ID   DNJC1_HUMAN             Reviewed;         554 AA.
AC   Q96KC8; B0YIZ8; Q5VX89; Q9H6B8;
DT   17-JAN-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-DEC-2001, sequence version 1.
DT   28-JAN-2026, entry version 194.
DE   RecName: Full=DnaJ homolog subfamily C member 1;
DE   AltName: Full=DnaJ protein homolog MTJ1;
DE   Flags: Precursor;
GN   Name=DNAJC1; Synonyms=HTJ1;
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], AND INTERACTION WITH SERPINA3.
RC   TISSUE=Liver;
RX   PubMed=14668352; DOI=10.1074/jbc.m310903200;
RA   Kroczynska B., Evangelista C.M., Samant S.S., Elguindi E.C., Blond S.Y.;
RT   "The SANT2 domain of the murine tumor cell DnaJ-like protein 1 human
RT   homologue interacts with alpha1-antichymotrypsin and kinetically interferes
RT   with its serpin inhibitory activity.";
RL   J. Biol. Chem. 279:11432-11443(2004).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Embryo;
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 [GENOMIC DNA].
RG   NHLBI resequencing and genotyping service (RS&G);
RL   Submitted (FEB-2007) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164054; DOI=10.1038/nature02462;
RA   Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA   Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA   Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA   Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA   Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA   Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA   Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA   Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA   Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA   Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA   Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA   Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA   Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA   Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA   McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA   Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA   Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA   Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA   Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA   Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA   Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA   Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA   Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT   "The DNA sequence and comparative analysis of human chromosome 10.";
RL   Nature 429:375-381(2004).
RN   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=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   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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-381 AND SER-430, 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   [8]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430, 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   [10]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Cervix carcinoma;
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [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).
RN   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479; SER-480 AND SER-484, 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   [13]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-479; SER-480 AND
RP   SER-492, 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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-479 AND SER-480, 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   [15]
RP   STRUCTURE BY NMR OF 327-385 AND 484-543.
RG   RIKEN structural genomics initiative (RSGI);
RT   "Solution structure of RSGI RUH-037, a Myb DNA-binding domain in human.";
RL   Submitted (NOV-2005) to the PDB data bank.
CC   -!- FUNCTION: May modulate protein synthesis. {ECO:0000250}.
CC   -!- SUBUNIT: Interacts (via J domain) with HSPA5. Interacts (via cytosolic
CC       domain) with ribosomes (By similarity). Interacts (via SANT 2 domain)
CC       with SERPINA3; the interaction delays the formation of the covalent
CC       inhibitory complex SERPINA3-chymotrypsin, but does not alter the
CC       catalytic activity of SERPINA3. Interacts (via SANT 2 domain) with
CC       ITIH4 (via C-terminus); the interaction protects ITIH4 against in vitro
CC       cleavage by kallikrein. {ECO:0000250, ECO:0000269|PubMed:14668352}.
CC   -!- INTERACTION:
CC       Q96KC8; Q6RW13-2: AGTRAP; NbExp=3; IntAct=EBI-296550, EBI-11522760;
CC       Q96KC8; P27449: ATP6V0C; NbExp=3; IntAct=EBI-296550, EBI-721179;
CC       Q96KC8; P13569: CFTR; NbExp=7; IntAct=EBI-296550, EBI-349854;
CC       Q96KC8; Q96FZ5: CMTM7; NbExp=3; IntAct=EBI-296550, EBI-2807956;
CC       Q96KC8; P78329: CYP4F2; NbExp=3; IntAct=EBI-296550, EBI-1752413;
CC       Q96KC8; P13473-2: LAMP2; NbExp=3; IntAct=EBI-296550, EBI-21591415;
CC       Q96KC8; Q04941: PLP2; NbExp=3; IntAct=EBI-296550, EBI-608347;
CC       Q96KC8; Q9NWS8: RMND1; NbExp=2; IntAct=EBI-296550, EBI-4401316;
CC       Q96KC8; P01011: SERPINA3; NbExp=3; IntAct=EBI-296550, EBI-296557;
CC       Q96KC8; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-296550, EBI-2623095;
CC       Q96KC8; Q5SNT2-2: TMEM201; NbExp=3; IntAct=EBI-296550, EBI-11994282;
CC       Q96KC8; O14798: TNFRSF10C; NbExp=3; IntAct=EBI-296550, EBI-717441;
CC   -!- SUBCELLULAR LOCATION: Endoplasmic reticulum membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}. Nucleus membrane;
CC       Single-pass type I membrane protein. Microsome membrane {ECO:0000250};
CC       Single-pass type I membrane protein {ECO:0000250}.
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DR   EMBL; AY225122; AAP50497.1; -; mRNA.
DR   EMBL; AK026062; BAB15343.1; -; mRNA.
DR   EMBL; AK027263; BAB55004.1; -; mRNA.
DR   EMBL; EF444973; ACA05978.1; -; Genomic_DNA.
DR   EMBL; EF444973; ACA05979.1; -; Genomic_DNA.
DR   EMBL; AL445431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AL359697; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC110894; AAI10895.1; -; mRNA.
DR   CCDS; CCDS7136.1; -.
DR   RefSeq; NP_071760.2; NM_022365.3.
DR   PDB; 2CQQ; NMR; -; A=327-385.
DR   PDB; 2CQR; NMR; -; A=484-543.
DR   PDBsum; 2CQQ; -.
DR   PDBsum; 2CQR; -.
DR   AlphaFoldDB; Q96KC8; -.
DR   SMR; Q96KC8; -.
DR   BioGRID; 122105; 392.
DR   FunCoup; Q96KC8; 2046.
DR   IntAct; Q96KC8; 71.
DR   MINT; Q96KC8; -.
DR   STRING; 9606.ENSP00000366179; -.
DR   GlyGen; Q96KC8; 2 sites, 1 O-linked glycan (1 site).
DR   iPTMnet; Q96KC8; -.
DR   MetOSite; Q96KC8; -.
DR   PhosphoSitePlus; Q96KC8; -.
DR   SwissPalm; Q96KC8; -.
DR   BioMuta; DNAJC1; -.
DR   DMDM; 27805464; -.
DR   jPOST; Q96KC8; -.
DR   MassIVE; Q96KC8; -.
DR   PaxDb; 9606-ENSP00000366179; -.
DR   PeptideAtlas; Q96KC8; -.
DR   ProteomicsDB; 77059; -.
DR   Pumba; Q96KC8; -.
DR   Antibodypedia; 2466; 88 antibodies from 23 providers.
DR   DNASU; 64215; -.
DR   Ensembl; ENST00000376980.8; ENSP00000366179.3; ENSG00000136770.12.
DR   GeneID; 64215; -.
DR   KEGG; hsa:64215; -.
DR   MANE-Select; ENST00000376980.8; ENSP00000366179.3; NM_022365.4; NP_071760.2.
DR   UCSC; uc001irc.4; human.
DR   AGR; HGNC:20090; -.
DR   ClinPGx; PA128394706; -.
DR   CTD; 64215; -.
DR   DisGeNET; 64215; -.
DR   GeneCards; DNAJC1; -.
DR   HGNC; HGNC:20090; DNAJC1.
DR   HPA; ENSG00000136770; Low tissue specificity.
DR   MIM; 611207; gene.
DR   OpenTargets; ENSG00000136770; -.
DR   VEuPathDB; HostDB:ENSG00000136770; -.
DR   eggNOG; KOG0724; Eukaryota.
DR   GeneTree; ENSGT00940000156678; -.
DR   HOGENOM; CLU_036945_2_0_1; -.
DR   InParanoid; Q96KC8; -.
DR   OMA; AAYWERK; -.
DR   OrthoDB; 1420887at2759; -.
DR   PAN-GO; Q96KC8; 1 GO annotation based on evolutionary models.
DR   PhylomeDB; Q96KC8; -.
DR   PathwayCommons; Q96KC8; -.
DR   SignaLink; Q96KC8; -.
DR   Agora; ENSG00000136770; -.
DR   BioGRID-ORCS; 64215; 5 hits in 1177 CRISPR screens.
DR   ChiTaRS; DNAJC1; human.
DR   EvolutionaryTrace; Q96KC8; -.
DR   GeneWiki; DNAJC1; -.
DR   GenomeRNAi; 64215; -.
DR   Pharos; Q96KC8; Tbio.
DR   PRO; PR:Q96KC8; -.
DR   Proteomes; UP000005640; Chromosome 10.
DR   RNAct; Q96KC8; protein.
DR   Bgee; ENSG00000136770; Expressed in secondary oocyte and 206 other cell types or tissues.
DR   ExpressionAtlas; Q96KC8; baseline and differential.
DR   GO; GO:0012505; C:endomembrane system; IBA:GO_Central.
DR   GO; GO:0005783; C:endoplasmic reticulum; ISS:UniProtKB.
DR   GO; GO:0005789; C:endoplasmic reticulum membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0031965; C:nuclear membrane; IEA:UniProtKB-SubCell.
DR   GO; GO:0005886; C:plasma membrane; IEA:Ensembl.
DR   GO; GO:0001671; F:ATPase activator activity; TAS:UniProtKB.
DR   GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR   GO; GO:0051087; F:protein-folding chaperone binding; IEA:Ensembl.
DR   GO; GO:0045861; P:negative regulation of proteolysis; TAS:UniProtKB.
DR   GO; GO:0006457; P:protein folding; IEA:Ensembl.
DR   GO; GO:0050708; P:regulation of protein secretion; IDA:UniProtKB.
DR   GO; GO:0006417; P:regulation of translation; IEA:Ensembl.
DR   CDD; cd06257; DnaJ; 1.
DR   CDD; cd00167; SANT; 2.
DR   FunFam; 1.10.10.60:FF:000255; DnaJ (Hsp40) homolog, subfamily C, member 1; 1.
DR   FunFam; 1.10.287.110:FF:000044; DnaJ (Hsp40) homolog, subfamily C, member 1; 1.
DR   FunFam; 1.10.10.60:FF:000180; DnaJ (Hsp40) homolog, subfamily C, member 2; 1.
DR   Gene3D; 1.10.287.110; DnaJ domain; 1.
DR   Gene3D; 1.10.10.60; Homeodomain-like; 2.
DR   InterPro; IPR001623; DnaJ_domain.
DR   InterPro; IPR018253; DnaJ_domain_CS.
DR   InterPro; IPR052606; DnaJ_domain_protein.
DR   InterPro; IPR009057; Homeodomain-like_sf.
DR   InterPro; IPR036869; J_dom_sf.
DR   InterPro; IPR001005; SANT/Myb.
DR   InterPro; IPR017884; SANT_dom.
DR   PANTHER; PTHR44653; DNAJ HOMOLOG SUBFAMILY C MEMBER 1; 1.
DR   PANTHER; PTHR44653:SF2; DNAJ HOMOLOG SUBFAMILY C MEMBER 1; 1.
DR   Pfam; PF00226; DnaJ; 1.
DR   Pfam; PF23082; Myb_DNA-binding_2; 2.
DR   PRINTS; PR00625; JDOMAIN.
DR   SMART; SM00271; DnaJ; 1.
DR   SMART; SM00717; SANT; 2.
DR   SUPFAM; SSF46565; Chaperone J-domain; 1.
DR   SUPFAM; SSF46689; Homeodomain-like; 2.
DR   PROSITE; PS00636; DNAJ_1; 1.
DR   PROSITE; PS50076; DNAJ_2; 1.
DR   PROSITE; PS51293; SANT; 2.
PE   1: Evidence at protein level;
KW   3D-structure; Chaperone; DNA-binding; Endoplasmic reticulum; Membrane;
KW   Microsome; Nucleus; Phosphoprotein; Proteomics identification;
KW   Reference proteome; Repeat; Signal; Transmembrane; Transmembrane helix.
FT   SIGNAL          1..47
FT                   /evidence="ECO:0000255"
FT   CHAIN           48..554
FT                   /note="DnaJ homolog subfamily C member 1"
FT                   /id="PRO_0000071042"
FT   TOPO_DOM        48..153
FT                   /note="Lumenal"
FT                   /evidence="ECO:0000250"
FT   TRANSMEM        154..174
FT                   /note="Helical"
FT                   /evidence="ECO:0000255"
FT   TOPO_DOM        175..554
FT                   /note="Cytoplasmic"
FT                   /evidence="ECO:0000250"
FT   DOMAIN          65..129
FT                   /note="J"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00286"
FT   DOMAIN          325..379
FT                   /note="SANT 1"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   DOMAIN          492..547
FT                   /note="SANT 2"
FT                   /evidence="ECO:0000255|PROSITE-ProRule:PRU00624"
FT   REGION          392..500
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        392..405
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        421..432
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        455..472
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        473..482
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        483..494
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         381
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         430
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163"
FT   MOD_RES         479
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         480
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692,
FT                   ECO:0007744|PubMed:23186163, ECO:0007744|PubMed:24275569"
FT   MOD_RES         484
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:21406692"
FT   MOD_RES         492
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:23186163"
FT   HELIX           332..344
FT                   /evidence="ECO:0007829|PDB:2CQQ"
FT   HELIX           352..360
FT                   /evidence="ECO:0007829|PDB:2CQQ"
FT   HELIX           364..376
FT                   /evidence="ECO:0007829|PDB:2CQQ"
FT   TURN            489..491
FT                   /evidence="ECO:0007829|PDB:2CQR"
FT   HELIX           499..511
FT                   /evidence="ECO:0007829|PDB:2CQR"
FT   STRAND          514..516
FT                   /evidence="ECO:0007829|PDB:2CQR"
FT   HELIX           517..523
FT                   /evidence="ECO:0007829|PDB:2CQR"
FT   HELIX           524..526
FT                   /evidence="ECO:0007829|PDB:2CQR"
FT   STRAND          528..530
FT                   /evidence="ECO:0007829|PDB:2CQR"
FT   HELIX           532..543
FT                   /evidence="ECO:0007829|PDB:2CQR"
SQ   SEQUENCE   554 AA;  63883 MW;  65EAAB16C65E2B46 CRC64;
     MTAPCSQPAQ LPGRRQLGLV PFPPPPPRTP LLWLLLLLLA AVAPARGWES GDLELFDLVE
     EVQLNFYQFL GVQQDASSAD IRKAYRKLSL TLHPDKNKDE NAETQFRQLV AIYEVLKDDE
     RRQRYDDILI NGLPDWRQPV FYYRRVRKMS NAELALLLFI ILTVGHYAVV WSIYLEKQLD
     ELLSRKKREK KKKTGSKSVD VSKLGASEKN ERLLMKPQWH DLLPCKLGIW FCLTLKALPH
     LIQDAGQFYA KYKETRLKEK EDALTRTELE TLQKQKKVKK PKPEFPVYTP LETTYIQSYD
     HGTSIEEIEE QMDDWLENRN RTQKKQAPEW TEEDLSQLTR SMVKFPGGTP GRWEKIAHEL
     GRSVTDVTTK AKQLKDSVTC SPGMVRLSEL KSTVQNSRPI KTATTLPDDM ITQREDAEGV
     AAEEEQEGDS GEQETGATDA RPRRRKPARL LEATAKPEPE EKSRAKRQKD FDIAEQNESS
     DEESLRKERA RSAEEPWTQN QQKLLELALQ QYPRGSSDRW DKIARCVPSK SKEDCIARYK
     LLVELVQKKK QAKS
//