ZC3HE_HUMAN
ID ZC3HE_HUMAN Reviewed; 736 AA.
AC Q6PJT7; A8MY46; B4DXU8; B4DZW7; B4E2H4; G3V5R4; Q6MZU4; Q6PJ32; Q6PUI6;
AC Q6PUI8; Q86TQ5; Q86TW0; Q86TW1; Q8NCT6; Q8NCZ3; Q8TDE2; Q9HAC9; Q9Y5A0;
DT 29-APR-2008, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2004, sequence version 1.
DT 03-AUG-2022, entry version 166.
DE RecName: Full=Zinc finger CCCH domain-containing protein 14;
DE AltName: Full=Mammalian suppressor of tau pathology-2;
DE Short=MSUT-2;
DE AltName: Full=Renal carcinoma antigen NY-REN-37;
GN Name=ZC3H14;
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 8).
RA Guo J.H.;
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 3 AND 4).
RA Zhou G., Wang X., Yu L.;
RT "Homo sapiens putative NY-REN-37 antigen alternatively spliced isoforms.";
RL Submitted (MAR-2004) to the EMBL/GenBank/DDBJ databases.
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 3; 9; 10 AND 11).
RC TISSUE=Embryo, Testis, Thymus, and Trachea;
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 [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Esophageal carcinoma, and Testis;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(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] (ISOFORMS 1 AND 6), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 91-736 (ISOFORM 2).
RC TISSUE=Muscle, Skin, and Testis;
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 [LARGE SCALE MRNA] OF 86-736 (ISOFORM 2), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 368-736 (ISOFORM 5), AND NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 630-736 (ISOFORM 1).
RC TISSUE=Neuroblastoma, and Placenta;
RA Li W.B., Gruber C., Jessee J., Polayes D.;
RT "Full-length cDNA libraries and normalization.";
RL Submitted (FEB-2003) to the EMBL/GenBank/DDBJ databases.
RN [9]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 563-736 (ISOFORM 2), AND IDENTIFICATION AS A
RP RENAL CANCER ANTIGEN.
RC TISSUE=Renal cell carcinoma;
RX PubMed=10508479;
RX DOI=10.1002/(sici)1097-0215(19991112)83:4<456::aid-ijc4>3.0.co;2-5;
RA Scanlan M.J., Gordan J.D., Williamson B., Stockert E., Bander N.H.,
RA Jongeneel C.V., Gure A.O., Jaeger D., Jaeger E., Knuth A., Chen Y.-T.,
RA Old L.J.;
RT "Antigens recognized by autologous antibody in patients with renal-cell
RT carcinoma.";
RL Int. J. Cancer 83:456-464(1999).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515 AND SER-620, 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 [11]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17630287; DOI=10.1073/pnas.0701244104;
RA Kelly S.M., Pabit S.A., Kitchen C.M., Guo P., Marfatia K.A., Murphy T.J.,
RA Corbett A.H., Berland K.M.;
RT "Recognition of polyadenosine RNA by zinc finger proteins.";
RL Proc. Natl. Acad. Sci. U.S.A. 104:12306-12311(2007).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Embryonic kidney;
RX PubMed=17525332; DOI=10.1126/science.1140321;
RA Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E.,
RA Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y.,
RA Gygi S.P., Elledge S.J.;
RT "ATM and ATR substrate analysis reveals extensive protein networks
RT responsive to DNA damage.";
RL Science 316:1160-1166(2007).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP 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 [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 ALTERNATIVE SPLICING (ISOFORMS 1; 3; 4 AND 6), AND SUBCELLULAR LOCATION.
RX PubMed=19303045; DOI=10.1016/j.gene.2009.02.022;
RA Leung S.W., Apponi L.H., Cornejo O.E., Kitchen C.M., Valentini S.R.,
RA Pavlath G.K., Dunham C.M., Corbett A.H.;
RT "Splice variants of the human ZC3H14 gene generate multiple isoforms of a
RT zinc finger polyadenosine RNA binding protein.";
RL Gene 439:71-78(2009).
RN [16]
RP INTERACTION WITH HOOK2.
RX PubMed=19273536; DOI=10.1093/hmg/ddp099;
RA Guthrie C.R., Schellenberg G.D., Kraemer B.C.;
RT "SUT-2 potentiates tau-induced neurotoxicity in Caenorhabditis elegans.";
RL Hum. Mol. Genet. 18:1825-1838(2009).
RN [17]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP 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 [18]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-357, 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 [19]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP 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 [20]
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 [21]
RP INVOLVEMENT IN MRT56, SUBCELLULAR LOCATION (ISOFORM 6), AND TISSUE
RP SPECIFICITY (ISOFORMS 1 AND 6).
RX PubMed=21734151; DOI=10.1073/pnas.1107103108;
RA Pak C., Garshasbi M., Kahrizi K., Gross C., Apponi L.H., Noto J.J.,
RA Kelly S.M., Leung S.W., Tzschach A., Behjati F., Abedini S.S., Mohseni M.,
RA Jensen L.R., Hu H., Huang B., Stahley S.N., Liu G., Williams K.R.,
RA Burdick S., Feng Y., Sanyal S., Bassell G.J., Ropers H.H., Najmabadi H.,
RA Corbett A.H., Moberg K.H., Kuss A.W.;
RT "Mutation of the conserved polyadenosine RNA binding protein, ZC3H14/dNab2,
RT impairs neural function in Drosophila and humans.";
RL Proc. Natl. Acad. Sci. U.S.A. 108:12390-12395(2011).
RN [22]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-515, AND IDENTIFICATION BY
RP 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 [23]
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 [24]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-240; SER-281; SER-327;
RP SER-343; SER-390; SER-409; SER-421; SER-498 AND SER-515, AND IDENTIFICATION
RP BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma, and Erythroleukemia;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [25]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-343 AND SER-515, 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 [26]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-175 AND LYS-413, 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 [27]
RP FUNCTION, MISCELLANEOUS, AND SUBCELLULAR LOCATION.
RX PubMed=24671764; DOI=10.1261/rna.043984.113;
RA Kelly S.M., Leung S.W., Pak C., Banerjee A., Moberg K.H., Corbett A.H.;
RT "A conserved role for the zinc finger polyadenosine RNA binding protein,
RT ZC3H14, in control of poly(A) tail length.";
RL RNA 20:681-688(2014).
RN [28]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-175 AND LYS-413, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [29]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-413, 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 [30]
RP INTERACTION WITH ZFC3H1.
RX PubMed=27871484; DOI=10.1016/j.molcel.2016.09.025;
RA Meola N., Domanski M., Karadoulama E., Chen Y., Gentil C., Pultz D.,
RA Vitting-Seerup K., Lykke-Andersen S., Andersen J.S., Sandelin A.,
RA Jensen T.H.;
RT "Identification of a nuclear exosome decay pathway for processed
RT transcripts.";
RL Mol. Cell 64:520-533(2016).
RN [31]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-99; LYS-139; LYS-175; LYS-198;
RP LYS-245; LYS-283; LYS-295; LYS-357; LYS-378; LYS-413 AND LYS-489, 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).
CC -!- FUNCTION: Involved in poly(A) tail length control in neuronal cells.
CC Binds the polyadenosine RNA oligonucleotides.
CC {ECO:0000269|PubMed:17630287, ECO:0000269|PubMed:24671764}.
CC -!- SUBUNIT: Interacts with HOOK2 (PubMed:19273536). Interacts with ZFC3H1
CC in a RNase-sensitive manner (PubMed:27871484).
CC {ECO:0000269|PubMed:19273536, ECO:0000269|PubMed:27871484}.
CC -!- INTERACTION:
CC Q6PJT7; P35638-2: DDIT3; NbExp=3; IntAct=EBI-740660, EBI-10173632;
CC Q6PJT7-6; P51808: DYNLT3; NbExp=3; IntAct=EBI-12147703, EBI-743027;
CC Q6PJT7-6; Q7Z3Y8: KRT27; NbExp=3; IntAct=EBI-12147703, EBI-3044087;
CC -!- SUBCELLULAR LOCATION: Nucleus speckle {ECO:0000269|PubMed:17630287,
CC ECO:0000269|PubMed:19303045, ECO:0000269|PubMed:24671764}.
CC Note=Colocalizes with poly(A) RNA in nuclear speckles.
CC {ECO:0000250|UniProtKB:Q7TMD5}.
CC -!- SUBCELLULAR LOCATION: [Isoform 1]: Nucleus speckle.
CC -!- SUBCELLULAR LOCATION: [Isoform 3]: Nucleus speckle.
CC -!- SUBCELLULAR LOCATION: [Isoform 6]: Cytoplasm
CC {ECO:0000269|PubMed:21734151}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=10;
CC Name=1; Synonyms=Isoform 1;
CC IsoId=Q6PJT7-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PJT7-2; Sequence=VSP_033171;
CC Name=3; Synonyms=Isoform 2;
CC IsoId=Q6PJT7-3; Sequence=VSP_033166, VSP_033171;
CC Name=4; Synonyms=Isoform 3 short;
CC IsoId=Q6PJT7-4; Sequence=VSP_033164, VSP_033168;
CC Name=5;
CC IsoId=Q6PJT7-5; Sequence=VSP_033167;
CC Name=6; Synonyms=Isoform 4;
CC IsoId=Q6PJT7-6; Sequence=VSP_033163, VSP_033165, VSP_033168,
CC VSP_033171;
CC Name=8;
CC IsoId=Q6PJT7-8; Sequence=VSP_033162, VSP_033169;
CC Name=9;
CC IsoId=Q6PJT7-9; Sequence=VSP_044645, VSP_033171;
CC Name=10;
CC IsoId=Q6PJT7-10; Sequence=VSP_055097, VSP_033166;
CC Name=11;
CC IsoId=Q6PJT7-11; Sequence=VSP_055096, VSP_033168, VSP_033171;
CC -!- TISSUE SPECIFICITY: Isoform 1 and isoform 6 are expressed in fetal and
CC adult brain. Isoform 1 and isoform 6 are expressed in fetal and adult
CC temporal lobe. {ECO:0000269|PubMed:21734151}.
CC -!- DISEASE: Intellectual developmental disorder, autosomal recessive 56
CC (MRT56) [MIM:617125]: A disorder characterized by significantly below
CC average general intellectual functioning associated with impairments in
CC adaptive behavior and manifested during the developmental period.
CC {ECO:0000269|PubMed:21734151}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- MISCELLANEOUS: ZC3H14 can functionally substitute for Nab2 in fly
CC neurons and can rescue defects in development and locomotion that are
CC present in dNab2 null flies.
CC -!- SIMILARITY: Belongs to the ZC3H14 family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAL83289.1; Type=Miscellaneous discrepancy; Note=Several sequencing errors.; Evidence={ECO:0000305};
CC Sequence=AAS90302.1; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=AAS90302.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
CC Sequence=AK021868; Type=Frameshift; Evidence={ECO:0000305};
CC Sequence=CAE45933.1; Type=Miscellaneous discrepancy; Note=Aberrant splicing.; Evidence={ECO:0000305};
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DR EMBL; AF474376; AAL83289.1; ALT_SEQ; mRNA.
DR EMBL; AY578060; AAS90299.1; -; mRNA.
DR EMBL; AY578061; AAS90300.1; -; mRNA.
DR EMBL; AY578062; AAS90301.1; -; mRNA.
DR EMBL; AY578063; AAS90302.1; ALT_SEQ; mRNA.
DR EMBL; AK021868; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK302136; BAG63510.1; -; mRNA.
DR EMBL; AK303123; BAG64229.1; -; mRNA.
DR EMBL; AK304275; BAG65136.1; -; mRNA.
DR EMBL; AL834215; CAD38897.1; -; mRNA.
DR EMBL; BX640716; CAE45835.1; -; mRNA.
DR EMBL; BX640876; CAE45933.1; ALT_SEQ; mRNA.
DR EMBL; AL162171; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471061; EAW81385.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81388.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81389.1; -; Genomic_DNA.
DR EMBL; CH471061; EAW81390.1; -; Genomic_DNA.
DR EMBL; BC011793; AAH11793.1; -; mRNA.
DR EMBL; BC023641; AAH23641.1; -; mRNA.
DR EMBL; BC027607; AAH27607.1; -; mRNA.
DR EMBL; BX248265; CAD62593.1; -; mRNA.
DR EMBL; BX248281; CAD62609.1; -; mRNA.
DR EMBL; BX248769; CAD66576.1; -; mRNA.
DR EMBL; AF155107; AAD42873.1; -; mRNA.
DR CCDS; CCDS32133.1; -. [Q6PJT7-1]
DR CCDS; CCDS32134.1; -. [Q6PJT7-3]
DR CCDS; CCDS32135.1; -. [Q6PJT7-4]
DR CCDS; CCDS32136.1; -. [Q6PJT7-6]
DR CCDS; CCDS55938.1; -. [Q6PJT7-9]
DR CCDS; CCDS86418.1; -. [Q6PJT7-5]
DR RefSeq; NP_001153575.1; NM_001160103.1. [Q6PJT7-2]
DR RefSeq; NP_001153576.1; NM_001160104.1. [Q6PJT7-9]
DR RefSeq; NP_001313236.1; NM_001326307.1. [Q6PJT7-5]
DR RefSeq; NP_079100.2; NM_024824.4. [Q6PJT7-1]
DR RefSeq; NP_997543.1; NM_207660.3. [Q6PJT7-3]
DR RefSeq; NP_997544.1; NM_207661.2. [Q6PJT7-4]
DR RefSeq; NP_997545.2; NM_207662.3. [Q6PJT7-6]
DR RefSeq; XP_005268125.1; XM_005268068.4.
DR AlphaFoldDB; Q6PJT7; -.
DR BioGRID; 122967; 144.
DR IntAct; Q6PJT7; 53.
DR STRING; 9606.ENSP00000251038; -.
DR GlyConnect; 2848; 1 O-Linked glycan (1 site). [Q6PJT7-2]
DR GlyGen; Q6PJT7; 13 sites, 2 O-linked glycans (13 sites).
DR iPTMnet; Q6PJT7; -.
DR MetOSite; Q6PJT7; -.
DR PhosphoSitePlus; Q6PJT7; -.
DR SwissPalm; Q6PJT7; -.
DR BioMuta; ZC3H14; -.
DR DMDM; 74737935; -.
DR EPD; Q6PJT7; -.
DR jPOST; Q6PJT7; -.
DR MassIVE; Q6PJT7; -.
DR MaxQB; Q6PJT7; -.
DR PaxDb; Q6PJT7; -.
DR PeptideAtlas; Q6PJT7; -.
DR PRIDE; Q6PJT7; -.
DR ProteomicsDB; 33599; -.
DR ProteomicsDB; 67217; -. [Q6PJT7-1]
DR ProteomicsDB; 67218; -. [Q6PJT7-2]
DR ProteomicsDB; 67219; -. [Q6PJT7-3]
DR ProteomicsDB; 67220; -. [Q6PJT7-4]
DR ProteomicsDB; 67221; -. [Q6PJT7-5]
DR ProteomicsDB; 67222; -. [Q6PJT7-6]
DR ProteomicsDB; 67223; -. [Q6PJT7-8]
DR Antibodypedia; 26309; 147 antibodies from 23 providers.
DR DNASU; 79882; -.
DR Ensembl; ENST00000251038.10; ENSP00000251038.5; ENSG00000100722.20. [Q6PJT7-1]
DR Ensembl; ENST00000302216.12; ENSP00000307025.8; ENSG00000100722.20. [Q6PJT7-3]
DR Ensembl; ENST00000318308.10; ENSP00000327176.6; ENSG00000100722.20. [Q6PJT7-6]
DR Ensembl; ENST00000336693.8; ENSP00000338002.4; ENSG00000100722.20. [Q6PJT7-4]
DR Ensembl; ENST00000393514.9; ENSP00000377150.5; ENSG00000100722.20. [Q6PJT7-5]
DR Ensembl; ENST00000406216.7; ENSP00000384682.3; ENSG00000100722.20. [Q6PJT7-8]
DR Ensembl; ENST00000555755.5; ENSP00000452475.1; ENSG00000100722.20. [Q6PJT7-9]
DR GeneID; 79882; -.
DR KEGG; hsa:79882; -.
DR MANE-Select; ENST00000251038.10; ENSP00000251038.5; NM_024824.5; NP_079100.2.
DR UCSC; uc001xww.4; human. [Q6PJT7-1]
DR CTD; 79882; -.
DR DisGeNET; 79882; -.
DR GeneCards; ZC3H14; -.
DR HGNC; HGNC:20509; ZC3H14.
DR HPA; ENSG00000100722; Tissue enriched (testis).
DR MalaCards; ZC3H14; -.
DR MIM; 613279; gene.
DR MIM; 617125; phenotype.
DR neXtProt; NX_Q6PJT7; -.
DR OpenTargets; ENSG00000100722; -.
DR Orphanet; 88616; Autosomal recessive non-syndromic intellectual disability.
DR PharmGKB; PA145007270; -.
DR VEuPathDB; HostDB:ENSG00000100722; -.
DR eggNOG; KOG3702; Eukaryota.
DR GeneTree; ENSGT00440000038430; -.
DR HOGENOM; CLU_022605_0_0_1; -.
DR InParanoid; Q6PJT7; -.
DR OMA; TFYHPTV; -.
DR OrthoDB; 893844at2759; -.
DR PhylomeDB; Q6PJT7; -.
DR TreeFam; TF329509; -.
DR PathwayCommons; Q6PJT7; -.
DR SignaLink; Q6PJT7; -.
DR BioGRID-ORCS; 79882; 16 hits in 1086 CRISPR screens.
DR ChiTaRS; ZC3H14; human.
DR GenomeRNAi; 79882; -.
DR Pharos; Q6PJT7; Tbio.
DR PRO; PR:Q6PJT7; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q6PJT7; protein.
DR Bgee; ENSG00000100722; Expressed in left testis and 206 other tissues.
DR ExpressionAtlas; Q6PJT7; baseline and differential.
DR Genevisible; Q6PJT7; HS.
DR GO; GO:1904115; C:axon cytoplasm; IDA:FlyBase.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0032839; C:dendrite cytoplasm; IDA:FlyBase.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:1990904; C:ribonucleoprotein complex; IDA:FlyBase.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0008143; F:poly(A) binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:1900364; P:negative regulation of mRNA polyadenylation; IBA:GO_Central.
DR GO; GO:0043488; P:regulation of mRNA stability; IBA:GO_Central.
DR InterPro; IPR040366; Nab2/ZC3H14.
DR InterPro; IPR000571; Znf_CCCH.
DR PANTHER; PTHR14738; PTHR14738; 1.
DR SMART; SM00356; ZnF_C3H1; 3.
DR PROSITE; PS50103; ZF_C3H1; 3.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Cytoplasm; Intellectual disability;
KW Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; RNA-binding; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..736
FT /note="Zinc finger CCCH domain-containing protein 14"
FT /id="PRO_0000331311"
FT ZN_FING 595..620
FT /note="C3H1-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 621..640
FT /note="C3H1-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 641..656
FT /note="C3H1-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 682..699
FT /note="C3H1-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT ZN_FING 701..719
FT /note="C3H1-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00723"
FT REGION 77..145
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 310..350
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 398..430
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 77..101
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 85
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ05"
FT MOD_RES 240
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 281
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 327
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 343
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 357
FT /note="N6-acetyllysine; alternate"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 390
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 409
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 421
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 498
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 515
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692,
FT ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT MOD_RES 527
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q8BJ05"
FT MOD_RES 620
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983"
FT CROSSLNK 99
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 139
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 175
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 198
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 245
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 283
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 295
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 357
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2); alternate"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 378
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 413
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25218447,
FT ECO:0007744|PubMed:25755297, ECO:0007744|PubMed:25772364,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 489
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..454
FT /note="Missing (in isoform 8)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_033162"
FT VAR_SEQ 1..298
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033163"
FT VAR_SEQ 1..34
FT /note="Missing (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:17974005, ECO:0000303|Ref.2"
FT /id="VSP_033164"
FT VAR_SEQ 95..113
FT /note="Missing (in isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055096"
FT VAR_SEQ 123..159
FT /note="Missing (in isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_055097"
FT VAR_SEQ 299..426
FT /note="VSSVVKVKKFNHDGEEEEEDDDYGSRTGSISSSVSVPAKPERRPSLPPSKQA
FT NKNLILKAISEAQESVTKTTNYSTVPQKQTLPVAPRTRTSQEELLAEVVQGQSRTPRIS
FT PPIKEEETKGDSVEKNQ -> MRMSSKFPSPPLPIFLPPEPVDLGSITSSSCSLNELDN
FT ISHLLRKISADINEIKGMKAAILTVEANLFDLNVRVSKNEAKISSLEVKMNEYSTTYEC
FT NRQFEDQEEDTESQSRTTDVKIIGFLRNVEK (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_033165"
FT VAR_SEQ 427..582
FT /note="Missing (in isoform 3 and isoform 10)"
FT /evidence="ECO:0000303|PubMed:14702039, ECO:0000303|Ref.2"
FT /id="VSP_033166"
FT VAR_SEQ 427..451
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|Ref.8"
FT /id="VSP_033167"
FT VAR_SEQ 452..582
FT /note="Missing (in isoform 4, isoform 6 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334, ECO:0000303|PubMed:17974005,
FT ECO:0000303|Ref.2"
FT /id="VSP_033168"
FT VAR_SEQ 455..582
FT /note="DMESMVHADTRSFILKKPKLSEEVVVAPNQESGMKTADSLRVLSGHLMQTRD
FT LVQPDKPASPKFIVTLDGVPSPPGYMSDQEEDMCFEGMKPVNQTAASNKGLRGLLHPQQ
FT LHLLSRQLEDPNGSFSN -> MRMSSKFPSPPLPIFLPPEPVDLGSITSSSCSLNELDN
FT ISHLLRKISADINEIKGMKAAILTVEANLFDLNVRVSKNEAKISSLEVKMNEYSTTYEC
FT NRQFEDQEEDTESQSRTTDVKIIGFLRNVEK (in isoform 8)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_033169"
FT VAR_SEQ 577..581
FT /note="Missing (in isoform 9)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_044645"
FT VAR_SEQ 669
FT /note="Missing (in isoform 2, isoform 3, isoform 6, isoform
FT 9 and isoform 11)"
FT /evidence="ECO:0000303|PubMed:10508479,
FT ECO:0000303|PubMed:14702039, ECO:0000303|PubMed:15489334,
FT ECO:0000303|Ref.2, ECO:0000303|Ref.8"
FT /id="VSP_033171"
FT CONFLICT 113
FT /note="A -> V (in Ref. 3; BAG63510)"
FT /evidence="ECO:0000305"
FT CONFLICT 323
FT /note="S -> P (in Ref. 3; BAG64229)"
FT /evidence="ECO:0000305"
FT CONFLICT 532
FT /note="M -> V (in Ref. 3; BAG65136)"
FT /evidence="ECO:0000305"
FT CONFLICT 674
FT /note="A -> V (in Ref. 7; AAH23641)"
FT /evidence="ECO:0000305"
FT CONFLICT 712
FT /note="C -> F (in Ref. 2; AAS90302 and 4; CAE45933)"
FT /evidence="ECO:0000305"
FT CONFLICT 718
FT /note="T -> P (in Ref. 3; BAG65136)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 736 AA; 82876 MW; BCF3E36CBA66170A CRC64;
MEIGTEISRK IRSAIKGKLQ ELGAYVDEEL PDYIMVMVAN KKSQDQMTED LSLFLGNNTI
RFTVWLHGVL DKLRSVTTEP SSLKSSDTNI FDSNVPSNKS NFSRGDERRH EAAVPPLAIP
SARPEKRDSR VSTSSQESKT TNVRQTYDDG AATRLMSTVK PLREPAPSED VIDIKPEPDD
LIDEDLNFVQ ENPLSQKKPT VTLTYGSSRP SIEIYRPPAS RNADSGVHLN RLQFQQQQNS
IHAAKQLDMQ SSWVYETGRL CEPEVLNSLE ETYSPFFRNN SEKMSMEDEN FRKRKLPVVS
SVVKVKKFNH DGEEEEEDDD YGSRTGSISS SVSVPAKPER RPSLPPSKQA NKNLILKAIS
EAQESVTKTT NYSTVPQKQT LPVAPRTRTS QEELLAEVVQ GQSRTPRISP PIKEEETKGD
SVEKNQGTQQ RQLLSRLQID PVMAETLQMS QDYYDMESMV HADTRSFILK KPKLSEEVVV
APNQESGMKT ADSLRVLSGH LMQTRDLVQP DKPASPKFIV TLDGVPSPPG YMSDQEEDMC
FEGMKPVNQT AASNKGLRGL LHPQQLHLLS RQLEDPNGSF SNAEMSELSV AQKPEKLLER
CKYWPACKNG DECAYHHPIS PCKAFPNCKF AEKCLFVHPN CKYDAKCTKP DCPFTHVSRR
IPVLSPKPAV APPAPPSSSQ LCRYFPACKK MECPFYHPKH CRFNTQCTRP DCTFYHPTIN
VPPRHALKWI RPQTSE
