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Protein

Histone H1.0

Gene

H1f0

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at transcript leveli

Functioni

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.

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

ReactomeiR-MMU-211227. Activation of DNA fragmentation factor.
R-MMU-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H1.0
Alternative name(s):
Histone H1'
Histone H1(0)
MyD196
Cleaved into the following chain:
Gene namesi
Name:H1f0
Synonyms:H1fv
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 15

Organism-specific databases

MGIiMGI:95893. H1f0.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Histone H1.0PRO_0000195913Add
BLAST
Initiator methionineiRemoved; alternateBy similarity
Chaini2 – 194193Histone H1.0, N-terminally processedPRO_0000423208Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionineBy similarity
Modified residuei2 – 21N-acetylthreonine; in Histone H1.0, N-terminally processedBy similarity
Modified residuei42 – 421CitrullineBy similarity

Keywords - PTMi

Acetylation, Citrullination

Proteomic databases

EPDiP10922.
MaxQBiP10922.
PaxDbiP10922.
PRIDEiP10922.
TopDownProteomicsiP10922.

PTM databases

iPTMnetiP10922.
PhosphoSiteiP10922.

Expressioni

Gene expression databases

BgeeiP10922.
CleanExiMM_H1F0.
GenevisibleiP10922. MM.

Interactioni

Protein-protein interaction databases

BioGridi200145. 4 interactions.
IntActiP10922. 3 interactions.
MINTiMINT-1868324.
STRINGi10090.ENSMUSP00000137309.

Structurei

3D structure databases

DisProtiDP00097.
ProteinModelPortaliP10922.
SMRiP10922. Positions 25-97.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini24 – 9774H15PROSITE-ProRule annotationAdd
BLAST

Sequence similaritiesi

Belongs to the histone H1/H5 family.PROSITE-ProRule annotation
Contains 1 H15 (linker histone H1/H5 globular) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00810000125570.
HOVERGENiHBG069502.
InParanoidiP10922.
KOiK11275.
OMAiDEPKRSV.
OrthoDBiEOG75QR72.
PhylomeDBiP10922.
TreeFamiTF313664.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

P10922-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MTENSTSAPA AKPKRAKASK KSTDHPKYSD MIVAAIQAEK NRAGSSRQSI
60 70 80 90 100
QKYIKSHYKV GENADSQIKL SIKRLVTTGV LKQTKGVGAS GSFRLAKGDE
110 120 130 140 150
PKRSVAFKKT KKEVKKVATP KKAAKPKKAA SKAPSKKPKA TPVKKAKKKP
160 170 180 190
AATPKKAKKP KVVKVKPVKA SKPKKAKTVK PKAKSSAKRA SKKK
Length:194
Mass (Da):20,861
Last modified:January 23, 2007 - v4
Checksum:i41EF06627E2AC81C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti65 – 651D → N in CAA31569 (PubMed:2846273).Curated
Sequence conflicti190 – 1901A → G in CAA31569 (PubMed:2846273).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13171 mRNA. Translation: CAA31569.1.
U18295 Genomic DNA. Translation: AAA69911.1.
AK051213 mRNA. Translation: BAC34559.1.
AK077473 mRNA. Translation: BAC36817.1.
AK145675 mRNA. Translation: BAE26583.1.
AK146077 mRNA. Translation: BAE26881.1.
BC003830 mRNA. Translation: AAH03830.1.
BC011493 mRNA. Translation: AAH11493.1.
BC110361 mRNA. Translation: AAI10362.1.
CCDSiCCDS56990.1.
PIRiI49150.
RefSeqiNP_032223.2. NM_008197.3.
UniGeneiMm.24350.

Genome annotation databases

EnsembliENSMUST00000180086; ENSMUSP00000137309; ENSMUSG00000096210.
GeneIDi14958.
KEGGimmu:14958.
UCSCiuc007wsd.1. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X13171 mRNA. Translation: CAA31569.1.
U18295 Genomic DNA. Translation: AAA69911.1.
AK051213 mRNA. Translation: BAC34559.1.
AK077473 mRNA. Translation: BAC36817.1.
AK145675 mRNA. Translation: BAE26583.1.
AK146077 mRNA. Translation: BAE26881.1.
BC003830 mRNA. Translation: AAH03830.1.
BC011493 mRNA. Translation: AAH11493.1.
BC110361 mRNA. Translation: AAI10362.1.
CCDSiCCDS56990.1.
PIRiI49150.
RefSeqiNP_032223.2. NM_008197.3.
UniGeneiMm.24350.

3D structure databases

DisProtiDP00097.
ProteinModelPortaliP10922.
SMRiP10922. Positions 25-97.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi200145. 4 interactions.
IntActiP10922. 3 interactions.
MINTiMINT-1868324.
STRINGi10090.ENSMUSP00000137309.

PTM databases

iPTMnetiP10922.
PhosphoSiteiP10922.

Proteomic databases

EPDiP10922.
MaxQBiP10922.
PaxDbiP10922.
PRIDEiP10922.
TopDownProteomicsiP10922.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000180086; ENSMUSP00000137309; ENSMUSG00000096210.
GeneIDi14958.
KEGGimmu:14958.
UCSCiuc007wsd.1. mouse.

Organism-specific databases

CTDi3005.
MGIiMGI:95893. H1f0.

Phylogenomic databases

eggNOGiKOG4012. Eukaryota.
ENOG4112541. LUCA.
GeneTreeiENSGT00810000125570.
HOVERGENiHBG069502.
InParanoidiP10922.
KOiK11275.
OMAiDEPKRSV.
OrthoDBiEOG75QR72.
PhylomeDBiP10922.
TreeFamiTF313664.

Enzyme and pathway databases

ReactomeiR-MMU-211227. Activation of DNA fragmentation factor.
R-MMU-2559584. Formation of Senescence-Associated Heterochromatin Foci (SAHF).

Miscellaneous databases

ChiTaRSiH1f0. mouse.
NextBioi287302.
PROiP10922.
SOURCEiSearch...

Gene expression databases

BgeeiP10922.
CleanExiMM_H1F0.
GenevisibleiP10922. MM.

Family and domain databases

Gene3Di1.10.10.10. 1 hit.
InterProiIPR005818. Histone_H1/H5_H15.
IPR005819. Histone_H5.
IPR011991. WHTH_DNA-bd_dom.
[Graphical view]
PfamiPF00538. Linker_histone. 1 hit.
[Graphical view]
PRINTSiPR00624. HISTONEH5.
SMARTiSM00526. H15. 1 hit.
[Graphical view]
SUPFAMiSSF46785. SSF46785. 1 hit.
PROSITEiPS51504. H15. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Early increase in histone H1(0) mRNA during differentiation of F9 cells to parietal endoderm."
    Alonso A., Breuer B., Bouterfa H., Doenecke D.
    EMBO J. 7:3003-3008(1988) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "An upstream control region required for inducible transcription of the mouse H1(zero) histone gene during terminal differentiation."
    Dong Y., Liu D., Skoultchi A.I.
    Mol. Cell. Biol. 15:1889-1900(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Strain: BALB/cJ.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Blastocyst, Placenta and Spinal ganglion.
  4. "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].
    Strain: FVB/N.
    Tissue: Mammary tumor and Salivary gland.
  5. "Complexity of the immediate early response of myeloid cells to terminal differentiation and growth arrest includes ICAM-1, Jun-B and histone variants."
    Lord K.A., Hoffman-Liebermann B., Liebermann D.A.
    Oncogene 5:387-396(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 2-42.

Entry informationi

Entry nameiH10_MOUSE
AccessioniPrimary (citable) accession number: P10922
Secondary accession number(s): Q3UKC0
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 1, 1989
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 132 of the entry and version 4 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.