DNJC1_HUMAN
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 03-AUG-2022, entry version 177.
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; 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; 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; 362.
DR IntAct; Q96KC8; 36.
DR MINT; Q96KC8; -.
DR STRING; 9606.ENSP00000366179; -.
DR iPTMnet; Q96KC8; -.
DR MetOSite; Q96KC8; -.
DR PhosphoSitePlus; Q96KC8; -.
DR BioMuta; DNAJC1; -.
DR DMDM; 27805464; -.
DR EPD; Q96KC8; -.
DR jPOST; Q96KC8; -.
DR MassIVE; Q96KC8; -.
DR MaxQB; Q96KC8; -.
DR PaxDb; Q96KC8; -.
DR PeptideAtlas; Q96KC8; -.
DR PRIDE; Q96KC8; -.
DR ProteomicsDB; 77059; -.
DR Antibodypedia; 2466; 92 antibodies from 24 providers.
DR DNASU; 64215; -.
DR Ensembl; ENST00000376980.8; ENSP00000366179.3; ENSG00000136770.11.
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 CTD; 64215; -.
DR DisGeNET; 64215; -.
DR GeneCards; DNAJC1; -.
DR HGNC; HGNC:20090; DNAJC1.
DR HPA; ENSG00000136770; Low tissue specificity.
DR MIM; 611207; gene.
DR neXtProt; NX_Q96KC8; -.
DR OpenTargets; ENSG00000136770; -.
DR PharmGKB; PA128394706; -.
DR VEuPathDB; HostDB:ENSG00000136770; -.
DR eggNOG; KOG0724; Eukaryota.
DR GeneTree; ENSGT00940000156678; -.
DR HOGENOM; CLU_036945_2_0_1; -.
DR InParanoid; Q96KC8; -.
DR OMA; KEECVAR; -.
DR OrthoDB; 972481at2759; -.
DR PhylomeDB; Q96KC8; -.
DR TreeFam; TF105161; -.
DR PathwayCommons; Q96KC8; -.
DR SignaLink; Q96KC8; -.
DR BioGRID-ORCS; 64215; 5 hits in 1098 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 204 other tissues.
DR ExpressionAtlas; Q96KC8; baseline and differential.
DR Genevisible; Q96KC8; HS.
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:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
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:0051087; F:chaperone binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
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 Gene3D; 1.10.287.110; -; 1.
DR InterPro; IPR001623; DnaJ_domain.
DR InterPro; IPR018253; DnaJ_domain_CS.
DR InterPro; IPR009057; Homeobox-like_sf.
DR InterPro; IPR036869; J_dom_sf.
DR InterPro; IPR017930; Myb_dom.
DR InterPro; IPR001005; SANT/Myb.
DR InterPro; IPR017884; SANT_dom.
DR Pfam; PF00226; DnaJ; 1.
DR Pfam; PF00249; Myb_DNA-binding; 1.
DR PRINTS; PR00625; JDOMAIN.
DR SMART; SM00271; DnaJ; 1.
DR SMART; SM00717; SANT; 2.
DR SUPFAM; SSF46565; SSF46565; 1.
DR SUPFAM; SSF46689; SSF46689; 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; Reference proteome; Repeat; Signal;
KW 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..409
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 434..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
