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Chromatin assembly factor 1 subunit A (CAF-1 subunit A) (Chromatin assembly factor I p150 subunit) (CAF-I 150 kDa subunit) (CAF-I p150) (hp150)

 CAF1A_HUMAN             Reviewed;         956 AA.
Q13111; Q6NXG5; Q7Z7K3; Q9UJY8;
18-OCT-2001, integrated into UniProtKB/Swiss-Prot.
28-MAR-2018, sequence version 3.
12-SEP-2018, entry version 175.
RecName: Full=Chromatin assembly factor 1 subunit A;
Short=CAF-1 subunit A;
AltName: Full=Chromatin assembly factor I p150 subunit;
Short=CAF-I 150 kDa subunit;
Short=CAF-I p150;
Short=hp150;
Name=CHAF1A; Synonyms=CAF, CAF1P150;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2
AND 3), AND VARIANT VAL-923.
PubMed=11250073; DOI=10.1016/S0378-1119(01)00335-3;
Dong H., Lin W., Zhang C.-K., Xiong H., Fu G., Jin W.-R., Chen R.,
Chen Z., Qi Z.-T., Huang G.M.;
"Genomic sequence and expression analyses of human chromatin assembly
factor 1 p150 gene.";
Gene 264:187-196(2001).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15057824; DOI=10.1038/nature02399;
Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J.,
Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M.,
Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E.,
Caenepeel S., Carrano A.V., Caoile C., Chan Y.M., Christensen M.,
Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C.,
Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M.,
Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T.,
Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H.,
Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S.,
Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J.,
Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M.,
Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J.,
Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D.,
Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A.,
Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I.,
Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E.,
Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M.,
Rubin E.M., Lucas S.M.;
"The DNA sequence and biology of human chromosome 19.";
Nature 428:529-535(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Brain, and Ovary;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[4]
NUCLEOTIDE SEQUENCE [MRNA] OF 6-956 (ISOFORM 1), AND VARIANT VAL-923.
TISSUE=Cervix adenocarcinoma;
PubMed=7600578; DOI=10.1016/S0092-8674(05)80015-7;
Kaufman P.D., Kobayashi R., Kessler N., Stillman B.;
"The p150 and p60 subunits of chromatin assembly factor I: a molecular
link between newly synthesized histones and DNA replication.";
Cell 81:1105-1114(1995).
[5]
INTERACTION WITH PCNA, AND SUBCELLULAR LOCATION.
PubMed=10052459; DOI=10.1016/S0092-8674(00)80661-3;
Shibahara K., Stillman B.;
"Replication-dependent marking of DNA by PCNA facilitates CAF-1-
coupled inheritance of chromatin.";
Cell 96:575-585(1999).
[6]
INTERACTION WITH PCNA.
PubMed=10648606; DOI=10.1128/MCB.20.4.1206-1218.2000;
Moggs J.G., Grandi P., Quivy J.P., Jonsson Z.O., Hubscher U.,
Becker P.B., Almouzni G.;
"A CAF-1-PCNA-mediated chromatin assembly pathway triggered by sensing
DNA damage.";
Mol. Cell. Biol. 20:1206-1218(2000).
[7]
REVIEW.
PubMed=10893180;
Ridgway P., Almouzni G.;
"CAF-1 and the inheritance of chromatin states: at the crossroads of
DNA replication and repair.";
J. Cell Sci. 113:2647-2658(2000).
[8]
HOMODIMERIZATION.
PubMed=11296234; DOI=10.1093/emboj/20.8.2015;
Quivy J.-P., Grandi P., Almouzni G.;
"Dimerization of the largest subunit of chromatin assembly factor 1:
importance in vitro and during Xenopus early development.";
EMBO J. 20:2015-2027(2001).
[9]
INTERACTION WITH MBD1.
PubMed=12697822; DOI=10.1128/MCB.23.9.3226-3236.2003;
Reese B.E., Bachman K.E., Baylin S.B., Rountree M.R.;
"The methyl-CpG binding protein MBD1 interacts with the p150 subunit
of chromatin assembly factor 1.";
Mol. Cell. Biol. 23:3226-3236(2003).
[10]
FUNCTION, AND INTERACTION WITH MBD1 AND SETDB1.
PubMed=15327775; DOI=10.1016/j.molcel.2004.06.043;
Sarraf S.A., Stancheva I.;
"Methyl-CpG binding protein MBD1 couples histone H3 methylation at
lysine 9 by SETDB1 to DNA replication and chromatin assembly.";
Mol. Cell 15:595-605(2004).
[11]
INTERACTION WITH CBX5.
PubMed=15882967; DOI=10.1016/j.bbrc.2005.04.016;
Lechner M.S., Schultz D.C., Negorev D., Maul G.G., Rauscher F.J. III;
"The mammalian heterochromatin protein 1 binds diverse nuclear
proteins through a common motif that targets the chromoshadow
domain.";
Biochem. Biophys. Res. Commun. 331:929-937(2005).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in
signaling networks.";
Cell 127:635-648(2006).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18220336; DOI=10.1021/pr0705441;
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D.,
Yates J.R. III;
"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for
efficient phosphoproteomic analysis.";
J. Proteome Res. 7:1346-1351(2008).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-224; THR-722; SER-772;
SER-775; SER-873 AND SER-951, AND IDENTIFICATION BY MASS SPECTROMETRY
[LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[15]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[16]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Leukemic T-cell;
PubMed=19690332; DOI=10.1126/scisignal.2000007;
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
Rodionov V., Han D.K.;
"Quantitative phosphoproteomic analysis of T cell receptor signaling
reveals system-wide modulation of protein-protein interactions.";
Sci. Signal. 2:RA46-RA46(2009).
[17]
INTERACTION WITH CBX5, AND MUTAGENESIS OF VAL-240 AND LEU-242.
PubMed=20562864; DOI=10.1038/ncb2075;
Nozawa R.S., Nagao K., Masuda H.T., Iwasaki O., Hirota T., Nozaki N.,
Kimura H., Obuse C.;
"Human POGZ modulates dissociation of HP1alpha from mitotic chromosome
arms through Aurora B activation.";
Nat. Cell Biol. 12:719-727(2010).
[18]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-123; SER-138; SER-141;
SER-143; SER-224; THR-722; SER-772; THR-865; SER-873 AND SER-951, AND
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
Mann M.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[19]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-65; SER-141; SER-143;
SER-206; THR-722; SER-772; SER-775 AND SER-951, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[20]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-141; SER-206; SER-310;
SER-772; SER-803; SER-868 AND SER-873, AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[21]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25218447; DOI=10.1038/nsmb.2890;
Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M.,
Vertegaal A.C.;
"Uncovering global SUMOylation signaling networks in a site-specific
manner.";
Nat. Struct. Mol. Biol. 21:927-936(2014).
[22]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[23]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-182, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
-!- FUNCTION: Core component of the CAF-1 complex, a complex thought
to mediate chromatin assembly in DNA replication and DNA repair.
Assembles histone octamers onto replicating DNA in vitro. CAF-1
performs the first step of the nucleosome assembly process,
bringing newly synthesized histones H3 and H4 to replicating DNA;
histones H2A/H2B can bind to this chromatin precursor subsequent
to DNA replication to complete the histone octamer. CHAF1A binds
to histones H3 and H4. It may play a role in heterochromatin
maintenance in proliferating cells by bringing newly synthesized
cbx proteins to heterochromatic DNA replication foci (By
similarity). {ECO:0000250, ECO:0000269|PubMed:15327775}.
-!- SUBUNIT: Homodimer. Part of the CAF-1 complex that contains RBBP4,
CHAF1B and CHAF1A. CHAF1A binds directly to CHAF1B. Only minor
amounts of RBBP4 are complexed with CHAF1A and CHAF1B in G1 phase.
CHAF1A binds directly to PCNA and to CBX1. Binds MBD1. Interacts
directly with CBX5 via the PxVxL motif. During DNA replication, it
forms a S phase-specific complex that facilitates DNA methylation
and histone H3 'Lys-9' methylation during replication-coupled
chromatin assembly and is at least composed of the CHAF1A, MBD1
and SETDB1. Interacts with CBX5. {ECO:0000269|PubMed:10052459,
ECO:0000269|PubMed:10648606, ECO:0000269|PubMed:12697822,
ECO:0000269|PubMed:15327775, ECO:0000269|PubMed:15882967,
ECO:0000269|PubMed:20562864}.
-!- INTERACTION:
Self; NbExp=3; IntAct=EBI-1020839, EBI-1020839;
P45973:CBX5; NbExp=7; IntAct=EBI-1020839, EBI-78219;
Q99684:GFI1; NbExp=4; IntAct=EBI-1020839, EBI-949368;
P84243:H3F3B; NbExp=2; IntAct=EBI-1020839, EBI-120658;
Q71DI3:HIST2H3A; NbExp=2; IntAct=EBI-1020839, EBI-750650;
Q9UIS9:MBD1; NbExp=3; IntAct=EBI-1020839, EBI-867196;
P16333:NCK1; NbExp=2; IntAct=EBI-1020839, EBI-389883;
P12004:PCNA; NbExp=4; IntAct=EBI-1020839, EBI-358311;
P27986:PIK3R1; NbExp=2; IntAct=EBI-1020839, EBI-79464;
Q04864:REL; NbExp=3; IntAct=EBI-1020839, EBI-307352;
P15884:TCF4; NbExp=3; IntAct=EBI-1020839, EBI-533224;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:10052459}.
Note=DNA replication foci.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Comment=Experimental confirmation may be lacking for some
isoforms.;
Name=1;
IsoId=Q13111-1; Sequence=Displayed;
Name=2;
IsoId=Q13111-2; Sequence=VSP_004149, VSP_004150;
Name=3;
IsoId=Q13111-3; Sequence=VSP_004151;
-!- DEVELOPMENTAL STAGE: Active complex is found in G1, S and G2
phases.
-!- DOMAIN: Contains one Pro-Xaa-Val-Xaa-Leu (PxVxL) motif, which is
required for interaction with chromoshadow domains. This motif
requires additional residues -7, -6, +4 and +5 of the central Val
which contact the chromoshadow domain.
-!- SIMILARITY: Belongs to the CHAF1A family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAA76736.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAF04291.1; Type=Erroneous initiation; Evidence={ECO:0000305};
Sequence=AAH52620.1; Type=Erroneous initiation; Note=Translation N-terminally extended.; Evidence={ECO:0000305};
Sequence=AAH52620.1; Type=Miscellaneous discrepancy; Note=Contaminating sequence. Potential poly-A sequence starting in position 426.; Evidence={ECO:0000305};
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EMBL; AF190465; AAF04291.1; ALT_INIT; Genomic_DNA.
EMBL; AC011498; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; KF459577; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC052620; AAH52620.1; ALT_SEQ; mRNA.
EMBL; BC067093; AAH67093.1; -; mRNA.
EMBL; U20979; AAA76736.1; ALT_INIT; mRNA.
CCDS; CCDS32875.1; -. [Q13111-1]
PIR; A56731; A56731.
RefSeq; NP_005474.2; NM_005483.2. [Q13111-1]
UniGene; Hs.79018; -.
ProteinModelPortal; Q13111; -.
SMR; Q13111; -.
BioGrid; 115349; 81.
ComplexPortal; CPX-569; Chromatin assembly factor 1 complex.
CORUM; Q13111; -.
DIP; DIP-31135N; -.
ELM; Q13111; -.
IntAct; Q13111; 53.
MINT; Q13111; -.
STRING; 9606.ENSP00000301280; -.
iPTMnet; Q13111; -.
PhosphoSitePlus; Q13111; -.
BioMuta; CHAF1A; -.
DMDM; 229462842; -.
EPD; Q13111; -.
MaxQB; Q13111; -.
PaxDb; Q13111; -.
PeptideAtlas; Q13111; -.
PRIDE; Q13111; -.
ProteomicsDB; 59160; -.
ProteomicsDB; 59161; -. [Q13111-2]
ProteomicsDB; 59162; -. [Q13111-3]
Ensembl; ENST00000301280; ENSP00000301280; ENSG00000167670. [Q13111-1]
GeneID; 10036; -.
KEGG; hsa:10036; -.
UCSC; uc002mal.4; human. [Q13111-1]
CTD; 10036; -.
DisGeNET; 10036; -.
EuPathDB; HostDB:ENSG00000167670.15; -.
GeneCards; CHAF1A; -.
HGNC; HGNC:1910; CHAF1A.
HPA; CAB015186; -.
MIM; 601246; gene.
neXtProt; NX_Q13111; -.
OpenTargets; ENSG00000167670; -.
PharmGKB; PA26446; -.
eggNOG; KOG4364; Eukaryota.
eggNOG; ENOG4111K9K; LUCA.
GeneTree; ENSGT00440000034888; -.
HOGENOM; HOG000111290; -.
HOVERGEN; HBG050779; -.
InParanoid; Q13111; -.
KO; K10750; -.
OrthoDB; EOG091G0VQK; -.
PhylomeDB; Q13111; -.
TreeFam; TF350377; -.
SIGNOR; Q13111; -.
ChiTaRS; CHAF1A; human.
GeneWiki; CHAF1A; -.
GenomeRNAi; 10036; -.
PMAP-CutDB; Q13111; -.
PRO; PR:Q13111; -.
Proteomes; UP000005640; Chromosome 19.
Bgee; ENSG00000167670; Expressed in 219 organ(s), highest expression level in secondary oocyte.
CleanEx; HS_CHAF1A; -.
ExpressionAtlas; Q13111; baseline and differential.
Genevisible; Q13111; HS.
GO; GO:0033186; C:CAF-1 complex; IDA:UniProtKB.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0032991; C:protein-containing complex; IDA:UniProtKB.
GO; GO:0003682; F:chromatin binding; TAS:ProtInc.
GO; GO:0070087; F:chromo shadow domain binding; IPI:BHF-UCL.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0051082; F:unfolded protein binding; TAS:ProtInc.
GO; GO:0007049; P:cell cycle; IEA:UniProtKB-KW.
GO; GO:0031497; P:chromatin assembly; IDA:UniProtKB.
GO; GO:0006281; P:DNA repair; IEA:UniProtKB-KW.
GO; GO:0006260; P:DNA replication; IEA:UniProtKB-KW.
GO; GO:0006335; P:DNA replication-dependent nucleosome assembly; IDA:UniProtKB.
InterPro; IPR029105; CAF1-p150_C2.
InterPro; IPR029091; CAF1_asu_N.
InterPro; IPR022043; CAF1A.
Pfam; PF15539; CAF1-p150_C2; 1.
Pfam; PF15557; CAF1-p150_N; 1.
Pfam; PF12253; CAF1A; 1.
1: Evidence at protein level;
Alternative splicing; Cell cycle; Chaperone; Complete proteome;
DNA damage; DNA repair; DNA replication; Isopeptide bond; Nucleus;
Phosphoprotein; Polymorphism; Reference proteome; Ubl conjugation.
CHAIN 1 956 Chromatin assembly factor 1 subunit A.
/FTId=PRO_0000089276.
REGION 1 314 Binds to CBX1 chromo shadow domain.
REGION 1 49 Binds to PCNA.
REGION 642 678 Necessary for homodimerization and
competence for chromatin assembly.
REGION 660 956 Binds to p60.
MOTIF 233 246 PxVxL motif.
COMPBIAS 323 453 Arg/Glu/Lys-rich.
COMPBIAS 602 608 Poly-Glu.
COMPBIAS 619 623 Poly-Asp.
COMPBIAS 905 911 Poly-Glu.
MOD_RES 65 65 Phosphoserine.
{ECO:0000244|PubMed:18220336,
ECO:0000244|PubMed:21406692}.
MOD_RES 123 123 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 138 138 Phosphoserine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 141 141 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 143 143 Phosphoserine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 206 206 Phosphoserine.
{ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 224 224 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231}.
MOD_RES 310 310 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 722 722 Phosphothreonine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
MOD_RES 772 772 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163}.
MOD_RES 775 775 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:21406692}.
MOD_RES 803 803 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 865 865 Phosphothreonine.
{ECO:0000244|PubMed:20068231}.
MOD_RES 868 868 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 873 873 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:23186163}.
MOD_RES 951 951 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692}.
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 182 182 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:25218447,
ECO:0000244|PubMed:28112733}.
VAR_SEQ 710 749 CFLETLPAQEEQTPKASKRERRDEQILAQLLPLLHGNVNG
-> HWVHPESRGDVCRTLRVSSPQSRYLNRLNSCVKSTLSC
FT (in isoform 2). {ECO:0000305}.
/FTId=VSP_004149.
VAR_SEQ 750 956 Missing (in isoform 2). {ECO:0000305}.
/FTId=VSP_004150.
VAR_SEQ 772 944 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_004151.
VARIANT 167 167 D -> V (in dbSNP:rs35651457).
/FTId=VAR_055329.
VARIANT 239 239 M -> V (in dbSNP:rs2230635).
/FTId=VAR_055330.
VARIANT 850 850 K -> R (in dbSNP:rs8100525).
/FTId=VAR_055331.
VARIANT 923 923 A -> V (in dbSNP:rs9352).
{ECO:0000269|PubMed:11250073,
ECO:0000269|PubMed:7600578}.
/FTId=VAR_055332.
VARIANT 950 950 A -> S (in dbSNP:rs243383).
/FTId=VAR_055333.
MUTAGEN 240 240 V->E: Abolishes interaction with CBX5;
when associated with E-242.
{ECO:0000269|PubMed:20562864}.
MUTAGEN 242 242 L->E: Abolishes interaction with CBX5;
when associated with E-240.
{ECO:0000269|PubMed:20562864}.
CONFLICT 775 775 S -> T (in Ref. 4; AAA76736).
{ECO:0000305}.
SEQUENCE 956 AA; 106910 MW; 90617F8FE8DB7FD0 CRC64;
MLEELECGAP GARGAATAMD CKDRPAFPVK KLIQARLPFK RLNLVPKGKA DDMSDDQGTS
VQSKSPDLEA SLDTLENNCH VGSDIDFRPK LVNGKGPLDN FLRNRIETSI GQSTVIIDLT
EDSNEQPDSL VDHNKLNSEA SPSREAINGQ REDTGDQQGL LKAIQNDKLA FPGETLSDIP
CKTEEEGVGC GGAGRRGDSQ ECSPRSCPEL TSGPRMCPRK EQDSWSEAGG ILFKGKVPMV
VLQDILAVRP PQIKSLPATP QGKNMTPESE VLESFPEEDS VLSHSSLSSP SSTSSPEGPP
APPKQHSSTS PFPTSTPLRR ITKKFVKGST EKNKLRLQRD QERLGKQLKL RAEREEKEKL
KEEAKRAKEE AKKKKEEEKE LKEKERREKR EKDEKEKAEK QRLKEERRKE RQEALEAKLE
EKRKKEEEKR LREEEKRIKA EKAEITRFFQ KPKTPQAPKT LAGSCGKFAP FEIKEHMVLA
PRRRTAFHPD LCSQLDQLLQ QQSGEFSFLK DLKGRQPLRS GPTHVSTRNA DIFNSDVVIV
ERGKGDGVPE RRKFGRMKLL QFCENHRPAY WGTWNKKTAL IRARDPWAQD TKLLDYEVDS
DEEWEEEEPG ESLSHSEGDD DDDMGEDEDE DDGFFVPHGY LSEDEGVTEE CADPENHKVR
QKLKAKEWDE FLAKGKRFRV LQPVKIGCVW AADRDCAGDD LKVLQQFAAC FLETLPAQEE
QTPKASKRER RDEQILAQLL PLLHGNVNGS KVIIREFQEH CRRGLLSNHT GSPRSPSTTY
LHTPTPSEDA AIPSKSRLKR LISENSVYEK RPDFRMCWYV HPQVLQSFQQ EHLPVPCQWS
YVTSVPSAPK EDSGSVPSTG PSQGTPISLK RKSAGSMCIT QFMKKRRHDG QIGAEDMDGF
QADTEEEEEE EGDCMIVDVP DAAEVQAPCG AASGAGGGVG VDTGKATLTA SPLGAS


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