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UniProtKB/Swiss-Prot entry P10412


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name H14_HUMAN
Primary accession number P10412
Secondary accession number Q4VB25
Integrated into Swiss-Prot on July 1, 1989
Sequence was last modified on January 23, 2007 (Sequence version 2)
Annotations were last modified on    December 16, 2008 (Entry version 85)
Name and origin of the protein
Protein name Histone H1.4
Synonym Histone H1b
Gene name
Name: HIST1H1E
Synonyms: H1F4
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/0888-7543(91)90183-F; PubMed=1916825 [NCBI, ExPASy, EBI, Israel, Japan]
Albig W., Kardalinou E., Drabent B., Zimmer A., Doenecke D.;
"Isolation and characterization of two human H1 histone genes within clusters of core histone genes.";
Genomics 10:940-948(1991).
[2]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
DOI=10.1016/S0888-7543(02)96850-3; PubMed=12408966 [NCBI, ExPASy, EBI, Israel, Japan]
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).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
DOI=10.1038/nature02055; PubMed=14574404 [NCBI, ExPASy, EBI, Israel, Japan]
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.;
"The DNA sequence and analysis of human chromosome 6.";
Nature 425:805-811(2003).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
PROTEIN SEQUENCE OF 2-219.
TISSUE=Spleen;
PubMed=3782055 [NCBI, ExPASy, EBI, Israel, Japan]
Ohe Y., Hayashi H., Iwai K.;
"Human spleen histone H1. Isolation and amino acid sequence of a main variant, H1b.";
J. Biochem. 100:359-368(1986).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18 AND SER-187, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[7]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1021/pr070152u; PubMed=17924679 [NCBI, ExPASy, EBI, Israel, Japan]
Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.;
"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra.";
J. Proteome Res. 6:4150-4162(2007).
[8]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-27 AND SER-36, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0611217104; PubMed=17287340 [NCBI, ExPASy, EBI, Israel, Japan]
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.;
"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry.";
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007).
[9]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND MASS SPECTROMETRY.
DOI=10.1016/j.molcel.2008.07.007; PubMed=18691976 [NCBI, ExPASy, EBI, Israel, Japan]
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.;
"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.";
Mol. Cell 31:438-448(2008).
[10]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18, AND MASS SPECTROMETRY.
DOI=10.1073/pnas.0805139105; PubMed=18669648 [NCBI, ExPASy, EBI, Israel, Japan]
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[11]
VARIANT [LARGE SCALE ANALYSIS] VAL-128.
DOI=10.1126/science.1133427; PubMed=16959974 [NCBI, ExPASy, EBI, Israel, Japan]
Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D., Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P., Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V., Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H., Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W., Velculescu V.E.;
"The consensus coding sequences of human breast and colorectal cancers.";
Science 314:268-274(2006).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
M60748; AAA63187.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF531302; AAN06702.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL353759; CAC04132.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096168; AAH96168.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC096169; AAH96169.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC099632; AAH99632.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR C40335; HSHU1B.
RefSeq NP_005312.1; -.
UniGene Hs.248133
3D structure databases
HSSP P08287; 1GHC. [HSSP ENTRY / PDB]
SMR P10412; 36-109.
ModBase P10412.
Protein-protein interaction databases
IntAct P10412; 6.
PTM databases
PhosphoSite P10412; -.
Organism-specific databases
GeneCards GC06P026264; -.
H-InvDB HIX0032905; -.
HGNC HGNC:4718; HIST1H1E.
GenAtlas HIST1H1E.
HPA CAB011506; -.
MIM 142220; gene. [NCBI / EBI]
PharmGKB PA29096; -.
GeneCards P10412.
Gene expression databases
ArrayExpress P10412; -.
CleanEx HS_HIST1H1E; -.
GermOnline ENSG00000168298; Homo sapiens.
Ontologies
GO
GO:0000786; Cellular component: nucleosome (non-traceable author statement from UniProtKB).
GO:0005634; Cellular component: nucleus (inferred from electronic annotation from InterPro).
GO:0003677; Molecular function: DNA binding (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0006334; Biological process: nucleosome assembly (non-traceable author statement from UniProtKB).
QuickGo view.
Family and domain databases
InterPro IPR005818; Histone_H1/H5.
IPR005819; Histone_H5.
IPR011991; Wing_hlx_DNA_bd.
Graphical view of domain structure.
Gene3D G3DSA:1.10.10.10; Wing_hlx_DNA_bd; 1.
Pfam PF00538; Linker_histone; 1.
Pfam graphical view of domain structure.
PRINTS PR00624; HISTONEH5.
SMART SM00526; H15; 1.
SMART graphical view of domain structure.
Proteomic databases
PeptideAtlas P10412; -.
Proteomics databases
PRIDE P10412; -.
Genome annotation databases
Ensembl ENSG00000168298; Homo sapiens. [Contig view]
GeneID 3008; -.
KEGG hsa:3008; -.
Phylogenomic databases
HOGENOM P10412; -.
HOVERGEN P10412; -.
Other
NextBio 11928; -.
SOURCE HIST1H1E; Homo sapiens.
ProtoNet P10412.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
Acetylation; Chromosomal protein; Direct protein sequencing; DNA-binding; Methylation; Nucleus; Phosphoprotein; Polymorphism.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom   To Length Description FTId
INIT_MET   1     1        Removed. 
CHAIN   2   219  218     Histone H1.4. PRO_0000195908
REGION   36   114  79     Globular. 
MOD_RES   2     2        N-acetylserine. 
MOD_RES   4     4        Phosphothreonine (By similarity). 
MOD_RES   18    18        Phosphothreonine. 
MOD_RES   26    26        N6-methyllysine; partial. 
MOD_RES   27    27        Phosphoserine. 
MOD_RES   36    36        Phosphoserine. 
MOD_RES   187   187        Phosphoserine. 
VARIANT   128   128  1     A -> V (in a colorectal cancer sample; somatic mutation). VAR_036203 
VARIANT   152   152  1     K -> R (in dbSNP:rs2298090 [NCBI]). VAR_049307 
Sequence information
Length: 219 AA [This is the length of the unprocessed precursor] Molecular weight: 21865 Da [This is the MW of the unprocessed precursor] CRC64: 1720FECCCBEBCC7F [This is a checksum on the sequence]
        10         20         30         40         50         60 
MSETAPAAPA APAPAEKTPV KKKARKSAGA AKRKASGPPV SELITKAVAA SKERSGVSLA 

        70         80         90        100        110        120 
ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG ASGSFKLNKK AASGEAKPKA 

       130        140        150        160        170        180 
KKAGAAKAKK PAGAAKKPKK ATGAATPKKS AKKTPKKAKK PAAAAGAKKA KSPKKAKAAK 

       190        200        210 
PKKAPKSPAK AKAVKPKAAK PKTAKPKAAK PKKAAAKKK 

P10412 in FASTA format

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