CND3_HUMAN
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 03-AUG-2022, entry version 185.
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 SMR; Q9BPX3; -.
DR BioGRID; 122089; 124.
DR ComplexPortal; CPX-979; Condensin I complex.
DR CORUM; Q9BPX3; -.
DR DIP; DIP-34891N; -.
DR IntAct; Q9BPX3; 41.
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; Q9BPX3; -.
DR PeptideAtlas; Q9BPX3; -.
DR PRIDE; Q9BPX3; -.
DR ProteomicsDB; 78586; -.
DR Antibodypedia; 23100; 188 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 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; MRGFWEG; -.
DR OrthoDB; 108186at2759; -.
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; 764 hits in 1091 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 160 other tissues.
DR ExpressionAtlas; Q9BPX3; baseline and differential.
DR Genevisible; Q9BPX3; HS.
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; IEA:Ensembl.
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; IEA:Ensembl.
DR GO; GO:1905820; P:positive regulation of chromosome separation; IEA:Ensembl.
DR Gene3D; 1.25.10.10; -; 1.
DR InterPro; IPR011989; ARM-like.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR027165; CND3.
DR InterPro; IPR025977; Cnd3_C.
DR PANTHER; PTHR14418; PTHR14418; 1.
DR Pfam; PF12719; Cnd3; 1.
DR SUPFAM; SSF48371; SSF48371; 1.
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
