P07305 (H10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H1.0

Alternative name(s):
Histone H1'
Histone H1(0)

Gene names

Name:	H1F0
Synonyms:	H1FV

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	194 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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.
Subcellular location	Nucleus. Chromosome. Note: The RNA edited version has been localized to nuclear speckles. During mitosis, it appears in the vicinity of condensed chromosomes. Ref.8
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). Ref.8
Post-translational modification	Phosphorylated upon DNA damage, probably by ATM or ATR. Phosphorylated on Ser-17 in RNA edited version. Ref.10 Ref.11 Ref.12
Sequence similarities	Belongs to the histone H1/H5 family. Contains 1 H15 (linker histone H1/H5 globular) domain.
RNA editing	Modified position: not applicable. 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. Ref.8

Ontologies

Keywords
Cellular component	Chromosome Nucleus
Coding sequence diversity	Alternative splicing RNA editing
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological process	DNA fragmentation involved in apoptotic nuclear change Traceable author statement. Source: Reactome nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	Golgi apparatus Inferred from direct assay. Source: HPA nucleoplasm Traceable author statement. Source: Reactome nucleosome Inferred from electronic annotation. Source: InterPro
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P07305-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

Isoform 2 (identifier: P07305-2)

The sequence of this isoform differs from the canonical sequence as follows:
     3-19: Missing.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed
	Chain	2 – 194	193	Histone H1.0		PRO_0000195904
Regions
	Domain	24 – 97	74	H15
Amino acid modifications
	Modified residue	2	1	N-acetylthreonine
	Modified residue	4	1	Deamidated asparagine; partial
	Modified residue	5	1	Phosphoserine Ref.12
	Modified residue	66	1	Phosphoserine Ref.11
	Modified residue	171	1	Phosphoserine Ref.10
Natural variations
	Alternative sequence	3 – 19	17	Missing in isoform 2.		VSP_042163
	Natural variant	1	1	M → MLGKGRQRRRRQRQRQSPVP RPSDRPAGLGLAKPARRALP TPEPGRKSSDSSLASPGAAL QTGPVVRGSGADPEAGFAQP PTRAGPLEGAFNSRTRQATM in RNA edited version.		VAR_054789
Experimental info
	Sequence conflict	65	1	D → H in AAH29046. Ref.7

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 03ED6F01919F8BE1	FASTA	194	20,863
	10 20 30 40 50 60 MTENSTSAPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI QKYIKSHYKV 70 80 90 100 110 120 GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKSDE PKKSVAFKKT KKEIKKVATP 130 140 150 160 170 180 KKASKPKKAA SKAPTKKPKA TPVKKAKKKL AATPKKAKKP KTVKAKPVKA SKPKKAKPVK 190 PKAKSSAKRA GKKK
	Isoform 2 [UniParc]. Checksum: 8CD558F288DB593A	FASTA	177	19,167
	10 20 30 40 50 60 MTKKSTDHPK YSDMIVAAIQ AEKNRAGSSR QSIQKYIKSH YKVGENADSQ IKLSIKRLVT 70 80 90 100 110 120 TGVLKQTKGV GASGSFRLAK SDEPKKSVAF KKTKKEIKKV ATPKKASKPK KAASKAPTKK 130 140 150 160 170 PKATPVKKAK KKLAATPKKA KKPKTVKAKP VKASKPKKAK PVKPKAKSSA KRAGKKK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Differential distribution of lysine and arginine residues in the closely related histones H1 and H5. Analysis of a human H1 gene." Doenecke D., Tonjes R. J. Mol. Biol. 187:461-464(1986) [PubMed: 3084796] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORM 1).
[2]	"A genome annotation-driven approach to cloning the human ORFeome." 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. Genome Biol. 5:R84.1-R84.11(2004) [PubMed: 15461802] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." 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. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[4]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2). Tissue: Brain.
[5]	"The DNA sequence of human chromosome 22." 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. Nature 402:489-495(1999) [PubMed: 10591208] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[7]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Colon and Placenta.
[8]	"Evidence for insertional RNA editing in humans." Zougman A., Ziolkowski P., Mann M., Wisniewski J.R. Curr. Biol. 18:1760-1765(2008) [PubMed: 18993075] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE (RNA EDITED VERSION), MASS SPECTROMETRY, RNA EDITING, SUBCELLULAR LOCATION, INDUCTION.
[9]	"The microheterogeneity of the mammalian H1(0) histone. Evidence for an age-dependent deamidation." Lindner H., Sarg B., Hoertnagl B., Helliger W. J. Biol. Chem. 273:13324-13330(1998) [PubMed: 9582379] [Abstract] Cited for: POST-TRANSLATIONAL MODIFICATIONS.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-171, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage." Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J. Science 316:1160-1166(2007) [PubMed: 17525332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-66, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[12]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-5, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[13]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+	Additional computationally mapped references.

Web resources

Wikipedia

Histone H1 entry

Cross-references

Sequence databases
EMBL GenBank DDBJ	X03473 Genomic DNA. Translation: CAA27190.1. CR456502 mRNA. Translation: CAG30388.1. CR542220 mRNA. Translation: CAG47016.1. AK299209 mRNA. Translation: BAG61248.1. AK312583 mRNA. Translation: BAG35477.1. Z97630 Genomic DNA. Translation: CAB42829.1. CH471095 Genomic DNA. Translation: EAW60188.1. BC000145 mRNA. Translation: AAH00145.1. BC029046 mRNA. Translation: AAH29046.1.
IPI	IPI00550239.
PIR	HSHU10. A24850.
RefSeq	NP_005309.1. NM_005318.3.
UniGene	Hs.727646.
3D structure databases
ProteinModelPortal	P07305.
SMR	P07305. Positions 25-97.
ModBase	Search...
Protein-protein interaction databases
DIP	DIP-41775N.
IntAct	P07305. 3 interactions.
MINT	MINT-276185.
STRING	P07305.
PTM databases
PhosphoSite	P07305.
Polymorphism databases
DMDM	121897.
Proteomic databases
PeptideAtlas	P07305.
PRIDE	P07305.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000340857; ENSP00000344504; ENSG00000189060.
GeneID	3005.
KEGG	hsa:3005.
UCSC	uc003aty.1. human.
Organism-specific databases
CTD	3005.
GeneCards	GC22P038201.
H-InvDB	HIX0203166.
HGNC	HGNC:4714. H1F0.
HPA	HPA000843.
MIM	142708. gene.
neXtProt	NX_P07305.
PharmGKB	PA29092.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20994.
GeneTree	ENSGT00550000074201.
HOVERGEN	HBG069502.
InParanoid	P07305.
OMA	IKKVATP.
OrthoDB	EOG4TTGKG.
PhylomeDB	P07305.
Enzyme and pathway databases
Reactome	REACT_578. Apoptosis.
Gene expression databases
ArrayExpress	P07305.
Bgee	P07305.
CleanEx	HS_H1F0.
Genevestigator	P07305.
GermOnline	ENSG00000189060. Homo sapiens.
Family and domain databases
InterPro	IPR005818. Histone_H1/H5. IPR005819. Histone_H5. IPR011991. WHTH_trsnscrt_rep_DNA-bd. [Graphical view]
Gene3D	G3DSA:1.10.10.10. Wing_hlx_DNA_bd. 1 hit.
KO	K11275.
Pfam	PF00538. Linker_histone. 1 hit. [Graphical view]
PRINTS	PR00624. HISTONEH5.
SMART	SM00526. H15. 1 hit. [Graphical view]
PROSITE	PS51504. H15. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	11916.
SOURCE	Search...

Entry information

Entry name

H10_HUMAN

Accession

Primary (citable) accession number: P07305
Secondary accession number(s): B2R6I0 , B4DRD6, Q6FG88, Q8N6R3

Entry history

Integrated into UniProtKB/Swiss-Prot:	April 1, 1988
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 117 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.