CBX2_HUMAN
ID CBX2_HUMAN Reviewed; 532 AA.
AC Q14781; Q0VDA5; Q9BTB1;
DT 24-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 11-OCT-2005, sequence version 2.
DT 03-AUG-2022, entry version 189.
DE RecName: Full=Chromobox protein homolog 2;
GN Name=CBX2;
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 [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=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 [3]
RP NUCLEOTIDE SEQUENCE [MRNA] OF 455-532.
RC TISSUE=Peripheral blood;
RX PubMed=7782071; DOI=10.1016/0888-7543(95)80091-y;
RA Gecz J., Gaunt S.J., Passage E., Burton R.D., Cudrey C., Pearce J.J.H.,
RA Fontes M.;
RT "Assignment of a Polycomb-like chromobox gene (CBX2) to human chromosome
RT 17q25.";
RL Genomics 26:130-133(1995).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY, AND IDENTIFICATION IN A PRC1-LIKE
RP HPRC-H COMPLEX WITH BMI1; CBX4; CBX8; PHC1; PHC2; PHC3; RING1 AND RNF2.
RX PubMed=12167701; DOI=10.1128/mcb.22.17.6070-6078.2002;
RA Levine S.S., Weiss A., Erdjument-Bromage H., Shao Z., Tempst P.,
RA Kingston R.E.;
RT "The core of the polycomb repressive complex is compositionally and
RT functionally conserved in flies and humans.";
RL Mol. Cell. Biol. 22:6070-6078(2002).
RN [5]
RP INTERACTION WITH H3C15; H3C1 AND RNF2, SUBCELLULAR LOCATION, DEVELOPMENTAL
RP STAGE, AND MUTAGENESIS OF ILE-17.
RX PubMed=18927235; DOI=10.1073/pnas.0805317105;
RA Vincenz C., Kerppola T.K.;
RT "Different polycomb group CBX family proteins associate with distinct
RT regions of chromatin using nonhomologous protein sequences.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:16572-16577(2008).
RN [6]
RP FUNCTION IN SEXUAL DEVELOPMENT, AND VARIANTS SRXY5 LEU-98 AND PRO-443.
RX PubMed=19361780; DOI=10.1016/j.ajhg.2009.03.016;
RA Biason-Lauber A., Konrad D., Meyer M., DeBeaufort C., Schoenle E.J.;
RT "Ovaries and female phenotype in a girl with 46,XY karyotype and mutations
RT in the CBX2 gene.";
RL Am. J. Hum. Genet. 84:658-663(2009).
RN [7]
RP IDENTIFICATION IN A PRC1-LIKE COMPLEX.
RX PubMed=19636380; DOI=10.1371/journal.pone.0006380;
RA Maertens G.N., El Messaoudi-Aubert S., Racek T., Stock J.K., Nicholls J.,
RA Rodriguez-Niedenfuhr M., Gil J., Peters G.;
RT "Several distinct polycomb complexes regulate and co-localize on the INK4a
RT tumor suppressor locus.";
RL PLoS ONE 4:E6380-E6380(2009).
RN [8]
RP FUNCTION, IDENTIFICATION BY MASS SPECTROMETRY (ISOFORM 2), IDENTIFICATION
RP IN A PRC1-LIKE COMPLEX, AND SUBCELLULAR LOCATION.
RX PubMed=21282530; DOI=10.1074/mcp.m110.002642;
RA Vandamme J., Volkel P., Rosnoblet C., Le Faou P., Angrand P.O.;
RT "Interaction proteomics analysis of polycomb proteins defines distinct PRC1
RT Complexes in mammalian cells.";
RL Mol. Cell. Proteomics 0:0-0(2011).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-302, 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 METHYLATION [LARGE SCALE ANALYSIS] AT ARG-247, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Colon carcinoma;
RX PubMed=24129315; DOI=10.1074/mcp.o113.027870;
RA Guo A., Gu H., Zhou J., Mulhern D., Wang Y., Lee K.A., Yang V., Aguiar M.,
RA Kornhauser J., Jia X., Ren J., Beausoleil S.A., Silva J.C., Vemulapalli V.,
RA Bedford M.T., Comb M.J.;
RT "Immunoaffinity enrichment and mass spectrometry analysis of protein
RT methylation.";
RL Mol. Cell. Proteomics 13:372-387(2014).
RN [11]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-146 AND LYS-153, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [12]
RP STRUCTURE BY NMR OF 6-69.
RG RIKEN structural genomics initiative (RSGI);
RT "Solution structure of the chromo domain of chromobox homolog 2 from
RT human.";
RL Submitted (JAN-2007) to the PDB data bank.
CC -!- FUNCTION: Component of a Polycomb group (PcG) multiprotein PRC1-like
CC complex, a complex class required to maintain the transcriptionally
CC repressive state of many genes, including Hox genes, throughout
CC development (PubMed:21282530). PcG PRC1 complex acts via chromatin
CC remodeling and modification of histones; it mediates monoubiquitination
CC of histone H2A 'Lys-119', rendering chromatin heritably changed in its
CC expressibility (PubMed:21282530). Binds to histone H3 trimethylated at
CC 'Lys-9' (H3K9me3) or at 'Lys-27' (H3K27me3) (By similarity). Plays a
CC role in the lineage differentiation of the germ layers in embryonic
CC development (By similarity). Involved in sexual development, acting as
CC activator of NR5A1 expression (PubMed:19361780).
CC {ECO:0000250|UniProtKB:P30658, ECO:0000269|PubMed:19361780,
CC ECO:0000269|PubMed:21282530}.
CC -!- SUBUNIT: Component of a PRC1-like complex (PubMed:12167701,
CC PubMed:19636380, PubMed:21282530). The composition of the PRC1 complex
CC may differ between the PRC1 complex in pluripotent embryonic stem cells
CC containing RNF2, CBX7 and PCGF2, and the PRC1 complex in
CC differentiating cells containing RNF2, CBX2, CBX4 and BMI1 (By
CC similarity). May interact with H3C15, H3C1 and RNF2 (PubMed:18927235).
CC Interacts (via chromodomain) with histone H3K9Me3 and H3K27me3 (By
CC similarity). {ECO:0000250|UniProtKB:P30658,
CC ECO:0000269|PubMed:12167701, ECO:0000269|PubMed:18927235,
CC ECO:0000269|PubMed:19636380, ECO:0000269|PubMed:21282530}.
CC -!- INTERACTION:
CC Q14781; Q6P158: DHX57; NbExp=3; IntAct=EBI-745934, EBI-1051531;
CC Q14781; P60409: KRTAP10-7; NbExp=3; IntAct=EBI-745934, EBI-10172290;
CC Q14781; P60411: KRTAP10-9; NbExp=3; IntAct=EBI-745934, EBI-10172052;
CC Q14781; P0C7H8: KRTAP2-3; NbExp=3; IntAct=EBI-745934, EBI-10196781;
CC Q14781; Q99750: MDFI; NbExp=3; IntAct=EBI-745934, EBI-724076;
CC Q14781; P0DJD3: RBMY1A1; NbExp=3; IntAct=EBI-745934, EBI-8638511;
CC Q14781; Q15415: RBMY1J; NbExp=3; IntAct=EBI-745934, EBI-8642021;
CC Q14781-2; Q8N9W6-4: BOLL; NbExp=3; IntAct=EBI-11974585, EBI-11983447;
CC Q14781-2; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-11974585, EBI-3867333;
CC Q14781-2; Q6P158: DHX57; NbExp=3; IntAct=EBI-11974585, EBI-1051531;
CC Q14781-2; G5E9A7: DMWD; NbExp=3; IntAct=EBI-11974585, EBI-10976677;
CC Q14781-2; Q00403: GTF2B; NbExp=3; IntAct=EBI-11974585, EBI-389564;
CC Q14781-2; Q9Y5Q9: GTF3C3; NbExp=3; IntAct=EBI-11974585, EBI-1054873;
CC Q14781-2; P59991: KRTAP12-2; NbExp=3; IntAct=EBI-11974585, EBI-10176379;
CC Q14781-2; P60328: KRTAP12-3; NbExp=3; IntAct=EBI-11974585, EBI-11953334;
CC Q14781-2; Q9BYR3: KRTAP4-4; NbExp=3; IntAct=EBI-11974585, EBI-11958132;
CC Q14781-2; Q99750: MDFI; NbExp=3; IntAct=EBI-11974585, EBI-724076;
CC Q14781-2; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-11974585, EBI-16439278;
CC Q14781-2; D3DTS7: PMP22; NbExp=3; IntAct=EBI-11974585, EBI-25882629;
CC Q14781-2; Q15415: RBMY1J; NbExp=3; IntAct=EBI-11974585, EBI-8642021;
CC Q14781-2; Q6ZRY4: RBPMS2; NbExp=3; IntAct=EBI-11974585, EBI-11987469;
CC Q14781-2; Q7Z699: SPRED1; NbExp=3; IntAct=EBI-11974585, EBI-5235340;
CC Q14781-2; Q13148: TARDBP; NbExp=6; IntAct=EBI-11974585, EBI-372899;
CC Q14781-2; P54577: YARS1; NbExp=3; IntAct=EBI-11974585, EBI-1048893;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:18927235,
CC ECO:0000269|PubMed:21282530}. Chromosome {ECO:0000269|PubMed:18927235}.
CC Note=Localized in distinct foci on chromatin and in chromocenters.
CC Localizes to the inactive X chromosome. Seems to be recruited to
CC H3K27me3, H3K9ac and H3K3me2 sites on chromatin.
CC {ECO:0000269|PubMed:18927235}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q14781-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q14781-2; Sequence=VSP_015816, VSP_015817;
CC -!- DEVELOPMENTAL STAGE: Expressed during interphase and metaphase.
CC {ECO:0000269|PubMed:18927235}.
CC -!- DISEASE: 46,XY sex reversal 5 (SRXY5) [MIM:613080]: A disorder of sex
CC development. Affected individuals have a 46,XY karyotype but present as
CC phenotypically normal females. {ECO:0000269|PubMed:19361780}. Note=The
CC disease is caused by variants affecting the gene represented in this
CC entry.
CC -!- MISCELLANEOUS: The human orthologuous proteins of Drosophila Polycomb
CC group protein Pc, CBX2, CBX4, CBX6, CBX7 and CBX8, show distinct
CC nuclear localizations, contribute differently to transcriptional
CC repression, and appear to be part of distinct PRC1-like protein
CC complexes. The hPRC-H complex purification reported by PubMed:12167701
CC probably presents a mixture of different complexes.
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DR EMBL; AC105337; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC004252; AAH04252.1; -; mRNA.
DR EMBL; BC119759; AAI19760.1; -; mRNA.
DR EMBL; BC119760; AAI19761.1; -; mRNA.
DR EMBL; X77824; CAA54839.1; -; Genomic_DNA.
DR CCDS; CCDS11764.1; -. [Q14781-2]
DR CCDS; CCDS32757.1; -. [Q14781-1]
DR PIR; I38007; I38007.
DR RefSeq; NP_005180.1; NM_005189.2. [Q14781-1]
DR RefSeq; NP_116036.1; NM_032647.3. [Q14781-2]
DR PDB; 2D9U; NMR; -; A=9-69.
DR PDB; 3H91; X-ray; 1.50 A; A/B=9-62.
DR PDB; 5EPK; X-ray; 1.80 A; A=8-62.
DR PDBsum; 2D9U; -.
DR PDBsum; 3H91; -.
DR PDBsum; 5EPK; -.
DR AlphaFoldDB; Q14781; -.
DR BMRB; Q14781; -.
DR SMR; Q14781; -.
DR BioGRID; 124228; 104.
DR CORUM; Q14781; -.
DR DIP; DIP-48604N; -.
DR IntAct; Q14781; 71.
DR MINT; Q14781; -.
DR STRING; 9606.ENSP00000308750; -.
DR BindingDB; Q14781; -.
DR ChEMBL; CHEMBL3779761; -.
DR iPTMnet; Q14781; -.
DR PhosphoSitePlus; Q14781; -.
DR BioMuta; CBX2; -.
DR DMDM; 77416853; -.
DR EPD; Q14781; -.
DR jPOST; Q14781; -.
DR MassIVE; Q14781; -.
DR MaxQB; Q14781; -.
DR PaxDb; Q14781; -.
DR PeptideAtlas; Q14781; -.
DR PRIDE; Q14781; -.
DR ProteomicsDB; 60169; -. [Q14781-1]
DR ProteomicsDB; 60170; -. [Q14781-2]
DR ABCD; Q14781; 2 sequenced antibodies.
DR Antibodypedia; 32656; 310 antibodies from 30 providers.
DR DNASU; 84733; -.
DR Ensembl; ENST00000269399.5; ENSP00000269399.5; ENSG00000173894.11. [Q14781-2]
DR Ensembl; ENST00000310942.9; ENSP00000308750.4; ENSG00000173894.11. [Q14781-1]
DR GeneID; 84733; -.
DR KEGG; hsa:84733; -.
DR MANE-Select; ENST00000310942.9; ENSP00000308750.4; NM_005189.3; NP_005180.1.
DR UCSC; uc002jxb.3; human. [Q14781-1]
DR CTD; 84733; -.
DR DisGeNET; 84733; -.
DR GeneCards; CBX2; -.
DR HGNC; HGNC:1552; CBX2.
DR HPA; ENSG00000173894; Tissue enhanced (lymphoid tissue, testis).
DR MalaCards; CBX2; -.
DR MIM; 602770; gene.
DR MIM; 613080; phenotype.
DR neXtProt; NX_Q14781; -.
DR OpenTargets; ENSG00000173894; -.
DR Orphanet; 242; 46,XY complete gonadal dysgenesis.
DR PharmGKB; PA26127; -.
DR VEuPathDB; HostDB:ENSG00000173894; -.
DR eggNOG; KOG2748; Eukaryota.
DR GeneTree; ENSGT00940000158816; -.
DR HOGENOM; CLU_027573_0_0_1; -.
DR InParanoid; Q14781; -.
DR OMA; FQQNKGP; -.
DR OrthoDB; 1628171at2759; -.
DR PhylomeDB; Q14781; -.
DR TreeFam; TF106456; -.
DR PathwayCommons; Q14781; -.
DR Reactome; R-HSA-2559580; Oxidative Stress Induced Senescence.
DR Reactome; R-HSA-3108214; SUMOylation of DNA damage response and repair proteins.
DR Reactome; R-HSA-3899300; SUMOylation of transcription cofactors.
DR Reactome; R-HSA-4551638; SUMOylation of chromatin organization proteins.
DR Reactome; R-HSA-4570464; SUMOylation of RNA binding proteins.
DR Reactome; R-HSA-4655427; SUMOylation of DNA methylation proteins.
DR Reactome; R-HSA-8939243; RUNX1 interacts with co-factors whose precise effect on RUNX1 targets is not known.
DR Reactome; R-HSA-8943724; Regulation of PTEN gene transcription.
DR SignaLink; Q14781; -.
DR SIGNOR; Q14781; -.
DR BioGRID-ORCS; 84733; 11 hits in 1079 CRISPR screens.
DR ChiTaRS; CBX2; human.
DR EvolutionaryTrace; Q14781; -.
DR GeneWiki; CBX2_(gene); -.
DR GenomeRNAi; 84733; -.
DR Pharos; Q14781; Tchem.
DR PRO; PR:Q14781; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q14781; protein.
DR Bgee; ENSG00000173894; Expressed in secondary oocyte and 133 other tissues.
DR Genevisible; Q14781; HS.
DR GO; GO:0000791; C:euchromatin; IEA:Ensembl.
DR GO; GO:0000792; C:heterochromatin; IBA:GO_Central.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0031519; C:PcG protein complex; IDA:UniProtKB.
DR GO; GO:0035102; C:PRC1 complex; IDA:UniProtKB.
DR GO; GO:0003682; F:chromatin binding; IEA:Ensembl.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0035064; F:methylated histone binding; IBA:GO_Central.
DR GO; GO:0030154; P:cell differentiation; IEA:UniProtKB-KW.
DR GO; GO:0006325; P:chromatin organization; IEA:UniProtKB-KW.
DR GO; GO:0045137; P:development of primary sexual characteristics; IMP:UniProtKB.
DR GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
DR IDEAL; IID00670; -.
DR InterPro; IPR042796; CBX2.
DR InterPro; IPR033773; CBX7_C.
DR InterPro; IPR016197; Chromo-like_dom_sf.
DR InterPro; IPR000953; Chromo/chromo_shadow_dom.
DR InterPro; IPR023780; Chromo_domain.
DR InterPro; IPR023779; Chromodomain_CS.
DR PANTHER; PTHR46860; PTHR46860; 1.
DR Pfam; PF17218; CBX7_C; 1.
DR Pfam; PF00385; Chromo; 1.
DR SMART; SM00298; CHROMO; 1.
DR SUPFAM; SSF54160; SSF54160; 1.
DR PROSITE; PS00598; CHROMO_1; 1.
DR PROSITE; PS50013; CHROMO_2; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; Chromatin regulator; Chromosome;
KW Differentiation; Disease variant; DNA-binding; Isopeptide bond;
KW Methylation; Nucleus; Phosphoprotein; Reference proteome; Repressor;
KW Sexual differentiation; Transcription; Transcription regulation;
KW Ubl conjugation.
FT CHAIN 1..532
FT /note="Chromobox protein homolog 2"
FT /id="PRO_0000080201"
FT DOMAIN 12..70
FT /note="Chromo"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00053"
FT DNA_BIND 75..87
FT /note="A.T hook"
FT REGION 1..66
FT /note="Involved in the interaction with H3C15 and H3C1"
FT /evidence="ECO:0000269|PubMed:18927235"
FT REGION 60..204
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 296..348
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 379..493
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOTIF 163..168
FT /note="Nuclear localization signal"
FT /evidence="ECO:0000255"
FT COMPBIAS 102..119
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 125..142
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..173
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 399..413
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 459..493
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 247
FT /note="Asymmetric dimethylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 247
FT /note="Omega-N-methylarginine; alternate"
FT /evidence="ECO:0007744|PubMed:24129315"
FT MOD_RES 302
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 146
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT CROSSLNK 153
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:28112733"
FT VAR_SEQ 97..211
FT /note="EPDAPSKSKSSSSSSSSTSSSSSSDEEDDSDLDAKRGPRGRETHPVPQKKAQ
FT ILVAKPELKDPIRKKRGRKPLPPEQKATRRPVSLAKVLKTARKDLGAPASKLPPPLSAP
FT VAGL -> VGGCAGYADPTSQHPLGVGGRQREGLGPSGRGWHFCQQSVPLLGKQEPPFF
FT LSLSFCCQGPQPAESSSPPLPGASCFSLSCTPLCWVAGSNCCRQALFPPRGSLGDGKEQ
FT EACVQ (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015816"
FT VAR_SEQ 212..532
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_015817"
FT VARIANT 98
FT /note="P -> L (in SRXY5; dbSNP:rs121908255)"
FT /evidence="ECO:0000269|PubMed:19361780"
FT /id="VAR_063751"
FT VARIANT 443
FT /note="R -> P (in SRXY5; dbSNP:rs121908256)"
FT /evidence="ECO:0000269|PubMed:19361780"
FT /id="VAR_063752"
FT MUTAGEN 17
FT /note="I->F: Reduced interaction with H3C15 and H3C1."
FT /evidence="ECO:0000269|PubMed:18927235"
FT STRAND 11..23
FT /evidence="ECO:0007829|PDB:3H91"
FT STRAND 26..33
FT /evidence="ECO:0007829|PDB:3H91"
FT HELIX 38..40
FT /evidence="ECO:0007829|PDB:3H91"
FT STRAND 42..45
FT /evidence="ECO:0007829|PDB:3H91"
FT HELIX 46..48
FT /evidence="ECO:0007829|PDB:3H91"
FT HELIX 53..59
FT /evidence="ECO:0007829|PDB:3H91"
SQ SEQUENCE 532 AA; 56081 MW; 3DB58A654568BDD4 CRC64;
MEELSSVGEQ VFAAECILSK RLRKGKLEYL VKWRGWSSKH NSWEPEENIL DPRLLLAFQK
KEHEKEVQNR KRGKRPRGRP RKLTAMSSCS RRSKLKEPDA PSKSKSSSSS SSSTSSSSSS
DEEDDSDLDA KRGPRGRETH PVPQKKAQIL VAKPELKDPI RKKRGRKPLP PEQKATRRPV
SLAKVLKTAR KDLGAPASKL PPPLSAPVAG LAALKAHAKE ACGGPSAMAT PENLASLMKG
MASSPGRGGI SWQSSIVHYM NRMTQSQAQA ASRLALKAQA TNKCGLGLDL KVRTQKGELG
MSPPGSKIPK APSGGAVEQK VGNTGGPPHT HGASRVPAGC PGPQPAPTQE LSLQVLDLQS
VKNGMPGVGL LARHATATKG VPATNPAPGK GTGSGLIGAS GATMPTDTSK SEKLASRAVA
PPTPASKRDC VKGSATPSGQ ESRTAPGEAR KAATLPEMSA GEESSSSDSD PDSASPPSTG
QNPSVSVQTS QDWKPTRSLI EHVFVTDVTA NLITVTVKES PTSVGFFNLR HY
