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Histone H1.5 (Histone H1a) (Histone H1b) (Histone H1s-3)

 H15_HUMAN               Reviewed;         226 AA.
P16401; Q14529; Q3MJ42;
01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
12-SEP-2018, entry version 172.
RecName: Full=Histone H1.5;
AltName: Full=Histone H1a;
AltName: Full=Histone H1b;
AltName: Full=Histone H1s-3;
Name=HIST1H1B; Synonyms=H1F5;
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], AND TISSUE SPECIFICITY.
PubMed=9031620; DOI=10.1016/S0378-1119(96)00582-3;
Albig W., Meergans T., Doenecke D.;
"Characterization of the H1.5 gene completes the set of human H1
subtype genes.";
Gene 184:141-148(1997).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=12408966; DOI=10.1006/geno.2002.6850;
Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
"The human and mouse replication-dependent histone genes.";
Genomics 80:487-498(2002).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=14574404; DOI=10.1038/nature02055;
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Liver;
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).
[5]
PROTEIN SEQUENCE OF 2-226.
TISSUE=Spleen;
PubMed=2613692; DOI=10.1093/oxfordjournals.jbchem.a122941;
Ohe Y., Hayashi H., Iwai K.;
"Human spleen histone H1. Isolation and amino acid sequences of three
minor variants, H1a, H1c, and H1d.";
J. Biochem. 106:844-857(1989).
[6]
PROTEIN SEQUENCE OF 2-17; 37-49; 58-78 AND 89-100, CLEAVAGE OF
INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
SPECTROMETRY.
TISSUE=Ovarian carcinoma;
Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
Submitted (DEC-2008) to UniProtKB.
[7]
SUBCELLULAR LOCATION.
PubMed=10997781; DOI=10.1023/A:1009262819961;
Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A.;
"The distribution of somatic H1 subtypes is non-random on active vs.
inactive chromatin: distribution in human fetal fibroblasts.";
Chromosome Res. 8:405-424(2000).
[8]
SUBCELLULAR LOCATION.
PubMed=11746507; DOI=10.1002/jcb.1224;
Parseghian M.H., Newcomb R.L., Hamkalo B.A.;
"Distribution of somatic H1 subtypes is non-random on active vs.
inactive chromatin II: distribution in human adult fibroblasts.";
J. Cell. Biochem. 83:643-659(2001).
[9]
SUBCELLULAR LOCATION.
PubMed=15911621; DOI=10.1074/jbc.M501627200;
Th'ng J.P., Sung R., Ye M., Hendzel M.J.;
"H1 family histones in the nucleus. Control of binding and
localization by the C-terminal domain.";
J. Biol. Chem. 280:27809-27814(2005).
[10]
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).
[11]
PHOSPHORYLATION AT THR-11; SER-18; THR-138; THR-155; SER-173 AND
SER-189.
PubMed=16377619; DOI=10.1074/jbc.M508957200;
Sarg B., Helliger W., Talasz H., Forg B., Lindner H.H.;
"Histone H1 phosphorylation occurs site-specifically during interphase
and mitosis: identification of a novel phosphorylation site on histone
H1.";
J. Biol. Chem. 281:6573-6580(2006).
[12]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11; SER-18 AND THR-39,
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).
[13]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND 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).
[14]
PHOSPHORYLATION AT THR-11 BY GSK3B.
PubMed=19136008; DOI=10.1016/j.jmb.2008.12.047;
Happel N., Stoldt S., Schmidt B., Doenecke D.;
"M phase-specific phosphorylation of histone H1.5 at threonine 10 by
GSK-3.";
J. Mol. Biol. 386:339-350(2009).
[15]
METHYLATION AT LYS-27.
PubMed=19552482; DOI=10.1021/pr9000652;
Lu A., Zougman A., Pudelko M., Bebenek M., Ziolkowski P., Mann M.,
Wisniewski J.R.;
"Mapping of lysine monomethylation of linker histones in human breast
and its cancer.";
J. Proteome Res. 8:4207-4215(2009).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND 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]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-168, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[18]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-18 AND THR-138, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
SCALE ANALYSIS] AT SER-2; SER-18 AND THR-138, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], 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).
[21]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22223895; DOI=10.1074/mcp.M111.015131;
Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C.,
Meinnel T., Giglione C.;
"Comparative large-scale characterisation of plant vs. mammal proteins
reveals similar and idiosyncratic N-alpha acetylation features.";
Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=22814378; DOI=10.1073/pnas.1210303109;
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
Aldabe R.;
"N-terminal acetylome analyses and functional insights of the N-
terminal acetyltransferase NatB.";
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
[23]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-11 AND SER-18, 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).
[24]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[25]
ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
VARIANT [LARGE SCALE ANALYSIS] ASP-86.
PubMed=16959974; DOI=10.1126/science.1133427;
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S.,
Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J.,
Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C.,
Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N.,
Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal
cancers.";
Science 314:268-274(2006).
-!- FUNCTION: Histone H1 protein binds to linker DNA between
nucleosomes forming the macromolecular structure known as the
chromatin fiber. Histones H1 are necessary for the condensation of
nucleosome chains into higher-order structured fibers. Acts also
as a regulator of individual gene transcription through chromatin
remodeling, nucleosome spacing and DNA methylation (By
similarity). {ECO:0000250}.
-!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=According to
PubMed:15911621 more commonly found in heterochromatin. According
to PubMed:10997781 associates with actively transcribed chromatin
and not heterochromatin.
-!- TISSUE SPECIFICITY: Ubiquitous. Expressed in the majority of the
cell lines tested and in testis. {ECO:0000269|PubMed:9031620}.
-!- DOMAIN: The C-terminal domain is required for high-affinity
binding to chromatin. {ECO:0000250}.
-!- PTM: H1 histones are progressively phosphorylated during the cell
cycle, becoming maximally phosphorylated during late G2 phase and
M phase, and being dephosphorylated sharply thereafter (By
similarity). Phosphorylated at Thr-11 by GSK3B during mitosis in
prometaphase and dephosphorylated in telophase. {ECO:0000250,
ECO:0000269|PubMed:16377619, ECO:0000269|PubMed:19136008}.
-!- PTM: Citrullination at Arg-57 (H1R54ci) by PADI4 takes place
within the DNA-binding site of H1 and results in its displacement
from chromatin and global chromatin decondensation, thereby
promoting pluripotency and stem cell maintenance.
{ECO:0000250|UniProtKB:P43276}.
-!- SIMILARITY: Belongs to the histone H1/H5 family.
{ECO:0000255|PROSITE-ProRule:PRU00837}.
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EMBL; X83509; CAA58498.1; -; Genomic_DNA.
EMBL; AF531304; AAN06704.1; -; Genomic_DNA.
EMBL; Z98744; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC069101; AAH69101.1; -; mRNA.
EMBL; BC101581; AAI01582.1; -; mRNA.
EMBL; BC101583; AAI01584.1; -; mRNA.
CCDS; CCDS4635.1; -.
PIR; S51660; S51660.
RefSeq; NP_005313.1; NM_005322.2.
UniGene; Hs.131956; -.
PDB; 2FE2; Model; -; A=2-226.
PDB; 2RHI; X-ray; 1.66 A; B=23-27.
PDBsum; 2FE2; -.
PDBsum; 2RHI; -.
ProteinModelPortal; P16401; -.
SMR; P16401; -.
BioGrid; 109264; 67.
IntAct; P16401; 15.
MINT; P16401; -.
STRING; 9606.ENSP00000330074; -.
iPTMnet; P16401; -.
PhosphoSitePlus; P16401; -.
SwissPalm; P16401; -.
BioMuta; HIST1H1B; -.
DMDM; 19856407; -.
EPD; P16401; -.
MaxQB; P16401; -.
PaxDb; P16401; -.
PeptideAtlas; P16401; -.
PRIDE; P16401; -.
ProteomicsDB; 53351; -.
TopDownProteomics; P16401; -.
DNASU; 3009; -.
Ensembl; ENST00000331442; ENSP00000330074; ENSG00000184357.
GeneID; 3009; -.
KEGG; hsa:3009; -.
UCSC; uc003njx.4; human.
CTD; 3009; -.
DisGeNET; 3009; -.
EuPathDB; HostDB:ENSG00000184357.4; -.
GeneCards; HIST1H1B; -.
HGNC; HGNC:4719; HIST1H1B.
HPA; CAB012241; -.
HPA; HPA055907; -.
MIM; 142711; gene.
neXtProt; NX_P16401; -.
OpenTargets; ENSG00000184357; -.
PharmGKB; PA29097; -.
eggNOG; KOG4012; Eukaryota.
eggNOG; ENOG4112541; LUCA.
GeneTree; ENSGT00670000097781; -.
HOGENOM; HOG000251627; -.
HOVERGEN; HBG009035; -.
InParanoid; P16401; -.
KO; K11275; -.
OMA; ECITAHP; -.
OrthoDB; EOG091G0XGD; -.
PhylomeDB; P16401; -.
TreeFam; TF313664; -.
Reactome; R-HSA-211227; Activation of DNA fragmentation factor.
Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
SIGNOR; P16401; -.
EvolutionaryTrace; P16401; -.
GeneWiki; HIST1H1B; -.
GenomeRNAi; 3009; -.
PRO; PR:P16401; -.
Proteomes; UP000005640; Chromosome 6.
Bgee; ENSG00000184357; Expressed in 48 organ(s), highest expression level in lung.
CleanEx; HS_HIST1H1B; -.
Genevisible; P16401; HS.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005720; C:nuclear heterochromatin; IDA:UniProtKB.
GO; GO:0000786; C:nucleosome; IEA:InterPro.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0031490; F:chromatin DNA binding; IMP:UniProtKB.
GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB.
GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
GO; GO:0006325; P:chromatin organization; IMP:UniProtKB.
GO; GO:0071169; P:establishment of protein localization to chromatin; IMP:UniProtKB.
GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IMP:UniProtKB.
GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
GO; GO:0030307; P:positive regulation of cell growth; IMP:UniProtKB.
GO; GO:0051574; P:positive regulation of histone H3-K9 methylation; IMP:UniProtKB.
GO; GO:0050821; P:protein stabilization; IMP:UniProtKB.
CDD; cd00073; H15; 1.
Gene3D; 1.10.10.10; -; 1.
InterPro; IPR005818; Histone_H1/H5_H15.
InterPro; IPR005819; Histone_H5.
InterPro; IPR036388; WH-like_DNA-bd_sf.
InterPro; IPR036390; WH_DNA-bd_sf.
Pfam; PF00538; Linker_histone; 1.
PRINTS; PR00624; HISTONEH5.
SMART; SM00526; H15; 1.
SUPFAM; SSF46785; SSF46785; 1.
PROSITE; PS51504; H15; 1.
1: Evidence at protein level;
3D-structure; Acetylation; Chromosome; Citrullination;
Complete proteome; Direct protein sequencing; DNA-binding;
Hydroxylation; Methylation; Nucleus; Phosphoprotein; Polymorphism;
Reference proteome.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|PubMed:2613692,
ECO:0000269|Ref.6}.
CHAIN 2 226 Histone H1.5.
/FTId=PRO_0000195909.
DOMAIN 39 112 H15. {ECO:0000255|PROSITE-
ProRule:PRU00837}.
MOD_RES 2 2 N-acetylserine; partial.
{ECO:0000244|PubMed:19413330,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:22223895,
ECO:0000244|PubMed:22814378,
ECO:0000244|PubMed:25944712,
ECO:0000269|Ref.6}.
MOD_RES 2 2 Phosphoserine.
{ECO:0000244|PubMed:21406692}.
MOD_RES 11 11 Phosphothreonine; by GSK3.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163,
ECO:0000269|PubMed:16377619,
ECO:0000269|PubMed:19136008}.
MOD_RES 17 17 N6-acetyllysine.
{ECO:0000250|UniProtKB:P43276}.
MOD_RES 18 18 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:19690332,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569,
ECO:0000269|PubMed:16377619}.
MOD_RES 27 27 N6-methyllysine.
{ECO:0000269|PubMed:19552482}.
MOD_RES 37 37 N6-(beta-hydroxybutyryl)lysine;
alternate.
{ECO:0000250|UniProtKB:P43277}.
MOD_RES 37 37 N6-succinyllysine; alternate.
{ECO:0000250|UniProtKB:P43276}.
MOD_RES 39 39 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 49 49 N6-acetyllysine.
{ECO:0000250|UniProtKB:P43276}.
MOD_RES 55 55 N6-(beta-hydroxybutyryl)lysine.
{ECO:0000250|UniProtKB:P43277}.
MOD_RES 57 57 Citrulline.
{ECO:0000250|UniProtKB:P43276}.
MOD_RES 67 67 N6-(beta-hydroxybutyryl)lysine.
{ECO:0000250|UniProtKB:P43277}.
MOD_RES 78 78 N6-acetyllysine.
{ECO:0000250|UniProtKB:P43276}.
MOD_RES 88 88 N6-(beta-hydroxybutyryl)lysine.
{ECO:0000250|UniProtKB:P43277}.
MOD_RES 93 93 N6-(beta-hydroxybutyryl)lysine.
{ECO:0000250|UniProtKB:P43277}.
MOD_RES 109 109 N6-(beta-hydroxybutyryl)lysine.
{ECO:0000250|UniProtKB:P43277}.
MOD_RES 138 138 Phosphothreonine.
{ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000269|PubMed:16377619}.
MOD_RES 155 155 Phosphothreonine.
{ECO:0000269|PubMed:16377619}.
MOD_RES 168 168 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 173 173 Phosphoserine.
{ECO:0000269|PubMed:16377619}.
MOD_RES 189 189 Phosphoserine.
{ECO:0000269|PubMed:16377619}.
VARIANT 86 86 G -> D (in a colorectal cancer sample;
somatic mutation).
{ECO:0000269|PubMed:16959974}.
/FTId=VAR_036204.
VARIANT 144 144 K -> R (in dbSNP:rs11970638).
/FTId=VAR_049308.
VARIANT 211 211 A -> T (in dbSNP:rs34144478).
/FTId=VAR_049309.
CONFLICT 216 218 Missing (in Ref. 5; AA sequence).
{ECO:0000305}.
SEQUENCE 226 AA; 22580 MW; 0BA1402101766FDF CRC64;
MSETAPAETA TPAPVEKSPA KKKATKKAAG AGAAKRKATG PPVSELITKA VAASKERNGL
SLAALKKALA AGGYDVEKNN SRIKLGLKSL VSKGTLVQTK GTGASGSFKL NKKAASGEAK
PKAKKAGAAK AKKPAGATPK KAKKAAGAKK AVKKTPKKAK KPAAAGVKKV AKSPKKAKAA
AKPKKATKSP AKPKAVKPKA AKPKAAKPKA AKPKAAKAKK AAAKKK


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