ULK3_HUMAN
ID ULK3_HUMAN Reviewed; 472 AA.
AC Q6PHR2; B2RXK3; B4DFT0; B4DRQ7; D3DW68; Q9NPN5; Q9UFS4;
DT 19-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 22-SEP-2009, sequence version 2.
DT 03-AUG-2022, entry version 163.
DE RecName: Full=Serine/threonine-protein kinase ULK3;
DE EC=2.7.11.1;
DE AltName: Full=Unc-51-like kinase 3;
GN Name=ULK3;
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 [LARGE SCALE MRNA] (ISOFORMS 1 AND 4).
RC TISSUE=Amygdala, and 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 [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16572171; DOI=10.1038/nature04601;
RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT "Analysis of the DNA sequence and duplication history of human chromosome
RT 15.";
RL Nature 440:671-675(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 2 AND 3).
RC TISSUE=Blood, and Brain;
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 162-472 (ISOFORM 2).
RG The European IMAGE consortium;
RL Submitted (JUL-2000) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-176, 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 FUNCTION, SUBCELLULAR LOCATION, AND INDUCTION.
RX PubMed=19279323; DOI=10.1101/gad.519709;
RA Young A.R., Narita M., Ferreira M., Kirschner K., Sadaie M., Darot J.F.,
RA Tavare S., Arakawa S., Shimizu S., Watt F.M., Narita M.;
RT "Autophagy mediates the mitotic senescence transition.";
RL Genes Dev. 23:798-803(2009).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AUTOPHOSPHORYLATION,
RP AND MUTAGENESIS OF LYS-44 AND LYS-139.
RX PubMed=19878745; DOI=10.1016/j.yexcr.2009.10.018;
RA Maloverjan A., Piirsoo M., Michelson P., Kogerman P., Osterlund T.;
RT "Identification of a novel serine/threonine kinase ULK3 as a positive
RT regulator of Hedgehog pathway.";
RL Exp. Cell Res. 316:627-637(2010).
RN [10]
RP FUNCTION, AUTOPHOSPHORYLATION, INTERACTION WITH SUFU, MUTAGENESIS OF
RP LYS-139, AND PHOSPHORYLATION AT SER-300; SER-350; SER-384 AND SER-464.
RX PubMed=20643644; DOI=10.1074/jbc.m110.133991;
RA Maloverjan A., Piirsoo M., Kasak L., Peil L., Osterlund T., Kogerman P.;
RT "Dual function of UNC-51-like kinase 3 (Ulk3) in the Sonic hedgehog
RT signaling pathway.";
RL J. Biol. Chem. 285:30079-30090(2010).
RN [11]
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).
CC -!- FUNCTION: Serine/threonine protein kinase that acts as a regulator of
CC Sonic hedgehog (SHH) signaling and autophagy. Acts as a negative
CC regulator of SHH signaling in the absence of SHH ligand: interacts with
CC SUFU, thereby inactivating the protein kinase activity and preventing
CC phosphorylation of GLI proteins (GLI1, GLI2 and/or GLI3). Positively
CC regulates SHH signaling in the presence of SHH: dissociates from SUFU,
CC autophosphorylates and mediates phosphorylation of GLI2, activating it
CC and promoting its nuclear translocation. Phosphorylates in vitro GLI2,
CC as well as GLI1 and GLI3, although less efficiently. Also acts as a
CC regulator of autophagy: following cellular senescence, able to induce
CC autophagy. {ECO:0000269|PubMed:19279323, ECO:0000269|PubMed:19878745,
CC ECO:0000269|PubMed:20643644}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-seryl-[protein] = ADP + H(+) + O-phospho-L-seryl-
CC [protein]; Xref=Rhea:RHEA:17989, Rhea:RHEA-COMP:9863, Rhea:RHEA-
CC COMP:11604, ChEBI:CHEBI:15378, ChEBI:CHEBI:29999, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:83421, ChEBI:CHEBI:456216; EC=2.7.11.1;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=ATP + L-threonyl-[protein] = ADP + H(+) + O-phospho-L-
CC threonyl-[protein]; Xref=Rhea:RHEA:46608, Rhea:RHEA-COMP:11060,
CC Rhea:RHEA-COMP:11605, ChEBI:CHEBI:15378, ChEBI:CHEBI:30013,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61977, ChEBI:CHEBI:456216;
CC EC=2.7.11.1;
CC -!- SUBUNIT: Interacts (via protein kinase domain) with SUFU.
CC {ECO:0000269|PubMed:20643644}.
CC -!- INTERACTION:
CC Q6PHR2; Q16543: CDC37; NbExp=2; IntAct=EBI-1383475, EBI-295634;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:19279323,
CC ECO:0000269|PubMed:19878745}. Note=Localizes to pre-autophagosomal
CC structure during cellular senescence.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=4;
CC Name=1;
CC IsoId=Q6PHR2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q6PHR2-2; Sequence=VSP_038147, VSP_038148;
CC Name=3;
CC IsoId=Q6PHR2-3; Sequence=VSP_039925;
CC Name=4;
CC IsoId=Q6PHR2-4; Sequence=VSP_057411;
CC -!- TISSUE SPECIFICITY: Widely expressed. Highest levels observed in fetal
CC brain. In adult tissues, high levels in brain, liver and kidney,
CC moderate levels in testis and adrenal gland and low levels in heart,
CC lung, stomach, thymus, prostate and placenta. In the brain, highest
CC expression in the hippocampus, high levels also detected in the
CC cerebellum, olfactory bulb and optic nerve. In the central nervous
CC system, lowest levels in the spinal cord.
CC {ECO:0000269|PubMed:19878745}.
CC -!- INDUCTION: Up-regulated during senescence.
CC {ECO:0000269|PubMed:19279323}.
CC -!- PTM: Autophosphorylated. Autophosphorylation is blocked by interaction
CC with SUFU. {ECO:0000269|PubMed:20643644}.
CC -!- MISCELLANEOUS: [Isoform 2]: May be produced at very low levels due to a
CC premature stop codon in the mRNA, leading to nonsense-mediated mRNA
CC decay. {ECO:0000305}.
CC -!- MISCELLANEOUS: [Isoform 3]: May be due to competing donor splice site.
CC {ECO:0000305}.
CC -!- SIMILARITY: Belongs to the protein kinase superfamily. Ser/Thr protein
CC kinase family. APG1/unc-51/ULK1 subfamily. {ECO:0000255|PROSITE-
CC ProRule:PRU00159}.
CC -!- SEQUENCE CAUTION:
CC Sequence=CAB55955.2; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK294245; BAG57541.1; -; mRNA.
DR EMBL; AK299380; BAG61369.1; -; mRNA.
DR EMBL; AL117482; CAB55955.2; ALT_INIT; mRNA.
DR EMBL; AC091230; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC036117; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC056423; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; CH471136; EAW99301.1; -; Genomic_DNA.
DR EMBL; CH471136; EAW99303.1; -; Genomic_DNA.
DR EMBL; BC157884; AAI57885.1; -; mRNA.
DR EMBL; AL360256; CAB96176.1; -; mRNA.
DR CCDS; CCDS45305.1; -. [Q6PHR2-1]
DR CCDS; CCDS76779.1; -. [Q6PHR2-3]
DR PIR; T17265; T17265.
DR RefSeq; NP_001092906.3; NM_001099436.3. [Q6PHR2-1]
DR RefSeq; NP_001271293.2; NM_001284364.2. [Q6PHR2-3]
DR RefSeq; NP_001271294.1; NM_001284365.2.
DR RefSeq; XP_005254346.1; XM_005254289.2. [Q6PHR2-4]
DR PDB; 4WZX; X-ray; 1.39 A; A=359-449.
DR PDB; 6FDY; X-ray; 1.70 A; U=2-277.
DR PDB; 6FDZ; X-ray; 2.55 A; U=2-277.
DR PDBsum; 4WZX; -.
DR PDBsum; 6FDY; -.
DR PDBsum; 6FDZ; -.
DR AlphaFoldDB; Q6PHR2; -.
DR SMR; Q6PHR2; -.
DR BioGRID; 117470; 21.
DR IntAct; Q6PHR2; 36.
DR STRING; 9606.ENSP00000400312; -.
DR BindingDB; Q6PHR2; -.
DR ChEMBL; CHEMBL5047; -.
DR DrugBank; DB12010; Fostamatinib.
DR DrugCentral; Q6PHR2; -.
DR iPTMnet; Q6PHR2; -.
DR PhosphoSitePlus; Q6PHR2; -.
DR BioMuta; ULK3; -.
DR DMDM; 259016166; -.
DR EPD; Q6PHR2; -.
DR jPOST; Q6PHR2; -.
DR MassIVE; Q6PHR2; -.
DR MaxQB; Q6PHR2; -.
DR PaxDb; Q6PHR2; -.
DR PeptideAtlas; Q6PHR2; -.
DR PRIDE; Q6PHR2; -.
DR ProteomicsDB; 4075; -.
DR ProteomicsDB; 67125; -. [Q6PHR2-1]
DR ProteomicsDB; 67126; -. [Q6PHR2-2]
DR ProteomicsDB; 67127; -. [Q6PHR2-3]
DR Antibodypedia; 27077; 409 antibodies from 34 providers.
DR DNASU; 25989; -.
DR Ensembl; ENST00000440863.7; ENSP00000400312.2; ENSG00000140474.14. [Q6PHR2-1]
DR Ensembl; ENST00000568667.5; ENSP00000457853.1; ENSG00000140474.14. [Q6PHR2-4]
DR Ensembl; ENST00000569437.5; ENSP00000456051.1; ENSG00000140474.14. [Q6PHR2-3]
DR GeneID; 25989; -.
DR KEGG; hsa:25989; -.
DR MANE-Select; ENST00000440863.7; ENSP00000400312.2; NM_001099436.4; NP_001092906.3.
DR UCSC; uc010ulq.3; human.
DR UCSC; uc059llp.1; human. [Q6PHR2-1]
DR CTD; 25989; -.
DR DisGeNET; 25989; -.
DR GeneCards; ULK3; -.
DR HGNC; HGNC:19703; ULK3.
DR HPA; ENSG00000140474; Low tissue specificity.
DR MIM; 613472; gene.
DR neXtProt; NX_Q6PHR2; -.
DR OpenTargets; ENSG00000140474; -.
DR PharmGKB; PA134908392; -.
DR VEuPathDB; HostDB:ENSG00000140474; -.
DR eggNOG; KOG0595; Eukaryota.
DR GeneTree; ENSGT00940000157689; -.
DR HOGENOM; CLU_000288_63_58_1; -.
DR InParanoid; Q6PHR2; -.
DR OMA; TQAVEHD; -.
DR OrthoDB; 642235at2759; -.
DR PhylomeDB; Q6PHR2; -.
DR TreeFam; TF324551; -.
DR BRENDA; 2.7.11.1; 2681.
DR PathwayCommons; Q6PHR2; -.
DR Reactome; R-HSA-5632684; Hedgehog 'on' state.
DR SignaLink; Q6PHR2; -.
DR SIGNOR; Q6PHR2; -.
DR BioGRID-ORCS; 25989; 5 hits in 659 CRISPR screens.
DR GenomeRNAi; 25989; -.
DR Pharos; Q6PHR2; Tchem.
DR PRO; PR:Q6PHR2; -.
DR Proteomes; UP000005640; Chromosome 15.
DR RNAct; Q6PHR2; protein.
DR Bgee; ENSG00000140474; Expressed in right hemisphere of cerebellum and 168 other tissues.
DR ExpressionAtlas; Q6PHR2; baseline and differential.
DR Genevisible; Q6PHR2; HS.
DR GO; GO:0005776; C:autophagosome; IBA:GO_Central.
DR GO; GO:0097542; C:ciliary tip; TAS:Reactome.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0000407; C:phagophore assembly site; TAS:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0106310; F:protein serine kinase activity; IEA:RHEA.
DR GO; GO:0004674; F:protein serine/threonine kinase activity; IDA:UniProtKB.
DR GO; GO:1905037; P:autophagosome organization; IBA:GO_Central.
DR GO; GO:0006914; P:autophagy; TAS:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; TAS:UniProtKB.
DR GO; GO:0072537; P:fibroblast activation; IMP:CACAO.
DR GO; GO:0045879; P:negative regulation of smoothened signaling pathway; IDA:UniProtKB.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; IBA:GO_Central.
DR GO; GO:0045880; P:positive regulation of smoothened signaling pathway; IDA:UniProtKB.
DR GO; GO:0046777; P:protein autophosphorylation; IDA:UniProtKB.
DR GO; GO:0007224; P:smoothened signaling pathway; IDA:FlyBase.
DR InterPro; IPR045269; Atg1-like.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR InterPro; IPR007330; MIT_dom.
DR InterPro; IPR036181; MIT_dom_sf.
DR InterPro; IPR000719; Prot_kinase_dom.
DR InterPro; IPR017441; Protein_kinase_ATP_BS.
DR InterPro; IPR008271; Ser/Thr_kinase_AS.
DR PANTHER; PTHR24348; PTHR24348; 1.
DR Pfam; PF04212; MIT; 2.
DR Pfam; PF00069; Pkinase; 1.
DR SMART; SM00745; MIT; 2.
DR SMART; SM00220; S_TKc; 1.
DR SUPFAM; SSF116846; SSF116846; 2.
DR SUPFAM; SSF56112; SSF56112; 1.
DR PROSITE; PS00107; PROTEIN_KINASE_ATP; 1.
DR PROSITE; PS50011; PROTEIN_KINASE_DOM; 1.
DR PROSITE; PS00108; PROTEIN_KINASE_ST; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Autophagy; Cytoplasm;
KW Kinase; Nucleotide-binding; Phosphoprotein; Reference proteome; Repeat;
KW Serine/threonine-protein kinase; Transferase.
FT CHAIN 1..472
FT /note="Serine/threonine-protein kinase ULK3"
FT /id="PRO_0000250150"
FT DOMAIN 14..270
FT /note="Protein kinase"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT DOMAIN 280..348
FT /note="MIT 1"
FT DOMAIN 375..444
FT /note="MIT 2"
FT ACT_SITE 137
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159,
FT ECO:0000255|PROSITE-ProRule:PRU10027"
FT BINDING 20..28
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT BINDING 44
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00159"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 300
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20643644"
FT MOD_RES 350
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20643644"
FT MOD_RES 384
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20643644"
FT MOD_RES 464
FT /note="Phosphoserine; by autocatalysis"
FT /evidence="ECO:0000269|PubMed:20643644"
FT VAR_SEQ 1..34
FT /note="MAGPGWGPPRLDGFILTERLGSGTYATVYKAYAK -> MQRNGSASRGLEKT
FT RLRLCREARIPESAFLTGLTRESWEARCWCA (in isoform 4)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_057411"
FT VAR_SEQ 205..214
FT /note="EALFGQPPFA -> GETSFPCFSP (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.6"
FT /id="VSP_038147"
FT VAR_SEQ 215..472
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334,
FT ECO:0000303|PubMed:17974005, ECO:0000303|Ref.6"
FT /id="VSP_038148"
FT VAR_SEQ 444..445
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039925"
FT VARIANT 101
FT /note="R -> H (in dbSNP:rs34945944)"
FT /id="VAR_057113"
FT VARIANT 445
FT /note="K -> R (in dbSNP:rs12898397)"
FT /id="VAR_059771"
FT MUTAGEN 44
FT /note="K->R: Decreased kinase activity."
FT /evidence="ECO:0000269|PubMed:19878745"
FT MUTAGEN 139
FT /note="K->R: Loss of kinase activity. Does not promote GLI1
FT nuclear localization."
FT /evidence="ECO:0000269|PubMed:19878745,
FT ECO:0000269|PubMed:20643644"
FT CONFLICT 47
FT /note="A -> S (in Ref. 1; BAG61369)"
FT /evidence="ECO:0000305"
FT STRAND 13..19
FT /evidence="ECO:0007829|PDB:6FDY"
FT STRAND 28..33
FT /evidence="ECO:0007829|PDB:6FDY"
FT STRAND 36..47
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 48..50
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 53..67
FT /evidence="ECO:0007829|PDB:6FDY"
FT STRAND 77..82
FT /evidence="ECO:0007829|PDB:6FDY"
FT STRAND 84..92
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 99..106
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 111..130
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 140..142
FT /evidence="ECO:0007829|PDB:6FDY"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6FDY"
FT STRAND 153..155
FT /evidence="ECO:0007829|PDB:6FDY"
FT TURN 177..179
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 182..186
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 194..208
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 218..226
FT /evidence="ECO:0007829|PDB:6FDY"
FT STRAND 235..237
FT /evidence="ECO:0007829|PDB:6FDZ"
FT HELIX 241..250
FT /evidence="ECO:0007829|PDB:6FDY"
FT TURN 255..257
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 261..265
FT /evidence="ECO:0007829|PDB:6FDY"
FT TURN 268..270
FT /evidence="ECO:0007829|PDB:6FDY"
FT HELIX 362..369
FT /evidence="ECO:0007829|PDB:4WZX"
FT TURN 370..372
FT /evidence="ECO:0007829|PDB:4WZX"
FT HELIX 374..390
FT /evidence="ECO:0007829|PDB:4WZX"
FT HELIX 396..416
FT /evidence="ECO:0007829|PDB:4WZX"
FT HELIX 421..445
FT /evidence="ECO:0007829|PDB:4WZX"
SQ SEQUENCE 472 AA; 53444 MW; 11D03E311AF36162 CRC64;
MAGPGWGPPR LDGFILTERL GSGTYATVYK AYAKKDTREV VAIKCVAKKS LNKASVENLL
TEIEILKGIR HPHIVQLKDF QWDSDNIYLI MEFCAGGDLS RFIHTRRILP EKVARVFMQQ
LASALQFLHE RNISHLDLKP QNILLSSLEK PHLKLADFGF AQHMSPWDEK HVLRGSPLYM
APEMVCQRQY DARVDLWSMG VILYEALFGQ PPFASRSFSE LEEKIRSNRV IELPLRPLLS
RDCRDLLQRL LERDPSRRIS FQDFFAHPWV DLEHMPSGES LGRATALVVQ AVKKDQEGDS
AAALSLYCKA LDFFVPALHY EVDAQRKEAI KAKVGQYVSR AEELKAIVSS SNQALLRQGT
SARDLLREMA RDKPRLLAAL EVASAAMAKE EAAGGEQDAL DLYQHSLGEL LLLLAAEPPG
RRRELLHTEV QNLMARAEYL KEQVKMRESR WEADTLDKEG LSESVRSSCT LQ
