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P07305 (H10_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 140. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Histone H1.0
Alternative name(s):
Histone H1'
Histone H1(0)

Cleaved into the following chain:

  1. Histone H1.0, N-terminally processed
Gene names
Name:H1F0
Synonyms:H1FV
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length194 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 on Ser-17 in RNA edited version.

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

Binary interactions

With

Entry

#Exp.

IntAct

Notes

E1P040142EBI-725224,EBI-7014446From a different organism.

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 194194Histone H1.0
PRO_0000423207
Initiator methionine11Removed; alternate Ref.9
Chain2 – 194193Histone H1.0, N-terminally processed
PRO_0000195904

Regions

Domain24 – 9774H15

Amino acid modifications

Modified residue11N-acetylmethionine Ref.10
Modified residue21N-acetylthreonine; partial; in Histone H1.0, N-terminally processed Ref.9 Ref.10
Modified residue41Deamidated asparagine; partial Ref.9
Modified residue421Citrulline By similarity

Natural variations

Alternative sequence3 – 1917Missing in isoform 2.
VSP_042163
Natural variant11M → MLGKGRQRRRRQRQRQSPVP RPSDRPAGLGLAKPARRALP TPEPGRKSSDSSLASPGAAL QTGPVVRGSGADPEAGFAQP PTRAGPLEGAFNSRTRQATM in RNA edited version.
VAR_054789

Experimental info

Sequence conflict651D → H in AAH29046. Ref.7

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified January 23, 2007. Version 3.
Checksum: 03ED6F01919F8BE1

FASTA19420,863
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 8CD558F288DB593A
Show »

FASTA17719,167

References

« Hide '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] [Europe PMC] [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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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. expand/collapse author list , 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] [Europe PMC] [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] [Europe PMC] [Abstract]
Cited for: PARTIAL PROTEIN SEQUENCE (RNA EDITED VERSION), IDENTIFICATION BY 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] [Europe PMC] [Abstract]
Cited for: ACETYLATION AT THR-2, CLEAVAGE OF INITIATOR METHIONINE, DEAMIDATION AT ASN-4.
[10]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 AND THR-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[11]"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] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
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.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [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.
PIRHSHU10. A24850.
RefSeqNP_005309.1. NM_005318.3.
UniGeneHs.745024.

3D structure databases

ProteinModelPortalP07305.
SMRP07305. Positions 25-97.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109260. 25 interactions.
DIPDIP-41775N.
IntActP07305. 8 interactions.
MINTMINT-276185.
STRING9606.ENSP00000344504.

PTM databases

PhosphoSiteP07305.

Polymorphism databases

DMDM121897.

Proteomic databases

PaxDbP07305.
PeptideAtlasP07305.
PRIDEP07305.

Protocols and materials databases

DNASU3005.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000340857; ENSP00000344504; ENSG00000189060. [P07305-1]
GeneID3005.
KEGGhsa:3005.
UCSCuc003aty.3. human. [P07305-1]

Organism-specific databases

CTD3005.
GeneCardsGC22P038201.
H-InvDBHIX0016454.
HGNCHGNC:4714. H1F0.
HPAHPA000843.
MIM142708. gene.
neXtProtNX_P07305.
PharmGKBPA29092.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG126832.
HOGENOMHOG000251627.
HOVERGENHBG069502.
InParanoidP07305.
KOK11275.
OMADEPKRSV.
OrthoDBEOG75QR72.
PhylomeDBP07305.
TreeFamTF313664.

Enzyme and pathway databases

ReactomeREACT_120956. Cellular responses to stress.
REACT_578. Apoptosis.

Gene expression databases

BgeeP07305.
CleanExHS_H1F0.
GenevestigatorP07305.

Family and domain databases

Gene3D1.10.10.10. 1 hit.
InterProIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSPR00624. HISTONEH5.
SMARTSM00526. H15. 1 hit.
[Graphical view]
PROSITEPS51504. H15. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSH1F0. human.
GenomeRNAi3005.
NextBio11916.
PROP07305.
SOURCESearch...

Entry information

Entry nameH10_HUMAN
AccessionPrimary (citable) accession number: P07305
Secondary accession number(s): B2R6I0 expand/collapse secondary AC list , B4DRD6, Q6FG88, Q8N6R3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 140 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM