ID   CDC26_HUMAN             Reviewed;          85 AA.
AC   Q8NHZ8;
DT   09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT   01-OCT-2002, sequence version 1.
DT   27-MAR-2024, entry version 178.
DE   RecName: Full=Anaphase-promoting complex subunit CDC26;
DE   AltName: Full=Anaphase-promoting complex subunit 12;
DE            Short=APC12;
DE   AltName: Full=Cell division cycle protein 26 homolog;
GN   Name=CDC26; Synonyms=ANAPC12, C9orf17;
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 IDENTIFICATION IN THE APC/C COMPLEX.
RX   PubMed=10922056; DOI=10.1073/pnas.97.16.8973;
RA   Gmachl M., Gieffers C., Podtelejnikov A.V., Mann M., Peters J.-M.;
RT   "The RING-H2 finger protein APC11 and the E2 enzyme UBC4 are sufficient to
RT   ubiquitinate substrates of the anaphase-promoting complex.";
RL   Proc. Natl. Acad. Sci. U.S.A. 97:8973-8978(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=15164053; DOI=10.1038/nature02465;
RA   Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L.,
RA   Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R.,
RA   Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S.,
RA   Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K.,
RA   Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y.,
RA   Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C.,
RA   Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E.,
RA   Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M.,
RA   Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J.,
RA   Frankish A., Frankland J.A., French L., Fricker D.G., Garner P.,
RA   Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S.,
RA   Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E.,
RA   Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D.,
RA   Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E.,
RA   Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K.,
RA   Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S.,
RA   Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J.,
RA   Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E.,
RA   McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V.,
RA   Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S.,
RA   Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K.,
RA   Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J.,
RA   Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M.,
RA   West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L.,
RA   Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M.,
RA   Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J.,
RA   Dunham I.;
RT   "DNA sequence and analysis of human chromosome 9.";
RL   Nature 429:369-374(2004).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Brain, 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   [4]
RP   FUNCTION OF THE APC/C.
RX   PubMed=18485873; DOI=10.1016/j.cell.2008.04.012;
RA   Jin L., Williamson A., Banerjee S., Philipp I., Rape M.;
RT   "Mechanism of ubiquitin-chain formation by the human anaphase-promoting
RT   complex.";
RL   Cell 133:653-665(2008).
RN   [5]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, 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   [6]
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   [7]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42 AND SER-82, AND
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   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82, AND IDENTIFICATION BY
RP   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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-42, AND IDENTIFICATION BY
RP   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   [10]
RP   INTERACTION WITH FBXO43.
RX   PubMed=34595750; DOI=10.1111/cge.14069;
RA   Wu H., Zhang X., Shen Q., Liu Y., Gao Y., Wang G., Lv M., Hua R., Xu Y.,
RA   Zhou P., Wei Z., Tao F., He X., Cao Y., Liu M.;
RT   "A homozygous loss-of-function mutation in FBXO43 causes human non-
RT   obstructive azoospermia.";
RL   Clin. Genet. 101:55-64(2022).
RN   [11]
RP   STRUCTURE BY ELECTRON MICROSCOPY OF THE APC/C.
RX   PubMed=16364912; DOI=10.1016/j.molcel.2005.11.008;
RA   Dube P., Herzog F., Gieffers C., Sander B., Riedel D., Mueller S.A.,
RA   Engel A., Peters J.-M., Stark H.;
RT   "Localization of the coactivator Cdh1 and the cullin subunit Apc2 in a
RT   cryo-electron microscopy model of vertebrate APC/C.";
RL   Mol. Cell 20:867-879(2005).
RN   [12]
RP   X-RAY CRYSTALLOGRAPHY (2.8 ANGSTROMS) OF 1-29 IN COMPLEX WITH CDC16.
RX   PubMed=19668213; DOI=10.1038/nsmb.1645;
RA   Wang J., Dye B.T., Rajashankar K.R., Kurinov I., Schulman B.A.;
RT   "Insights into anaphase promoting complex TPR subdomain assembly from a
RT   CDC26-APC6 structure.";
RL   Nat. Struct. Mol. Biol. 16:987-989(2009).
RN   [13]
RP   STRUCTURE BY ELECTRON MICROSCOPY (7.4 ANGSTROMS) OF THE APC/C, AND SUBUNIT.
RX   PubMed=25043029; DOI=10.1038/nature13543;
RA   Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT   "Molecular architecture and mechanism of the anaphase-promoting complex.";
RL   Nature 513:388-393(2014).
RN   [14] {ECO:0007744|PDB:4UI9, ECO:0007744|PDB:5A31}
RP   STRUCTURE BY ELECTRON MICROSCOPY (3.60 ANGSTROMS) OF APC/C, AND SUBUNIT.
RX   PubMed=26083744; DOI=10.1038/nature14471;
RA   Chang L., Zhang Z., Yang J., McLaughlin S.H., Barford D.;
RT   "Atomic structure of the APC/C and its mechanism of protein
RT   ubiquitination.";
RL   Nature 522:450-454(2015).
CC   -!- FUNCTION: Component of the anaphase promoting complex/cyclosome
CC       (APC/C), a cell cycle-regulated E3 ubiquitin ligase that controls
CC       progression through mitosis and the G1 phase of the cell cycle. The
CC       APC/C complex acts by mediating ubiquitination and subsequent
CC       degradation of target proteins: it mainly mediates the formation of
CC       'Lys-11'-linked polyubiquitin chains and, to a lower extent, the
CC       formation of 'Lys-48'- and 'Lys-63'-linked polyubiquitin chains. May
CC       recruit the E2 ubiquitin-conjugating enzymes to the complex.
CC       {ECO:0000269|PubMed:18485873}.
CC   -!- PATHWAY: Protein modification; protein ubiquitination.
CC   -!- SUBUNIT: V-shaped homodimer. Interacts with CDC16. The mammalian APC/C
CC       is composed at least of 14 distinct subunits ANAPC1, ANAPC2,
CC       CDC27/APC3, ANAPC4, ANAPC5, CDC16/APC6, ANAPC7, CDC23/APC8, ANAPC10,
CC       ANAPC11, CDC26/APC12, ANAPC13, ANAPC15 and ANAPC16 that assemble into a
CC       complex of at least 19 chains with a combined molecular mass of around
CC       1.2 MDa; APC/C interacts with FZR1 and FBXO5. Interacts with FBXO43.
CC       {ECO:0000269|PubMed:10922056, ECO:0000269|PubMed:19668213,
CC       ECO:0000269|PubMed:25043029, ECO:0000269|PubMed:26083744,
CC       ECO:0000269|PubMed:34595750}.
CC   -!- INTERACTION:
CC       Q8NHZ8; P54253: ATXN1; NbExp=3; IntAct=EBI-2555941, EBI-930964;
CC       Q8NHZ8; Q13042: CDC16; NbExp=15; IntAct=EBI-2555941, EBI-994830;
CC       Q8NHZ8; Q13042-1: CDC16; NbExp=5; IntAct=EBI-2555941, EBI-15798699;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- SIMILARITY: Belongs to the CDC26 family. {ECO:0000305}.
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DR   EMBL; AF503918; AAM34207.1; -; mRNA.
DR   EMBL; AL449305; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; BC042534; AAH42534.1; -; mRNA.
DR   EMBL; BC066300; AAH66300.1; -; mRNA.
DR   CCDS; CCDS6790.1; -.
DR   RefSeq; NP_644815.1; NM_139286.3.
DR   RefSeq; XP_016870062.1; XM_017014573.1.
DR   RefSeq; XP_016870063.1; XM_017014574.1.
DR   RefSeq; XP_016870064.1; XM_017014575.1.
DR   PDB; 3HYM; X-ray; 2.80 A; A/C/E/G/I/K=1-29.
DR   PDB; 4UI9; EM; 3.60 A; G/W=1-85.
DR   PDB; 5A31; EM; 4.30 A; G/W=1-85.
DR   PDB; 5G04; EM; 4.00 A; G/W=1-85.
DR   PDB; 5G05; EM; 3.40 A; G/W=1-85.
DR   PDB; 5KHR; EM; 6.10 A; G/W=1-85.
DR   PDB; 5KHU; EM; 4.80 A; G/W=1-85.
DR   PDB; 5L9T; EM; 6.40 A; G/W=1-85.
DR   PDB; 5L9U; EM; 6.40 A; G/W=1-85.
DR   PDB; 5LCW; EM; 4.00 A; G/W=1-85.
DR   PDB; 6Q6G; EM; 3.20 A; G/W=1-85.
DR   PDB; 6Q6H; EM; 3.20 A; G/W=1-85.
DR   PDB; 6TLJ; EM; 3.80 A; G/W=1-85.
DR   PDB; 6TM5; EM; 3.90 A; G/W=1-85.
DR   PDB; 6TNT; EM; 3.78 A; G/W=1-85.
DR   PDB; 7QE7; EM; 2.90 A; G/W=1-85.
DR   PDB; 8PKP; EM; 3.20 A; G/W=1-85.
DR   PDB; 8TAR; EM; 4.00 A; G/W=1-85.
DR   PDB; 8TAU; EM; 3.50 A; G/W=1-85.
DR   PDBsum; 3HYM; -.
DR   PDBsum; 4UI9; -.
DR   PDBsum; 5A31; -.
DR   PDBsum; 5G04; -.
DR   PDBsum; 5G05; -.
DR   PDBsum; 5KHR; -.
DR   PDBsum; 5KHU; -.
DR   PDBsum; 5L9T; -.
DR   PDBsum; 5L9U; -.
DR   PDBsum; 5LCW; -.
DR   PDBsum; 6Q6G; -.
DR   PDBsum; 6Q6H; -.
DR   PDBsum; 6TLJ; -.
DR   PDBsum; 6TM5; -.
DR   PDBsum; 6TNT; -.
DR   PDBsum; 7QE7; -.
DR   PDBsum; 8PKP; -.
DR   PDBsum; 8TAR; -.
DR   PDBsum; 8TAU; -.
DR   AlphaFoldDB; Q8NHZ8; -.
DR   EMDB; EMD-10516; -.
DR   EMDB; EMD-10518; -.
DR   EMDB; EMD-10536; -.
DR   EMDB; EMD-13931; -.
DR   EMDB; EMD-17751; -.
DR   EMDB; EMD-2924; -.
DR   EMDB; EMD-2925; -.
DR   EMDB; EMD-3385; -.
DR   EMDB; EMD-3386; -.
DR   EMDB; EMD-3387; -.
DR   EMDB; EMD-3388; -.
DR   EMDB; EMD-3389; -.
DR   EMDB; EMD-3390; -.
DR   EMDB; EMD-4037; -.
DR   EMDB; EMD-41140; -.
DR   EMDB; EMD-41142; -.
DR   EMDB; EMD-4465; -.
DR   EMDB; EMD-4466; -.
DR   EMDB; EMD-4467; -.
DR   SMR; Q8NHZ8; -.
DR   BioGRID; 128878; 61.
DR   ComplexPortal; CPX-1860; Anaphase-promoting core complex.
DR   DIP; DIP-48551N; -.
DR   IntAct; Q8NHZ8; 39.
DR   MINT; Q8NHZ8; -.
DR   STRING; 9606.ENSP00000363322; -.
DR   iPTMnet; Q8NHZ8; -.
DR   PhosphoSitePlus; Q8NHZ8; -.
DR   BioMuta; CDC26; -.
DR   DMDM; 74751322; -.
DR   EPD; Q8NHZ8; -.
DR   jPOST; Q8NHZ8; -.
DR   MassIVE; Q8NHZ8; -.
DR   MaxQB; Q8NHZ8; -.
DR   PaxDb; 9606-ENSP00000363322; -.
DR   PeptideAtlas; Q8NHZ8; -.
DR   ProteomicsDB; 73794; -.
DR   Pumba; Q8NHZ8; -.
DR   TopDownProteomics; Q8NHZ8; -.
DR   Antibodypedia; 44232; 112 antibodies from 22 providers.
DR   DNASU; 246184; -.
DR   Ensembl; ENST00000374206.4; ENSP00000363322.3; ENSG00000176386.9.
DR   GeneID; 246184; -.
DR   KEGG; hsa:246184; -.
DR   MANE-Select; ENST00000374206.4; ENSP00000363322.3; NM_139286.4; NP_644815.1.
DR   UCSC; uc004bgw.4; human.
DR   AGR; HGNC:17839; -.
DR   CTD; 246184; -.
DR   DisGeNET; 246184; -.
DR   GeneCards; CDC26; -.
DR   HGNC; HGNC:17839; CDC26.
DR   HPA; ENSG00000176386; Low tissue specificity.
DR   MIM; 614533; gene.
DR   neXtProt; NX_Q8NHZ8; -.
DR   OpenTargets; ENSG00000176386; -.
DR   PharmGKB; PA25974; -.
DR   VEuPathDB; HostDB:ENSG00000176386; -.
DR   eggNOG; ENOG502S5GK; Eukaryota.
DR   GeneTree; ENSGT00390000008457; -.
DR   HOGENOM; CLU_190086_0_0_1; -.
DR   InParanoid; Q8NHZ8; -.
DR   OMA; NREQMIN; -.
DR   OrthoDB; 5404165at2759; -.
DR   PhylomeDB; Q8NHZ8; -.
DR   TreeFam; TF101057; -.
DR   PathwayCommons; Q8NHZ8; -.
DR   Reactome; R-HSA-141430; Inactivation of APC/C via direct inhibition of the APC/C complex.
DR   Reactome; R-HSA-174048; APC/C:Cdc20 mediated degradation of Cyclin B.
DR   Reactome; R-HSA-174084; Autodegradation of Cdh1 by Cdh1:APC/C.
DR   Reactome; R-HSA-174154; APC/C:Cdc20 mediated degradation of Securin.
DR   Reactome; R-HSA-174178; APC/C:Cdh1 mediated degradation of Cdc20 and other APC/C:Cdh1 targeted proteins in late mitosis/early G1.
DR   Reactome; R-HSA-174184; Cdc20:Phospho-APC/C mediated degradation of Cyclin A.
DR   Reactome; R-HSA-176407; Conversion from APC/C:Cdc20 to APC/C:Cdh1 in late anaphase.
DR   Reactome; R-HSA-176408; Regulation of APC/C activators between G1/S and early anaphase.
DR   Reactome; R-HSA-176409; APC/C:Cdc20 mediated degradation of mitotic proteins.
DR   Reactome; R-HSA-176412; Phosphorylation of the APC/C.
DR   Reactome; R-HSA-179409; APC-Cdc20 mediated degradation of Nek2A.
DR   Reactome; R-HSA-2467813; Separation of Sister Chromatids.
DR   Reactome; R-HSA-2559582; Senescence-Associated Secretory Phenotype (SASP).
DR   Reactome; R-HSA-68867; Assembly of the pre-replicative complex.
DR   Reactome; R-HSA-69017; CDK-mediated phosphorylation and removal of Cdc6.
DR   Reactome; R-HSA-8853884; Transcriptional Regulation by VENTX.
DR   Reactome; R-HSA-9687136; Aberrant regulation of mitotic exit in cancer due to RB1 defects.
DR   Reactome; R-HSA-983168; Antigen processing: Ubiquitination & Proteasome degradation.
DR   SignaLink; Q8NHZ8; -.
DR   SIGNOR; Q8NHZ8; -.
DR   UniPathway; UPA00143; -.
DR   BioGRID-ORCS; 246184; 491 hits in 1123 CRISPR screens.
DR   ChiTaRS; CDC26; human.
DR   EvolutionaryTrace; Q8NHZ8; -.
DR   GenomeRNAi; 246184; -.
DR   Pharos; Q8NHZ8; Tbio.
DR   PRO; PR:Q8NHZ8; -.
DR   Proteomes; UP000005640; Chromosome 9.
DR   RNAct; Q8NHZ8; Protein.
DR   Bgee; ENSG00000176386; Expressed in calcaneal tendon and 104 other cell types or tissues.
DR   ExpressionAtlas; Q8NHZ8; baseline and differential.
DR   GO; GO:0005680; C:anaphase-promoting complex; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR   GO; GO:0031145; P:anaphase-promoting complex-dependent catabolic process; NAS:ComplexPortal.
DR   GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0070979; P:protein K11-linked ubiquitination; IDA:UniProtKB.
DR   GO; GO:0051445; P:regulation of meiotic cell cycle; NAS:ComplexPortal.
DR   GO; GO:0007346; P:regulation of mitotic cell cycle; IBA:GO_Central.
DR   DisProt; DP01453; -.
DR   InterPro; IPR018860; APC_suCDC26.
DR   PANTHER; PTHR28579; ANAPHASE-PROMOTING COMPLEX SUBUNIT CDC26; 1.
DR   PANTHER; PTHR28579:SF1; ANAPHASE-PROMOTING COMPLEX SUBUNIT CDC26; 1.
DR   Pfam; PF10471; ANAPC_CDC26; 1.
DR   Genevisible; Q8NHZ8; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Coiled coil; Mitosis; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation pathway.
FT   CHAIN           1..85
FT                   /note="Anaphase-promoting complex subunit CDC26"
FT                   /id="PRO_0000271194"
FT   REGION          30..85
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COILED          7..38
FT                   /evidence="ECO:0000255"
FT   COMPBIAS        71..85
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         42
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         82
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692"
FT   HELIX           14..16
FT                   /evidence="ECO:0007829|PDB:3HYM"
FT   HELIX           17..25
FT                   /evidence="ECO:0007829|PDB:3HYM"
SQ   SEQUENCE   85 AA;  9777 MW;  134970EE68F0142C CRC64;
     MLRRKPTRLE LKLDDIEEFE NIRKDLETRK KQKEDVEVVG GSDGEGAIGL SSDPKSREQM
     INDRIGYKPQ PKPNNRSSQF GSLEF
//