; SER-366; SER-368; SER-427; SER-431 AND
RP SER-437, VARIANT [LARGE SCALE ANALYSIS] VAL-83, AND IDENTIFICATION BY MASS
RP 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 [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-131; SER-142; SER-257;
RP SER-277 AND TYR-849, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [23]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117 AND LYS-170, AND
RP IDENTIFICATION BY MASS 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 [24]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25114211; DOI=10.1073/pnas.1413825111;
RA Impens F., Radoshevich L., Cossart P., Ribet D.;
RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by
RT external stimuli.";
RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
RN [25]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-117, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99; LYS-111; LYS-117; LYS-170;
RP LYS-177; LYS-593 AND LYS-659, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [27]
RP VARIANT [LARGE SCALE ANALYSIS] LEU-658.
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., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
RN [28]
RP VARIANTS [LARGE SCALE ANALYSIS] VAL-584 AND LEU-658.
RX PubMed=17344846; DOI=10.1038/nature05610;
RA Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G.,
RA Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S.,
RA Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G.,
RA Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K.,
RA Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D.,
RA Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R.,
RA Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A.,
RA Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F.,
RA Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F.,
RA Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G.,
RA Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R.,
RA Futreal P.A., Stratton M.R.;
RT "Patterns of somatic mutation in human cancer genomes.";
RL Nature 446:153-158(2007).
CC -!- FUNCTION: Has a role in pre-mRNA splicing. Phosphorylates SF2/ASF.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Identified in the spliceosome C complex. Interacts with Clk1
CC C-terminus. {ECO:0000269|PubMed:11991638}.
CC -!- INTERACTION:
CC Q13523; P49407: ARRB1; NbExp=2; IntAct=EBI-395940, EBI-743313;
CC Q13523; P32121: ARRB2; NbExp=3; IntAct=EBI-395940, EBI-714559;
CC Q13523; Q9Y2Y9: KLF13; NbExp=5; IntAct=EBI-395940, EBI-1255893;
CC Q13523; Q9H1D9: POLR3F; NbExp=2; IntAct=EBI-395940, EBI-710067;
CC Q13523; P04590: gag; Xeno; NbExp=6; IntAct=EBI-395940, EBI-780156;
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- PTM: Phosphorylated by Clk1.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. CMGC Ser/Thr
CC protein kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH09844.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=BAA25462.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AY029347; AAK38155.1; -; mRNA.
DR EMBL; AF283465; AAM19101.1; -; mRNA.
DR EMBL; AB011108; BAA25462.1; ALT_INIT; mRNA.
DR EMBL; AK291244; BAF83933.1; -; mRNA.
DR EMBL; AL138831; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL033383; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55146.1; -; Genomic_DNA.
DR EMBL; BC009844; AAH09844.1; ALT_FRAME; mRNA.
DR EMBL; BC034969; AAH34969.1; -; mRNA.
DR EMBL; U48736; AAB03268.1; -; mRNA.
DR CCDS; CCDS4488.1; -.
DR RefSeq; NP_003904.3; NM_003913.4.
DR RefSeq; XP_016866899.1; XM_017011410.1.
DR RefSeq; XP_016866900.1; XM_017011411.1.
DR RefSeq; XP_016866901.1; XM_017011412.1.
DR RefSeq; XP_016866902.1; XM_017011413.1.
DR RefSeq; XP_016866903.1; XM_017011414.1.
DR RefSeq; XP_016866904.1; XM_017011415.1.
DR RefSeq; XP_016866905.1; XM_017011416.1.
DR RefSeq; XP_016866906.1; XM_017011417.1.
DR RefSeq; XP_016866907.1; XM_017011418.1.
DR RefSeq; XP_016866908.1; XM_017011419.1.
DR RefSeq; XP_016866909.1; XM_017011420.1.
DR RefSeq; XP_016866910.1; XM_017011421.1.
DR RefSeq; XP_016866911.1; XM_017011422.1.
DR RefSeq; XP_016866912.1; XM_017011423.1.
DR RefSeq; XP_016866913.1; XM_017011424.1.
DR RefSeq; XP_016866914.1; XM_017011425.1.
DR RefSeq; XP_016866915.1; XM_017011426.1.
DR RefSeq; XP_016866916.1; XM_017011427.1.
DR RefSeq; XP_016866917.1; XM_017011428.1.
DR RefSeq; XP_016866918.1; XM_017011429.1.
DR RefSeq; XP_016866919.1; XM_017011430.1.
DR RefSeq; XP_016866920.1; XM_017011431.1.
DR PDB; 4IAN; X-ray; 2.44 A; A/B=657-1007.
DR PDB; 4IFC; X-ray; 2.13 A; A/B=657-1007.
DR PDB; 4IIR; X-ray; 2.00 A; A/B=657-1007.
DR PDB; 4IJP; X-ray; 2.25 A; A/B=657-1007.
DR PDB; 6CNH; X-ray; 2.00 A; A=657-1005.
DR PDB; 6PJJ; X-ray; 2.40 A; A/B/C/D=657-1005.
DR PDB; 6PK6; X-ray; 2.10 A; A=657-1005.
DR PDB; 6QX9; EM; 3.28 A; K=1-1007.
DR PDBsum; 4IAN; -.
DR PDBsum; 4IFC; -.
DR PDBsum; 4IIR; -.
DR PDBsum; 4IJP; -.
DR PDBsum; 6CNH; -.
DR PDBsum; 6PJJ; -.
DR PDBsum; 6PK6; -.
DR PDBsum; 6QX9; -.
DR AlphaFoldDB; Q13523; -.
DR SMR; Q13523; -.
DR BioGRID; 114416; 258.
DR CORUM; Q13523; -.
DR IntAct; Q13523; 110.
DR MINT; Q13523; -.
DR STRING; 9606.ENSP00000337194; -.
DR BindingDB; Q13523; -.
DR ChEMBL; CHEMBL1908382; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q13523; -.
DR GlyGen; Q13523; 2 sites, 2 O-linked glycans (2 sites).
DR iPTMnet; Q13523; -.
DR MetOSite; Q13523; -.
DR PhosphoSitePlus; Q13523; -.
DR SwissPalm; Q13523; -.
DR BioMuta; PRPF4B; -.
DR DMDM; 317373526; -.
DR EPD; Q13523; -.
DR jPOST; Q13523; -.
DR MassIVE; Q13523; -.
DR MaxQB; Q13523; -.
DR PaxDb; Q13523; -.
DR PeptideAtlas; Q13523; -.
DR PRIDE; Q13523; -.
DR ProteomicsDB; 59518; -.
DR Antibodypedia; 9532; 170 antibodies from 27 providers.
DR DNASU; 8899; -.
DR Ensembl; ENST00000337659.11; ENSP00000337194.6; ENSG00000112739.17.
DR Ensembl; ENST00000480058.5; ENSP00000433547.1; ENSG00000112739.17.
DR GeneID; 8899; -.
DR KEGG; hsa:8899; -.
DR MANE-Select; ENST00000337659.11; ENSP00000337194.6; NM_003913.5; NP_003904.3.
DR UCSC; uc003mvv.4; human.
DR CTD; 8899; -.
DR DisGeNET; 8899; -.
DR GeneCards; PRPF4B; -.
DR HGNC; HGNC:17346; PRPF4B.
DR HPA; ENSG00000112739; Low tissue specificity.
DR MIM; 602338; gene.
DR neXtProt; NX_Q13523; -.
DR OpenTargets; ENSG00000112739; -.
DR PharmGKB; PA38447; -.
DR VEuPathDB; HostDB:ENSG00000112739; -.
DR eggNOG; KOG0670; Eukaryota.
DR GeneTree; ENSGT00940000155562; -.
DR HOGENOM; CLU_000288_5_3_1; -.
DR InParanoid; Q13523; -.
DR OMA; ARFDINF; -.
DR OrthoDB; 915778at2759; -.
DR PhylomeDB; Q13523; -.
DR TreeFam; TF315246; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q13523; -.
DR SignaLink; Q13523; -.
DR SIGNOR; Q13523; -.
DR BioGRID-ORCS; 8899; 348 hits in 1114 CRISPR screens.
DR ChiTaRS; PRPF4B; human.
DR GeneWiki; PRPF4B; -.
DR GenomeRNAi; 8899; -.
DR Pharos; Q13523; Tchem.
DR PRO; PR:Q13523; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q13523; protein.
DR Bgee; ENSG00000112739; Expressed in endothelial cell and 204 other tissues.
DR ExpressionAtlas; Q13523; baseline and differential.
DR Genevisible; Q13523; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0005694; C:chromosome; IEA:Ensembl.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004672; F:protein kinase activity; TAS:ProtInc.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IEA:UniProtKB-KW.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0045292; P:mRNA cis splicing, via spliceosome; IEA:InterPro.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0006468; P:protein phosphorylation; IBA:GO_Central.
DR GO; GO:0008380; P:RNA splicing; TAS:ProtInc.
DR CDD; cd14135; STKc_PRP4; 1.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR InterPro; IPR044092; STKc_PRP4.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; ATP-binding; Isopeptide bond; Kinase;
KW mRNA processing; mRNA splicing; Nucleotide-binding; Nucleus;
KW Phosphoprotein; Reference proteome; Serine/threonine-protein kinase;
KW Spliceosome; Transferase; Ubl conjugation.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT CHAIN 2..1007
FT /note="Serine/threonine-protein kinase PRP4 homolog"
FT /id="PRO_0000086586"
FT DOMAIN 687..1006
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT REGION 1..99
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 140..533
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 559..583
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 10..39
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 40..58
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 81..99
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 144..158
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 159..173
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 182..198
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 199..214
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 228..304
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 311..345
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 346..360
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 361..380
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 398..431
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 441..499
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 500..520
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 561..579
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 815
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 693..701
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 717
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22223895, ECO:0007744|PubMed:22814378"
FT MOD_RES 8
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RKH1"
FT MOD_RES 20
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 23
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 32
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 87
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 93
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 99
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:Q61136"
FT MOD_RES 131
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 140
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332"
FT MOD_RES 142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:21406692"
FT MOD_RES 166
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 239
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 241
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 257
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:24275569"
FT MOD_RES 277
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 283
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 292
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 328
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 354
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 356
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 366
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 368
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 385
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 427
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 431
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 437
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 518
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT MOD_RES 519
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 520
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 565
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 569
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 578
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 580
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692"
FT MOD_RES 717
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 849
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 852
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q5RKH1"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 111
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 117
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:28112733"
FT CROSSLNK 170
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 177
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 593
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 659
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VARIANT 83
FT /note="I -> V (in dbSNP:rs9503893)"
FT /evidence="ECO:0000269|PubMed:11418604,
FT ECO:0000269|PubMed:12077342, ECO:0000269|PubMed:14702039,
FT ECO:0000269|PubMed:9628581, ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT /id="VAR_046969"
FT VARIANT 584
FT /note="I -> V (in dbSNP:rs56267049)"
FT /evidence="ECO:0000269|PubMed:17344846"
FT /id="VAR_047798"
FT VARIANT 658
FT /note="F -> L (in a breast cancer sample; somatic mutation;
FT dbSNP:rs1230491406)"
FT /evidence="ECO:0000269|PubMed:16959974,
FT ECO:0000269|PubMed:17344846"
FT /id="VAR_035633"
FT CONFLICT 468
FT /note="P -> T (in Ref. 7; AAH34969)"
FT /evidence="ECO:0000305"
FT CONFLICT 610
FT /note="K -> R (in Ref. 4; BAF83933)"
FT /evidence="ECO:0000305"
FT CONFLICT 754
FT /note="F -> L (in Ref. 7; AAH34969)"
FT /evidence="ECO:0000305"
FT CONFLICT 851
FT /note="V -> F (in Ref. 7; AAH34969)"
FT /evidence="ECO:0000305"
FT STRAND 671..673
FT /evidence="ECO:0007829|PDB:4IIR"
FT TURN 684..686
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 687..694
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 697..699
FT /evidence="ECO:0007829|PDB:4IJP"
FT STRAND 700..706
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 707..709
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 713..718
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 724..742
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 753..759
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 762..767
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 774..781
FT /evidence="ECO:0007829|PDB:4IIR"
FT TURN 783..785
FT /evidence="ECO:0007829|PDB:6CNH"
FT HELIX 789..808
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 818..820
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 821..823
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 830..832
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 839..842
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 853..855
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 858..862
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 869..884
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 894..905
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 910..915
FT /evidence="ECO:0007829|PDB:4IIR"
FT TURN 920..922
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 929..932
FT /evidence="ECO:0007829|PDB:4IIR"
FT STRAND 936..939
FT /evidence="ECO:0007829|PDB:6PK6"
FT STRAND 943..947
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 955..959
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 967..983
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 988..990
FT /evidence="ECO:0007829|PDB:6CNH"
FT HELIX 994..998
FT /evidence="ECO:0007829|PDB:4IIR"
FT HELIX 1001..1004
FT /evidence="ECO:0007829|PDB:4IIR"
SQ SEQUENCE 1007 AA; 116987 MW; EC8C1538A61EDA78 CRC64;
MAAAETQSLR EQPEMEDANS EKSINEENGE VSEDQSQNKH SRHKKKKHKH RSKHKKHKHS
SEEDKDKKHK HKHKHKKHKR KEIIDASDKE GMSPAKRTKL DDLALLEDLE KQRALIKAEL
DNELMEGKVQ SGMGLILQGY ESGSEEEGEI HEKARNGNRS STRSSSTKGK LELVDNKITT
KKRSKSRSKE RTRHRSDKKK SKGGIEIVKE KTTRSKSKER KKSKSPSKRS KSQDQARKSK
SPTLRRRSQE KIGKARSPTD DKVKIEDKSK SKDRKKSPII NESRSRDRGK KSRSPVDLRG
KSKDRRSRSK ERKSKRSETD KEKKPIKSPS KDASSGKENR SPSRRPGRSP KRRSLSPKPR
DKSRRSRSPL LNDRRSKQSK SPSRTLSPGR RAKSRSLERK RREPERRRLS SPRTRPRDDI
LSRRERSKDA SPINRWSPTR RRSRSPIRRR SRSPLRRSRS PRRRSRSPRR RDRGRRSRSR
LRRRSRSRGG RRRRSRSKVK EDKFKGSLSE GMKVEQESSS DDNLEDFDVE EEDEEALIEQ
RRIQRQAIVQ KYKYLAEDSN MSVPSEPSSP QSSTRTRSPS PDDILERVAA DVKEYERENV
DTFEASVKAK HNLMTVEQNN GSSQKKLLAP DMFTESDDMF AAYFDSARLR AAGIGKDFKE
NPNLRDNWTD AEGYYRVNIG EVLDKRYNVY GYTGQGVFSN VVRARDNARA NQEVAVKIIR
NNELMQKTGL KELEFLKKLN DADPDDKFHC LRLFRHFYHK QHLCLVFEPL SMNLREVLKK
YGKDVGLHIK AVRSYSQQLF LALKLLKRCN ILHADIKPDN ILVNESKTIL KLCDFGSASH
VADNDITPYL VSRFYRAPEI IIGKSYDYGI DMWSVGCTLY ELYTGKILFP GKTNNHMLKL
AMDLKGKMPN KMIRKGVFKD QHFDQNLNFM YIEVDKVTER EKVTVMSTIN PTKDLLADLI
GCQRLPEDQR KKVHQLKDLL DQILMLDPAK RISINQALQH AFIQEKI
