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Histone H1.0 (Histone H1') (Histone H1(0)) [Cleaved into: Histone H1.0, N-terminally processed]

 H10_HUMAN               Reviewed;         194 AA.
P07305; B2R6I0; B4DRD6; Q6FG88; Q8N6R3;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 3.
25-OCT-2017, entry version 175.
RecName: Full=Histone H1.0;
AltName: Full=Histone H1';
AltName: Full=Histone H1(0);
Contains:
RecName: Full=Histone H1.0, N-terminally processed;
Name=H1F0; Synonyms=H1FV;
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] (ISOFORM 1).
PubMed=3084796; DOI=10.1016/0022-2836(86)90446-8;
Doenecke D., Tonjes R.;
"Differential distribution of lysine and arginine residues in the
closely related histones H1 and H5. Analysis of a human H1 gene.";
J. Mol. Biol. 187:461-464(1986).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
PubMed=15461802; DOI=10.1186/gb-2004-5-10-r84;
Collins J.E., Wright C.L., Edwards C.A., Davis M.P., Grinham J.A.,
Cole C.G., Goward M.E., Aguado B., Mallya M., Mokrab Y., Huckle E.J.,
Beare D.M., Dunham I.;
"A genome annotation-driven approach to cloning the human ORFeome.";
Genome Biol. 5:R84.1-R84.11(2004).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
TISSUE=Brain;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=10591208; DOI=10.1038/990031;
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M.,
Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K.,
Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P.,
Bird C.P., Blakey S.E., Bridgeman A.M., Buck D., Burgess J.,
Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G.,
Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R.,
Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E.,
Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G.,
Evans K.L., Fey J.M., Fleming K., French L., Garner A.A.,
Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C.,
Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S.,
Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A.,
Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M.,
Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T.,
Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J.,
Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T.,
Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T.,
Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L.,
Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M.,
Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L.,
Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L.,
Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N.,
Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J.,
Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S.,
Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T.,
Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I.,
Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H.,
Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L.,
Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z.,
Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P.,
Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S.,
Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J.,
Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T.,
Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J.,
Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R.,
Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S.,
Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E.,
Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P.,
Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E.,
O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X.,
Khan A.S., Lane L., Tilahun Y., Wright H.;
"The DNA sequence of human chromosome 22.";
Nature 402:489-495(1999).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
[7]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Colon, and Placenta;
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).
[8]
PARTIAL PROTEIN SEQUENCE (RNA EDITED VERSION), IDENTIFICATION BY MASS
SPECTROMETRY, RNA EDITING, SUBCELLULAR LOCATION, AND INDUCTION.
PubMed=18993075; DOI=10.1016/j.cub.2008.09.059;
Zougman A., Ziolkowski P., Mann M., Wisniewski J.R.;
"Evidence for insertional RNA editing in humans.";
Curr. Biol. 18:1760-1765(2008).
[9]
ACETYLATION AT THR-2, CLEAVAGE OF INITIATOR METHIONINE, AND
DEAMIDATION AT ASN-4.
PubMed=9582379; DOI=10.1074/jbc.273.21.13324;
Lindner H., Sarg B., Hoertnagl B., Helliger W.;
"The microheterogeneity of the mammalian H1(0) histone. Evidence for
an age-dependent deamidation.";
J. Biol. Chem. 273:13324-13330(1998).
[10]
ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-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).
[11]
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).
[12]
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).
[13]
ADP-RIBOSYLATION AT SER-104.
PubMed=27723750; DOI=10.1038/nchembio.2180;
Leidecker O., Bonfiglio J.J., Colby T., Zhang Q., Atanassov I.,
Zaja R., Palazzo L., Stockum A., Ahel I., Matic I.;
"Serine is a new target residue for endogenous ADP-ribosylation on
histones.";
Nat. Chem. Biol. 12:998-1000(2016).
-!- FUNCTION: Histones H1 are necessary for the condensation of
nucleosome chains into higher-order structures. The H1F0 histones
are found in cells that are in terminal stages of differentiation
or that have low rates of cell division.
-!- INTERACTION:
P04014:E1 (xeno); NbExp=2; IntAct=EBI-725224, EBI-7014446;
Q8IYW5:RNF168; NbExp=2; IntAct=EBI-725224, EBI-914207;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000255|PROSITE-
ProRule:PRU00837, ECO:0000269|PubMed:18993075}. Chromosome
{ECO:0000255|PROSITE-ProRule:PRU00837,
ECO:0000269|PubMed:18993075}. Note=The RNA edited version has been
localized to nuclear speckles. During mitosis, it appears in the
vicinity of condensed chromosomes.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P07305-1; Sequence=Displayed;
Name=2;
IsoId=P07305-2; Sequence=VSP_042163;
-!- INDUCTION: Both the unedited and the RNA edited versions are
induced by butyrate (at protein level). Only RNA edited version is
induced by DTT, vinblastine or TNF (at protein level).
{ECO:0000269|PubMed:18993075}.
-!- PTM: Phosphorylated on Ser-17 in RNA edited version.
{ECO:0000269|PubMed:18993075}.
-!- PTM: ADP-ribosylated on Ser-104 in response to DNA damage.
{ECO:0000269|PubMed:27723750}.
-!- RNA EDITING: Modified_positions=Not_applicable; Note=Partially
edited. In approximately 3.6% of the mRNA molecules, a new
initiator methionine is created by a single uridine insertion in
the 5'-UTR, causing an N-terminal extension of 99 amino acids. The
existence of the RNA edited version is supported by direct protein
sequencing by MS/MS of the following peptides specific to that
version: 12-21; 22-33; 37-47; 48-67; 68-83; 84-94 and 97-113. The
RNA edited version is called ET-H1.0.
{ECO:0000269|PubMed:18993075};
-!- SIMILARITY: Belongs to the histone H1/H5 family.
{ECO:0000255|PROSITE-ProRule:PRU00837}.
-!- WEB RESOURCE: Name=Wikipedia; Note=Histone H1 entry;
URL="https://en.wikipedia.org/wiki/Histone_H1";
-----------------------------------------------------------------------
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EMBL; X03473; CAA27190.1; -; Genomic_DNA.
EMBL; CR456502; CAG30388.1; -; mRNA.
EMBL; CR542220; CAG47016.1; -; mRNA.
EMBL; AK299209; BAG61248.1; -; mRNA.
EMBL; AK312583; BAG35477.1; -; mRNA.
EMBL; Z97630; CAB42829.1; -; Genomic_DNA.
EMBL; CH471095; EAW60188.1; -; Genomic_DNA.
EMBL; BC000145; AAH00145.1; -; mRNA.
EMBL; BC029046; AAH29046.1; -; mRNA.
CCDS; CCDS13956.1; -. [P07305-1]
PIR; A24850; HSHU10.
RefSeq; NP_005309.1; NM_005318.3. [P07305-1]
UniGene; Hs.745024; -.
ProteinModelPortal; P07305; -.
SMR; P07305; -.
BioGrid; 109260; 31.
DIP; DIP-41775N; -.
ELM; P07305; -.
IntAct; P07305; 12.
MINT; MINT-276185; -.
STRING; 9606.ENSP00000344504; -.
BindingDB; P07305; -.
ChEMBL; CHEMBL3707465; -.
iPTMnet; P07305; -.
PhosphoSitePlus; P07305; -.
BioMuta; H1F0; -.
DMDM; 121897; -.
EPD; P07305; -.
MaxQB; P07305; -.
PaxDb; P07305; -.
PeptideAtlas; P07305; -.
PRIDE; P07305; -.
TopDownProteomics; P07305-1; -. [P07305-1]
DNASU; 3005; -.
Ensembl; ENST00000340857; ENSP00000344504; ENSG00000189060. [P07305-1]
GeneID; 3005; -.
KEGG; hsa:3005; -.
UCSC; uc003aty.4; human. [P07305-1]
CTD; 3005; -.
DisGeNET; 3005; -.
EuPathDB; HostDB:ENSG00000189060.5; -.
GeneCards; H1F0; -.
H-InvDB; HIX0016454; -.
HGNC; HGNC:4714; H1F0.
HPA; HPA000843; -.
MIM; 142708; gene.
neXtProt; NX_P07305; -.
OpenTargets; ENSG00000189060; -.
PharmGKB; PA29092; -.
eggNOG; KOG4012; Eukaryota.
eggNOG; ENOG4112541; LUCA.
GeneTree; ENSGT00810000125570; -.
HOGENOM; HOG000251627; -.
HOVERGEN; HBG069502; -.
InParanoid; P07305; -.
KO; K11275; -.
OMA; FEQPKGP; -.
OrthoDB; EOG091G0LIU; -.
PhylomeDB; P07305; -.
TreeFam; TF313664; -.
Reactome; R-HSA-211227; Activation of DNA fragmentation factor.
Reactome; R-HSA-2559584; Formation of Senescence-Associated Heterochromatin Foci (SAHF).
ChiTaRS; H1F0; human.
GenomeRNAi; 3005; -.
PRO; PR:P07305; -.
Proteomes; UP000005640; Chromosome 22.
Bgee; ENSG00000189060; -.
CleanEx; HS_H1F0; -.
Genevisible; P07305; HS.
GO; GO:0015629; C:actin cytoskeleton; IDA:HPA.
GO; GO:0005794; C:Golgi apparatus; IDA:HPA.
GO; GO:0016604; C:nuclear body; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; IDA:UniProtKB.
GO; GO:0005719; C:nuclear euchromatin; IDA:UniProtKB.
GO; GO:0005654; C:nucleoplasm; TAS:Reactome.
GO; GO:0000786; C:nucleosome; IEA:InterPro.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0003680; F:AT DNA binding; IEA:Ensembl.
GO; GO:0031490; F:chromatin DNA binding; IDA:UniProtKB.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0006309; P:apoptotic DNA fragmentation; TAS:Reactome.
GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
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;
Acetylation; ADP-ribosylation; Alternative splicing; Chromosome;
Citrullination; Complete proteome; Direct protein sequencing;
DNA-binding; Nucleus; Phosphoprotein; Reference proteome; RNA editing.
CHAIN 1 194 Histone H1.0.
/FTId=PRO_0000423207.
INIT_MET 1 1 Removed; alternate.
{ECO:0000244|PubMed:19413330,
ECO:0000269|PubMed:9582379}.
CHAIN 2 194 Histone H1.0, N-terminally processed.
/FTId=PRO_0000195904.
DOMAIN 24 97 H15. {ECO:0000255|PROSITE-
ProRule:PRU00837}.
MOD_RES 1 1 N-acetylmethionine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 2 2 N-acetylthreonine; partial; in Histone
H1.0, N-terminally processed.
{ECO:0000244|PubMed:19413330,
ECO:0000269|PubMed:9582379}.
MOD_RES 4 4 Deamidated asparagine; partial.
{ECO:0000269|PubMed:9582379}.
MOD_RES 42 42 Citrulline.
{ECO:0000250|UniProtKB:P43275}.
MOD_RES 104 104 ADP-ribosylserine.
{ECO:0000269|PubMed:27723750}.
VAR_SEQ 3 19 Missing (in isoform 2).
{ECO:0000303|PubMed:14702039}.
/FTId=VSP_042163.
VARIANT 1 1 M -> MLGKGRQRRRRQRQRQSPVPRPSDRPAGLGLAKPAR
RALPTPEPGRKSSDSSLASPGAALQTGPVVRGSGADPEAGF
AQPPTRAGPLEGAFNSRTRQATM (in RNA edited
version).
/FTId=VAR_054789.
CONFLICT 65 65 D -> H (in Ref. 7; AAH29046).
{ECO:0000305}.
SEQUENCE 194 AA; 20863 MW; 03ED6F01919F8BE1 CRC64;
MTENSTSAPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI QKYIKSHYKV
GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKSDE PKKSVAFKKT KKEIKKVATP
KKASKPKKAA SKAPTKKPKA TPVKKAKKKL AATPKKAKKP KTVKAKPVKA SKPKKAKPVK
PKAKSSAKRA GKKK


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3623BP-50 Histone H3 Blocking Peptide target: Histone H3 50 μg
3624BP-50 Histone H4 Blocking Peptide target: Histone H4 50 μg
3622BP-50 Histone H2B Blocking Peptide target: Histone H2B 50 μg


 

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