H1X_HUMAN
ID H1X_HUMAN Reviewed; 213 AA.
AC Q92522;
DT 15-JUL-1999, integrated into UniProtKB/Swiss-Prot.
DT 01-FEB-1997, sequence version 1.
DT 03-AUG-2022, entry version 192.
DE RecName: Full=Histone H1.10 {ECO:0000305};
DE AltName: Full=Histone H1x;
GN Name=H1-10 {ECO:0000312|HGNC:HGNC:4722};
GN Synonyms=H1FX {ECO:0000312|HGNC:HGNC:4722};
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].
RX PubMed=8964515; DOI=10.1016/0378-1119(96)00020-0;
RA Yamamoto T., Horikoshi M.;
RT "Cloning of the cDNA encoding a novel subtype of histone H1.";
RL Gene 173:281-285(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Lung;
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 PROTEIN SEQUENCE OF 2-19; 48-57; 76-86; 95-118 AND 128-143, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND IDENTIFICATION BY MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Calvo F., Kolch W.;
RL Submitted (FEB-2008) to UniProtKB.
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND IDENTIFICATION BY MASS
RP 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 [5]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17924679; DOI=10.1021/pr070152u;
RA Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
RT "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells
RT and high confident phosphopeptide identification by cross-validation of
RT MS/MS and MS/MS/MS spectra.";
RL J. Proteome Res. 6:4150-4162(2007).
RN [6]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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 [7]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [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 [8]
RP INTERACTION WITH RRP1B.
RX PubMed=19710015; DOI=10.1074/jbc.m109.023457;
RA Crawford N.P., Yang H., Mattaini K.R., Hunter K.W.;
RT "The metastasis efficiency modifier ribosomal RNA processing 1 homolog B
RT (RRP1B) is a chromatin-associated factor.";
RL J. Biol. Chem. 284:28660-28673(2009).
RN [9]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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 [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-47, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, AND IDENTIFICATION BY
RP 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 [12]
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 [13]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE SCALE
RP ANALYSIS] AT SER-2; SER-31 AND SER-33, CLEAVAGE OF INITIATOR METHIONINE
RP [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE
RP 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 [14]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22223895; DOI=10.1074/mcp.m111.015131;
RA Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T.,
RA Giglione C.;
RT "Comparative large-scale characterisation of plant vs. mammal proteins
RT reveals similar and idiosyncratic N-alpha acetylation features.";
RL Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012).
RN [15]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-2 AND SER-31, 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 PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-31, 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).
CC -!- FUNCTION: Histones H1 are necessary for the condensation of nucleosome
CC chains into higher-order structures.
CC -!- SUBUNIT: Interacts with RRP1B. {ECO:0000269|PubMed:19710015}.
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome.
CC -!- TISSUE SPECIFICITY: Expressed ubiquitously.
CC -!- PTM: Citrullination at Arg-62 (H1R54ci) by PADI4 takes place within the
CC DNA-binding site of H1 and results in its displacement from chromatin
CC and global chromatin decondensation, thereby promoting pluripotency and
CC stem cell maintenance. {ECO:0000250|UniProtKB:P43275}.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family. {ECO:0000255|PROSITE-
CC ProRule:PRU00837}.
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DR EMBL; D64142; BAA11018.1; -; mRNA.
DR EMBL; BC000426; AAH00426.1; -; mRNA.
DR EMBL; BC010435; AAH10435.1; -; mRNA.
DR CCDS; CCDS3057.1; -.
DR PIR; JC4928; JC4928.
DR RefSeq; NP_006017.1; NM_006026.3.
DR PDB; 2LSO; NMR; -; A=44-123.
DR PDB; 6L9Z; X-ray; 2.50 A; S=1-213.
DR PDB; 7K60; EM; 3.12 A; U=1-213.
DR PDB; 7K63; EM; 3.03 A; U=44-120.
DR PDBsum; 2LSO; -.
DR PDBsum; 6L9Z; -.
DR PDBsum; 7K60; -.
DR PDBsum; 7K63; -.
DR AlphaFoldDB; Q92522; -.
DR BMRB; Q92522; -.
DR SMR; Q92522; -.
DR BioGRID; 114461; 176.
DR CORUM; Q92522; -.
DR DIP; DIP-36358N; -.
DR IntAct; Q92522; 94.
DR MINT; Q92522; -.
DR STRING; 9606.ENSP00000329662; -.
DR GlyGen; Q92522; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q92522; -.
DR MetOSite; Q92522; -.
DR PhosphoSitePlus; Q92522; -.
DR SwissPalm; Q92522; -.
DR BioMuta; H1FX; -.
DR DMDM; 6016184; -.
DR EPD; Q92522; -.
DR jPOST; Q92522; -.
DR MassIVE; Q92522; -.
DR MaxQB; Q92522; -.
DR PaxDb; Q92522; -.
DR PeptideAtlas; Q92522; -.
DR PRIDE; Q92522; -.
DR ProteomicsDB; 75281; -.
DR TopDownProteomics; Q92522; -.
DR Antibodypedia; 33244; 103 antibodies from 23 providers.
DR DNASU; 8971; -.
DR Ensembl; ENST00000333762.6; ENSP00000329662.4; ENSG00000184897.6.
DR GeneID; 8971; -.
DR KEGG; hsa:8971; -.
DR MANE-Select; ENST00000333762.6; ENSP00000329662.4; NM_006026.4; NP_006017.1.
DR UCSC; uc003elx.3; human.
DR CTD; 8971; -.
DR DisGeNET; 8971; -.
DR GeneCards; H1-10; -.
DR HGNC; HGNC:4722; H1-10.
DR HPA; ENSG00000184897; Tissue enriched (bone).
DR MIM; 602785; gene.
DR neXtProt; NX_Q92522; -.
DR OpenTargets; ENSG00000184897; -.
DR VEuPathDB; HostDB:ENSG00000184897; -.
DR eggNOG; KOG4012; Eukaryota.
DR GeneTree; ENSGT00730000111536; -.
DR HOGENOM; CLU_102232_0_0_1; -.
DR InParanoid; Q92522; -.
DR OMA; HKKGATT; -.
DR OrthoDB; 1565299at2759; -.
DR PhylomeDB; Q92522; -.
DR TreeFam; TF313664; -.
DR PathwayCommons; Q92522; -.
DR SignaLink; Q92522; -.
DR BioGRID-ORCS; 8971; 10 hits in 1079 CRISPR screens.
DR ChiTaRS; H1FX; human.
DR GeneWiki; H1FX; -.
DR GenomeRNAi; 8971; -.
DR Pharos; Q92522; Tbio.
DR PRO; PR:Q92522; -.
DR Proteomes; UP000005640; Chromosome 3.
DR RNAct; Q92522; protein.
DR Bgee; ENSG00000184897; Expressed in ventricular zone and 187 other tissues.
DR Genevisible; Q92522; HS.
DR GO; GO:0005730; C:nucleolus; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0045296; F:cadherin binding; HDA:BHF-UCL.
DR GO; GO:0003690; F:double-stranded DNA binding; IBA:GO_Central.
DR GO; GO:0031492; F:nucleosomal DNA binding; IBA:GO_Central.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR GO; GO:0030261; P:chromosome condensation; IBA:GO_Central.
DR GO; GO:0045910; P:negative regulation of DNA recombination; IBA:GO_Central.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR CDD; cd00073; H15; 1.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005819; H1/H5.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR036388; WH-like_DNA-bd_sf.
DR InterPro; IPR036390; WH_DNA-bd_sf.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR SUPFAM; SSF46785; SSF46785; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Chromosome; Citrullination;
KW Direct protein sequencing; DNA-binding; Nucleus; Phosphoprotein;
KW Reference proteome.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895"
FT CHAIN 2..213
FT /note="Histone H1.10"
FT /id="PRO_0000195912"
FT DOMAIN 44..118
FT /note="H15"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00837"
FT REGION 22..49
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 107..213
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 152..175
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 189..213
FT /note="Basic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 2
FT /note="N-acetylserine"
FT /evidence="ECO:0000269|Ref.3, ECO:0007744|PubMed:19413330,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:22223895"
FT MOD_RES 2
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:17081983,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163"
FT MOD_RES 31
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 33
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21406692"
FT MOD_RES 47
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 62
FT /note="Citrulline"
FT /evidence="ECO:0000250|UniProtKB:P43275"
FT HELIX 47..58
FT /evidence="ECO:0007829|PDB:6L9Z"
FT HELIX 67..74
FT /evidence="ECO:0007829|PDB:6L9Z"
FT TURN 82..84
FT /evidence="ECO:0007829|PDB:6L9Z"
FT HELIX 85..98
FT /evidence="ECO:0007829|PDB:6L9Z"
FT STRAND 101..105
FT /evidence="ECO:0007829|PDB:2LSO"
FT TURN 108..111
FT /evidence="ECO:0007829|PDB:6L9Z"
FT STRAND 112..116
FT /evidence="ECO:0007829|PDB:7K63"
FT TURN 120..122
FT /evidence="ECO:0007829|PDB:2LSO"
SQ SEQUENCE 213 AA; 22487 MW; 11548D85C5448FF2 CRC64;
MSVELEEALP VTTAEGMAKK VTKAGGSAAL SPSKKRKNSK KKNQPGKYSQ LVVETIRRLG
ERNGSSLAKI YTEAKKVPWF DQQNGRTYLK YSIKALVQND TLLQVKGTGA NGSFKLNRKK
LEGGGERRGA PAAATAPAPT AHKAKKAAPG AAGSRRADKK PARGQKPEQR SHKKGAGAKK
DKGGKAKKTA AAGGKKVKKA AKPSVPKVPK GRK
