SMC5_HUMAN
ID SMC5_HUMAN Reviewed; 1101 AA.
AC Q8IY18; A6NM81; O60335; Q05D92; Q5VZ60; Q96SB9;
DT 09-JAN-2007, integrated into UniProtKB/Swiss-Prot.
DT 09-JAN-2007, sequence version 2.
DT 03-AUG-2022, entry version 151.
DE RecName: Full=Structural maintenance of chromosomes protein 5;
DE Short=SMC protein 5;
DE Short=SMC-5;
DE Short=hSMC5;
GN Name=SMC5; Synonyms=KIAA0594, SMC5L1;
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], INTERACTION WITH SMC6, SUBCELLULAR LOCATION,
RP TISSUE SPECIFICITY, AND VARIANTS ILE-306 AND ARG-308.
RX PubMed=11408570; DOI=10.1091/mbc.12.6.1583;
RA Taylor E.M., Moghraby J.S., Lees J.H., Smit B., Moens P.B., Lehmann A.R.;
RT "Characterization of a novel human SMC heterodimer homologous to the
RT Schizosaccharomyces pombe Rad18/Spr18 complex.";
RL Mol. Biol. Cell 12:1583-1594(2001).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ILE-306.
RC TISSUE=Brain;
RX PubMed=9628581; DOI=10.1093/dnares/5.1.31;
RA Nagase T., Ishikawa K., Miyajima N., Tanaka A., Kotani H., Nomura N.,
RA Ohara O.;
RT "Prediction of the coding sequences of unidentified human genes. IX. The
RT complete sequences of 100 new cDNA clones from brain which can code for
RT large proteins in vitro.";
RL DNA Res. 5:31-39(1998).
RN [3]
RP SEQUENCE REVISION.
RX PubMed=12168954; DOI=10.1093/dnares/9.3.99;
RA Nakajima D., Okazaki N., Yamakawa H., Kikuno R., Ohara O., Nagase T.;
RT "Construction of expression-ready cDNA clones for KIAA genes: manual
RT curation of 330 KIAA cDNA clones.";
RL DNA Res. 9:99-106(2002).
RN [4]
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANTS ILE-306 AND ARG-308.
RC TISSUE=Mammary gland, and Uterus;
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 INTERACTION WITH NSMCE2.
RX PubMed=16055714; DOI=10.1128/mcb.25.16.7021-7032.2005;
RA Potts P.R., Yu H.;
RT "Human MMS21/NSE2 is a SUMO ligase required for DNA repair.";
RL Mol. Cell. Biol. 25:7021-7032(2005).
RN [7]
RP FUNCTION.
RX PubMed=16810316; DOI=10.1038/sj.emboj.7601218;
RA Potts P.R., Porteus M.H., Yu H.;
RT "Human SMC5/6 complex promotes sister chromatid homologous recombination by
RT recruiting the SMC1/3 cohesin complex to double-strand breaks.";
RL EMBO J. 25:3377-3388(2006).
RN [8]
RP FUNCTION, AND SUBCELLULAR LOCATION.
RX PubMed=17589526; DOI=10.1038/nsmb1259;
RA Potts P.R., Yu H.;
RT "The SMC5/6 complex maintains telomere length in ALT cancer cells through
RT SUMOylation of telomere-binding proteins.";
RL Nat. Struct. Mol. Biol. 14:581-590(2007).
RN [9]
RP SUMOYLATION, UBIQUITINATION, AND IDENTIFICATION IN THE SMC5-SMC6 COMPLEX.
RX PubMed=18086888; DOI=10.1128/mcb.00767-07;
RA Taylor E.M., Copsey A.C., Hudson J.J., Vidot S., Lehmann A.R.;
RT "Identification of the proteins, including MAGEG1, that make up the human
RT SMC5-6 protein complex.";
RL Mol. Cell. Biol. 28:1197-1206(2008).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, 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 [11]
RP FUNCTION.
RX PubMed=19502785; DOI=10.4161/cc.8.14.8979;
RA Behlke-Steinert S., Touat-Todeschini L., Skoufias D.A., Margolis R.L.;
RT "SMC5 and MMS21 are required for chromosome cohesion and mitotic
RT progression.";
RL Cell Cycle 8:2211-2218(2009).
RN [12]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, 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 [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-25 AND SER-35, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=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 [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-35, AND IDENTIFICATION BY
RP 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 [16]
RP INTERACTION WITH RAD18 AND SLF2, SUBCELLULAR LOCATION, AND IDENTIFICATION
RP BY MASS SPECTROMETRY.
RX PubMed=25931565; DOI=10.1126/science.1253671;
RA Raeschle M., Smeenk G., Hansen R.K., Temu T., Oka Y., Hein M.Y.,
RA Nagaraj N., Long D.T., Walter J.C., Hofmann K., Storchova Z., Cox J.,
RA Bekker-Jensen S., Mailand N., Mann M.;
RT "DNA repair. Proteomics reveals dynamic assembly of repair complexes during
RT bypass of DNA cross-links.";
RL Science 348:1253671-1253671(2015).
RN [17]
RP FUNCTION, DEGRADATION (MICROBIAL INFECTION), AND SUBUNIT (MICROBIAL
RP INFECTION).
RX PubMed=26983541; DOI=10.1038/nature17170;
RA Decorsiere A., Mueller H., van Breugel P.C., Abdul F., Gerossier L.,
RA Beran R.K., Livingston C.M., Niu C., Fletcher S.P., Hantz O., Strubin M.;
RT "Hepatitis B virus X protein identifies the Smc5/6 complex as a host
RT restriction factor.";
RL Nature 531:386-389(2016).
CC -!- FUNCTION: Core component of the SMC5-SMC6 complex, a complex involved
CC in repair of DNA double-strand breaks by homologous recombination. The
CC complex may promote sister chromatid homologous recombination by
CC recruiting the SMC1-SMC3 cohesin complex to double-strand breaks. The
CC complex is required for telomere maintenance via recombination in ALT
CC (alternative lengthening of telomeres) cell lines and mediates
CC sumoylation of shelterin complex (telosome) components which is
CC proposed to lead to shelterin complex disassembly in ALT-associated PML
CC bodies (APBs). Required for recruitment of telomeres to PML nuclear
CC bodies. Required for sister chromatid cohesion during prometaphase and
CC mitotic progression; the function seems to be independent of SMC6.
CC SMC5-SMC6 complex may prevent transcription of episomal DNA, such as
CC circular viral DNA genome (PubMed:26983541).
CC {ECO:0000269|PubMed:16810316, ECO:0000269|PubMed:17589526,
CC ECO:0000269|PubMed:19502785, ECO:0000269|PubMed:26983541}.
CC -!- SUBUNIT: Forms a heterodimer with SMC6 (PubMed:11408570). Component of
CC the SMC5-SMC6 complex which consists at least of SMC5, SMC6, NSMCE2,
CC NSMCE1, NSMCE4A or EID3 and NSMCE3 (PubMed:18086888). Interacts with
CC NSMCE2 (PubMed:16055714). Interacts with SLF2; this interaction induces
CC an association of the SLF1-SLF2 complex with the SMC5-SMC6 complex
CC (PubMed:25931565). Interacts with RAD18; this interaction is increased
CC in a SLF1 or SLF2-dependent manner (PubMed:25931565).
CC {ECO:0000269|PubMed:11408570, ECO:0000269|PubMed:16055714,
CC ECO:0000269|PubMed:18086888, ECO:0000269|PubMed:25931565}.
CC -!- SUBUNIT: (Microbial infection) SMC5-SMC6 complex interacts with
CC Hepatitis B X protein. {ECO:0000269|PubMed:26983541}.
CC -!- INTERACTION:
CC Q8IY18; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-605405, EBI-11988027;
CC Q8IY18; Q8N140: EID3; NbExp=4; IntAct=EBI-605405, EBI-744483;
CC Q8IY18; Q8IX21: SLF2; NbExp=2; IntAct=EBI-605405, EBI-2682240;
CC Q8IY18; Q96SB8: SMC6; NbExp=5; IntAct=EBI-605405, EBI-605415;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:11408570,
CC ECO:0000269|PubMed:25931565}. Chromosome
CC {ECO:0000250|UniProtKB:Q8CG46}. Nucleus, PML body
CC {ECO:0000269|PubMed:17589526}. Chromosome, telomere
CC {ECO:0000269|PubMed:17589526}. Note=Associates with chromatin
CC (PubMed:25931565). Colocalizes with SMC6 on the X-Y chromosome pair
CC within the sex vesicle during late pachytene/diplotene (By similarity).
CC Localizes to PML nuclear bodies in ALT cell lines (PubMed:17589526).
CC Accumulates with RAD18 and the SLF1-SLF2 complex at replication-coupled
CC DNA interstrand repair and DNA double-strand breaks (DSBs) sites on
CC chromatin in a ubiquitin-dependent manner (PubMed:25931565).
CC {ECO:0000250|UniProtKB:Q8CG46, ECO:0000269|PubMed:25931565}.
CC -!- TISSUE SPECIFICITY: Widely expressed (PubMed:11408570). Strongly
CC expressed in testis (PubMed:11408570). {ECO:0000269|PubMed:11408570}.
CC -!- DOMAIN: The flexible hinge domain, which separates the large
CC intramolecular coiled coil regions, allows the heterotypic interaction
CC with the corresponding domain of SMC6, forming a V-shaped heterodimer.
CC {ECO:0000250}.
CC -!- PTM: Sumoylated. {ECO:0000269|PubMed:18086888}.
CC -!- PTM: Ubiquitinated. {ECO:0000269|PubMed:18086888}.
CC -!- PTM: (Microbial infection) SMC5-SMC6 complex is degraded by the
CC activity of Hepatitis B X protein. {ECO:0000269|PubMed:26983541}.
CC -!- SIMILARITY: Belongs to the SMC family. SMC5 subfamily. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH17666.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence.; Evidence={ECO:0000305};
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DR EMBL; AJ310550; CAC39247.1; -; mRNA.
DR EMBL; AB011166; BAA25520.2; -; mRNA.
DR EMBL; AL162390; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC017666; AAH17666.1; ALT_SEQ; mRNA.
DR EMBL; BC038225; AAH38225.1; -; mRNA.
DR CCDS; CCDS6632.1; -.
DR RefSeq; NP_055925.2; NM_015110.3.
DR AlphaFoldDB; Q8IY18; -.
DR SMR; Q8IY18; -.
DR BioGRID; 116754; 46.
DR ComplexPortal; CPX-5992; SMC5-SMC6 SUMO ligase complex, EID3 variant.
DR ComplexPortal; CPX-6086; SMC5-SMC6 SUMO ligase complex, NSE4EA variant.
DR IntAct; Q8IY18; 23.
DR MINT; Q8IY18; -.
DR STRING; 9606.ENSP00000354957; -.
DR iPTMnet; Q8IY18; -.
DR MetOSite; Q8IY18; -.
DR PhosphoSitePlus; Q8IY18; -.
DR BioMuta; SMC5; -.
DR DMDM; 122070387; -.
DR EPD; Q8IY18; -.
DR jPOST; Q8IY18; -.
DR MassIVE; Q8IY18; -.
DR MaxQB; Q8IY18; -.
DR PaxDb; Q8IY18; -.
DR PeptideAtlas; Q8IY18; -.
DR PRIDE; Q8IY18; -.
DR ProteomicsDB; 71087; -.
DR Antibodypedia; 26866; 200 antibodies from 27 providers.
DR DNASU; 23137; -.
DR Ensembl; ENST00000361138.7; ENSP00000354957.5; ENSG00000198887.9.
DR GeneID; 23137; -.
DR KEGG; hsa:23137; -.
DR MANE-Select; ENST00000361138.7; ENSP00000354957.5; NM_015110.4; NP_055925.2.
DR UCSC; uc004ahr.3; human.
DR CTD; 23137; -.
DR DisGeNET; 23137; -.
DR GeneCards; SMC5; -.
DR HGNC; HGNC:20465; SMC5.
DR HPA; ENSG00000198887; Low tissue specificity.
DR MIM; 609386; gene.
DR neXtProt; NX_Q8IY18; -.
DR OpenTargets; ENSG00000198887; -.
DR PharmGKB; PA134993662; -.
DR VEuPathDB; HostDB:ENSG00000198887; -.
DR eggNOG; KOG0979; Eukaryota.
DR GeneTree; ENSGT00550000074816; -.
DR HOGENOM; CLU_004969_1_0_1; -.
DR InParanoid; Q8IY18; -.
DR OMA; SAEFFPG; -.
DR OrthoDB; 100993at2759; -.
DR PhylomeDB; Q8IY18; -.
DR TreeFam; TF105708; -.
DR PathwayCommons; Q8IY18; -.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR SignaLink; Q8IY18; -.
DR SIGNOR; Q8IY18; -.
DR BioGRID-ORCS; 23137; 578 hits in 1090 CRISPR screens.
DR ChiTaRS; SMC5; human.
DR GeneWiki; SMC5; -.
DR GenomeRNAi; 23137; -.
DR Pharos; Q8IY18; Tbio.
DR PRO; PR:Q8IY18; -.
DR Proteomes; UP000005640; Chromosome 9.
DR RNAct; Q8IY18; protein.
DR Bgee; ENSG00000198887; Expressed in sural nerve and 195 other tissues.
DR Genevisible; Q8IY18; HS.
DR GO; GO:0030054; C:cell junction; IDA:HPA.
DR GO; GO:0000775; C:chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0000781; C:chromosome, telomeric region; IDA:UniProtKB.
DR GO; GO:0005737; C:cytoplasm; IEA:Ensembl.
DR GO; GO:0035061; C:interchromatin granule; IDA:UniProtKB.
DR GO; GO:0016607; C:nuclear speck; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0016605; C:PML body; IDA:UniProtKB.
DR GO; GO:0000803; C:sex chromosome; ISS:UniProtKB.
DR GO; GO:0035861; C:site of double-strand break; IDA:UniProtKB.
DR GO; GO:0030915; C:Smc5-Smc6 complex; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0016887; F:ATP hydrolysis activity; IEA:InterPro.
DR GO; GO:0003697; F:single-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
DR GO; GO:0006974; P:cellular response to DNA damage stimulus; IDA:UniProtKB.
DR GO; GO:0090398; P:cellular senescence; IMP:UniProtKB.
DR GO; GO:0030261; P:chromosome condensation; IEA:Ensembl.
DR GO; GO:0007059; P:chromosome segregation; IEA:Ensembl.
DR GO; GO:0000724; P:double-strand break repair via homologous recombination; IMP:UniProtKB.
DR GO; GO:0018393; P:internal peptidyl-lysine acetylation; IEA:Ensembl.
DR GO; GO:0044772; P:mitotic cell cycle phase transition; IEA:Ensembl.
DR GO; GO:0051984; P:positive regulation of chromosome segregation; IMP:UniProtKB.
DR GO; GO:0034184; P:positive regulation of maintenance of mitotic sister chromatid cohesion; IMP:UniProtKB.
DR GO; GO:0071459; P:protein localization to chromosome, centromeric region; IEA:Ensembl.
DR GO; GO:0016925; P:protein sumoylation; IC:ComplexPortal.
DR GO; GO:0032204; P:regulation of telomere maintenance; IC:ComplexPortal.
DR GO; GO:0019827; P:stem cell population maintenance; IEA:Ensembl.
DR GO; GO:0000722; P:telomere maintenance via recombination; IMP:UniProtKB.
DR Gene3D; 3.40.50.300; -; 2.
DR InterPro; IPR027417; P-loop_NTPase.
DR InterPro; IPR003395; RecF/RecN/SMC_N.
DR InterPro; IPR027131; SMC5.
DR PANTHER; PTHR45916; PTHR45916; 1.
DR Pfam; PF02463; SMC_N; 1.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW ATP-binding; Cell cycle; Cell division; Chromosome; Coiled coil;
KW DNA damage; DNA recombination; DNA repair; Mitosis; Nucleotide-binding;
KW Nucleus; Phosphoprotein; Reference proteome; Telomere; Ubl conjugation.
FT CHAIN 1..1101
FT /note="Structural maintenance of chromosomes protein 5"
FT /id="PRO_0000270951"
FT REGION 1..43
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 446..646
FT /note="Flexible hinge"
FT COILED 207..445
FT /evidence="ECO:0000255"
FT COILED 647..828
FT /evidence="ECO:0000255"
FT COILED 888..927
FT /evidence="ECO:0000255"
FT COMPBIAS 1..16
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 80..87
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000255"
FT MOD_RES 25
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 35
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT VARIANT 306
FT /note="V -> I (in dbSNP:rs1180116)"
FT /evidence="ECO:0000269|PubMed:11408570,
FT ECO:0000269|PubMed:15489334, ECO:0000269|PubMed:9628581"
FT /id="VAR_029824"
FT VARIANT 308
FT /note="C -> R (in dbSNP:rs1180117)"
FT /evidence="ECO:0000269|PubMed:11408570,
FT ECO:0000269|PubMed:15489334"
FT /id="VAR_029825"
FT VARIANT 682
FT /note="H -> R (in dbSNP:rs11142365)"
FT /id="VAR_061869"
SQ SEQUENCE 1101 AA; 128806 MW; 54393D50688A914A CRC64;
MATPSKKTST PSPQPSKRAL PRDPSSEVPS KRKNSAPQLP LLQSSGPFVE GSIVRISMEN
FLTYDICEVS PGPHLNMIVG ANGTGKSSIV CAICLGLAGK PAFMGRADKV GFFVKRGCSR
GMVEIELFRA SGNLVITREI DVAKNQSFWF INKKSTTQKI VEEKVAALNI QVGNLCQFLP
QDKVGEFAKL SKIELLEATE KSIGPPEMHK YHCELKNLRE KEKQLETSCK EKTEYLQKMV
QRNERYKQDV ERFYERKRHL DLIEMLEAKR PWVEYENVRQ EYEEVKLVRD RVKEEVRKLK
EGQIPVTCRI EEMENERHNL EARIKEKATD IKEASQKCKQ KQDVIERKDK HIEELQQALI
VKQNEELDRQ RRIGNTRKMI EDLQNELKTT ENCENLQPQI DAITNDLRRI QDEKALCEGE
IIDKRRERET LEKEKKSVDD HIVRFDNLMN QKEDKLRQRF RDTYDAVLWL RNNRDKFKQR
VCEPIMLTIN MKDNKNAKYI ENHIPSNDLR AFVFESQEDM EVFLKEVRDN KKLRVNAVIA
PKSSYADKAP SRSLNELKQY GFFSYLRELF DAPDPVMSYL CCQYHIHEVP VGTEKTRERI
ERVIQETRLK QIYTAEEKYV VKTSFYSNKV ISSNTSLKVA QFLTVTVDLE QRRHLEEQLK
EIHRKLQAVD SGLIALRETS KHLEHKDNEL RQKKKELLER KTKKRQLEQK ISSKLGSLKL
MEQDTCNLEE EERKASTKIK EINVQKAKLV TELTNLIKIC TSLHIQKVDL ILQNTTVISE
KNKLESDYMA ASSQLRLTEQ HFIELDENRQ RLLQKCKELM KRARQVCNLG AEQTLPQEYQ
TQVPTIPNGH NSSLPMVFQD LPNTLDEIDA LLTEERSRAS CFTGLNPTIV QEYTKREEEI
EQLTEELKGK KVELDQYREN ISQVKERWLN PLKELVEKIN EKFSNFFSSM QCAGEVDLHT
ENEEDYDKYG IRIRVKFRSS TQLHELTPHH QSGGERSVST MLYLMALQEL NRCPFRVVDE
INQGMDPINE RRVFEMVVNT ACKENTSQYF FITPKLLQNL PYSEKMTVLF VYNGPHMLEP
NTWNLKAFQR RRRRITFTQP S
