ID   CND3_HUMAN              Reviewed;        1015 AA.
AC   Q9BPX3; Q3MJE0; Q96SV9; Q9BUR3; Q9BVY1; Q9H914; Q9H9Z6; Q9HBI9;
DT   23-APR-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-JUN-2001, sequence version 1.
DT   24-JAN-2024, entry version 193.
DE   RecName: Full=Condensin complex subunit 3;
DE   AltName: Full=Chromosome-associated protein G;
DE   AltName: Full=Condensin subunit CAP-G;
DE            Short=hCAP-G;
DE   AltName: Full=Melanoma antigen NY-MEL-3;
DE   AltName: Full=Non-SMC condensin I complex subunit G;
DE   AltName: Full=XCAP-G homolog;
GN   Name=NCAPG; Synonyms=CAPG, NYMEL3;
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], TISSUE SPECIFICITY, AND VARIANT ILE-581.
RC   TISSUE=Melanocyte;
RX   PubMed=10910072;
RA   Jaeger D., Stockert E., Jaeger E., Guere A.O., Scanlan M.J., Knuth A.,
RA   Old L.J., Chen Y.-T.;
RT   "Serological cloning of a melanocyte rab guanosine 5'-triphosphate-binding
RT   protein and a chromosome condensation protein from a melanoma complementary
RT   DNA library.";
RL   Cancer Res. 60:3584-3591(2000).
RN   [2]
RP   NUCLEOTIDE SEQUENCE [MRNA], IDENTIFICATION IN A CONDENSIN COMPLEX WITH
RP   SMC2; SMC4; NCAPD2 AND NCAPH, AND FUNCTION OF THE COMPLEX.
RX   PubMed=11136719; DOI=10.1074/jbc.c000873200;
RA   Kimura K., Cuvier O., Hirano T.;
RT   "Chromosome condensation by a human condensin complex in Xenopus egg
RT   extracts.";
RL   J. Biol. Chem. 276:5417-5420(2001).
RN   [3]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RC   TISSUE=Erythroleukemia;
RA   Minami T., Doi T., Tachibana K., Okada Y.;
RT   "Differentiation responsive gene.";
RL   Submitted (APR-1998) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Teratocarcinoma;
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   [5]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Placenta;
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   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, AND
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   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC   TISSUE=Platelet;
RX   PubMed=18088087; DOI=10.1021/pr0704130;
RA   Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J.,
RA   Schuetz C., Walter U., Gambaryan S., Sickmann A.;
RT   "Phosphoproteome of resting human platelets.";
RL   J. Proteome Res. 7:526-534(2008).
RN   [8]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, AND
RP   IDENTIFICATION BY 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   [9]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674; SER-973; SER-975 AND
RP   SER-1002, AND 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   [10]
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   [11]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-674 AND SER-1015,
RP   AND IDENTIFICATION BY 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   [12]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-674; THR-931 AND
RP   SER-1015, AND 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   [13]
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   [14]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-674 AND SER-1015, 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   [15]
RP   PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-390; SER-674 AND THR-931, AND
RP   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   [16]
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=25944712; DOI=10.1002/pmic.201400617;
RA   Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA   Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT   "N-terminome analysis of the human mitochondrial proteome.";
RL   Proteomics 15:2519-2524(2015).
RN   [17]
RP   VARIANT [LARGE SCALE ANALYSIS] THR-265.
RX   PubMed=16959974; DOI=10.1126/science.1133427;
RA   Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA   Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA   Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA   Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA   Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA   Velculescu V.E.;
RT   "The consensus coding sequences of human breast and colorectal cancers.";
RL   Science 314:268-274(2006).
CC   -!- FUNCTION: Regulatory subunit of the condensin complex, a complex
CC       required for conversion of interphase chromatin into mitotic-like
CC       condense chromosomes. The condensin complex probably introduces
CC       positive supercoils into relaxed DNA in the presence of type I
CC       topoisomerases and converts nicked DNA into positive knotted forms in
CC       the presence of type II topoisomerases. {ECO:0000269|PubMed:11136719}.
CC   -!- SUBUNIT: Component of the condensin complex, which contains the SMC2
CC       and SMC4 heterodimer, and three non SMC subunits that probably regulate
CC       the complex: NCAPH/BRRN1, NCAPD2/CAPD2 and NCAPG.
CC       {ECO:0000269|PubMed:11136719}.
CC   -!- INTERACTION:
CC       Q9BPX3; Q15021: NCAPD2; NbExp=2; IntAct=EBI-970214, EBI-1044041;
CC       Q9BPX3; Q15003: NCAPH; NbExp=8; IntAct=EBI-970214, EBI-1046410;
CC   -!- SUBCELLULAR LOCATION: Nucleus. Cytoplasm. Chromosome. Note=In
CC       interphase cells, the majority of the condensin complex is found in the
CC       cytoplasm, while a minority of the complex is associated with
CC       chromatin. A subpopulation of the complex however remains associated
CC       with chromosome foci in interphase cells. During mitosis, most of the
CC       condensin complex is associated with the chromatin. At the onset of
CC       prophase, the regulatory subunits of the complex are phosphorylated by
CC       CDK1, leading to condensin's association with chromosome arms and to
CC       chromosome condensation. Dissociation from chromosomes is observed in
CC       late telophase.
CC   -!- TISSUE SPECIFICITY: Highly expressed in testis.
CC       {ECO:0000269|PubMed:10910072}.
CC   -!- PTM: Phosphorylated by CDK1. Its phosphorylation, as well as that of
CC       NCAPD2 and NCAPH subunits, activates the condensin complex and is
CC       required for chromosome condensation (By similarity). {ECO:0000250}.
CC   -!- MISCELLANEOUS: Overexpressed in some cancer lines and some tumor cells.
CC   -!- SIMILARITY: Belongs to the CND3 (condensin subunit 3) family.
CC       {ECO:0000305}.
CC   -!- SEQUENCE CAUTION:
CC       Sequence=AAH00827.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB14429.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC       Sequence=BAB55165.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR   EMBL; AF235023; AAG30732.1; -; mRNA.
DR   EMBL; AF331796; AAG49627.1; -; mRNA.
DR   EMBL; AB013299; BAB21557.1; -; mRNA.
DR   EMBL; AK022512; BAB14069.1; -; mRNA.
DR   EMBL; AK023147; BAB14429.1; ALT_INIT; mRNA.
DR   EMBL; AK027511; BAB55165.1; ALT_INIT; mRNA.
DR   EMBL; BC000827; AAH00827.1; ALT_INIT; mRNA.
DR   EMBL; BC101476; AAI01477.1; -; mRNA.
DR   CCDS; CCDS3424.1; -.
DR   RefSeq; NP_071741.2; NM_022346.4.
DR   PDB; 6IGX; X-ray; 3.00 A; B/D=1-900.
DR   PDBsum; 6IGX; -.
DR   AlphaFoldDB; Q9BPX3; -.
DR   EMDB; EMD-10827; -.
DR   SMR; Q9BPX3; -.
DR   BioGRID; 122089; 202.
DR   ComplexPortal; CPX-979; Condensin I complex.
DR   CORUM; Q9BPX3; -.
DR   DIP; DIP-34891N; -.
DR   IntAct; Q9BPX3; 42.
DR   MINT; Q9BPX3; -.
DR   STRING; 9606.ENSP00000251496; -.
DR   GlyGen; Q9BPX3; 1 site, 1 O-linked glycan (1 site).
DR   iPTMnet; Q9BPX3; -.
DR   MetOSite; Q9BPX3; -.
DR   PhosphoSitePlus; Q9BPX3; -.
DR   SwissPalm; Q9BPX3; -.
DR   BioMuta; NCAPG; -.
DR   DMDM; 30172941; -.
DR   EPD; Q9BPX3; -.
DR   jPOST; Q9BPX3; -.
DR   MassIVE; Q9BPX3; -.
DR   MaxQB; Q9BPX3; -.
DR   PaxDb; 9606-ENSP00000251496; -.
DR   PeptideAtlas; Q9BPX3; -.
DR   ProteomicsDB; 78586; -.
DR   Pumba; Q9BPX3; -.
DR   Antibodypedia; 23100; 203 antibodies from 30 providers.
DR   DNASU; 64151; -.
DR   Ensembl; ENST00000251496.7; ENSP00000251496.2; ENSG00000109805.10.
DR   GeneID; 64151; -.
DR   KEGG; hsa:64151; -.
DR   MANE-Select; ENST00000251496.7; ENSP00000251496.2; NM_022346.5; NP_071741.2.
DR   UCSC; uc003gpp.5; human.
DR   AGR; HGNC:24304; -.
DR   CTD; 64151; -.
DR   DisGeNET; 64151; -.
DR   GeneCards; NCAPG; -.
DR   HGNC; HGNC:24304; NCAPG.
DR   HPA; ENSG00000109805; Tissue enhanced (bone marrow, lymphoid tissue).
DR   MIM; 606280; gene.
DR   neXtProt; NX_Q9BPX3; -.
DR   OpenTargets; ENSG00000109805; -.
DR   PharmGKB; PA162397165; -.
DR   VEuPathDB; HostDB:ENSG00000109805; -.
DR   eggNOG; KOG2025; Eukaryota.
DR   GeneTree; ENSGT00390000001577; -.
DR   HOGENOM; CLU_004446_2_0_1; -.
DR   InParanoid; Q9BPX3; -.
DR   OMA; FRATQIT; -.
DR   OrthoDB; 3686298at2759; -.
DR   PhylomeDB; Q9BPX3; -.
DR   TreeFam; TF101160; -.
DR   PathwayCommons; Q9BPX3; -.
DR   Reactome; R-HSA-2514853; Condensation of Prometaphase Chromosomes.
DR   SignaLink; Q9BPX3; -.
DR   SIGNOR; Q9BPX3; -.
DR   BioGRID-ORCS; 64151; 798 hits in 1172 CRISPR screens.
DR   ChiTaRS; NCAPG; human.
DR   GeneWiki; NCAPG; -.
DR   GenomeRNAi; 64151; -.
DR   Pharos; Q9BPX3; Tbio.
DR   PRO; PR:Q9BPX3; -.
DR   Proteomes; UP000005640; Chromosome 4.
DR   RNAct; Q9BPX3; Protein.
DR   Bgee; ENSG00000109805; Expressed in ventricular zone and 162 other cell types or tissues.
DR   ExpressionAtlas; Q9BPX3; baseline and differential.
DR   GO; GO:0000793; C:condensed chromosome; IBA:GO_Central.
DR   GO; GO:0000779; C:condensed chromosome, centromeric region; IEA:Ensembl.
DR   GO; GO:0000794; C:condensed nuclear chromosome; ISO:ComplexPortal.
DR   GO; GO:0000796; C:condensin complex; IDA:UniProtKB.
DR   GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR   GO; GO:0005829; C:cytosol; TAS:Reactome.
DR   GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR   GO; GO:0005634; C:nucleus; NAS:UniProtKB.
DR   GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR   GO; GO:0007076; P:mitotic chromosome condensation; IDA:UniProtKB.
DR   GO; GO:1905821; P:positive regulation of chromosome condensation; IDA:ComplexPortal.
DR   GO; GO:0051984; P:positive regulation of chromosome segregation; ISO:ComplexPortal.
DR   GO; GO:1905820; P:positive regulation of chromosome separation; ISO:ComplexPortal.
DR   Gene3D; 1.25.10.10; Leucine-rich Repeat Variant; 1.
DR   InterPro; IPR011989; ARM-like.
DR   InterPro; IPR016024; ARM-type_fold.
DR   InterPro; IPR027165; CND3.
DR   InterPro; IPR025977; Cnd3_C.
DR   PANTHER; PTHR14418:SF5; CONDENSIN COMPLEX SUBUNIT 3; 1.
DR   PANTHER; PTHR14418; CONDENSIN COMPLEX SUBUNIT 3-RELATED; 1.
DR   Pfam; PF12719; Cnd3; 1.
DR   SUPFAM; SSF48371; ARM repeat; 1.
DR   Genevisible; Q9BPX3; HS.
PE   1: Evidence at protein level;
KW   3D-structure; Cell cycle; Cell division; Chromosome; Cytoplasm;
KW   DNA condensation; Mitosis; Nucleus; Phosphoprotein; Reference proteome;
KW   Repeat.
FT   CHAIN           1..1015
FT                   /note="Condensin complex subunit 3"
FT                   /id="PRO_0000095041"
FT   REPEAT          94..131
FT                   /note="HEAT 1"
FT   REPEAT          138..173
FT                   /note="HEAT 2"
FT   REPEAT          174..212
FT                   /note="HEAT 3"
FT   REPEAT          238..275
FT                   /note="HEAT 4"
FT   REPEAT          276..313
FT                   /note="HEAT 5"
FT   REPEAT          399..436
FT                   /note="HEAT 6"
FT   REPEAT          439..478
FT                   /note="HEAT 7"
FT   REPEAT          617..654
FT                   /note="HEAT 8"
FT   REPEAT          687..724
FT                   /note="HEAT 9"
FT   REPEAT          865..907
FT                   /note="HEAT 10"
FT   REGION          941..994
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        941..966
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        967..994
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         390
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT   MOD_RES         674
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18669648, ECO:0007744|PubMed:18691976,
FT                   ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT   MOD_RES         931
FT                   /note="Phosphothreonine"
FT                   /evidence="ECO:0007744|PubMed:20068231,
FT                   ECO:0007744|PubMed:23186163"
FT   MOD_RES         973
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         975
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1002
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:18669648"
FT   MOD_RES         1015
FT                   /note="Phosphoserine"
FT                   /evidence="ECO:0007744|PubMed:17081983,
FT                   ECO:0007744|PubMed:18691976, ECO:0007744|PubMed:19690332,
FT                   ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:21406692"
FT   VARIANT         64
FT                   /note="A -> P (in dbSNP:rs35722563)"
FT                   /id="VAR_053041"
FT   VARIANT         265
FT                   /note="M -> T (in a colorectal cancer sample; somatic
FT                   mutation)"
FT                   /evidence="ECO:0000269|PubMed:16959974"
FT                   /id="VAR_036125"
FT   VARIANT         581
FT                   /note="M -> I (in dbSNP:rs3795243)"
FT                   /evidence="ECO:0000269|PubMed:10910072"
FT                   /id="VAR_053042"
FT   CONFLICT        115
FT                   /note="R -> G (in Ref. 4; BAB14069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        276
FT                   /note="F -> V (in Ref. 1; AAG30732)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        519
FT                   /note="S -> P (in Ref. 4; BAB55165)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        676
FT                   /note="D -> V (in Ref. 4; BAB14069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        681
FT                   /note="K -> R (in Ref. 4; BAB14069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        704
FT                   /note="V -> A (in Ref. 4; BAB14069)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        836
FT                   /note="N -> D (in Ref. 4; BAB55165)"
FT                   /evidence="ECO:0000305"
FT   CONFLICT        1010
FT                   /note="L -> F (in Ref. 1; AAG30732)"
FT                   /evidence="ECO:0000305"
FT   HELIX           10..17
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   STRAND          19..21
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           24..37
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   STRAND          38..40
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           42..52
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           53..55
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           63..77
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           96..105
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           112..128
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           139..150
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   STRAND          153..155
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           156..165
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   TURN            166..169
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   STRAND          172..176
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           178..189
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           193..202
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           209..214
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           215..218
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   STRAND          219..221
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           222..235
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           238..240
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           243..254
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           259..268
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           270..276
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           281..287
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   TURN            288..292
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           294..305
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           310..313
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           314..316
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           333..348
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           352..360
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           364..375
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           396..407
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           408..411
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           417..432
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   STRAND          434..436
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           438..452
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           455..469
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           554..569
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           573..575
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           581..587
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           589..593
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           598..612
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           616..632
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           635..652
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           655..657
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           692..697
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   TURN            698..701
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           705..720
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           727..738
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           740..742
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           746..760
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           764..782
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           789..792
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           795..805
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           826..840
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           847..855
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           864..877
FT                   /evidence="ECO:0007829|PDB:6IGX"
FT   HELIX           881..895
FT                   /evidence="ECO:0007829|PDB:6IGX"
SQ   SEQUENCE   1015 AA;  114334 MW;  D9ACC205C48F3AF5 CRC64;
     MGAERRLLSI KEAFRLAQQP HQNQAKLVVA LSRTYRTMDD KTVFHEEFIH YLKYVMVVYK
     REPAVERVIE FAAKFVTSFH QSDMEDDEEE EDGGLLNYLF TFLLKSHEAN SNAVRFRVCL
     LINKLLGSMP ENAQIDDDVF DKINKAMLIR LKDKIPNVRI QAVLALSRLQ DPKDDECPVV
     NAYATLIEND SNPEVRRAVL SCIAPSAKTL PKIVGRTKDV KEAVRKLAYQ VLAEKVHMRA
     MSIAQRVMLL QQGLNDRSDA VKQAMQKHLL QGWLRFSEGN ILELLHRLDV ENSSEVAVSV
     LNALFSITPL SELVGLCKNN DGRKLIPVET LTPEIALYWC ALCEYLKSKG DEGEEFLEQI
     LPEPVVYADY LLSYIQSIPV VNEEHRGDFS YIGNLMTKEF IGQQLILIIK SLDTSEEGGR
     KKLLAVLQEI LILPTIPISL VSFLVERLLH IIIDDNKRTQ IVTEIISEIR APIVTVGVNN
     DPADVRKKEL KMAEIKVKLI EAKEALENCI TLQDFNRASE LKEEIKALED ARINLLKETE
     QLEIKEVHIE KNDAETLQKC LILCYELLKQ MSISTGLSAT MNGIIESLIL PGIISIHPVV
     RNLAVLCLGC CGLQNQDFAR KHFVLLLQVL QIDDVTIKIS ALKAIFDQLM TFGIEPFKTK
     KIKTLHCEGT EINSDDEQES KEVEETATAK NVLKLLSDFL DSEVSELRTG AAEGLAKLMF
     SGLLVSSRIL SRLILLWYNP VTEEDVQLRH CLGVFFPVFA YASRTNQECF EEAFLPTLQT
     LANAPASSPL AEIDITNVAE LLVDLTRPSG LNPQAKTSQD YQALTVHDNL AMKICNEILT
     SPCSPEIRVY TKALSSLELS SHLAKDLLVL LNEILEQVKD RTCLRALEKI KIQLEKGNKE
     FGDQAEAAQD ATLTTTTFQN EDEKNKEVYM TPLRGVKATQ ASKSTQLKTN RGQRKVTVSA
     RTNRRCQTAE ADSESDHEVP EPESEMKMRL PRRAKTAALE KSKLNLAQFL NEDLS
//