HNRPK_HUMAN
ID HNRPK_HUMAN Reviewed; 463 AA.
AC P61978; Q07244; Q15671; Q59F98; Q5T6W4; Q60577; Q6IBN1; Q922Y7; Q96J62;
DT 07-JUN-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-JUN-2004, sequence version 1.
DT 03-AUG-2022, entry version 209.
DE RecName: Full=Heterogeneous nuclear ribonucleoprotein K;
DE Short=hnRNP K;
DE AltName: Full=Transformation up-regulated nuclear protein;
DE Short=TUNP;
GN Name=HNRNPK; Synonyms=HNRPK;
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 1), AND SUBCELLULAR LOCATION.
RX PubMed=1729596; DOI=10.1128/mcb.12.1.164-171.1992;
RA Matunis M.J., Michael W.M., Dreyfuss G.;
RT "Characterization and primary structure of the poly(C)-binding
RT heterogeneous nuclear ribonucleoprotein complex K protein.";
RL Mol. Cell. Biol. 12:164-171(1992).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND PHOSPHORYLATION.
RX PubMed=8107114; DOI=10.1006/jmbi.1994.1116;
RA Dejgaard K., Leffers H., Rasmussen H.H., Madsen P., Kruse T.A., Gesser B.,
RA Nielsen H., Celis J.E.;
RT "Identification, molecular cloning, expression and chromosome mapping of a
RT family of transformation upregulated hnRNP-K proteins derived by
RT alternative splicing.";
RL J. Mol. Biol. 236:33-48(1994).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
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 3).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Tongue;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y.,
RA Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A.,
RA Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y.,
RA Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T.,
RA Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y.,
RA Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S.,
RA Nomura N.;
RT "Human protein factory for converting the transcriptome into an in vitro-
RT expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15164053; DOI=10.1038/nature02465;
RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA Dunham I.;
RT "DNA sequence and analysis of human chromosome 9.";
RL Nature 429:369-374(2004).
RN [8]
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 [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Muscle;
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 [10]
RP PROTEIN SEQUENCE OF 1-52; 70-103; 149-163; 192-201; 208-219; 317-325;
RP 378-405 AND 423-456, ACETYLATION AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Lung carcinoma;
RA Bienvenut W.V., Vousden K.H., Lukashchuk N.;
RL Submitted (MAR-2008) to UniProtKB.
RN [11]
RP PROTEIN SEQUENCE OF 38-46; 149-163; 208-219; 306-316 AND 378-396, AND
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Brain, Cajal-Retzius cell, and Fetal brain cortex;
RA Lubec G., Afjehi-Sadat L., Chen W.-Q., Sun Y.;
RL Submitted (DEC-2008) to UniProtKB.
RN [12]
RP INTERACTION WITH HCV CORE PROTEIN (MICROBIAL INFECTION).
RX PubMed=9651361; DOI=10.1074/jbc.273.28.17651;
RA Hsieh T.-Y., Matsumoto M., Chou H.-C., Schneider R., Hwang S.B., Lee A.S.,
RA Lai M.M.C.;
RT "Hepatitis C virus core protein interacts with heterogeneous nuclear
RT ribonucleoprotein K.";
RL J. Biol. Chem. 273:17651-17659(1998).
RN [13]
RP INTERACTION WITH DDX1.
RX PubMed=12183465; DOI=10.1074/jbc.m206981200;
RA Chen H.C., Lin W.C., Tsay Y.G., Lee S.C., Chang C.J.;
RT "An RNA helicase, DDX1, interacting with poly(A) RNA and heterogeneous
RT nuclear ribonucleoprotein K.";
RL J. Biol. Chem. 277:40403-40409(2002).
RN [14]
RP MASS SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=11840567;
RX DOI=10.1002/1615-9861(200202)2:2<212::aid-prot212>3.0.co;2-h;
RA Harris R.A., Yang A., Stein R.C., Lucy K., Brusten L., Herath A.,
RA Parekh R., Waterfield M.D., O'Hare M.J., Neville M.A., Page M.J.,
RA Zvelebil M.J.;
RT "Cluster analysis of an extensive human breast cancer cell line protein
RT expression map database.";
RL Proteomics 2:212-223(2002).
RN [15]
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 [16]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
RN [17]
RP FUNCTION, INTERACTION WITH MDM2 AND TP53, SUBCELLULAR LOCATION,
RP UBIQUITINATION, AND INDUCTION.
RX PubMed=16360036; DOI=10.1016/j.cell.2005.09.032;
RA Moumen A., Masterson P., O'Connor M.J., Jackson S.P.;
RT "hnRNP K: an HDM2 target and transcriptional coactivator of p53 in response
RT to DNA damage.";
RL Cell 123:1065-1078(2005).
RN [18]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-284, AND IDENTIFICATION BY
RP 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 [19]
RP INTERACTION WITH ANKRD28, AND PHOSPHORYLATION AT SER-284.
RX PubMed=16564677; DOI=10.1016/j.cellsig.2006.01.019;
RA Kwiek N.C., Thacker D.F., Datto M.B., Megosh H.B., Haystead T.A.J.;
RT "PITK, a PP1 targeting subunit that modulates the phosphorylation of the
RT transcriptional regulator hnRNP K.";
RL Cell. Signal. 18:1769-1778(2006).
RN [20]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND SER-379, AND
RP IDENTIFICATION BY 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 [21]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [22]
RP INTERACTION WITH ASFV PROTEIN P30, AND SUBCELLULAR LOCATION.
RX PubMed=18775702; DOI=10.1016/j.febslet.2008.08.031;
RA Hernaez B., Escribano J.M., Alonso C.;
RT "African swine fever virus protein p30 interaction with heterogeneous
RT nuclear ribonucleoprotein K (hnRNP-K) during infection.";
RL FEBS Lett. 582:3275-3280(2008).
RN [23]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-116; SER-216 AND SER-284, 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 [25]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP 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 [26]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216 AND TYR-380, AND
RP IDENTIFICATION BY MASS 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 [27]
RP FUNCTION.
RX PubMed=20673990; DOI=10.1016/j.cell.2010.06.040;
RA Huarte M., Guttman M., Feldser D., Garber M., Koziol M.J.,
RA Kenzelmann-Broz D., Khalil A.M., Zuk O., Amit I., Rabani M., Attardi L.D.,
RA Regev A., Lander E.S., Jacks T., Rinn J.L.;
RT "A large intergenic noncoding RNA induced by p53 mediates global gene
RT repression in the p53 response.";
RL Cell 142:409-419(2010).
RN [28]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-216; SER-284 AND SER-379, 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 [29]
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 [30]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-214; SER-216; SER-284 AND
RP SER-379, AND 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 [31]
RP GLYCOSYLATION.
RX PubMed=22967762; DOI=10.1016/j.bbagen.2012.08.024;
RA Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F.,
RA Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.;
RT "Characterization of O-GlcNAc cycling and proteomic identification of
RT differentially O-GlcNAcylated proteins during G1/S transition.";
RL Biochim. Biophys. Acta 1820:1839-1848(2012).
RN [32]
RP SUBCELLULAR LOCATION.
RX PubMed=22721921; DOI=10.1016/j.ejcb.2012.05.005;
RA Cervero P., Himmel M., Kruger M., Linder S.;
RT "Proteomic analysis of podosome fractions from macrophages reveals
RT similarities to spreading initiation centres.";
RL Eur. J. Cell Biol. 91:908-922(2012).
RN [33]
RP FUNCTION, SUMOYLATION AT LYS-422, UBIQUITINATION, AND MUTAGENESIS OF
RP LYS-422 AND ASP-424.
RX PubMed=22825850; DOI=10.1074/jbc.m112.390120;
RA Pelisch F., Pozzi B., Risso G., Munoz M.J., Srebrow A.;
RT "DNA damage-induced heterogeneous nuclear ribonucleoprotein K SUMOylation
RT regulates p53 transcriptional activation.";
RL J. Biol. Chem. 287:30789-30799(2012).
RN [34]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [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 [35]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-36; SER-75; SER-216; SER-284;
RP SER-379 AND SER-420, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP 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 [36]
RP INTERACTION WITH IVNS1ABP.
RX PubMed=23825951; DOI=10.1371/journal.ppat.1003460;
RA Tsai P.L., Chiou N.T., Kuss S., Garcia-Sastre A., Lynch K.W.,
RA Fontoura B.M.;
RT "Cellular RNA binding proteins NS1-BP and hnRNP K regulate influenza A
RT virus RNA splicing.";
RL PLoS Pathog. 9:E1003460-E1003460(2013).
RN [37]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-75; SER-116 AND SER-284, AND
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 [38]
RP METHYLATION [LARGE SCALE ANALYSIS] AT ARG-316, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [39]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-405 AND LYS-422, 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 [40]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-163 AND LYS-422, AND
RP IDENTIFICATION BY MASS 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 [41]
RP INTERACTION WITH PPIA.
RX PubMed=25678563; DOI=10.1093/brain/awv005;
RA Lauranzano E., Pozzi S., Pasetto L., Stucchi R., Massignan T., Paolella K.,
RA Mombrini M., Nardo G., Lunetta C., Corbo M., Mora G., Bendotti C.,
RA Bonetto V.;
RT "Peptidylprolyl isomerase A governs TARDBP function and assembly in
RT heterogeneous nuclear ribonucleoprotein complexes.";
RL Brain 138:974-991(2015).
RN [42]
RP INVOLVEMENT IN AUKS.
RX PubMed=26173930; DOI=10.1002/humu.22837;
RA Au P.Y., You J., Caluseriu O., Schwartzentruber J., Majewski J.,
RA Bernier F.P., Ferguson M., Valle D., Parboosingh J.S., Sobreira N.,
RA Innes A.M., Kline A.D.;
RT "GeneMatcher aids in the identification of a new malformation syndrome with
RT intellectual disability, unique facial dysmorphisms, and skeletal and
RT connective tissue abnormalities caused by de novo variants in HNRNPK.";
RL Hum. Mutat. 36:1009-1014(2015).
RN [43]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-422, 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 [44]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [45]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-34; LYS-52; LYS-60; LYS-163;
RP LYS-219; LYS-405 AND LYS-422, 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 [46]
RP FUNCTION, AND SUBUNIT.
RX PubMed=33174841; DOI=10.7554/elife.58478;
RA Hollensen A.K., Thomsen H.S., Lloret-Llinares M., Kamstrup A.B.,
RA Jensen J.M., Luckmann M., Birkmose N., Palmfeldt J., Jensen T.H.,
RA Hansen T.B., Damgaard C.K.;
RT "circZNF827 nucleates a transcription inhibitory complex to balance
RT neuronal differentiation.";
RL Elife 9:0-0(2020).
RN [47]
RP STRUCTURE BY NMR OF 375-463.
RX PubMed=10369774; DOI=10.1006/jmbi.1999.2818;
RA Baber J.L., Libutti D., Levens D., Tjandra N.;
RT "High precision solution structure of the C-terminal KH domain of
RT heterogeneous nuclear ribonucleoprotein K, a c-myc transcription factor.";
RL J. Mol. Biol. 289:949-962(1999).
RN [48]
RP STRUCTURE BY NMR OF 379-463 IN COMPLEX WITH SINGLE-STRANDED DNA.
RX PubMed=12093748; DOI=10.1093/emboj/cdf352;
RA Braddock D.T., Baber J.L., Levens D., Clore G.M.;
RT "Molecular basis of sequence-specific single-stranded DNA recognition by KH
RT domains: solution structure of a complex between hnRNP K KH3 and single-
RT stranded DNA.";
RL EMBO J. 21:3476-3485(2002).
CC -!- FUNCTION: One of the major pre-mRNA-binding proteins. Binds tenaciously
CC to poly(C) sequences. Likely to play a role in the nuclear metabolism
CC of hnRNAs, particularly for pre-mRNAs that contain cytidine-rich
CC sequences. Can also bind poly(C) single-stranded DNA. Plays an
CC important role in p53/TP53 response to DNA damage, acting at the level
CC of both transcription activation and repression. When sumoylated, acts
CC as a transcriptional coactivator of p53/TP53, playing a role in
CC p21/CDKN1A and 14-3-3 sigma/SFN induction (By similarity). As far as
CC transcription repression is concerned, acts by interacting with long
CC intergenic RNA p21 (lincRNA-p21), a non-coding RNA induced by p53/TP53.
CC This interaction is necessary for the induction of apoptosis, but not
CC cell cycle arrest. As part of a ribonucleoprotein complex composed at
CC least of ZNF827, HNRNPL and the circular RNA circZNF827 that nucleates
CC the complex on chromatin, may negatively regulate the transcription of
CC genes involved in neuronal differentiation (PubMed:33174841).
CC {ECO:0000250, ECO:0000269|PubMed:16360036, ECO:0000269|PubMed:20673990,
CC ECO:0000269|PubMed:22825850, ECO:0000269|PubMed:33174841}.
CC -!- SUBUNIT: Interacts with RBM42 and ZIK1 (By similarity). Interacts with
CC BRDT (By similarity). Identified in the spliceosome C complex
CC (PubMed:11991638). Interacts with ANKRD28 (PubMed:16564677). Interacts
CC with ASFV p30 protein (PubMed:18775702). Interacts with DDX1
CC (PubMed:12183465). Interacts with MDM2; this interaction leads to
CC ubiquitination and proteasomal degradation (PubMed:16360036). Interacts
CC with p53/TP53 (PubMed:16360036). Interacts with IVNS1ABP
CC (PubMed:23825951). Interacts with PPIA/CYPA (PubMed:25678563). Part of
CC a transcription inhibitory ribonucleoprotein complex composed at least
CC of the circular RNA circZNF827, ZNF827 and HNRNPL (PubMed:33174841).
CC {ECO:0000250|UniProtKB:P61979, ECO:0000250|UniProtKB:P61980,
CC ECO:0000269|PubMed:11991638, ECO:0000269|PubMed:12093748,
CC ECO:0000269|PubMed:12183465, ECO:0000269|PubMed:16360036,
CC ECO:0000269|PubMed:16564677, ECO:0000269|PubMed:18775702,
CC ECO:0000269|PubMed:23825951, ECO:0000269|PubMed:25678563,
CC ECO:0000269|PubMed:33174841}.
CC -!- SUBUNIT: (Microbial infection) Interacts with HCV core protein
CC (PubMed:9651361). {ECO:0000269|PubMed:9651361}.
CC -!- INTERACTION:
CC P61978; Q9NYB9: ABI2; NbExp=6; IntAct=EBI-304185, EBI-743598;
CC P61978; P07550: ADRB2; NbExp=2; IntAct=EBI-304185, EBI-491169;
CC P61978; P55064: AQP5; NbExp=3; IntAct=EBI-304185, EBI-746103;
CC P61978; Q9UBB4: ATXN10; NbExp=3; IntAct=EBI-304185, EBI-702390;
CC P61978; O14965: AURKA; NbExp=2; IntAct=EBI-304185, EBI-448680;
CC P61978; Q5I0X4: C6orf226; NbExp=7; IntAct=EBI-304185, EBI-10244057;
CC P61978; Q14011: CIRBP; NbExp=9; IntAct=EBI-304185, EBI-538850;
CC P61978; Q5D0E6: DALRD3; NbExp=3; IntAct=EBI-304185, EBI-2871865;
CC P61978; P09172: DBH; NbExp=3; IntAct=EBI-304185, EBI-8589586;
CC P61978; Q92608: DOCK2; NbExp=6; IntAct=EBI-304185, EBI-448771;
CC P61978; Q96D16: FBXL18; NbExp=6; IntAct=EBI-304185, EBI-744419;
CC P61978; P14136: GFAP; NbExp=3; IntAct=EBI-304185, EBI-744302;
CC P61978; P62993: GRB2; NbExp=10; IntAct=EBI-304185, EBI-401755;
CC P61978; P61978: HNRNPK; NbExp=4; IntAct=EBI-304185, EBI-304185;
CC P61978; P14866: HNRNPL; NbExp=4; IntAct=EBI-304185, EBI-719024;
CC P61978; Q8WVV9: HNRNPLL; NbExp=9; IntAct=EBI-304185, EBI-535849;
CC P61978; Q00839: HNRNPU; NbExp=2; IntAct=EBI-304185, EBI-351126;
CC P61978; P42858: HTT; NbExp=12; IntAct=EBI-304185, EBI-466029;
CC P61978; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-304185, EBI-1055254;
CC P61978; Q07666: KHDRBS1; NbExp=3; IntAct=EBI-304185, EBI-1364;
CC P61978; Q6IPE9: MARK4; NbExp=6; IntAct=EBI-304185, EBI-10250211;
CC P61978; P43243: MATR3; NbExp=4; IntAct=EBI-304185, EBI-352602;
CC P61978; Q00987: MDM2; NbExp=2; IntAct=EBI-304185, EBI-389668;
CC P61978; P19404: NDUFV2; NbExp=3; IntAct=EBI-304185, EBI-713665;
CC P61978; P29474: NOS3; NbExp=3; IntAct=EBI-304185, EBI-1391623;
CC P61978; Q9Y5E9: PCDHB14; NbExp=6; IntAct=EBI-304185, EBI-10329013;
CC P61978; Q99873: PRMT1; NbExp=3; IntAct=EBI-304185, EBI-78738;
CC P61978; Q8WWY3: PRPF31; NbExp=6; IntAct=EBI-304185, EBI-1567797;
CC P61978; P79522: PRR3; NbExp=7; IntAct=EBI-304185, EBI-2803328;
CC P61978; Q96PU8: QKI; NbExp=7; IntAct=EBI-304185, EBI-945792;
CC P61978; Q9Y272: RASD1; NbExp=6; IntAct=EBI-304185, EBI-740818;
CC P61978; Q96PK6: RBM14; NbExp=3; IntAct=EBI-304185, EBI-954272;
CC P61978; P98179: RBM3; NbExp=6; IntAct=EBI-304185, EBI-2949699;
CC P61978; Q9BTD8: RBM42; NbExp=3; IntAct=EBI-304185, EBI-746862;
CC P61978; P38159: RBMX; NbExp=11; IntAct=EBI-304185, EBI-743526;
CC P61978; P0DJD3: RBMY1A1; NbExp=3; IntAct=EBI-304185, EBI-8638511;
CC P61978; Q15415: RBMY1J; NbExp=4; IntAct=EBI-304185, EBI-8642021;
CC P61978; Q14D33: RTP5; NbExp=3; IntAct=EBI-304185, EBI-10217913;
CC P61978; P09012: SNRPA; NbExp=4; IntAct=EBI-304185, EBI-607085;
CC P61978; O60504: SORBS3; NbExp=4; IntAct=EBI-304185, EBI-741237;
CC P61978; Q9UQ90: SPG7; NbExp=6; IntAct=EBI-304185, EBI-717201;
CC P61978; P12931: SRC; NbExp=6; IntAct=EBI-304185, EBI-621482;
CC P61978; Q13148: TARDBP; NbExp=3; IntAct=EBI-304185, EBI-372899;
CC P61978; Q9NYB0: TERF2IP; NbExp=2; IntAct=EBI-304185, EBI-750109;
CC P61978; P04637: TP53; NbExp=2; IntAct=EBI-304185, EBI-366083;
CC P61978; Q9H3D4: TP63; NbExp=2; IntAct=EBI-304185, EBI-2337775;
CC P61978; P29597: TYK2; NbExp=4; IntAct=EBI-304185, EBI-1383454;
CC P61978; Q01081: U2AF1; NbExp=4; IntAct=EBI-304185, EBI-632461;
CC P61978; Q96MU7: YTHDC1; NbExp=4; IntAct=EBI-304185, EBI-2849854;
CC P61978; G3V1X1: ZFC3H1; NbExp=3; IntAct=EBI-304185, EBI-6448783;
CC P61978; Q66K41: ZNF385C; NbExp=7; IntAct=EBI-304185, EBI-8651919;
CC P61978; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-304185, EBI-16429014;
CC P61978; Q3KQV3: ZNF792; NbExp=3; IntAct=EBI-304185, EBI-10240849;
CC P61978; Q8N9J2; NbExp=6; IntAct=EBI-304185, EBI-10268244;
CC P61978; Q8V1E7: C'204L; Xeno; NbExp=5; IntAct=EBI-304185, EBI-8068745;
CC P61978; Q8AZK7: EBNA-LP; Xeno; NbExp=2; IntAct=EBI-304185, EBI-1185167;
CC P61978; PRO_0000037666 [P29846]; Xeno; NbExp=9; IntAct=EBI-304185, EBI-8847394;
CC P61978-1; P61978-1: HNRNPK; NbExp=3; IntAct=EBI-431928, EBI-431928;
CC P61978-2; Q8IZP0-5: ABI1; NbExp=3; IntAct=EBI-7060731, EBI-11743294;
CC P61978-2; Q9NYB9-2: ABI2; NbExp=6; IntAct=EBI-7060731, EBI-11096309;
CC P61978-2; P41238: APOBEC1; NbExp=3; IntAct=EBI-7060731, EBI-12819523;
CC P61978-2; Q9NRW3: APOBEC3C; NbExp=3; IntAct=EBI-7060731, EBI-1044593;
CC P61978-2; Q14011: CIRBP; NbExp=3; IntAct=EBI-7060731, EBI-538850;
CC P61978-2; Q8NE01: CNNM3; NbExp=3; IntAct=EBI-7060731, EBI-741032;
CC P61978-2; Q92608: DOCK2; NbExp=3; IntAct=EBI-7060731, EBI-448771;
CC P61978-2; Q9NVF9: ETNK2; NbExp=3; IntAct=EBI-7060731, EBI-751864;
CC P61978-2; Q9NU39: FOXD4L1; NbExp=5; IntAct=EBI-7060731, EBI-11320806;
CC P61978-2; Q6VB84: FOXD4L3; NbExp=3; IntAct=EBI-7060731, EBI-11961494;
CC P61978-2; P02008: HBZ; NbExp=3; IntAct=EBI-7060731, EBI-719843;
CC P61978-2; P61978-2: HNRNPK; NbExp=5; IntAct=EBI-7060731, EBI-7060731;
CC P61978-2; Q8WVV9: HNRNPLL; NbExp=6; IntAct=EBI-7060731, EBI-535849;
CC P61978-2; Q6NXR0: IRGC; NbExp=3; IntAct=EBI-7060731, EBI-12021374;
CC P61978-2; Q6ZWB6: KCTD8; NbExp=3; IntAct=EBI-7060731, EBI-6426198;
CC P61978-2; Q5VWX1: KHDRBS2; NbExp=4; IntAct=EBI-7060731, EBI-742808;
CC P61978-2; O75525: KHDRBS3; NbExp=3; IntAct=EBI-7060731, EBI-722504;
CC P61978-2; Q13351: KLF1; NbExp=3; IntAct=EBI-7060731, EBI-8284732;
CC P61978-2; P36507: MAP2K2; NbExp=3; IntAct=EBI-7060731, EBI-1056930;
CC P61978-2; P43243: MATR3; NbExp=4; IntAct=EBI-7060731, EBI-352602;
CC P61978-2; Q8IVT4: MGC50722; NbExp=3; IntAct=EBI-7060731, EBI-14086479;
CC P61978-2; Q8IVT2: MISP; NbExp=3; IntAct=EBI-7060731, EBI-2555085;
CC P61978-2; Q9BYD2: MRPL9; NbExp=3; IntAct=EBI-7060731, EBI-726059;
CC P61978-2; Q86VE0: MYPOP; NbExp=3; IntAct=EBI-7060731, EBI-2858213;
CC P61978-2; A8MTQ0: NOTO; NbExp=3; IntAct=EBI-7060731, EBI-17490746;
CC P61978-2; Q9NQX5: NPDC1; NbExp=5; IntAct=EBI-7060731, EBI-748927;
CC P61978-2; Q9Y5E9: PCDHB14; NbExp=3; IntAct=EBI-7060731, EBI-10329013;
CC P61978-2; Q9HCN3: PGAP6; NbExp=3; IntAct=EBI-7060731, EBI-10310808;
CC P61978-2; Q8WWY3: PRPF31; NbExp=8; IntAct=EBI-7060731, EBI-1567797;
CC P61978-2; P79522: PRR3; NbExp=5; IntAct=EBI-7060731, EBI-2803328;
CC P61978-2; Q96PU8: QKI; NbExp=3; IntAct=EBI-7060731, EBI-945792;
CC P61978-2; Q9BTL3: RAMAC; NbExp=5; IntAct=EBI-7060731, EBI-744023;
CC P61978-2; Q86YV0: RASAL3; NbExp=3; IntAct=EBI-7060731, EBI-3437896;
CC P61978-2; Q9Y272: RASD1; NbExp=3; IntAct=EBI-7060731, EBI-740818;
CC P61978-2; Q96PK6: RBM14; NbExp=4; IntAct=EBI-7060731, EBI-954272;
CC P61978-2; P98179: RBM3; NbExp=3; IntAct=EBI-7060731, EBI-2949699;
CC P61978-2; P38159: RBMX; NbExp=8; IntAct=EBI-7060731, EBI-743526;
CC P61978-2; P0DJD3-2: RBMY1A1; NbExp=3; IntAct=EBI-7060731, EBI-11994018;
CC P61978-2; Q15415: RBMY1J; NbExp=3; IntAct=EBI-7060731, EBI-8642021;
CC P61978-2; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-7060731, EBI-11987469;
CC P61978-2; P78317: RNF4; NbExp=3; IntAct=EBI-7060731, EBI-2340927;
CC P61978-2; Q9UNE2: RPH3AL; NbExp=3; IntAct=EBI-7060731, EBI-2855824;
CC P61978-2; Q14D33: RTP5; NbExp=5; IntAct=EBI-7060731, EBI-10217913;
CC P61978-2; P09012: SNRPA; NbExp=3; IntAct=EBI-7060731, EBI-607085;
CC P61978-2; O60504: SORBS3; NbExp=3; IntAct=EBI-7060731, EBI-741237;
CC P61978-2; Q9UQ90: SPG7; NbExp=3; IntAct=EBI-7060731, EBI-717201;
CC P61978-2; P84103: SRSF3; NbExp=3; IntAct=EBI-7060731, EBI-372557;
CC P61978-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-7060731, EBI-372899;
CC P61978-2; Q7RTU1: TCF23; NbExp=3; IntAct=EBI-7060731, EBI-12127592;
CC P61978-2; P07101-3: TH; NbExp=3; IntAct=EBI-7060731, EBI-12001016;
CC P61978-2; Q08117-2: TLE5; NbExp=5; IntAct=EBI-7060731, EBI-11741437;
CC P61978-2; P04637: TP53; NbExp=2; IntAct=EBI-7060731, EBI-366083;
CC P61978-2; P29597: TYK2; NbExp=3; IntAct=EBI-7060731, EBI-1383454;
CC P61978-2; Q7KZS0: UBE2I; NbExp=3; IntAct=EBI-7060731, EBI-10180829;
CC P61978-2; Q96MU7: YTHDC1; NbExp=3; IntAct=EBI-7060731, EBI-2849854;
CC P61978-2; Q9H9D4: ZNF408; NbExp=3; IntAct=EBI-7060731, EBI-347633;
CC P61978-2; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-7060731, EBI-11035148;
CC P61978-2; Q86XF7: ZNF575; NbExp=5; IntAct=EBI-7060731, EBI-14069183;
CC P61978-2; A0A0S2Z5X4: ZNF688; NbExp=3; IntAct=EBI-7060731, EBI-16429014;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:1729596}. Nucleus,
CC nucleoplasm {ECO:0000269|PubMed:16360036, ECO:0000269|PubMed:1729596,
CC ECO:0000269|PubMed:18775702, ECO:0000269|PubMed:22721921}. Cell
CC projection, podosome {ECO:0000269|PubMed:22721921}. Note=Recruited to
CC p53/TP53-responsive promoters, in the presence of functional p53/TP53
CC (PubMed:16360036). In case of ASFV infection, there is a shift in the
CC localization which becomes predominantly nuclear (PubMed:18775702).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=P61978-1, Q07244-1;
CC Sequence=Displayed;
CC Name=2;
CC IsoId=P61978-2, Q07244-2;
CC Sequence=VSP_002822;
CC Name=3;
CC IsoId=P61978-3; Sequence=VSP_021669, VSP_002822;
CC -!- INDUCTION: By DNA damage, including ionizing radiations and phleomycin
CC treatment or UV irradiation. This induction requires ATM kinase
CC activity (ionizing radiations and phleomycin) or ATR activity (UV
CC irradiation). Up-regulation is due to protein stabilization.
CC Constitutive protein levels are controlled by MDM2-mediated
CC ubiquitination and degradation via the proteasome pathway.
CC {ECO:0000269|PubMed:16360036}.
CC -!- PTM: Arg-296 and Arg-299 are dimethylated, probably to asymmetric
CC dimethylarginine.
CC -!- PTM: Sumoylated by CBX4. Sumoylation is increased upon DNA damage, such
CC as that produced by doxorubicin, etoposide, UV light and camptothecin,
CC due to enhanced CBX4 phosphorylation by HIPK2 under these conditions.
CC {ECO:0000269|PubMed:16564677, ECO:0000269|PubMed:22825850,
CC ECO:0000269|PubMed:8107114}.
CC -!- PTM: Ubiquitinated by MDM2. Doxorubicin treatment does not affect
CC monoubiquitination, but slightly decreases HNRNPK poly-ubiquitination.
CC {ECO:0000269|PubMed:16360036, ECO:0000269|PubMed:22825850}.
CC -!- PTM: O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.
CC {ECO:0000269|PubMed:22967762}.
CC -!- MASS SPECTROMETRY: [Isoform 1]: Mass=50976.25; Method=MALDI;
CC Evidence={ECO:0000269|PubMed:11840567};
CC -!- DISEASE: Au-Kline syndrome (AUKS) [MIM:616580]: A disorder
CC characterized by intellectual disability, facial dysmorphism, cardiac
CC defects, and connective tissue and skeletal abnormalities. Dysmorphic
CC features include long palpebral fissures, ptosis, a broad prominent
CC nasal bridge, hypoplastic alae nasi, an open downturned mouth, ears
CC with underdeveloped and thick helices, high palate, and a unique tongue
CC with a prominent median crease. Hypotonia, hyporeflexia, and high pain
CC tolerance are additional features. {ECO:0000269|PubMed:26173930}.
CC Note=The disease is caused by variants affecting the gene represented
CC in this entry.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92799.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/HNRNPKID44314ch9q21.html";
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DR EMBL; S74678; AAB20770.1; -; mRNA.
DR EMBL; X72727; CAA51267.1; -; mRNA.
DR EMBL; CR456771; CAG33052.1; -; mRNA.
DR EMBL; AB209562; BAD92799.1; ALT_INIT; mRNA.
DR EMBL; AK291336; BAF84025.1; -; mRNA.
DR EMBL; AB451263; BAG70077.1; -; mRNA.
DR EMBL; AB451390; BAG70204.1; -; mRNA.
DR EMBL; AL354733; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471089; EAW62675.1; -; Genomic_DNA.
DR EMBL; CH471089; EAW62677.1; -; Genomic_DNA.
DR EMBL; BC000355; AAH00355.1; -; mRNA.
DR EMBL; BC014980; AAH14980.1; -; mRNA.
DR CCDS; CCDS6667.1; -.
DR CCDS; CCDS6668.1; -. [P61978-2]
DR PIR; S43363; S43363.
DR RefSeq; NP_001305115.1; NM_001318186.1.
DR RefSeq; NP_001305116.1; NM_001318187.1. [P61978-3]
DR RefSeq; NP_001305117.1; NM_001318188.1. [P61978-1]
DR RefSeq; NP_002131.2; NM_002140.4. [P61978-2]
DR RefSeq; NP_112552.1; NM_031262.3. [P61978-1]
DR RefSeq; NP_112553.1; NM_031263.3. [P61978-2]
DR RefSeq; XP_005252017.1; XM_005251960.2. [P61978-2]
DR RefSeq; XP_005252020.1; XM_005251963.3. [P61978-3]
DR RefSeq; XP_005252022.1; XM_005251965.2. [P61978-3]
DR RefSeq; XP_016870157.1; XM_017014668.1. [P61978-1]
DR PDB; 1J5K; NMR; -; A=379-463.
DR PDB; 1KHM; NMR; -; A=379-463.
DR PDB; 1ZZI; X-ray; 1.80 A; A/B=385-463.
DR PDB; 1ZZJ; X-ray; 2.30 A; A/B/C=385-463.
DR PDB; 1ZZK; X-ray; 0.95 A; A=385-463.
DR PDB; 7CRU; X-ray; 2.80 A; B/D=18-38.
DR PDBsum; 1J5K; -.
DR PDBsum; 1KHM; -.
DR PDBsum; 1ZZI; -.
DR PDBsum; 1ZZJ; -.
DR PDBsum; 1ZZK; -.
DR PDBsum; 7CRU; -.
DR AlphaFoldDB; P61978; -.
DR SMR; P61978; -.
DR BioGRID; 109431; 567.
DR CORUM; P61978; -.
DR DIP; DIP-31805N; -.
DR IntAct; P61978; 253.
DR MINT; P61978; -.
DR STRING; 9606.ENSP00000365439; -.
DR DrugBank; DB11638; Artenimol.
DR DrugBank; DB12695; Phenethyl Isothiocyanate.
DR MoonDB; P61978; Predicted.
DR GlyGen; P61978; 2 sites, 1 O-linked glycan (2 sites).
DR iPTMnet; P61978; -.
DR MetOSite; P61978; -.
DR PhosphoSitePlus; P61978; -.
DR SwissPalm; P61978; -.
DR BioMuta; HNRNPK; -.
DR DMDM; 48429103; -.
DR SWISS-2DPAGE; P61978; -.
DR CPTAC; CPTAC-1028; -.
DR EPD; P61978; -.
DR jPOST; P61978; -.
DR MassIVE; P61978; -.
DR MaxQB; P61978; -.
DR PaxDb; P61978; -.
DR PeptideAtlas; P61978; -.
DR PRIDE; P61978; -.
DR ProteomicsDB; 57352; -.
DR ProteomicsDB; 57353; -. [P61978-2]
DR ProteomicsDB; 57354; -. [P61978-3]
DR TopDownProteomics; P61978-1; -. [P61978-1]
DR Antibodypedia; 2214; 618 antibodies from 40 providers.
DR DNASU; 3190; -.
DR Ensembl; ENST00000351839.7; ENSP00000317788.4; ENSG00000165119.21. [P61978-1]
DR Ensembl; ENST00000360384.9; ENSP00000353552.5; ENSG00000165119.21. [P61978-1]
DR Ensembl; ENST00000376263.8; ENSP00000365439.3; ENSG00000165119.21. [P61978-2]
DR Ensembl; ENST00000376281.8; ENSP00000365458.4; ENSG00000165119.21. [P61978-2]
DR GeneID; 3190; -.
DR KEGG; hsa:3190; -.
DR MANE-Select; ENST00000376263.8; ENSP00000365439.3; NM_031263.4; NP_112553.1. [P61978-2]
DR UCSC; uc004anf.5; human.
DR UCSC; uc004ang.5; human.
DR CTD; 3190; -.
DR DisGeNET; 3190; -.
DR GeneCards; HNRNPK; -.
DR GeneReviews; HNRNPK; -.
DR HGNC; HGNC:5044; HNRNPK.
DR HPA; ENSG00000165119; Low tissue specificity.
DR MalaCards; HNRNPK; -.
DR MIM; 600712; gene.
DR MIM; 616580; phenotype.
DR neXtProt; NX_P61978; -.
DR OpenTargets; ENSG00000165119; -.
DR Orphanet; 352665; Neurodevelopmental disorder-craniofacial dysmorphism-cardiac defect-skeletal anomalies syndrome due to 9q21.3 microdeletion.
DR Orphanet; 453504; Neurodevelopmental disorder-craniofacial dysmorphism-cardiac defect-skeletal anomalies syndrome due to a point mutation.
DR PharmGKB; PA162391350; -.
DR VEuPathDB; HostDB:ENSG00000165119; -.
DR eggNOG; KOG2192; Eukaryota.
DR GeneTree; ENSGT00940000153434; -.
DR InParanoid; P61978; -.
DR OMA; SSWERFP; -.
DR OrthoDB; 394765at2759; -.
DR PhylomeDB; P61978; -.
DR TreeFam; TF316335; -.
DR PathwayCommons; P61978; -.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-72163; mRNA Splicing - Major Pathway.
DR Reactome; R-HSA-72203; Processing of Capped Intron-Containing Pre-mRNA.
DR Reactome; R-HSA-9610379; HCMV Late Events.
DR SignaLink; P61978; -.
DR SIGNOR; P61978; -.
DR BioGRID-ORCS; 3190; 808 hits in 1081 CRISPR screens.
DR ChiTaRS; HNRNPK; human.
DR EvolutionaryTrace; P61978; -.
DR GeneWiki; HNRPK; -.
DR GenomeRNAi; 3190; -.
DR Pharos; P61978; Tbio.
DR PRO; PR:P61978; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; P61978; protein.
DR Bgee; ENSG00000165119; Expressed in calcaneal tendon and 100 other tissues.
DR ExpressionAtlas; P61978; baseline and differential.
DR Genevisible; P61978; HS.
DR GO; GO:0071013; C:catalytic step 2 spliceosome; IDA:UniProtKB.
DR GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR GO; GO:0000785; C:chromatin; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0010494; C:cytoplasmic stress granule; ISS:ARUK-UCL.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0005925; C:focal adhesion; HDA:UniProtKB.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0002102; C:podosome; IEA:UniProtKB-SubCell.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:UniProtKB.
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:0003729; F:mRNA binding; IBA:GO_Central.
DR GO; GO:0019904; F:protein domain specific binding; IPI:UniProtKB.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0000398; P:mRNA splicing, via spliceosome; IC:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IMP:MGI.
DR GO; GO:0048025; P:negative regulation of mRNA splicing, via spliceosome; IEA:Ensembl.
DR GO; GO:0045892; P:negative regulation of transcription, DNA-templated; IMP:UniProtKB.
DR GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IMP:BHF-UCL.
DR GO; GO:0048260; P:positive regulation of receptor-mediated endocytosis; IMP:BHF-UCL.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR GO; GO:0010468; P:regulation of gene expression; IBA:GO_Central.
DR GO; GO:1902165; P:regulation of intrinsic apoptotic signaling pathway in response to DNA damage by p53 class mediator; IEA:Ensembl.
DR GO; GO:0010988; P:regulation of low-density lipoprotein particle clearance; IMP:BHF-UCL.
DR GO; GO:0048024; P:regulation of mRNA splicing, via spliceosome; IBA:GO_Central.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR GO; GO:0006396; P:RNA processing; TAS:ProtInc.
DR GO; GO:0007165; P:signal transduction; TAS:ProtInc.
DR Gene3D; 3.30.1370.10; -; 3.
DR InterPro; IPR033090; hnRNP_K.
DR InterPro; IPR004087; KH_dom.
DR InterPro; IPR004088; KH_dom_type_1.
DR InterPro; IPR036612; KH_dom_type_1_sf.
DR InterPro; IPR012987; ROK_N.
DR PANTHER; PTHR10288:SF262; PTHR10288:SF262; 1.
DR Pfam; PF00013; KH_1; 3.
DR Pfam; PF08067; ROKNT; 1.
DR SMART; SM00322; KH; 3.
DR SUPFAM; SSF54791; SSF54791; 3.
DR PROSITE; PS50084; KH_TYPE_1; 3.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Activator; Alternative splicing; Cell junction;
KW Cell projection; Cytoplasm; Direct protein sequencing; DNA-binding;
KW Glycoprotein; Host-virus interaction; Intellectual disability;
KW Isopeptide bond; Methylation; mRNA processing; mRNA splicing; Nucleus;
KW Phosphoprotein; Reference proteome; Repeat; Repressor; Ribonucleoprotein;
KW RNA-binding; Spliceosome; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..463
FT /note="Heterogeneous nuclear ribonucleoprotein K"
FT /id="PRO_0000050096"
FT DOMAIN 42..104
FT /note="KH 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 54..76
FT /note="1-1"
FT REPEAT 59..62
FT /note="3-1"
FT DOMAIN 144..209
FT /note="KH 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 245..250
FT /note="2-1"
FT REPEAT 257..260
FT /note="3-2"
FT REPEAT 267..270
FT /note="3-3"
FT REPEAT 295..298
FT /note="3-4"
FT REPEAT 324..329
FT /note="2-2"
FT DOMAIN 387..451
FT /note="KH 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00117"
FT REPEAT 399..421
FT /note="1-2"
FT REPEAT 404..407
FT /note="3-5"
FT REGION 1..276
FT /note="Necessary for interaction with DDX1"
FT /evidence="ECO:0000269|PubMed:12183465"
FT REGION 1..37
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 35..197
FT /note="Interaction with ASFV p30"
FT REGION 54..421
FT /note="2 X 22 AA approximate repeats"
FT REGION 59..407
FT /note="5 X 4 AA repeats of G-X-G-G"
FT REGION 209..337
FT /note="Interaction with ZIK1"
FT /evidence="ECO:0000250"
FT REGION 236..273
FT /note="RNA-binding RGG-box"
FT REGION 245..329
FT /note="2 X 6 AA approximate repeats"
FT REGION 250..329
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 19..37
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000269|Ref.10, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:22814378"
FT MOD_RES 34
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 36
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 39
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 75
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 116
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 198
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 214
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 216
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
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 219
FT /note="N6-succinyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 284
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:16564677,
FT ECO:0007744|PubMed:17081983, ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 316
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 377
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 379
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16964243,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 380
FT /note="Phosphotyrosine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 405
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0000250|UniProtKB:P61979"
FT MOD_RES 420
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 34
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:28112733"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 60
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 163
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 219
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 405
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:28112733"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO); alternate"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 422
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:25114211,
FT ECO:0007744|PubMed:25218447, ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT VAR_SEQ 111..134
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|Ref.4"
FT /id="VSP_021669"
FT VAR_SEQ 459..463
FT /note="SGKFF -> ADVEGF (in isoform 2 and isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334, ECO:0000303|Ref.4"
FT /id="VSP_002822"
FT MUTAGEN 422
FT /note="K->R: Loss of sumoylation. Loss of TP53
FT transcriptional stimulation."
FT /evidence="ECO:0000269|PubMed:22825850"
FT MUTAGEN 424
FT /note="D->A: Loss of sumoylation."
FT /evidence="ECO:0000269|PubMed:22825850"
FT CONFLICT 32
FT /note="A -> D (in Ref. 2; CAA51267)"
FT /evidence="ECO:0000305"
FT STRAND 377..380
FT /evidence="ECO:0007829|PDB:1KHM"
FT HELIX 381..384
FT /evidence="ECO:0007829|PDB:1KHM"
FT STRAND 388..395
FT /evidence="ECO:0007829|PDB:1ZZK"
FT TURN 396..398
FT /evidence="ECO:0007829|PDB:1ZZK"
FT HELIX 399..402
FT /evidence="ECO:0007829|PDB:1ZZK"
FT HELIX 405..407
FT /evidence="ECO:0007829|PDB:1ZZK"
FT HELIX 408..417
FT /evidence="ECO:0007829|PDB:1ZZK"
FT STRAND 420..423
FT /evidence="ECO:0007829|PDB:1ZZK"
FT STRAND 430..439
FT /evidence="ECO:0007829|PDB:1ZZK"
FT HELIX 441..459
FT /evidence="ECO:0007829|PDB:1ZZK"
SQ SEQUENCE 463 AA; 50976 MW; 0F70EE169B2A064A CRC64;
METEQPEETF PNTETNGEFG KRPAEDMEEE QAFKRSRNTD EMVELRILLQ SKNAGAVIGK
GGKNIKALRT DYNASVSVPD SSGPERILSI SADIETIGEI LKKIIPTLEE GLQLPSPTAT
SQLPLESDAV ECLNYQHYKG SDFDCELRLL IHQSLAGGII GVKGAKIKEL RENTQTTIKL
FQECCPHSTD RVVLIGGKPD RVVECIKIIL DLISESPIKG RAQPYDPNFY DETYDYGGFT
MMFDDRRGRP VGFPMRGRGG FDRMPPGRGG RPMPPSRRDY DDMSPRRGPP PPPPGRGGRG
GSRARNLPLP PPPPPRGGDL MAYDRRGRPG DRYDGMVGFS ADETWDSAID TWSPSEWQMA
YEPQGGSGYD YSYAGGRGSY GDLGGPIITT QVTIPKDLAG SIIGKGGQRI KQIRHESGAS
IKIDEPLEGS EDRIITITGT QDQIQNAQYL LQNSVKQYSG KFF
