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Protein

Putative histone H2B type 2-C

Gene

HIST2H2BC

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Protein uncertaini

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

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Putative histone H2B type 2-C
Alternative name(s):
Histone H2B.t
Short name:
H2B/t
Gene namesi
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:20516. HIST2H2BC.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Polymorphism and mutation databases

DMDMi74709215.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 193192Putative histone H2B type 2-CPRO_0000244824Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylprolineBy similarity
Modified residuei6 – 61N6-acetyllysine; alternate1 Publication
Modified residuei6 – 61N6-crotonyllysine; alternate1 Publication
Cross-linki6 – 6Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity
Modified residuei12 – 121N6-acetyllysine; alternateBy similarity
Modified residuei12 – 121N6-crotonyllysine; alternate1 Publication
Modified residuei13 – 131N6-acetyllysine; alternate1 Publication
Modified residuei13 – 131N6-crotonyllysine; alternate1 Publication
Modified residuei15 – 151Phosphoserine; by STK4/MST11 Publication
Modified residuei16 – 161N6-acetyllysine; alternate1 Publication
Modified residuei16 – 161N6-crotonyllysine; alternate1 Publication
Modified residuei17 – 171N6-acetyllysine; alternateBy similarity
Modified residuei17 – 171N6-crotonyllysine; alternate1 Publication
Modified residuei21 – 211N6-acetyllysine; alternate1 Publication
Modified residuei21 – 211N6-crotonyllysine; alternate1 Publication
Modified residuei24 – 241N6-acetyllysine; alternateBy similarity
Modified residuei24 – 241N6-crotonyllysine; alternate1 Publication
Modified residuei35 – 351N6-crotonyllysine1 Publication
Modified residuei37 – 371Phosphoserine; by AMPKBy similarity
Modified residuei47 – 471N6-methyllysineBy similarity
Modified residuei58 – 581N6,N6-dimethyllysineBy similarity
Modified residuei80 – 801Dimethylated arginineBy similarity
Modified residuei86 – 861N6,N6,N6-trimethyllysine; alternateBy similarity
Modified residuei86 – 861N6-acetyllysine; alternateBy similarity
Modified residuei87 – 871Omega-N-methylarginineBy similarity
Modified residuei93 – 931Omega-N-methylarginineBy similarity

Post-translational modificationi

Phosphorylation at Ser-37 (H2BS36ph) by AMPK in response to stress promotes transcription (By similarity). Phosphorylated on Ser-15 (H2BS14ph) by STK4/MST1 during apoptosis; which facilitates apoptotic chromatin condensation. Also phosphorylated on Ser-15 in response to DNA double strand breaks (DSBs), and in correlation with somatic hypermutation and immunoglobulin class-switch recombination.By similarity1 Publication
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.1 Publication

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ6DN03.
MaxQBiQ6DN03.
PRIDEiQ6DN03.

PTM databases

iPTMnetiQ6DN03.

Expressioni

Organism-specific databases

HPAiHPA042205.
HPA043013.
HPA048671.

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.

Protein-protein interaction databases

IntActiQ6DN03. 1 interaction.

Structurei

3D structure databases

ProteinModelPortaliQ6DN03.
SMRiQ6DN03. Positions 5-93.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

HOVERGENiHBG081588.
InParanoidiQ6DN03.

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.

Sequencei

Sequence statusi: Complete.

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

Q6DN03-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MPEPAKFAPA PKKGSKKAVT KAQKKDGKKR KRSRKESYSI YVYKVLKRVH
60 70 80 90 100
PDTGIWCKAM GIMNSFLNDI FERIAGEASR LAHYNKRSTI TSRRSRRPCA
110 120 130 140 150
CCCPASWPST PCPRAPRRSP STPAPSESLP GPGARSLPPS LPPRVAGCFV
160 170 180 190
SKGSFQGHLT TSVKESFLCC QSQLMFLASR LVNFRRAHNT KHR
Length:193
Mass (Da):21,472
Last modified:January 23, 2007 - v3
Checksum:i1AA494C8A167792B
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY656810 Genomic DNA. Translation: AAT72343.1.
AY131977 Genomic DNA. No translation available.
AK299891 mRNA. Translation: BAH13163.1.
UniGeneiHs.666643.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY656810 Genomic DNA. Translation: AAT72343.1.
AY131977 Genomic DNA. No translation available.
AK299891 mRNA. Translation: BAH13163.1.
UniGeneiHs.666643.

3D structure databases

ProteinModelPortaliQ6DN03.
SMRiQ6DN03. Positions 5-93.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ6DN03. 1 interaction.

PTM databases

iPTMnetiQ6DN03.

Polymorphism and mutation databases

DMDMi74709215.

Proteomic databases

EPDiQ6DN03.
MaxQBiQ6DN03.
PRIDEiQ6DN03.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Organism-specific databases

GeneCardsiHIST2H2BC.
HGNCiHGNC:20516. HIST2H2BC.
HPAiHPA042205.
HPA043013.
HPA048671.
neXtProtiNX_Q6DN03.
GenAtlasiSearch...

Phylogenomic databases

HOVERGENiHBG081588.
InParanoidiQ6DN03.

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.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The human and mouse replication-dependent histone genes."
    Marzluff W.F., Gongidi P., Woods K.R., Jin J., Maltais L.J.
    Genomics 80:487-498(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  2. "Functional characterization of a human histone gene cluster duplication."
    Braastad C.D., Hovhannisyan H., van Wijnen A.J., Stein J.L., Stein G.S.
    Gene 342:35-40(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Tissue: Brain.
  4. "Apoptotic phosphorylation of histone H2B is mediated by mammalian sterile twenty kinase."
    Cheung W.L., Ajiro K., Samejima K., Kloc M., Cheung P., Mizzen C.A., Beeser A., Etkin L.D., Chernoff J., Earnshaw W.C., Allis C.D.
    Cell 113:507-517(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-15.
  5. "Inhibition of core histones acetylation by carcinogenic nickel(II)."
    Golebiowski F., Kasprzak K.S.
    Mol. Cell. Biochem. 279:133-139(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION AT LYS-6; LYS-13; LYS-16 AND LYS-21.
  6. "Identification of 67 histone marks and histone lysine crotonylation as a new type of histone modification."
    Tan M., Luo H., Lee S., Jin F., Yang J.S., Montellier E., Buchou T., Cheng Z., Rousseaux S., Rajagopal N., Lu Z., Ye Z., Zhu Q., Wysocka J., Ye Y., Khochbin S., Ren B., Zhao Y.
    Cell 146:1016-1028(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: CROTONYLATION AT LYS-6; LYS-12; LYS-13; LYS-16; LYS-17; LYS-21; LYS-24 AND LYS-35.

Entry informationi

Entry nameiH2B2C_HUMAN
AccessioniPrimary (citable) accession number: Q6DN03
Secondary accession number(s): B7Z677
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: January 23, 2007
Last modified: March 16, 2016
This is version 89 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Miscellaneous

The mouse orthologous protein seems not to exist.

Caution

Could be the product of a pseudogene. In contrast to other H2B histones, it does not contain the conserved residue in C-terminus that is the target of monoubiquitination.Curated

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  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.