HELZ2_HUMAN
ID HELZ2_HUMAN Reviewed; 2649 AA.
AC Q9BYK8; Q3C2G2; Q4VXQ1; Q8TEF3; Q96ND3; Q9C094;
DT 30-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT 11-JAN-2011, sequence version 6.
DT 03-AUG-2022, entry version 198.
DE RecName: Full=Helicase with zinc finger domain 2 {ECO:0000305};
DE AltName: Full=ATP-dependent helicase PRIC285;
DE AltName: Full=Helicase with zinc finger 2, transcriptional coactivator;
DE AltName: Full=PPAR-alpha-interacting complex protein 285;
DE AltName: Full=PPAR-gamma DNA-binding domain-interacting protein 1;
DE Short=PDIP1;
DE Short=PPAR-gamma DBD-interacting protein 1;
DE AltName: Full=Peroxisomal proliferator-activated receptor A-interacting complex 285 kDa protein;
DE EC=3.6.4.-;
GN Name=HELZ2 {ECO:0000312|HGNC:HGNC:30021}; Synonyms=KIAA1769, PRIC285;
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), AND VARIANTS ASN-788; ARG-1123;
RP LEU-2016 AND GLU-2049.
RX PubMed=12189208; DOI=10.1073/pnas.182426699;
RA Surapureddi S., Yu S., Bu H., Hashimoto T., Yeldandi A.V., Kashireddy P.,
RA Cherkaoui-Malki M., Qi C., Zhu Y.-J., Rao M.S., Reddy J.K.;
RT "Identification of a transcriptionally active peroxisome proliferator-
RT activated receptor alpha-interacting cofactor complex in rat liver and
RT characterization of PRIC285 as a coactivator.";
RL Proc. Natl. Acad. Sci. U.S.A. 99:11836-11841(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), FUNCTION, INTERACTION WITH
RP PPARG, TISSUE SPECIFICITY, DOMAIN, AND VARIANTS ASN-788; ARG-1123; LEU-2016
RP AND GLU-2049.
RX PubMed=16239304; DOI=10.1210/en.2005-0450;
RA Tomaru T., Satoh T., Yoshino S., Ishizuka T., Hashimoto K., Monden T.,
RA Yamada M., Mori M.;
RT "Isolation and characterization of a transcriptional cofactor and its novel
RT isoform that bind the DNA-binding domain of peroxisome proliferator-
RT activated receptor gamma.";
RL Endocrinology 147:377-388(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND VARIANTS ASN-788;
RP ARG-1123; LEU-2016 AND GLU-2049.
RC TISSUE=Brain;
RX PubMed=11214970; DOI=10.1093/dnares/7.6.347;
RA Nagase T., Kikuno R., Hattori A., Kondo Y., Okumura K., Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. XIX. The
RT complete sequences of 100 new cDNA clones from brain which code for large
RT proteins in vitro.";
RL DNA Res. 7:347-355(2000).
RN [4]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=11780052; DOI=10.1038/414865a;
RA Deloukas P., Matthews L.H., Ashurst J.L., Burton J., Gilbert J.G.R.,
RA Jones M., Stavrides G., Almeida J.P., Babbage A.K., Bagguley C.L.,
RA Bailey J., Barlow K.F., Bates K.N., Beard L.M., Beare D.M., Beasley O.P.,
RA Bird C.P., Blakey S.E., Bridgeman A.M., Brown A.J., Buck D., Burrill W.D.,
RA Butler A.P., Carder C., Carter N.P., Chapman J.C., Clamp M., Clark G.,
RA Clark L.N., Clark S.Y., Clee C.M., Clegg S., Cobley V.E., Collier R.E.,
RA Connor R.E., Corby N.R., Coulson A., Coville G.J., Deadman R., Dhami P.D.,
RA Dunn M., Ellington A.G., Frankland J.A., Fraser A., French L., Garner P.,
RA Grafham D.V., Griffiths C., Griffiths M.N.D., Gwilliam R., Hall R.E.,
RA Hammond S., Harley J.L., Heath P.D., Ho S., Holden J.L., Howden P.J.,
RA Huckle E., Hunt A.R., Hunt S.E., Jekosch K., Johnson C.M., Johnson D.,
RA Kay M.P., Kimberley A.M., King A., Knights A., Laird G.K., Lawlor S.,
RA Lehvaeslaiho M.H., Leversha M.A., Lloyd C., Lloyd D.M., Lovell J.D.,
RA Marsh V.L., Martin S.L., McConnachie L.J., McLay K., McMurray A.A.,
RA Milne S.A., Mistry D., Moore M.J.F., Mullikin J.C., Nickerson T.,
RA Oliver K., Parker A., Patel R., Pearce T.A.V., Peck A.I.,
RA Phillimore B.J.C.T., Prathalingam S.R., Plumb R.W., Ramsay H., Rice C.M.,
RA Ross M.T., Scott C.E., Sehra H.K., Shownkeen R., Sims S., Skuce C.D.,
RA Smith M.L., Soderlund C., Steward C.A., Sulston J.E., Swann R.M.,
RA Sycamore N., Taylor R., Tee L., Thomas D.W., Thorpe A., Tracey A.,
RA Tromans A.C., Vaudin M., Wall M., Wallis J.M., Whitehead S.L.,
RA Whittaker P., Willey D.L., Williams L., Williams S.A., Wilming L.,
RA Wray P.W., Hubbard T., Durbin R.M., Bentley D.R., Beck S., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 20.";
RL Nature 414:865-871(2001).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1526-2649 (ISOFORMS 1/2).
RC TISSUE=Spleen;
RA Jikuya H., Takano J., Nomura N., Kikuno R., Nagase T., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human spleen.";
RL Submitted (JAN-2002) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2194-2649 (ISOFORMS 1/2).
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 [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1006, AND IDENTIFICATION BY
RP 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 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 [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1006, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
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 [11]
RP FUNCTION, INTERACTION WITH PPARG AND THRAP3, AND SUBCELLULAR LOCATION.
RX PubMed=23525231; DOI=10.1210/me.2012-1332;
RA Katano-Toki A., Satoh T., Tomaru T., Yoshino S., Ishizuka T., Ishii S.,
RA Ozawa A., Shibusawa N., Tsuchiya T., Saito T., Shimizu H., Hashimoto K.,
RA Okada S., Yamada M., Mori M.;
RT "THRAP3 interacts with HELZ2 and plays a novel role in adipocyte
RT differentiation.";
RL Mol. Endocrinol. 27:769-780(2013).
RN [12]
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 [13]
RP IDENTIFICATION BY MASS 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).
CC -!- FUNCTION: Helicase that acts as a transcriptional coactivator for a
CC number of nuclear receptors including PPARA, PPARG, THRA, THRB and
CC RXRA. {ECO:0000269|PubMed:16239304, ECO:0000269|PubMed:23525231}.
CC -!- SUBUNIT: Interacts with PPARA (via DNA-binding domain) and PPARG; the
CC interaction stimulates the transcriptional activity of PPARA and PPARG.
CC Interacts with THRAP3; the interaction is direct and HELZ2 and THRAP3
CC synergistically enhance the transcriptional activity of PPARG. It is
CC probably part of the peroxisome proliferator activated receptor alpha
CC interacting complex (PRIC). {ECO:0000269|PubMed:16239304,
CC ECO:0000269|PubMed:23525231}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:23525231}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=PDIP1-beta;
CC IsoId=Q9BYK8-1; Sequence=Displayed;
CC Name=2; Synonyms=PDIP1-alpha;
CC IsoId=Q9BYK8-2; Sequence=VSP_007297, VSP_007298;
CC -!- TISSUE SPECIFICITY: Expressed in various tissues including heart,
CC pancreas, skeletal muscle, colon, spleen, liver, kidney, lung,
CC peripheral blood and placenta. {ECO:0000269|PubMed:16239304}.
CC -!- DOMAIN: Contains 5 Leu-Xaa-Xaa-Leu-Leu (LXXLL) motifs. These motifs are
CC not required for interaction with PPARG. {ECO:0000269|PubMed:16239304}.
CC -!- MISCELLANEOUS: [Isoform 1]: More abundantly expressed than isoform 2.
CC -!- SIMILARITY: Belongs to the DNA2/NAM7 helicase family. {ECO:0000305}.
CC -!- CAUTION: PubMed:12189208 experiments have been carried out partly in
CC rat and partly in human. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAB21860.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAB70969.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AF517673; AAM74197.1; -; mRNA.
DR EMBL; AB201715; BAE46995.1; -; mRNA.
DR EMBL; AB051556; BAB21860.2; ALT_INIT; mRNA.
DR EMBL; AL121829; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AK074171; BAB84997.1; -; mRNA.
DR EMBL; AK055611; BAB70969.1; ALT_FRAME; mRNA.
DR CCDS; CCDS13527.1; -. [Q9BYK8-2]
DR CCDS; CCDS33508.1; -. [Q9BYK8-1]
DR RefSeq; NP_001032412.2; NM_001037335.2. [Q9BYK8-1]
DR RefSeq; NP_208384.3; NM_033405.3. [Q9BYK8-2]
DR AlphaFoldDB; Q9BYK8; -.
DR SMR; Q9BYK8; -.
DR BioGRID; 124528; 59.
DR IntAct; Q9BYK8; 10.
DR STRING; 9606.ENSP00000417401; -.
DR iPTMnet; Q9BYK8; -.
DR PhosphoSitePlus; Q9BYK8; -.
DR BioMuta; HELZ2; -.
DR DMDM; 317373591; -.
DR EPD; Q9BYK8; -.
DR jPOST; Q9BYK8; -.
DR MassIVE; Q9BYK8; -.
DR MaxQB; Q9BYK8; -.
DR PaxDb; Q9BYK8; -.
DR PeptideAtlas; Q9BYK8; -.
DR PRIDE; Q9BYK8; -.
DR ProteomicsDB; 79663; -. [Q9BYK8-1]
DR ProteomicsDB; 79664; -. [Q9BYK8-2]
DR Antibodypedia; 63897; 47 antibodies from 17 providers.
DR DNASU; 85441; -.
DR Ensembl; ENST00000427522.6; ENSP00000393257.2; ENSG00000130589.16. [Q9BYK8-2]
DR Ensembl; ENST00000467148.1; ENSP00000417401.1; ENSG00000130589.16. [Q9BYK8-1]
DR GeneID; 85441; -.
DR KEGG; hsa:85441; -.
DR MANE-Select; ENST00000467148.2; ENSP00000417401.1; NM_001037335.2; NP_001032412.2.
DR UCSC; uc002yfl.2; human. [Q9BYK8-1]
DR CTD; 85441; -.
DR DisGeNET; 85441; -.
DR GeneCards; HELZ2; -.
DR HGNC; HGNC:30021; HELZ2.
DR HPA; ENSG00000130589; Low tissue specificity.
DR MIM; 611265; gene.
DR neXtProt; NX_Q9BYK8; -.
DR OpenTargets; ENSG00000130589; -.
DR VEuPathDB; HostDB:ENSG00000130589; -.
DR eggNOG; KOG1804; Eukaryota.
DR eggNOG; KOG2102; Eukaryota.
DR GeneTree; ENSGT00940000160694; -.
DR HOGENOM; CLU_000407_0_0_1; -.
DR InParanoid; Q9BYK8; -.
DR OMA; ATLQYCC; -.
DR OrthoDB; 5044at2759; -.
DR PhylomeDB; Q9BYK8; -.
DR PathwayCommons; Q9BYK8; -.
DR Reactome; R-HSA-1368082; RORA activates gene expression.
DR Reactome; R-HSA-1368108; BMAL1:CLOCK,NPAS2 activates circadian gene expression.
DR Reactome; R-HSA-1989781; PPARA activates gene expression.
DR Reactome; R-HSA-2151201; Transcriptional activation of mitochondrial biogenesis.
DR Reactome; R-HSA-2426168; Activation of gene expression by SREBF (SREBP).
DR Reactome; R-HSA-381340; Transcriptional regulation of white adipocyte differentiation.
DR Reactome; R-HSA-400206; Regulation of lipid metabolism by PPARalpha.
DR Reactome; R-HSA-400253; Circadian Clock.
DR Reactome; R-HSA-9707564; Cytoprotection by HMOX1.
DR Reactome; R-HSA-9707616; Heme signaling.
DR SignaLink; Q9BYK8; -.
DR BioGRID-ORCS; 85441; 23 hits in 1082 CRISPR screens.
DR ChiTaRS; HELZ2; human.
DR GeneWiki; PRIC285; -.
DR GenomeRNAi; 85441; -.
DR Pharos; Q9BYK8; Tdark.
DR PRO; PR:Q9BYK8; -.
DR Proteomes; UP000005640; Chromosome 20.
DR RNAct; Q9BYK8; protein.
DR Bgee; ENSG00000130589; Expressed in granulocyte and 99 other tissues.
DR Genevisible; Q9BYK8; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0030374; F:nuclear receptor coactivator activity; IDA:GO_Central.
DR GO; GO:0004540; F:ribonuclease activity; IEA:InterPro.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0003724; F:RNA helicase activity; IBA:GO_Central.
DR GO; GO:0000184; P:nuclear-transcribed mRNA catabolic process, nonsense-mediated decay; IBA:GO_Central.
DR GO; GO:0045944; P:positive regulation of transcription by RNA polymerase II; IDA:UniProtKB.
DR CDD; cd18808; SF1_C_Upf1; 2.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR045055; DNA2/NAM7-like.
DR InterPro; IPR041679; DNA2/NAM7-like_C.
DR InterPro; IPR041677; DNA2/NAM7_AAA_11.
DR InterPro; IPR031191; HELZ2.
DR InterPro; IPR012340; NA-bd_OB-fold.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR001900; RNase_II/R.
DR InterPro; IPR022966; RNase_II/R_CS.
DR InterPro; IPR036236; Znf_C2H2_sf.
DR PANTHER; PTHR10887; PTHR10887; 1.
DR PANTHER; PTHR10887:SF428; PTHR10887:SF428; 1.
DR Pfam; PF13086; AAA_11; 2.
DR Pfam; PF13087; AAA_12; 2.
DR Pfam; PF00773; RNB; 1.
DR SMART; SM00955; RNB; 1.
DR SUPFAM; SSF50249; SSF50249; 2.
DR SUPFAM; SSF52540; SSF52540; 2.
DR SUPFAM; SSF57667; SSF57667; 1.
DR PROSITE; PS00028; ZINC_FINGER_C2H2_1; 1.
PE 1: Evidence at protein level;
KW Activator; Alternative splicing; ATP-binding; DNA-binding; Helicase;
KW Hydrolase; Metal-binding; Nucleotide-binding; Nucleus; Phosphoprotein;
KW Reference proteome; Repeat; Transcription; Transcription regulation; Zinc;
KW Zinc-finger.
FT CHAIN 1..2649
FT /note="Helicase with zinc finger domain 2"
FT /id="PRO_0000058561"
FT ZN_FING 40..64
FT /note="C2H2-type; atypical"
FT REGION 9..32
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 563..1059
FT /note="Interaction with THRAP3"
FT /evidence="ECO:0000269|PubMed:23525231"
FT REGION 2135..2649
FT /note="Interaction with THRAP3"
FT /evidence="ECO:0000269|PubMed:23525231"
FT MOTIF 667..670
FT /note="DEAA box"
FT MOTIF 1075..1079
FT /note="LXXLL motif 1"
FT MOTIF 1118..1122
FT /note="LXXLL motif 2"
FT MOTIF 1173..1177
FT /note="LXXLL motif 3"
FT MOTIF 2012..2016
FT /note="LXXLL motif 4"
FT MOTIF 2229..2233
FT /note="LXXLL motif 5"
FT BINDING 544..551
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT BINDING 2174..2181
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 1006
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..569
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12189208,
FT ECO:0000303|PubMed:16239304"
FT /id="VSP_007297"
FT VAR_SEQ 570..576
FT /note="LICTHTN -> MSSSPSR (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:12189208,
FT ECO:0000303|PubMed:16239304"
FT /id="VSP_007298"
FT VARIANT 788
FT /note="S -> N (in dbSNP:rs438363)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:12189208, ECO:0000269|PubMed:16239304"
FT /id="VAR_015597"
FT VARIANT 1123
FT /note="H -> R (in dbSNP:rs310632)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:12189208, ECO:0000269|PubMed:16239304"
FT /id="VAR_015598"
FT VARIANT 1152
FT /note="S -> L (in dbSNP:rs35817585)"
FT /id="VAR_047038"
FT VARIANT 1308
FT /note="V -> L (in dbSNP:rs310631)"
FT /id="VAR_047039"
FT VARIANT 1381
FT /note="R -> K (in dbSNP:rs3810487)"
FT /id="VAR_047040"
FT VARIANT 1821
FT /note="L -> R (in dbSNP:rs3810486)"
FT /id="VAR_047041"
FT VARIANT 1889
FT /note="T -> A (in dbSNP:rs34980032)"
FT /id="VAR_047042"
FT VARIANT 2016
FT /note="P -> L (in dbSNP:rs3810485)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:12189208, ECO:0000269|PubMed:16239304"
FT /id="VAR_015599"
FT VARIANT 2049
FT /note="Q -> E (in dbSNP:rs3810483)"
FT /evidence="ECO:0000269|PubMed:11214970,
FT ECO:0000269|PubMed:12189208, ECO:0000269|PubMed:16239304"
FT /id="VAR_015600"
FT VARIANT 2170
FT /note="T -> M (in dbSNP:rs3810481)"
FT /id="VAR_047043"
FT CONFLICT 196
FT /note="V -> A (in Ref. 2; BAE46995)"
FT /evidence="ECO:0000305"
FT CONFLICT 327..329
FT /note="FNR -> SNH (in Ref. 2; BAE46995)"
FT /evidence="ECO:0000305"
FT CONFLICT 442
FT /note="E -> G (in Ref. 2; BAE46995)"
FT /evidence="ECO:0000305"
FT CONFLICT 836
FT /note="G -> D (in Ref. 2; BAE46995)"
FT /evidence="ECO:0000305"
FT CONFLICT 1873
FT /note="V -> A (in Ref. 2; BAE46995)"
FT /evidence="ECO:0000305"
FT CONFLICT 2203
FT /note="G -> S (in Ref. 2; BAE46995)"
FT /evidence="ECO:0000305"
FT CONFLICT 2383
FT /note="V -> A (in Ref. 2; BAE46995)"
FT /evidence="ECO:0000305"
FT CONFLICT 2626
FT /note="F -> L (in Ref. 2; BAE46995)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 2649 AA; 294651 MW; 419573D5AEE700D7 CRC64;
MAVWEAEQLG GLQRGDLLTP PAPDGDGRTA PLGQPPGAQL YCPACLVTCH SQEAFENHCA
SSEHAQMVAF DQALPWEHRS PPPGLSKFEL CPKPDLCEYG DACTKAHSAQ ELQEWVRRTQ
AVELRGQAAW QDGLVPYQER LLAEYQRSSS EVLVLAETLD GVRVTCNQPL MYQAQERKTQ
YSWTFAVHSE EPLLHVALLK QEPGADFSLV APGLPPGRLY ARGERFRVPS STADFQVGVR
VQAASFGTFE QWVVFDFGRR PVLLQKLGLQ LGQGRRPGPC RNLALGHPEE MERWHTGNRH
VVPGVERTAE QTALMAKYKG PALALEFNRS SVASGPISPT NYRQRMHQFL YEEEAAQQQL
VAKLTLRGQV FLKTALQTPA LNMLFAPPGA LYAEVPVPSS LMPDTDQGFL LGRAVSTALV
APVPAPDNTV FEVRLERRAS SEQALWLLLP ARCCLALGLQ PEARLVLEVQ FQIDPMTFRL
WHQAVDTLPE EQLVVPDLPT CALPRPWSVP PLRRGNRKQE LAVALIAGWG PGDGRRVPPL
LIYGPFGTGK TYTLAMASLE VIRRPETKVL ICTHTNSAAD IYIREYFHSH VSGGHPEATP
LRVMYTDRPL SQTDPVTLQY CCLTDDRQAF RPPTRAELAR HRVVVTTTSQ ARELRVPVGF
FSHILIDEAA QMLECEALTP LAYASHGTRL VLAGDHMQVT PRLFSVARAR AAEHTLLHRL
FLCYQQETHE VARQSRLVFH ENYRCTDAIV SFISRHFYVA KGNPIHARGK VPPHPRHYPL
MFCHVAGSPD RDMSMASWLN LAEIAQVVEK VQEAYNTWPS CWGGREQRCI CVVSHGAQVS
ALRQELRRRD LGQVSVGSFE ILPGRQFRVV VLSTVHTCQS LLSPGALAPE FFTDARVLNT
VLTRAQSQLV VVGDAVALCS FGACGKLWES FIRECVERHS VCPEGLSMEQ VEQGVAQRRR
WPPRGTQAGA AGNWEAAPEP VGDLAEEQAA VVTAMVKAEP GDEALSPASR DITATTAQTE
AAAAPAGDAV KEDVVPGACA AGAAAAAGVE STEAEDAEAD FWPWDGELNA DDAILRELLD
ESQKVMVTVG EDGLLDTVAR PESLQQARLY ENLPPAALRK LLHAEPERYR HCSFVPETFE
RASAIPLDDA SSGPIQVRGR LDCGMAFAGD EVLVQLLSGD KAPEGRLRGR VLGVLKRKRH
ELAFVCRMDT WDPRIMVPIN GSVTKIFVAE LKDPSQVPIY SLRKGRLQRV GLERLTAEAR
HSRLFWVQIV LWRQGFYYPL GIVREVLPEA STWEQGLRIL GLEYSLRVPP SDQATITKVL
QKYHTELGRV AGRREDCRAF LTFTVDPQGA CNLDDALSVR DLGPRCEVAV HITDVASFVP
RDGVLDVEAR RQGAAFYAPG REPVPMLPAS LCQDVLSLLP GRDRLAISLF LTMEKASGQL
KSLRFAPSVV QSDRQLSYEE AEEVIRQHPG AGRELPARLD SVDACVVAAC YFSRLLRRHR
LRSDCFYEQP DEDGTLGFRA AHIMVKEYMI QFNRLVAEFL VGSECTRTVT PLRWQPAPRS
QQLKALCEKH GDRVPLSLHL GHHLHGGGGS PPDTRLHLLA SLWKQVQFAA RTQDYEQMVD
LVTTDDMHPF LAPAGRDLRK ALERSAFGRC ARGHQQQGGH YSLQVDWYTW ATSPIRRYLD
VVLQRQILLA LGHGGSAYSA RDIDGLCQAF SLQHALAQSY QRRARSLHLA VQLKAQPLDK
LGFVVDVEAG SRCFRLLFPS NRETLPDPCP VPYGSLQLAE HPHALAGRPG LRLLWRRRVY
SAQGSSPPLP LPGTVPDPHT LAVETALWKQ LLELVELQRW PEAAALIQEK GEASQRRELV
QVQRSHCGHF LEVARELGSG DTLQVQLGTS LQHGFLVPSP QLWTVAPGFS LCLEHVERPG
DCFSGRVYRA PRDRYRDVDE YACVWEPFCA LESATGAVAE NDSVTLQHLS VSWEASRTPQ
GQLQGAFRLE AAFLEENCAD INFSCCYLCI RLEGLPAPTA SPRPGPSSLG PGLNVDPGTY
TWVAHGQTQD WDQERRADRQ EAPRRVHLFV HHMGMEKVPE EVLRPGTLFT VELLPKQLPD
LRKEEAVRGL EEASPLVTSI ALGRPVPQPL CRVIPSRFLE RQTYNIPGGR HKLNPSQNVA
VREALEKPFT VIQGPPGTGK TIVGLHIVFW FHKSNQEQVQ PGGPPRGEKR LGGPCILYCG
PSNKSVDVLA GLLLRRMELK PLRVYSEQAE ASEFPVPRVG SRKLLRKSPR EGRPNQSLRS
ITLHHRIRQA PNPYSSEIKA FDTRLQRGEL FSREDLVWYK KVLWEARKFE LDRHEVILCT
CSCAASASLK ILDVRQILVD EAGMATEPET LIPLVQFPQA EKVVLLGDHK QLRPVVKNER
LQNLGLDRSL FERYHEDAHM LDTQYRMHEG ICAFPSVAFY KSKLKTWQGL RRPPSVLGHA
GKESCPVIFG HVQGHERSLL VSTDEGNENS KANLEEVAEV VRITKQLTLG RTVEPQDIAV
LTPYNAQASE ISKALRREGI AGVAVSSITK SQGSEWRYVL VSTVRTCAKS DLDQRPTKSW
LKKFLGFVVD PNQVNVAVTR AQEGLCLIGD HLLLRCCPLW RSLLDFCEAQ QTLVPAGQVR
VCRRPTMPS
