ZN644_HUMAN
ID ZN644_HUMAN Reviewed; 1327 AA.
AC Q9H582; A2RU71; Q2TAM0; Q5TCC0; Q6BEP7; Q6P446; Q6PI06; Q7LG67; Q9ULJ9;
DT 07-DEC-2004, integrated into UniProtKB/Swiss-Prot.
DT 07-DEC-2004, sequence version 2.
DT 03-AUG-2022, entry version 173.
DE RecName: Full=Zinc finger protein 644;
DE AltName: Full=Zinc finger motif enhancer-binding protein 2;
DE Short=Zep-2;
GN Name=ZNF644; Synonyms=KIAA1221, ZEP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
RA Fukamizu A.;
RT "Zep-2: zinc finger motif enhancer binding protein-2.";
RL Submitted (OCT-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Pericardium;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Duodenum, Eye, and Skin;
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 [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 46-1327 (ISOFORM 1).
RC TISSUE=Brain;
RX PubMed=10574462; DOI=10.1093/dnares/6.5.337;
RA Nagase T., Ishikawa K., Kikuno R., Hirosawa M., Nomura N., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XV. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 6:337-345(1999).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, 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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-309 AND SER-1000, 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 [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000, 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1000 AND SER-1189, 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 [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-199; SER-820 AND SER-1000,
RP AND IDENTIFICATION 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 [12]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-39; LYS-319; LYS-339; LYS-346;
RP LYS-627; LYS-641; LYS-645; LYS-658; LYS-718; LYS-762 AND LYS-1094, 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 [13]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-346, 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 [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-39; LYS-346; LYS-645; LYS-658;
RP LYS-712; LYS-718; LYS-762 AND LYS-1094, AND IDENTIFICATION BY MASS
RP 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 [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-346; LYS-553; LYS-712; LYS-718;
RP LYS-733; LYS-762 AND LYS-1094, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-39; LYS-82; LYS-112; LYS-168;
RP LYS-185; LYS-193; LYS-213; LYS-263; LYS-284; LYS-294; LYS-299; LYS-319;
RP LYS-339; LYS-344; LYS-346; LYS-388; LYS-390; LYS-485; LYS-509; LYS-553;
RP LYS-573; LYS-589; LYS-598; LYS-603; LYS-627; LYS-641; LYS-645; LYS-658;
RP LYS-676; LYS-712; LYS-718; LYS-720; LYS-727; LYS-733; LYS-762; LYS-763;
RP LYS-791; LYS-795; LYS-817; LYS-835; LYS-843; LYS-962; LYS-1009; LYS-1031;
RP LYS-1088; LYS-1094; LYS-1110; LYS-1133; LYS-1157; LYS-1165; LYS-1176;
RP LYS-1192; LYS-1205; LYS-1234 AND LYS-1308, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17]
RP VARIANT [LARGE SCALE ANALYSIS] GLN-53.
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 [18]
RP VARIANTS MYP21 VAL-587; GLY-672; GLY-680 AND TYR-699, AND TISSUE
RP SPECIFICITY.
RX PubMed=21695231; DOI=10.1371/journal.pgen.1002084;
RA Shi Y., Li Y., Zhang D., Zhang H., Li Y., Lu F., Liu X., He F., Gong B.,
RA Cai L., Li R., Liao S., Ma S., Lin H., Cheng J., Zheng H., Shan Y.,
RA Chen B., Hu J., Jin X., Zhao P., Chen Y., Zhang Y., Lin Y., Li X., Fan Y.,
RA Yang H., Wang J., Yang Z.;
RT "Exome sequencing identifies ZNF644 mutations in high myopia.";
RL PLoS Genet. 7:E1002084-E1002084(2011).
RN [19]
RP VARIANTS MYP21 MET-242 AND VAL-274, AND VARIANTS TYR-706; GLU-707 AND
RP HIS-1100.
RX PubMed=22539872;
RA Tran-Viet K.N., St Germain E., Soler V., Powell C., Lim S.H., Klemm T.,
RA Saw S.M., Young T.L.;
RT "Study of a US cohort supports the role of ZNF644 and high-grade myopia
RT susceptibility.";
RL Mol. Vis. 18:937-944(2012).
RN [20]
RP VARIANTS MYP21 LYS-305; ALA-401; SER-956; CYS-1089 AND GLY-1278.
RX PubMed=24991186;
RA Xiang X., Wang T., Tong P., Li Y., Guo H., Wan A., Xia L., Liu Y., Li Y.,
RA Tian Q., Shen L., Cai X., Tian L., Jin X., Xia K., Hu Z.;
RT "New ZNF644 mutations identified in patients with high myopia.";
RL Mol. Vis. 20:939-946(2014).
RN [21]
RP VARIANTS MYP21 GLY-672; THR-683 AND HIS-851, AND VARIANTS MET-369 AND
RP THR-550.
RX PubMed=25525168; DOI=10.1167/iovs.14-14850;
RA Jiang D., Li J., Xiao X., Li S., Jia X., Sun W., Guo X., Zhang Q.;
RT "Detection of mutations in LRPAP1, CTSH, LEPREL1, ZNF644, SLC39A5, and SCO2
RT in 298 families with early-onset high myopia by exome sequencing.";
RL Invest. Ophthalmol. Vis. Sci. 56:339-345(2015).
CC -!- FUNCTION: May be involved in transcriptional regulation.
CC -!- SUBCELLULAR LOCATION: Nucleus.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q9H582-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9H582-2; Sequence=VSP_012158, VSP_012159;
CC Name=3;
CC IsoId=Q9H582-3; Sequence=VSP_015855, VSP_015856;
CC -!- TISSUE SPECIFICITY: Expressed in liver, placenta, retina and retinal
CC pigment epithelium. {ECO:0000269|PubMed:21695231}.
CC -!- DISEASE: Myopia 21, autosomal dominant (MYP21) [MIM:614167]: A
CC refractive error of the eye, in which parallel rays from a distant
CC object come to focus in front of the retina, vision being better for
CC near objects than for far. {ECO:0000269|PubMed:21695231,
CC ECO:0000269|PubMed:22539872, ECO:0000269|PubMed:24991186,
CC ECO:0000269|PubMed:25525168}. Note=The disease is caused by variants
CC affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the krueppel C2H2-type zinc-finger protein
CC family. {ECO:0000305}.
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DR EMBL; AB019255; BAD32777.1; -; mRNA.
DR EMBL; AK291520; BAF84209.1; -; mRNA.
DR EMBL; AL136109; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471097; EAW73118.1; -; Genomic_DNA.
DR EMBL; BC050656; AAH50656.1; -; mRNA.
DR EMBL; BC063683; AAH63683.2; -; mRNA.
DR EMBL; BC110841; AAI10842.1; -; mRNA.
DR EMBL; BC132776; AAI32777.1; -; mRNA.
DR EMBL; BC132778; AAI32779.1; -; mRNA.
DR EMBL; AB033047; BAA86535.1; -; mRNA.
DR CCDS; CCDS731.1; -. [Q9H582-1]
DR CCDS; CCDS732.1; -. [Q9H582-3]
DR RefSeq; NP_057704.2; NM_016620.3. [Q9H582-3]
DR RefSeq; NP_115562.3; NM_032186.4. [Q9H582-3]
DR RefSeq; NP_958357.1; NM_201269.2. [Q9H582-1]
DR RefSeq; XP_016857977.1; XM_017002488.1. [Q9H582-1]
DR RefSeq; XP_016857978.1; XM_017002489.1. [Q9H582-1]
DR RefSeq; XP_016857979.1; XM_017002490.1. [Q9H582-1]
DR RefSeq; XP_016857980.1; XM_017002491.1. [Q9H582-1]
DR RefSeq; XP_016857981.1; XM_017002492.1. [Q9H582-3]
DR RefSeq; XP_016857982.1; XM_017002493.1. [Q9H582-3]
DR RefSeq; XP_016857983.1; XM_017002494.1. [Q9H582-3]
DR AlphaFoldDB; Q9H582; -.
DR BioGRID; 123913; 160.
DR IntAct; Q9H582; 98.
DR MINT; Q9H582; -.
DR STRING; 9606.ENSP00000337008; -.
DR iPTMnet; Q9H582; -.
DR PhosphoSitePlus; Q9H582; -.
DR BioMuta; ZNF644; -.
DR DMDM; 56404958; -.
DR EPD; Q9H582; -.
DR jPOST; Q9H582; -.
DR MassIVE; Q9H582; -.
DR MaxQB; Q9H582; -.
DR PaxDb; Q9H582; -.
DR PeptideAtlas; Q9H582; -.
DR PRIDE; Q9H582; -.
DR ProteomicsDB; 80897; -. [Q9H582-1]
DR ProteomicsDB; 80898; -. [Q9H582-2]
DR ProteomicsDB; 80899; -. [Q9H582-3]
DR Antibodypedia; 46920; 43 antibodies from 14 providers.
DR DNASU; 84146; -.
DR Ensembl; ENST00000337393.10; ENSP00000337008.5; ENSG00000122482.22. [Q9H582-1]
DR Ensembl; ENST00000347275.9; ENSP00000340828.5; ENSG00000122482.22. [Q9H582-3]
DR Ensembl; ENST00000361321.5; ENSP00000354659.5; ENSG00000122482.22. [Q9H582-3]
DR Ensembl; ENST00000370440.5; ENSP00000359469.1; ENSG00000122482.22. [Q9H582-1]
DR GeneID; 84146; -.
DR KEGG; hsa:84146; -.
DR MANE-Select; ENST00000337393.10; ENSP00000337008.5; NM_201269.3; NP_958357.1.
DR UCSC; uc001dnv.4; human. [Q9H582-1]
DR CTD; 84146; -.
DR DisGeNET; 84146; -.
DR GeneCards; ZNF644; -.
DR HGNC; HGNC:29222; ZNF644.
DR HPA; ENSG00000122482; Low tissue specificity.
DR MalaCards; ZNF644; -.
DR MIM; 614159; gene.
DR MIM; 614167; phenotype.
DR neXtProt; NX_Q9H582; -.
DR OpenTargets; ENSG00000122482; -.
DR PharmGKB; PA134984168; -.
DR VEuPathDB; HostDB:ENSG00000122482; -.
DR eggNOG; KOG1721; Eukaryota.
DR GeneTree; ENSGT00940000158258; -.
DR HOGENOM; CLU_005590_0_0_1; -.
DR InParanoid; Q9H582; -.
DR OMA; QSALFIH; -.
DR OrthoDB; 1318335at2759; -.
DR PhylomeDB; Q9H582; -.
DR TreeFam; TF333705; -.
DR PathwayCommons; Q9H582; -.
DR SignaLink; Q9H582; -.
DR BioGRID-ORCS; 84146; 23 hits in 1084 CRISPR screens.
DR ChiTaRS; ZNF644; human.
DR GeneWiki; ZNF644; -.
DR GenomeRNAi; 84146; -.
DR Pharos; Q9H582; Tbio.
DR PRO; PR:Q9H582; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9H582; protein.
DR Bgee; ENSG00000122482; Expressed in calcaneal tendon and 183 other tissues.
DR ExpressionAtlas; Q9H582; baseline and differential.
DR Genevisible; Q9H582; HS.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0000981; F:DNA-binding transcription factor activity, RNA polymerase II-specific; IDA:GO_Central.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0000978; F:RNA polymerase II cis-regulatory region sequence-specific DNA binding; IDA:GO_Central.
DR GO; GO:0001222; F:transcription corepressor binding; IPI:ARUK-UCL.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IBA:GO_Central.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR InterPro; IPR013087; Znf_C2H2_type.
DR SMART; SM00355; ZnF_C2H2; 8.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 4.
DR PROSITE; PS50157; ZINC_FINGER_C2H2_2; 3.
PE 1: Evidence at protein level;
KW Alternative splicing; Disease variant; DNA-binding; Isopeptide bond;
KW Metal-binding; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW Transcription; Transcription regulation; Ubl conjugation; Zinc;
KW Zinc-finger.
FT CHAIN 1..1327
FT /note="Zinc finger protein 644"
FT /id="PRO_0000047698"
FT ZN_FING 410..432
FT /note="C2H2-type 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 448..470
FT /note="C2H2-type 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 496..518
FT /note="C2H2-type 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 525..548
FT /note="C2H2-type 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 586..609
FT /note="C2H2-type 5"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 963..987
FT /note="C2H2-type 6"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT ZN_FING 1038..1060
FT /note="C2H2-type 7"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00042"
FT REGION 126..147
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 779..804
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 788..804
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 199
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 309
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 820
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1000
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 1189
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT CROSSLNK 39
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 82
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 112
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 168
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 185
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 193
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 213
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 263
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 284
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 294
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 299
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 319
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 339
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 344
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 346
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO1); alternate"
FT /evidence="ECO:0007744|PubMed:25114211"
FT CROSSLNK 346
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:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 388
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 390
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 485
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 509
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 553
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 573
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 589
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 598
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 603
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 627
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 641
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 645
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 658
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 676
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 712
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT CROSSLNK 718
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 720
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 727
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 733
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:28112733"
FT CROSSLNK 762
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 763
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 791
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 795
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 817
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 835
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 843
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 962
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1009
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1031
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1088
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1094
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 1110
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1133
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1157
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1165
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1176
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1192
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1205
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1234
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 1308
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..1222
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015855"
FT VAR_SEQ 1223..1229
FT /note="MDLTMHS -> MLIRQNL (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_015856"
FT VAR_SEQ 1230..1232
FT /note="ALD -> GLI (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_012158"
FT VAR_SEQ 1233..1327
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|Ref.1"
FT /id="VSP_012159"
FT VARIANT 53
FT /note="E -> Q (in a breast cancer sample; somatic
FT mutation)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_035593"
FT VARIANT 242
FT /note="T -> M (in MYP21; unknown pathological significance;
FT dbSNP:rs143932357)"
FT /evidence="ECO:0000269|PubMed:22539872"
FT /id="VAR_073995"
FT VARIANT 274
FT /note="E -> V (in MYP21; unknown pathological significance;
FT dbSNP:rs774685437)"
FT /evidence="ECO:0000269|PubMed:22539872"
FT /id="VAR_073996"
FT VARIANT 305
FT /note="E -> K (in MYP21; unknown pathological significance;
FT dbSNP:rs149597385)"
FT /evidence="ECO:0000269|PubMed:24991186"
FT /id="VAR_073997"
FT VARIANT 369
FT /note="K -> M (variant of uncertain significance)"
FT /evidence="ECO:0000269|PubMed:25525168"
FT /id="VAR_073998"
FT VARIANT 401
FT /note="T -> A (in MYP21; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24991186"
FT /id="VAR_073999"
FT VARIANT 550
FT /note="A -> T (in dbSNP:rs754440728)"
FT /evidence="ECO:0000269|PubMed:25525168"
FT /id="VAR_074000"
FT VARIANT 556
FT /note="M -> V (in dbSNP:rs17131242)"
FT /id="VAR_052885"
FT VARIANT 587
FT /note="I -> V (in MYP21; dbSNP:rs146936371)"
FT /evidence="ECO:0000269|PubMed:21695231"
FT /id="VAR_066389"
FT VARIANT 672
FT /note="S -> G (in MYP21; dbSNP:rs387907109)"
FT /evidence="ECO:0000269|PubMed:21695231,
FT ECO:0000269|PubMed:25525168"
FT /id="VAR_066390"
FT VARIANT 680
FT /note="R -> G (in MYP21)"
FT /evidence="ECO:0000269|PubMed:21695231"
FT /id="VAR_066391"
FT VARIANT 683
FT /note="R -> T (in MYP21; unknown pathological significance;
FT dbSNP:rs201546602)"
FT /evidence="ECO:0000269|PubMed:25525168"
FT /id="VAR_074001"
FT VARIANT 699
FT /note="C -> Y (in MYP21)"
FT /evidence="ECO:0000269|PubMed:21695231"
FT /id="VAR_066392"
FT VARIANT 706
FT /note="H -> Y (in dbSNP:rs908368905)"
FT /evidence="ECO:0000269|PubMed:22539872"
FT /id="VAR_074002"
FT VARIANT 707
FT /note="K -> E (in dbSNP:rs12117237)"
FT /evidence="ECO:0000269|PubMed:22539872"
FT /id="VAR_074003"
FT VARIANT 794
FT /note="A -> V (in dbSNP:rs10922938)"
FT /id="VAR_052886"
FT VARIANT 851
FT /note="D -> H (in MYP21; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:25525168"
FT /id="VAR_074004"
FT VARIANT 956
FT /note="T -> S (in MYP21; unknown pathological significance;
FT dbSNP:rs1050960158)"
FT /evidence="ECO:0000269|PubMed:24991186"
FT /id="VAR_074005"
FT VARIANT 1089
FT /note="Y -> C (in MYP21; unknown pathological significance;
FT dbSNP:rs193167060)"
FT /evidence="ECO:0000269|PubMed:24991186"
FT /id="VAR_074006"
FT VARIANT 1100
FT /note="R -> H (in dbSNP:rs140271599)"
FT /evidence="ECO:0000269|PubMed:22539872"
FT /id="VAR_074007"
FT VARIANT 1278
FT /note="E -> G (in MYP21; unknown pathological
FT significance)"
FT /evidence="ECO:0000269|PubMed:24991186"
FT /id="VAR_074008"
FT CONFLICT 296
FT /note="D -> M (in Ref. 1; BAD32777)"
FT /evidence="ECO:0000305"
FT CONFLICT 1125
FT /note="L -> P (in Ref. 1; BAD32777)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1327 AA; 149565 MW; 53CE36BE21FC5056 CRC64;
MRSFLQQDVN KTKSRLNVLN GLANNMDDLK INTDITGAKE ELLDDNNFIS DKESGVHKPK
DCQTSFQKNN TLTLPEELSK DKSENALSGG QSSLFIHAGA PTVSSENFIL PKGAAVNGPV
SHSSLTKTSN MNKGSVSLTT GQPVDQPTTE SCSTLKVAAD LQLSTPQKAS QHQVLFLLSD
VAHAKNPTHS NKKLPTSASV GCDIQNSVGS NIKSDGTLIN QVEVGEDGED LLVKDDCVNT
VTGISSGTDG FRSENDTNWD PQKEFIQFLM TNEETVDKAP PHSKIGLEKK RKRKMDVSKI
TRYTEDCFSD SNCVPNKSKM QEVDFLEQNE ELQAVDSQKY ALSKVKPEST DEDLESVDAF
QHLIYNPDKC GEESSPVHTS TFLSNTLKKK CEESDSESPA TFSTEEPSFY PCTKCNVNFR
EKKHLHRHMM YHLDGNSHFR HLNVPRPYAC RECGRTFRDR NSLLKHMIIH QERRQKLMEE
IRELKELQDE GRSARLQCPQ CVFGTNCPKT FVQHAKTHEK DKRYYCCEEC NFMAVTENEL
ECHRGIAHGA VVKCPMVTSD IAQRKTQKKT FMKDSVVGSS KKSATYICKM CPFTTSAKSV
LKKHTEYLHS SSCVDSFGSP LGLDKRKNDI LEEPVDSDST KTLTKQQSTT FPKNSALKQD
VKRTFGSTSQ SSSFSKIHKR PHRIQKARKS IAQSGVNMCN QNSSPHKNVT IKSSVDQKPK
YFHQAAKEKS NAKANSHYLY RHKYENYRMI KKSGESYPVH FKKEEASSLN SLHLFSSSSN
SHNNFISDPH KPDAKRPESF KDHRRVAVKR VIKESKKESS VGGEDLDSYP DFLHKMTVVV
LQKLNSAEKK DSYETEDESS WDNVELGDYT TQAIEDETYS DINQEHVNLF PLFKSKVEGQ
EPGENATLSY DQNDGFYFEY YEDTGSNNFL HEIHDPQHLE TADASLSKHS SVFHWTDLSL
EKKSCPYCPA TFETGVGLSN HVRGHLHRAG LSYEARHVVS PEQIATSDKM QHFKRTGTGT
PVKRVRKAIE KSETTSEHTC QLCGGWFDTK IGLSNHVRGH LKRLGKTKWD AHKSPICVLN
EMMQNEEKYE KILKALNSRR IIPRPFVAQK LASSDDFISQ NVIPLEAYRN GLKTEALSVS
ASEEEGLNFL NEYDETKPEL PSGKKNQSLT LIELLKNKRM GEERNSAISP QKIHNQTARK
RFVQKCVLPL NEDSPLMYQP QKMDLTMHSA LDCKQKKSRS RSGSKKKMLT LPHGADEVYI
LRCRFCGLVF RGPLSVQEDW IKHLQRHIVN ANLPRTGAGM VEVTSLLKKP ASITETSFSL
LMAEAAS
