UniProtKB - P02253 (H12_BOVIN)
Protein
Histone H1.2
Gene
H1-2
Organism
Bos taurus (Bovine)
Status
Functioni
Histone H1 protein binds to linker DNA between nucleosomes forming the macromolecular structure known as the chromatin fiber. Histones H1 are necessary for the condensation of nucleosome chains into higher-order structured fibers. Acts also as a regulator of individual gene transcription through chromatin remodeling, nucleosome spacing and DNA methylation (By similarity).By similarity
GO - Molecular functioni
- double-stranded DNA binding Source: GO_Central
- nucleosomal DNA binding Source: GO_Central
GO - Biological processi
- chromosome condensation Source: GO_Central
- negative regulation of chromatin silencing Source: GO_Central
- negative regulation of DNA recombination Source: GO_Central
- nucleosome assembly Source: InterPro
- nucleosome positioning Source: GO_Central
Keywordsi
Molecular function | DNA-binding |
Names & Taxonomyi
Protein namesi | Recommended name: Histone H1.2Alternative name(s): CTL-1 |
Gene namesi | Name:H1-2By similarity |
Organismi | Bos taurus (Bovine) |
Taxonomic identifieri | 9913 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Laurasiatheria › Artiodactyla › Ruminantia › Pecora › Bovidae › Bovinae › Bos |
Proteomesi |
|
Subcellular locationi
Nucleus
Other locations
Note: Mainly localizes in euchromatin.By similarity
Nucleus
- nucleus Source: GO_Central
Other locations
- nucleosome Source: InterPro
Keywords - Cellular componenti
Chromosome, NucleusPTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Initiator methioninei | Removed1 Publication | |||
ChainiPRO_0000195903 | 2 – 213 | Histone H1.2Add BLAST | 212 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 2 | N-acetylserine; partialBy similarity | 1 | |
Modified residuei | 2 | PhosphoserineBy similarity | 1 | |
Modified residuei | 17 | N6-acetyllysineBy similarity | 1 | |
Modified residuei | 23 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 26 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 27 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 34 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 34 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 34 | N6-methyllysine; alternateBy similarity | 1 | |
Modified residuei | 46 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 52 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 52 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 54 | CitrullineBy similarity | 1 | |
Modified residuei | 63 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 64 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 64 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 64 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 75 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 81 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 85 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 85 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 85 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 90 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 90 | N6-(beta-hydroxybutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 90 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 97 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 97 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 97 | N6-succinyllysine; alternateBy similarity | 1 | |
Modified residuei | 104 | Phosphoserine; by PKC1 Publication | 1 | |
Modified residuei | 106 | N6-(beta-hydroxybutyryl)lysineBy similarity | 1 | |
Modified residuei | 110 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 117 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 121 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 129 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 136 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 146 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 148 | N6-(2-hydroxyisobutyryl)lysineBy similarity | 1 | |
Modified residuei | 159 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 159 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 168 | N6-(2-hydroxyisobutyryl)lysine; alternateBy similarity | 1 | |
Modified residuei | 168 | N6-crotonyllysine; alternateBy similarity | 1 | |
Modified residuei | 187 | N6-methyllysine; by EHMT1 and EHMT2By similarity | 1 | |
Modified residuei | 188 | ADP-ribosylserineBy similarity | 1 |
Post-translational modificationi
H1 histones are progressively phosphorylated during the cell cycle, becoming maximally phosphorylated during late G2 phase and M phase, and being dephosphorylated sharply thereafter.By similarity
Crotonylation (Kcr) is specifically present in male germ cells and marks testis-specific genes in post-meiotic cells, including X-linked genes that escape sex chromosome inactivation in haploid cells. Crotonylation marks active promoters and enhancers and confers resistance to transcriptional repressors. It is also associated with post-meiotically activated genes on autosomes.By similarity
ADP-ribosylated on Ser-188 in response to DNA damage.By similarity
Citrullination at Arg-54 (H1R54ci) by PADI4 takes place within the DNA-binding site of H1 and results in its displacement from chromatin and global chromatin decondensation, thereby promoting pluripotency and stem cell maintenance.By similarity
Keywords - PTMi
Acetylation, ADP-ribosylation, Citrullination, Hydroxylation, Methylation, PhosphoproteinProteomic databases
PaxDbi | P02253 |
PeptideAtlasi | P02253 |
PRIDEi | P02253 |
PTM databases
iPTMneti | P02253 |
Expressioni
Gene expression databases
Bgeei | ENSBTAG00000011677, Expressed in conceptus and 18 other tissues |
Interactioni
Binary interactionsi
P02253
With | #Exp. | IntAct |
---|---|---|
SIR2rp1 [Q57V41] from Trypanosoma brucei brucei (strain 927/4 GUTat10.1). | 7 | EBI-7580031,EBI-7579996 |
Protein-protein interaction databases
BioGRIDi | 170598, 4 interactors |
IntActi | P02253, 1 interactor |
MINTi | P02253 |
STRINGi | 9913.ENSBTAP00000015499 |
Family & Domainsi
Domains and Repeats
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Domaini | 36 – 109 | H15PROSITE-ProRule annotationAdd BLAST | 74 |
Domaini
The C-terminal domain is required for high-affinity binding to chromatin.By similarity
Sequence similaritiesi
Belongs to the histone H1/H5 family.PROSITE-ProRule annotation
Phylogenomic databases
eggNOGi | KOG4012, Eukaryota |
HOGENOMi | CLU_052897_7_0_1 |
InParanoidi | P02253 |
OMAi | NSAITHG |
OrthoDBi | 1565299at2759 |
TreeFami | TF313664 |
Family and domain databases
CDDi | cd00073, H15, 1 hit |
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View protein in InterPro IPR005819, H1/H5 IPR005818, Histone_H1/H5_H15 IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
Pfami | View protein in Pfam PF00538, Linker_histone, 1 hit |
PRINTSi | PR00624, HISTONEH5 |
SMARTi | View protein in SMART SM00526, H15, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit |
PROSITEi | View protein in PROSITE PS51504, H15, 1 hit |
i Sequence
Sequence statusi: Complete.
: The displayed sequence is further processed into a mature form. Sequence processingi
P02253-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MSETAPAAPA AAPPAEKTPV KKKAAKKPAG ARRKASGPPV SELITKAVAA
60 70 80 90 100
SKERSGVSLA ALKKALAAAG YDVEKNNSRI KLGLKSLVSK GTLVQTKGTG
110 120 130 140 150
ASGSFKLNKK AATGEAKPKA KKAGAAKPKK AAGAAKKTKK ATGAATPKKT
160 170 180 190 200
AKKTPKKAKK PAAAAVTKKV AKSPKKAKAA KPKKAAKSAA KAVKPKAAKP
210
KVAKPKKAAP KKK
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DAAA02055500 Genomic DNA No translation available. BC133454 mRNA Translation: AAI33455.1 |
PIRi | A92316, HSBO11 |
RefSeqi | NP_001076894.1, NM_001083425.1 |
Genome annotation databases
GeneIDi | 513971 |
KEGGi | bta:513971 |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | DAAA02055500 Genomic DNA No translation available. BC133454 mRNA Translation: AAI33455.1 |
PIRi | A92316, HSBO11 |
RefSeqi | NP_001076894.1, NM_001083425.1 |
3D structure databases
SMRi | P02253 |
ModBasei | Search... |
Protein-protein interaction databases
BioGRIDi | 170598, 4 interactors |
IntActi | P02253, 1 interactor |
MINTi | P02253 |
STRINGi | 9913.ENSBTAP00000015499 |
PTM databases
iPTMneti | P02253 |
Proteomic databases
PaxDbi | P02253 |
PeptideAtlasi | P02253 |
PRIDEi | P02253 |
Genome annotation databases
GeneIDi | 513971 |
KEGGi | bta:513971 |
Organism-specific databases
CTDi | 3006 |
Phylogenomic databases
eggNOGi | KOG4012, Eukaryota |
HOGENOMi | CLU_052897_7_0_1 |
InParanoidi | P02253 |
OMAi | NSAITHG |
OrthoDBi | 1565299at2759 |
TreeFami | TF313664 |
Gene expression databases
Bgeei | ENSBTAG00000011677, Expressed in conceptus and 18 other tissues |
Family and domain databases
CDDi | cd00073, H15, 1 hit |
Gene3Di | 1.10.10.10, 1 hit |
InterProi | View protein in InterPro IPR005819, H1/H5 IPR005818, Histone_H1/H5_H15 IPR036388, WH-like_DNA-bd_sf IPR036390, WH_DNA-bd_sf |
Pfami | View protein in Pfam PF00538, Linker_histone, 1 hit |
PRINTSi | PR00624, HISTONEH5 |
SMARTi | View protein in SMART SM00526, H15, 1 hit |
SUPFAMi | SSF46785, SSF46785, 1 hit |
PROSITEi | View protein in PROSITE PS51504, H15, 1 hit |
ProtoNeti | Search... |
MobiDBi | Search... |
Entry informationi
Entry namei | H12_BOVIN | |
Accessioni | P02253Primary (citable) accession number: P02253 Secondary accession number(s): A3KN02 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 21, 1986 |
Last sequence update: | October 3, 2012 | |
Last modified: | April 7, 2021 | |
This is version 143 of the entry and version 2 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |
Miscellaneousi
Keywords - Technical termi
Direct protein sequencing, Reference proteomeDocuments
- SIMILARITY comments
Index of protein domains and families