Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Protein

Histone H2B.1, sperm

Gene
N/A
Organism
Psammechinus miliaris (Green sea urchin) (Echinus miliaris)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Core component of nucleosome. Nucleosomes wrap and compact DNA into chromatin, limiting DNA accessibility to the cellular machineries which require DNA as a template. Histones thereby play a central role in transcription regulation, DNA repair, DNA replication and chromosomal stability. DNA accessibility is regulated via a complex set of post-translational modifications of histones, also called histone code, and nucleosome remodeling.

GO - Molecular functioni

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B.1, sperm
OrganismiPsammechinus miliaris (Green sea urchin) (Echinus miliaris)
Taxonomic identifieri7660 [NCBI]
Taxonomic lineageiEukaryotaMetazoaEchinodermataEleutherozoaEchinozoaEchinoideaEuechinoideaEchinaceaEchinoidaEchinidaePsammechinus

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemoved1 Publication
Chaini2 – 137136Histone H2B.1, spermPRO_0000239650Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei11 – 111Phosphoserine1 Publication
Modified residuei16 – 161Phosphoserine1 Publication
Glycosylationi124 – 1241O-linked (GlcNAc)By similarity
Cross-linki132 – 132Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity

Post-translational modificationi

Monoubiquitination of Lys-132 gives a specific tag for epigenetic transcriptional activation and is also prerequisite for histone H3 'Lys-4' and 'Lys-79' methylation.By similarity
Phosphorylated on SPKK motifs 2 and 3; which may regulate DNA binding. Dephosphorylated during maturation of spermatids to mature sperm and rephosphorylated at fertilization.1 Publication
GlcNAcylation at Ser-124 promotes monoubiquitination of Lys-132. It fluctuates in response to extracellular glucose, and associates with transcribed genes (By similarity).By similarity

Keywords - PTMi

Glycoprotein, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

PRIDEiQ27749.

PTM databases

iPTMnetiQ27749.

Expressioni

Developmental stagei

Expressed only during spermatogenesis.1 Publication

Interactioni

Subunit structurei

The nucleosome is a histone octamer containing two molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and two H2A-H2B heterodimers. The octamer wraps approximately 147 bp of DNA.

Structurei

3D structure databases

ProteinModelPortaliQ27749.
SMRiQ27749. Positions 16-137.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi6 – 94SPKK motif 1
Motifi11 – 144SPKK motif 2
Motifi16 – 194SPKK motif 3

Domaini

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00621. HISTONEH2B.
SMARTiSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00357. HISTONE_H2B. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

Q27749-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPSQKSPTKR SPTKRSPQKG GKGAKRGGKA GKRRRGVAVK RRRRRRESYG
60 70 80 90 100
IYIYKVLKQV HPDTGISSRA MSVMNSFVND VFERIASEAG RLTTYNRRNT
110 120 130
VSSREVQTAV RLLLPGELAK HAVSEGTKAV TKYTTSR
Length:137
Mass (Da):15,319
Last modified:January 23, 2007 - v3
Checksum:i03ABA1F20A17A821
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11086 mRNA. Translation: AAA30020.1.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
M11086 mRNA. Translation: AAA30020.1.

3D structure databases

ProteinModelPortaliQ27749.
SMRiQ27749. Positions 16-137.
ModBaseiSearch...
MobiDBiSearch...

PTM databases

iPTMnetiQ27749.

Proteomic databases

PRIDEiQ27749.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR007125. Histone_H2A/H2B/H3.
IPR000558. Histone_H2B.
[Graphical view]
PANTHERiPTHR23428. PTHR23428. 1 hit.
PfamiPF00125. Histone. 1 hit.
[Graphical view]
PRINTSiPR00621. HISTONEH2B.
SMARTiSM00427. H2B. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS00357. HISTONE_H2B. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "Synthesis of sperm and late histone cDNAs of the sea urchin with a primer complementary to the conserved 3' terminal palindrome: evidence for tissue-specific and more general histone gene variants."
    Busslinger M., Barberis A.
    Proc. Natl. Acad. Sci. U.S.A. 82:5676-5680(1985) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA], DEVELOPMENTAL STAGE.
    Tissue: Testis.
  2. "The partial amino acid sequences of the two H2B histones from sperm of the sea urchin Psammechinus miliaris."
    Strickland M., Strickland W.N., Brandt W.F., von Holt C.
    Biochim. Biophys. Acta 536:289-297(1978) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 2-51.
  3. "Phosphorylation at clustered -Ser-Pro-X-Lys/Arg- motifs in sperm-specific histones H1 and H2B."
    Hill C.S., Packman L.C., Thomas J.O.
    EMBO J. 9:805-813(1990) [PubMed] [Europe PMC] [Abstract]
    Cited for: PROTEIN SEQUENCE OF 11-26, PHOSPHORYLATION AT SER-11 AND SER-16.

Entry informationi

Entry nameiH2BS1_PSAMI
AccessioniPrimary (citable) accession number: Q27749
Entry historyi
Integrated into UniProtKB/Swiss-Prot: June 13, 2006
Last sequence update: January 23, 2007
Last modified: January 20, 2016
This is version 74 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)

Miscellaneousi

Keywords - Technical termi

Direct protein sequencing

Documents

  1. 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.