H1 10 | ENSG00000184897 | NCBI 8971

Details for: H1 10

Gene ID: 8971

Symbol: H1 10

Ensembl ID: ENSG00000184897

Description: H1.10 linker histone

Associated with

Cadherin binding
(GO:0045296)
Chromosome
(GO:0005694)
Chromosome condensation
(GO:0030261)
Double-stranded dna binding
(GO:0003690)
Negative regulation of dna recombination
(GO:0045910)
Nucleolus
(GO:0005730)
Nucleoplasm
(GO:0005654)
Nucleosomal dna binding
(GO:0031492)
Nucleosome
(GO:0000786)
Nucleosome assembly
(GO:0006334)
Nucleus
(GO:0005634)
Rna binding
(GO:0003723)
Structural constituent of chromatin
(GO:0030527)

Other Information

Proteins

Histone H1x

Genular Protein ID: 1988749589

Symbol: H1X_HUMAN

Name: Histone H1x

UniProtKB Accession Codes:

Q92522

Database IDs:

Citations:

PubMed ID: 8964515

Title: Cloning of the cDNA encoding a novel subtype of histone H1.

PubMed ID: 8964515

DOI: 10.1016/0378-1119(96)00020-0

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 17924679

Title: 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.

PubMed ID: 17924679

DOI: 10.1021/pr070152u

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19710015

Title: The metastasis efficiency modifier ribosomal RNA processing 1 homolog B (RRP1B) is a chromatin-associated factor.

PubMed ID: 19710015

DOI: 10.1074/jbc.m109.023457

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 19608861

Title: Lysine acetylation targets protein complexes and co-regulates major cellular functions.

PubMed ID: 19608861

DOI: 10.1126/science.1175371

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 22223895

Title: Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features.

PubMed ID: 22223895

DOI: 10.1074/mcp.m111.015131

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

Sequence Information:

Length: 213
Mass: 22487
Checksum: 11548D85C5448FF2
Sequence:

MSVELEEALP VTTAEGMAKK VTKAGGSAAL SPSKKRKNSK KKNQPGKYSQ LVVETIRRLG 
ERNGSSLAKI YTEAKKVPWF DQQNGRTYLK YSIKALVQND TLLQVKGTGA NGSFKLNRKK 
LEGGGERRGA PAAATAPAPT AHKAKKAAPG AAGSRRADKK PARGQKPEQR SHKKGAGAKK 
DKGGKAKKTA AAGGKKVKKA AKPSVPKVPK GRK

The gene details are incomplete or unavailable at the moment.

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.

Details for: H1 10

Associated with

Other Information

Cloning of the cDNA encoding a novel subtype of histone H1. PubMed ID: 8964515

The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC). PubMed ID: 15489334

Global, in vivo, and site-specific phosphorylation dynamics in signaling networks. PubMed ID: 17081983

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. PubMed ID: 17924679

A quantitative atlas of mitotic phosphorylation. PubMed ID: 18669648

Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach. PubMed ID: 19413330

The metastasis efficiency modifier ribosomal RNA processing 1 homolog B (RRP1B) is a chromatin-associated factor. PubMed ID: 19710015

Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions. PubMed ID: 19690332

Lysine acetylation targets protein complexes and co-regulates major cellular functions. PubMed ID: 19608861

Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis. PubMed ID: 20068231

Initial characterization of the human central proteome. PubMed ID: 21269460

System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation. PubMed ID: 21406692

Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features. PubMed ID: 22223895

Toward a comprehensive characterization of a human cancer cell phosphoproteome. PubMed ID: 23186163

An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome. PubMed ID: 24275569