Full text data of HIST1H1C
HIST1H1C
(H1F2)
[Confidence: low (only semi-automatic identification from reviews)]
Histone H1.2 (Histone H1c; Histone H1d; Histone H1s-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histone H1.2 (Histone H1c; Histone H1d; Histone H1s-1)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
P16403
ID H12_HUMAN Reviewed; 213 AA.
AC P16403; A8K4I2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Histone H1.2;
DE AltName: Full=Histone H1c;
DE AltName: Full=Histone H1d;
DE AltName: Full=Histone H1s-1;
GN Name=HIST1H1C; Synonyms=H1F2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2759094;
RA Eick S., Nicolai M., Mumberg D., Doenecke D.;
RT "Human H1 histones: conserved and varied sequence elements in two H1
RT subtype genes.";
RL Eur. J. Cell Biol. 49:110-115(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-213.
RC TISSUE=Spleen;
RX PubMed=2613692;
RA Ohe Y., Hayashi H., Iwai K.;
RT "Human spleen histone H1. Isolation and amino acid sequences of three
RT minor variants, H1a, H1c, and H1d.";
RL J. Biochem. 106:844-857(1989).
RN [9]
RP PROTEIN SEQUENCE OF 2-17; 34-46; 55-75 AND 86-97, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT LYS-34, AND
RP MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 2-17; 34-46; 55-63 AND 65-75, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [11]
RP NOMENCLATURE.
RX PubMed=8003976; DOI=10.1002/pro.5560030406;
RA Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A.;
RT "A proposal for a coherent mammalian histone H1 nomenclature
RT correlated with amino acid sequences.";
RL Protein Sci. 3:575-587(1994).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=10997781; DOI=10.1023/A:1009262819961;
RA Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A.;
RT "The distribution of somatic H1 subtypes is non-random on active vs.
RT inactive chromatin: distribution in human fetal fibroblasts.";
RL Chromosome Res. 8:405-424(2000).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=15911621; DOI=10.1074/jbc.M501627200;
RA Th'ng J.P., Sung R., Ye M., Hendzel M.J.;
RT "H1 family histones in the nucleus. Control of binding and
RT localization by the C-terminal domain.";
RL J. Biol. Chem. 280:27809-27814(2005).
RN [14]
RP IDENTIFICATION BY MASS 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [16]
RP IDENTIFICATION BY 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP METHYLATION AT LYS-187 BY EHMT1 AND EHMT2, MUTAGENESIS OF LYS-187, AND
RP MASS SPECTROMETRY.
RX PubMed=20334638; DOI=10.1186/1756-8935-3-7;
RA Weiss T., Hergeth S., Zeissler U., Izzo A., Tropberger P., Zee B.M.,
RA Dundr M., Garcia B.A., Daujat S., Schneider R.;
RT "Histone H1 variant-specific lysine methylation by G9a/KMT1C and
RT Glp1/KMT1D.";
RL Epigenetics Chromatin 3:7-7(2010).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2 AND THR-146, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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.,
RA Buerckstuemmer T., 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 [21]
RP CROTONYLATION AT LYS-34; LYS-64; LYS-85; LYS-90; LYS-97; LYS-159 AND
RP LYS-168.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation
RT as a new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Histone H1 protein binds to linker DNA between
CC nucleosomes forming the macromolecular structure known as the
CC chromatin fiber. Histones H1 are necessary for the condensation of
CC nucleosome chains into higher-order structured fibers. Acts also
CC as a regulator of individual gene transcription through chromatin
CC remodeling, nucleosome spacing and DNA methylation (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes
CC in euchromatin. Distribution goes in parallel with DNA
CC concentration.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity
CC binding to chromatin (By similarity).
CC -!- PTM: H1 histones are progressively phosphorylated during the cell
CC cycle, becoming maximally phosphorylated during late G2 phase and
CC M phase, and being dephosphorylated sharply thereafter (By
CC similarity).
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC cells and marks testis-specific genes in post-meiotic cells,
CC including X-linked genes that escape sex chromosome inactivation
CC in haploid cells. Crotonylation marks active promoters and
CC enhancers and confers resistance to transcriptional repressors. It
CC is also associated with post-meiotically activated genes on
CC autosomes.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
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DR EMBL; X57129; CAA40408.1; -; Genomic_DNA.
DR EMBL; AF531300; AAN06700.1; -; Genomic_DNA.
DR EMBL; AK290947; BAF83636.1; -; mRNA.
DR EMBL; AB451259; BAG70073.1; -; mRNA.
DR EMBL; AB451385; BAG70199.1; -; mRNA.
DR EMBL; U91328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55515.1; -; Genomic_DNA.
DR EMBL; BC002649; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S26364; HSHU11.
DR RefSeq; NP_005310.1; NM_005319.3.
DR UniGene; Hs.7644; -.
DR ProteinModelPortal; P16403; -.
DR SMR; P16403; 36-109.
DR IntAct; P16403; 20.
DR MINT; MINT-1149485; -.
DR STRING; 9606.ENSP00000339566; -.
DR PhosphoSite; P16403; -.
DR DMDM; 417101; -.
DR PaxDb; P16403; -.
DR PeptideAtlas; P16403; -.
DR PRIDE; P16403; -.
DR DNASU; 3006; -.
DR Ensembl; ENST00000343677; ENSP00000339566; ENSG00000187837.
DR GeneID; 3006; -.
DR KEGG; hsa:3006; -.
DR UCSC; uc003nfw.3; human.
DR CTD; 3006; -.
DR GeneCards; GC06M026055; -.
DR HGNC; HGNC:4716; HIST1H1C.
DR HPA; CAB011507; -.
DR MIM; 142710; gene.
DR neXtProt; NX_P16403; -.
DR PharmGKB; PA29094; -.
DR eggNOG; NOG258621; -.
DR HOGENOM; HOG000251627; -.
DR HOVERGEN; HBG009035; -.
DR InParanoid; P16403; -.
DR KO; K11275; -.
DR OMA; MSETAPX; -.
DR OrthoDB; EOG74TX2T; -.
DR PhylomeDB; P16403; -.
DR Reactome; REACT_578; Apoptosis.
DR GeneWiki; HIST1H1C; -.
DR GenomeRNAi; 3006; -.
DR NextBio; 11920; -.
DR PRO; PR:P16403; -.
DR Bgee; P16403; -.
DR CleanEx; HS_HIST1H1C; -.
DR Genevestigator; P16403; -.
DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR005819; Histone_H5.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Complete proteome; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 213 Histone H1.2.
FT /FTId=PRO_0000195906.
FT DOMAIN 36 109 H15.
FT MOD_RES 2 2 N-acetylserine; partial.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 34 34 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 34 34 N6-methyllysine; alternate.
FT MOD_RES 64 64 N6-crotonyl-L-lysine.
FT MOD_RES 85 85 N6-crotonyl-L-lysine.
FT MOD_RES 90 90 N6-crotonyl-L-lysine.
FT MOD_RES 97 97 N6-crotonyl-L-lysine.
FT MOD_RES 104 104 Phosphoserine; by PKC (By similarity).
FT MOD_RES 146 146 Phosphothreonine.
FT MOD_RES 159 159 N6-crotonyl-L-lysine.
FT MOD_RES 168 168 N6-crotonyl-L-lysine.
FT MOD_RES 187 187 N6-methyllysine; by EHMT1 and EHMT2.
FT CROSSLNK 17 17 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 206 206 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 18 18 A -> V (in dbSNP:rs2230653).
FT /FTId=VAR_003618.
FT VARIANT 113 113 S -> A (in dbSNP:rs34810376).
FT /FTId=VAR_049304.
FT VARIANT 124 124 G -> A (in dbSNP:rs12111009).
FT /FTId=VAR_049305.
FT MUTAGEN 187 187 K->R: Abolishes methylation.
SQ SEQUENCE 213 AA; 21365 MW; AA66EA1901D8D56B CRC64;
MSETAPAAPA AAPPAEKAPV KKKAAKKAGG TPRKASGPPV SELITKAVAA SKERSGVSLA
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKV
KKAGGTKPKK PVGAAKKPKK AAGGATPKKS AKKTPKKAKK PAAATVTKKV AKSPKKAKVA
KPKKAAKSAA KAVKPKAAKP KVVKPKKAAP KKK
//
ID H12_HUMAN Reviewed; 213 AA.
AC P16403; A8K4I2;
DT 01-AUG-1990, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 2.
DT 22-JAN-2014, entry version 142.
DE RecName: Full=Histone H1.2;
DE AltName: Full=Histone H1c;
DE AltName: Full=Histone H1d;
DE AltName: Full=Histone H1s-1;
GN Name=HIST1H1C; Synonyms=H1F2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2759094;
RA Eick S., Nicolai M., Mumberg D., Doenecke D.;
RT "Human H1 histones: conserved and varied sequence elements in two H1
RT subtype genes.";
RL Eur. J. Cell Biol. 49:110-115(1989).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=12408966; DOI=10.1016/S0888-7543(02)96850-3;
RA Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.;
RT "The human and mouse replication-dependent histone genes.";
RL Genomics 80:487-498(2002).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=19054851; DOI=10.1038/nmeth.1273;
RA Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R.,
RA Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y.,
RA Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.,
RA Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H.,
RA Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M.,
RA Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T.,
RA Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A.,
RA Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K.,
RA Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S.,
RA Isogai T., Imai J., Watanabe S., Nomura N.;
RT "Human protein factory for converting the transcriptome into an in
RT vitro-expressed proteome.";
RL Nat. Methods 5:1011-1017(2008).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E.,
RA Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R.,
RA Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S.,
RA Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J.,
RA Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P.,
RA Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E.,
RA Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A.,
RA Frankland J., French L., Garner P., Garnett J., Ghori M.J.,
RA Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M.,
RA Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S.,
RA Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R.,
RA Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E.,
RA Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A.,
RA Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C.,
RA Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M.,
RA Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K.,
RA McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T.,
RA Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R.,
RA Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W.,
RA Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M.,
RA Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L.,
RA Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J.,
RA Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B.,
RA Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L.,
RA Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W.,
RA Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A.,
RA Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [8]
RP PROTEIN SEQUENCE OF 2-213.
RC TISSUE=Spleen;
RX PubMed=2613692;
RA Ohe Y., Hayashi H., Iwai K.;
RT "Human spleen histone H1. Isolation and amino acid sequences of three
RT minor variants, H1a, H1c, and H1d.";
RL J. Biochem. 106:844-857(1989).
RN [9]
RP PROTEIN SEQUENCE OF 2-17; 34-46; 55-75 AND 86-97, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, METHYLATION AT LYS-34, AND
RP MASS SPECTROMETRY.
RC TISSUE=Ovarian carcinoma;
RA Bienvenut W.V., Lilla S., von Kriegsheim A., Lempens A., Kolch W.;
RL Submitted (DEC-2008) to UniProtKB.
RN [10]
RP PROTEIN SEQUENCE OF 2-17; 34-46; 55-63 AND 65-75, CLEAVAGE OF
RP INITIATOR METHIONINE, ACETYLATION AT SER-2, AND MASS SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [11]
RP NOMENCLATURE.
RX PubMed=8003976; DOI=10.1002/pro.5560030406;
RA Parseghian M.H., Henschen A.H., Krieglstein K.G., Hamkalo B.A.;
RT "A proposal for a coherent mammalian histone H1 nomenclature
RT correlated with amino acid sequences.";
RL Protein Sci. 3:575-587(1994).
RN [12]
RP SUBCELLULAR LOCATION.
RX PubMed=10997781; DOI=10.1023/A:1009262819961;
RA Parseghian M.H., Newcomb R.L., Winokur S.T., Hamkalo B.A.;
RT "The distribution of somatic H1 subtypes is non-random on active vs.
RT inactive chromatin: distribution in human fetal fibroblasts.";
RL Chromosome Res. 8:405-424(2000).
RN [13]
RP SUBCELLULAR LOCATION.
RX PubMed=15911621; DOI=10.1074/jbc.M501627200;
RA Th'ng J.P., Sung R., Ye M., Hendzel M.J.;
RT "H1 family histones in the nucleus. Control of binding and
RT localization by the C-terminal domain.";
RL J. Biol. Chem. 280:27809-27814(2005).
RN [14]
RP IDENTIFICATION BY MASS 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.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [15]
RP UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-206, AND MASS
RP SPECTROMETRY.
RC TISSUE=Mammary cancer;
RX PubMed=17370265; DOI=10.1002/pmic.200600410;
RA Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.;
RT "Tryptic digestion of ubiquitin standards reveals an improved strategy
RT for identifying ubiquitinated proteins by mass spectrometry.";
RL Proteomics 7:868-874(2007).
RN [16]
RP IDENTIFICATION BY 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 [17]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [18]
RP METHYLATION AT LYS-187 BY EHMT1 AND EHMT2, MUTAGENESIS OF LYS-187, AND
RP MASS SPECTROMETRY.
RX PubMed=20334638; DOI=10.1186/1756-8935-3-7;
RA Weiss T., Hergeth S., Zeissler U., Izzo A., Tropberger P., Zee B.M.,
RA Dundr M., Garcia B.A., Daujat S., Schneider R.;
RT "Histone H1 variant-specific lysine methylation by G9a/KMT1C and
RT Glp1/KMT1D.";
RL Epigenetics Chromatin 3:7-7(2010).
RN [19]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2 AND THR-146, AND MASS SPECTROMETRY.
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.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [20]
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.,
RA Buerckstuemmer T., 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 [21]
RP CROTONYLATION AT LYS-34; LYS-64; LYS-85; LYS-90; LYS-97; LYS-159 AND
RP LYS-168.
RX PubMed=21925322; DOI=10.1016/j.cell.2011.08.008;
RA Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T.,
RA Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q.,
RA Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.;
RT "Identification of 67 histone marks and histone lysine crotonylation
RT as a new type of histone modification.";
RL Cell 146:1016-1028(2011).
RN [22]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, PHOSPHORYLATION [LARGE
RP SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [23]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT SER-2, AND MASS SPECTROMETRY.
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E.,
RA Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K.,
RA Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-
RT terminal acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
CC -!- FUNCTION: Histone H1 protein binds to linker DNA between
CC nucleosomes forming the macromolecular structure known as the
CC chromatin fiber. Histones H1 are necessary for the condensation of
CC nucleosome chains into higher-order structured fibers. Acts also
CC as a regulator of individual gene transcription through chromatin
CC remodeling, nucleosome spacing and DNA methylation (By
CC similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus. Chromosome. Note=Mainly localizes
CC in euchromatin. Distribution goes in parallel with DNA
CC concentration.
CC -!- DOMAIN: The C-terminal domain is required for high-affinity
CC binding to chromatin (By similarity).
CC -!- PTM: H1 histones are progressively phosphorylated during the cell
CC cycle, becoming maximally phosphorylated during late G2 phase and
CC M phase, and being dephosphorylated sharply thereafter (By
CC similarity).
CC -!- PTM: Crotonylation (Kcr) is specifically present in male germ
CC cells and marks testis-specific genes in post-meiotic cells,
CC including X-linked genes that escape sex chromosome inactivation
CC in haploid cells. Crotonylation marks active promoters and
CC enhancers and confers resistance to transcriptional repressors. It
CC is also associated with post-meiotically activated genes on
CC autosomes.
CC -!- SIMILARITY: Belongs to the histone H1/H5 family.
CC -!- SIMILARITY: Contains 1 H15 (linker histone H1/H5 globular) domain.
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DR EMBL; X57129; CAA40408.1; -; Genomic_DNA.
DR EMBL; AF531300; AAN06700.1; -; Genomic_DNA.
DR EMBL; AK290947; BAF83636.1; -; mRNA.
DR EMBL; AB451259; BAG70073.1; -; mRNA.
DR EMBL; AB451385; BAG70199.1; -; mRNA.
DR EMBL; U91328; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471087; EAW55515.1; -; Genomic_DNA.
DR EMBL; BC002649; -; NOT_ANNOTATED_CDS; mRNA.
DR PIR; S26364; HSHU11.
DR RefSeq; NP_005310.1; NM_005319.3.
DR UniGene; Hs.7644; -.
DR ProteinModelPortal; P16403; -.
DR SMR; P16403; 36-109.
DR IntAct; P16403; 20.
DR MINT; MINT-1149485; -.
DR STRING; 9606.ENSP00000339566; -.
DR PhosphoSite; P16403; -.
DR DMDM; 417101; -.
DR PaxDb; P16403; -.
DR PeptideAtlas; P16403; -.
DR PRIDE; P16403; -.
DR DNASU; 3006; -.
DR Ensembl; ENST00000343677; ENSP00000339566; ENSG00000187837.
DR GeneID; 3006; -.
DR KEGG; hsa:3006; -.
DR UCSC; uc003nfw.3; human.
DR CTD; 3006; -.
DR GeneCards; GC06M026055; -.
DR HGNC; HGNC:4716; HIST1H1C.
DR HPA; CAB011507; -.
DR MIM; 142710; gene.
DR neXtProt; NX_P16403; -.
DR PharmGKB; PA29094; -.
DR eggNOG; NOG258621; -.
DR HOGENOM; HOG000251627; -.
DR HOVERGEN; HBG009035; -.
DR InParanoid; P16403; -.
DR KO; K11275; -.
DR OMA; MSETAPX; -.
DR OrthoDB; EOG74TX2T; -.
DR PhylomeDB; P16403; -.
DR Reactome; REACT_578; Apoptosis.
DR GeneWiki; HIST1H1C; -.
DR GenomeRNAi; 3006; -.
DR NextBio; 11920; -.
DR PRO; PR:P16403; -.
DR Bgee; P16403; -.
DR CleanEx; HS_HIST1H1C; -.
DR Genevestigator; P16403; -.
DR GO; GO:0000786; C:nucleosome; NAS:UniProtKB.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; NAS:UniProtKB.
DR GO; GO:0006334; P:nucleosome assembly; NAS:UniProtKB.
DR Gene3D; 1.10.10.10; -; 1.
DR InterPro; IPR005818; Histone_H1/H5_H15.
DR InterPro; IPR005819; Histone_H5.
DR InterPro; IPR011991; WHTH_DNA-bd_dom.
DR Pfam; PF00538; Linker_histone; 1.
DR PRINTS; PR00624; HISTONEH5.
DR SMART; SM00526; H15; 1.
DR PROSITE; PS51504; H15; 1.
PE 1: Evidence at protein level;
KW Acetylation; Chromosome; Complete proteome; Direct protein sequencing;
KW DNA-binding; Isopeptide bond; Methylation; Nucleus; Phosphoprotein;
KW Polymorphism; Reference proteome; Ubl conjugation.
FT INIT_MET 1 1 Removed.
FT CHAIN 2 213 Histone H1.2.
FT /FTId=PRO_0000195906.
FT DOMAIN 36 109 H15.
FT MOD_RES 2 2 N-acetylserine; partial.
FT MOD_RES 2 2 Phosphoserine.
FT MOD_RES 34 34 N6-crotonyl-L-lysine; alternate.
FT MOD_RES 34 34 N6-methyllysine; alternate.
FT MOD_RES 64 64 N6-crotonyl-L-lysine.
FT MOD_RES 85 85 N6-crotonyl-L-lysine.
FT MOD_RES 90 90 N6-crotonyl-L-lysine.
FT MOD_RES 97 97 N6-crotonyl-L-lysine.
FT MOD_RES 104 104 Phosphoserine; by PKC (By similarity).
FT MOD_RES 146 146 Phosphothreonine.
FT MOD_RES 159 159 N6-crotonyl-L-lysine.
FT MOD_RES 168 168 N6-crotonyl-L-lysine.
FT MOD_RES 187 187 N6-methyllysine; by EHMT1 and EHMT2.
FT CROSSLNK 17 17 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT CROSSLNK 206 206 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin).
FT VARIANT 18 18 A -> V (in dbSNP:rs2230653).
FT /FTId=VAR_003618.
FT VARIANT 113 113 S -> A (in dbSNP:rs34810376).
FT /FTId=VAR_049304.
FT VARIANT 124 124 G -> A (in dbSNP:rs12111009).
FT /FTId=VAR_049305.
FT MUTAGEN 187 187 K->R: Abolishes methylation.
SQ SEQUENCE 213 AA; 21365 MW; AA66EA1901D8D56B CRC64;
MSETAPAAPA AAPPAEKAPV KKKAAKKAGG TPRKASGPPV SELITKAVAA SKERSGVSLA
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKV
KKAGGTKPKK PVGAAKKPKK AAGGATPKKS AKKTPKKAKK PAAATVTKKV AKSPKKAKVA
KPKKAAKSAA KAVKPKAAKP KVVKPKKAAP KKK
//
MIM
142710
*RECORD*
*FIELD* NO
142710
*FIELD* TI
*142710 HISTONE GENE CLUSTER 1, H1 HISTONE FAMILY, MEMBER C; HIST1H1C
;;HISTONE GENE CLUSTER 1, H1C;;
read moreHIST1 CLUSTER, H1C;;
H1C;;
H1.2;;
H1 HISTONE FAMILY, MEMBER 2, FORMERLY; H1F2; FORMERLY
*FIELD* TX
For background information on histones, histone gene clusters, and the
H1 histone family, see HIST1H1A (142709).
CLONING
Eick et al. (1989) cloned the genes encoding H1.2 and H1.1 (HIST1H1A;
142709).
GENE FUNCTION
Several reports described an activity that modifies
nitrotyrosine-containing proteins and their immunoreactivity to
antibodies against nitrotyrosine (e.g., Kamisaki et al., 1998). Without
knowing the product of the reaction, this activity has been called a
'denitrase.' These studies used some nonspecific proteins that have
multiple tyrosine residues, e.g., albumin, as substrate to study the
mechanism of the reaction. Irie et al. (2003) developed an assay
strategy for determining the substrate for denitrase combining 2D-gel
electrophoresis and an on-blot enzyme assay. They found that histone
H1.2, an isoform protein of linker histone, was one such substrate. H1.2
has only 1 tyrosine residue in the entire molecule, which ensured the
exact position of the substrate to be involved. It had been reported
that histones are the most prominent nitrated proteins in cancer
tissues. It was also demonstrated that tyrosine nitration of histone H1
occurs in vivo. Conceiving that H1.2 might be an intrinsic substrate for
denitrase, they performed further experiments demonstrating that the
denitrase activity behaves as an enzymatic activity because the reaction
was time-dependent and was destroyed by heat or trypsin treatment. The
activity was shown to be specific for histone H1.2, to differ from
proteasome activity, and to require no additional cofactors.
Konishi et al. (2003) found that histone H1.2 was a cytochrome
c-releasing factor that appeared in the cytoplasm after exposure of
cells to x-ray irradiation. While all nuclear histone H1 forms were
released into the cytoplasm in a p53 (TP53; 191170)-dependent manner
after irradiation, only H1.2 induced cytochrome c release from isolated
mitochondria in a BAK (BAK1; 600516)-dependent manner. Reducing H1.2
expression enhanced cellular resistance to apoptosis induced by x-ray
irradiation or etoposide, but not that induced by other apoptotic
stimuli. Thymocytes and small intestines of H1.2-deficient mice
exhibited increased cellular resistance to x-ray-induced apoptosis.
Konishi et al. (2003) concluded that histone H1.2 has a role in
transmitting apoptotic signals from the nucleus to the mitochondria
following DNA double-strand breaks.
See HIST1H1A (142709) for additional functional information on H1
histones.
MAPPING
By PCR analysis of chromosomal DNA from a panel of human/rodent somatic
cell hybrids and by fluorescence in situ hybridization, Albig et al.
(1993) demonstrated that 6 human histone H1 genes, including H1.2, are
located on chromosome 6p22.2-p21.1. By analysis of a YAC contig, Albig
et al. (1997) mapped the H1.2 gene to chromosome 6p21.3 within a cluster
of 35 histone genes, including H1.1 to H1.4 (HIST1H1E; 142220) and H1T
(HIST1H1T; 142712). The H1.5 gene (HIST1H1B; 142711) is part of a
separate subcluster within the same chromosomal region.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 6p22-p21, which they called histone
gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H1C.
*FIELD* RF
1. Albig, W.; Drabent, B.; Kunz, J.; Kalff-Suske, M.; Grzeschik, K.-H.;
Doenecke, D.: All known human H1 histone genes except the H1(0) gene
are clustered on chromosome 6. Genomics 16: 649-654, 1993.
2. Albig, W.; Kioschis, P.; Poustka, A.; Meergans, K.; Doenecke, D.
: Human histone gene organization: nonregular arrangement within a
large cluster. Genomics 40: 314-322, 1997.
3. Eick, S.; Nicolai, M.; Mumberg, D.; Doenecke, D.: Human H1 histones:
conserved and varied sequence elements in two H1 subtype genes. Europ.
J. Cell Biol. 49: 110-115, 1989.
4. Irie, Y.; Saeki, M.; Kamisaki, Y.; Martin, E.; Murad, F.: Histone
H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine
immunoreactivity in proteins. Proc. Nat. Acad. Sci. 100: 5634-5639,
2003.
5. Kamisaki, Y.; Wada, K.; Bian, K.; Balabanli, B.; Davis, K.; Martin,
E.; Behbod, F.; Lee, Y.-C.; Murad, F.: An activity in rat tissues
that modifies nitrotyrosine-containing proteins. Proc. Nat. Acad.
Sci. 95: 11584-11589, 1998.
6. Konishi, A.; Shimizu, S.; Hirota, J.; Takao, T.; Fan, Y.; Matsuoka,
Y.; Zhang, L.; Yoneda, Y.; Fujii, Y.; Skoultchi, A. I.; Tsujimoto,
Y.: Involvement of histone H1.2 in apoptosis induced by DNA double-strand
breaks. Cell 114: 673-688, 2003.
7. 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.
*FIELD* CN
Matthew B. Gross - updated: 06/24/2010
Patricia A. Hartz - updated: 5/3/2006
Victor A. McKusick - updated: 6/19/2003
Rebekah S. Rasooly - updated: 7/8/1998
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
mgross: 06/24/2010
mgross: 5/26/2010
mgross: 6/7/2006
terry: 5/3/2006
alopez: 6/24/2003
terry: 6/19/2003
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/9/1998
alopez: 7/8/1998
alopez: 2/11/1998
mark: 9/22/1996
carol: 6/28/1993
carol: 6/25/1993
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 9/15/1989
*RECORD*
*FIELD* NO
142710
*FIELD* TI
*142710 HISTONE GENE CLUSTER 1, H1 HISTONE FAMILY, MEMBER C; HIST1H1C
;;HISTONE GENE CLUSTER 1, H1C;;
read moreHIST1 CLUSTER, H1C;;
H1C;;
H1.2;;
H1 HISTONE FAMILY, MEMBER 2, FORMERLY; H1F2; FORMERLY
*FIELD* TX
For background information on histones, histone gene clusters, and the
H1 histone family, see HIST1H1A (142709).
CLONING
Eick et al. (1989) cloned the genes encoding H1.2 and H1.1 (HIST1H1A;
142709).
GENE FUNCTION
Several reports described an activity that modifies
nitrotyrosine-containing proteins and their immunoreactivity to
antibodies against nitrotyrosine (e.g., Kamisaki et al., 1998). Without
knowing the product of the reaction, this activity has been called a
'denitrase.' These studies used some nonspecific proteins that have
multiple tyrosine residues, e.g., albumin, as substrate to study the
mechanism of the reaction. Irie et al. (2003) developed an assay
strategy for determining the substrate for denitrase combining 2D-gel
electrophoresis and an on-blot enzyme assay. They found that histone
H1.2, an isoform protein of linker histone, was one such substrate. H1.2
has only 1 tyrosine residue in the entire molecule, which ensured the
exact position of the substrate to be involved. It had been reported
that histones are the most prominent nitrated proteins in cancer
tissues. It was also demonstrated that tyrosine nitration of histone H1
occurs in vivo. Conceiving that H1.2 might be an intrinsic substrate for
denitrase, they performed further experiments demonstrating that the
denitrase activity behaves as an enzymatic activity because the reaction
was time-dependent and was destroyed by heat or trypsin treatment. The
activity was shown to be specific for histone H1.2, to differ from
proteasome activity, and to require no additional cofactors.
Konishi et al. (2003) found that histone H1.2 was a cytochrome
c-releasing factor that appeared in the cytoplasm after exposure of
cells to x-ray irradiation. While all nuclear histone H1 forms were
released into the cytoplasm in a p53 (TP53; 191170)-dependent manner
after irradiation, only H1.2 induced cytochrome c release from isolated
mitochondria in a BAK (BAK1; 600516)-dependent manner. Reducing H1.2
expression enhanced cellular resistance to apoptosis induced by x-ray
irradiation or etoposide, but not that induced by other apoptotic
stimuli. Thymocytes and small intestines of H1.2-deficient mice
exhibited increased cellular resistance to x-ray-induced apoptosis.
Konishi et al. (2003) concluded that histone H1.2 has a role in
transmitting apoptotic signals from the nucleus to the mitochondria
following DNA double-strand breaks.
See HIST1H1A (142709) for additional functional information on H1
histones.
MAPPING
By PCR analysis of chromosomal DNA from a panel of human/rodent somatic
cell hybrids and by fluorescence in situ hybridization, Albig et al.
(1993) demonstrated that 6 human histone H1 genes, including H1.2, are
located on chromosome 6p22.2-p21.1. By analysis of a YAC contig, Albig
et al. (1997) mapped the H1.2 gene to chromosome 6p21.3 within a cluster
of 35 histone genes, including H1.1 to H1.4 (HIST1H1E; 142220) and H1T
(HIST1H1T; 142712). The H1.5 gene (HIST1H1B; 142711) is part of a
separate subcluster within the same chromosomal region.
By genomic sequence analysis, Marzluff et al. (2002) determined that the
histone gene cluster on chromosome 6p22-p21, which they called histone
gene cluster-1 (HIST1), contains 55 histone genes, including HIST1H1C.
*FIELD* RF
1. Albig, W.; Drabent, B.; Kunz, J.; Kalff-Suske, M.; Grzeschik, K.-H.;
Doenecke, D.: All known human H1 histone genes except the H1(0) gene
are clustered on chromosome 6. Genomics 16: 649-654, 1993.
2. Albig, W.; Kioschis, P.; Poustka, A.; Meergans, K.; Doenecke, D.
: Human histone gene organization: nonregular arrangement within a
large cluster. Genomics 40: 314-322, 1997.
3. Eick, S.; Nicolai, M.; Mumberg, D.; Doenecke, D.: Human H1 histones:
conserved and varied sequence elements in two H1 subtype genes. Europ.
J. Cell Biol. 49: 110-115, 1989.
4. Irie, Y.; Saeki, M.; Kamisaki, Y.; Martin, E.; Murad, F.: Histone
H1.2 is a substrate for denitrase, an activity that reduces nitrotyrosine
immunoreactivity in proteins. Proc. Nat. Acad. Sci. 100: 5634-5639,
2003.
5. Kamisaki, Y.; Wada, K.; Bian, K.; Balabanli, B.; Davis, K.; Martin,
E.; Behbod, F.; Lee, Y.-C.; Murad, F.: An activity in rat tissues
that modifies nitrotyrosine-containing proteins. Proc. Nat. Acad.
Sci. 95: 11584-11589, 1998.
6. Konishi, A.; Shimizu, S.; Hirota, J.; Takao, T.; Fan, Y.; Matsuoka,
Y.; Zhang, L.; Yoneda, Y.; Fujii, Y.; Skoultchi, A. I.; Tsujimoto,
Y.: Involvement of histone H1.2 in apoptosis induced by DNA double-strand
breaks. Cell 114: 673-688, 2003.
7. 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.
*FIELD* CN
Matthew B. Gross - updated: 06/24/2010
Patricia A. Hartz - updated: 5/3/2006
Victor A. McKusick - updated: 6/19/2003
Rebekah S. Rasooly - updated: 7/8/1998
*FIELD* CD
Victor A. McKusick: 6/4/1986
*FIELD* ED
mgross: 06/24/2010
mgross: 5/26/2010
mgross: 6/7/2006
terry: 5/3/2006
alopez: 6/24/2003
terry: 6/19/2003
tkritzer: 3/31/2003
alopez: 8/26/1998
alopez: 7/9/1998
alopez: 7/8/1998
alopez: 2/11/1998
mark: 9/22/1996
carol: 6/28/1993
carol: 6/25/1993
supermim: 3/16/1992
supermim: 3/20/1990
ddp: 10/27/1989
root: 9/15/1989