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Protein

Histone H2B type W-T

Gene

H2BFWT

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 3 out of 5-Experimental evidence at protein leveli

Functioni

Atypical histone H2B. Nucleosomes containing it are structurally and dynamically indistinguishable from those containing conventional H2B. However, unlike conventional H2B, does not recruit chromosome condensation factors and does not participate in the assembly of mitotic chromosomes. May be important for telomere function.1 Publication

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Histone H2B type W-T
Alternative name(s):
H2B histone family member W testis-specific
Gene namesi
Name:H2BFWT
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome X

Organism-specific databases

HGNCiHGNC:27252. H2BFWT.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Membrane, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA134930988.

Polymorphism and mutation databases

DMDMi223590216.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 175175Histone H2B type W-TPRO_0000244828Add
BLAST

Proteomic databases

PaxDbiQ7Z2G1.
PRIDEiQ7Z2G1.

PTM databases

iPTMnetiQ7Z2G1.
PhosphoSiteiQ7Z2G1.

Expressioni

Tissue specificityi

Testis-specific. Present in sperm cells (at protein level).1 Publication

Gene expression databases

BgeeiQ7Z2G1.
CleanExiHS_H2BFWT.

Organism-specific databases

HPAiHPA056289.

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

STRINGi9606.ENSP00000354723.

Structurei

3D structure databases

ProteinModelPortaliQ7Z2G1.
SMRiQ7Z2G1. Positions 48-164.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the histone H2B family.Curated

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
HOGENOMiHOG000231213.
InParanoidiQ7Z2G1.
KOiK11252.
OrthoDBiEOG7Z95PV.
PhylomeDBiQ7Z2G1.
TreeFamiTF300212.

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.

Q7Z2G1-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MLRTEVPRLP RSTTAIVWSC HLMATASAMA GPSSETTSEE QLITQEPKEA
60 70 80 90 100
NSTTSQKQSK QRKRGRHGPR RCHSNCRGDS FATYFRRVLK QVHQGLSLSR
110 120 130 140 150
EAVSVMDSLV HDILDRIATE AGRLARSTKR QTITAWETRM AVRLLLPGQM
160 170
GKLAESEGTK AVLRTSLYAI QQQRK
Length:175
Mass (Da):19,618
Last modified:February 10, 2009 - v2
Checksum:iC47C922CBBE96BCC
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti87 – 871R → W.
Corresponds to variant rs17332043 [ dbSNP | Ensembl ].
VAR_049315
Natural varianti123 – 1231R → H.2 Publications
Corresponds to variant rs553509 [ dbSNP | Ensembl ].
VAR_054318

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY283369 Genomic DNA. Translation: AAP37489.1.
AY283370 mRNA. Translation: AAP37490.1.
AL034485 Genomic DNA. Translation: CAI43100.2.
CH471120 Genomic DNA. Translation: EAX02765.1.
BC038109 mRNA. Translation: AAH38109.1.
BC118604 mRNA. Translation: AAI18605.1.
BC121816 mRNA. Translation: AAI21817.1.
CCDSiCCDS35362.1.
RefSeqiNP_001002916.3. NM_001002916.4.
UniGeneiHs.127778.

Genome annotation databases

EnsembliENST00000217926; ENSP00000354723; ENSG00000123569.
ENST00000611083; ENSP00000482103; ENSG00000123569.
GeneIDi158983.
KEGGihsa:158983.
UCSCiuc004elr.4. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AY283369 Genomic DNA. Translation: AAP37489.1.
AY283370 mRNA. Translation: AAP37490.1.
AL034485 Genomic DNA. Translation: CAI43100.2.
CH471120 Genomic DNA. Translation: EAX02765.1.
BC038109 mRNA. Translation: AAH38109.1.
BC118604 mRNA. Translation: AAI18605.1.
BC121816 mRNA. Translation: AAI21817.1.
CCDSiCCDS35362.1.
RefSeqiNP_001002916.3. NM_001002916.4.
UniGeneiHs.127778.

3D structure databases

ProteinModelPortaliQ7Z2G1.
SMRiQ7Z2G1. Positions 48-164.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi9606.ENSP00000354723.

PTM databases

iPTMnetiQ7Z2G1.
PhosphoSiteiQ7Z2G1.

Polymorphism and mutation databases

DMDMi223590216.

Proteomic databases

PaxDbiQ7Z2G1.
PRIDEiQ7Z2G1.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000217926; ENSP00000354723; ENSG00000123569.
ENST00000611083; ENSP00000482103; ENSG00000123569.
GeneIDi158983.
KEGGihsa:158983.
UCSCiuc004elr.4. human.

Organism-specific databases

CTDi158983.
GeneCardsiH2BFWT.
H-InvDBHIX0016960.
HIX0056199.
HGNCiHGNC:27252. H2BFWT.
HPAiHPA056289.
MIMi300507. gene.
neXtProtiNX_Q7Z2G1.
PharmGKBiPA134930988.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1744. Eukaryota.
ENOG4111NV5. LUCA.
HOGENOMiHOG000231213.
InParanoidiQ7Z2G1.
KOiK11252.
OrthoDBiEOG7Z95PV.
PhylomeDBiQ7Z2G1.
TreeFamiTF300212.

Miscellaneous databases

GeneWikiiH2BFWT.
GenomeRNAii158983.
NextBioi87858.
PROiQ7Z2G1.
SOURCEiSearch...

Gene expression databases

BgeeiQ7Z2G1.
CleanExiHS_H2BFWT.

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. "Novel human testis-specific histone H2B encoded by the interrupted gene on the X chromosome."
    Churikov D., Siino J., Svetlova M., Zhang K., Gineitis A., Bradbury E.M., Zalensky A.
    Genomics 84:745-756(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], TISSUE SPECIFICITY, SUBCELLULAR LOCATION, VARIANT HIS-123.
    Tissue: Testis.
  2. "The DNA sequence of the human X chromosome."
    Ross M.T., Grafham D.V., Coffey A.J., Scherer S., McLay K., Muzny D., Platzer M., Howell G.R., Burrows C., Bird C.P., Frankish A., Lovell F.L., Howe K.L., Ashurst J.L., Fulton R.S., Sudbrak R., Wen G., Jones M.C.
    , Hurles M.E., Andrews T.D., Scott C.E., Searle S., Ramser J., Whittaker A., Deadman R., Carter N.P., Hunt S.E., Chen R., Cree A., Gunaratne P., Havlak P., Hodgson A., Metzker M.L., Richards S., Scott G., Steffen D., Sodergren E., Wheeler D.A., Worley K.C., Ainscough R., Ambrose K.D., Ansari-Lari M.A., Aradhya S., Ashwell R.I., Babbage A.K., Bagguley C.L., Ballabio A., Banerjee R., Barker G.E., Barlow K.F., Barrett I.P., Bates K.N., Beare D.M., Beasley H., Beasley O., Beck A., Bethel G., Blechschmidt K., Brady N., Bray-Allen S., Bridgeman A.M., Brown A.J., Brown M.J., Bonnin D., Bruford E.A., Buhay C., Burch P., Burford D., Burgess J., Burrill W., Burton J., Bye J.M., Carder C., Carrel L., Chako J., Chapman J.C., Chavez D., Chen E., Chen G., Chen Y., Chen Z., Chinault C., Ciccodicola A., Clark S.Y., Clarke G., Clee C.M., Clegg S., Clerc-Blankenburg K., Clifford K., Cobley V., Cole C.G., Conquer J.S., Corby N., Connor R.E., David R., Davies J., Davis C., Davis J., Delgado O., Deshazo D., Dhami P., Ding Y., Dinh H., Dodsworth S., Draper H., Dugan-Rocha S., Dunham A., Dunn M., Durbin K.J., Dutta I., Eades T., Ellwood M., Emery-Cohen A., Errington H., Evans K.L., Faulkner L., Francis F., Frankland J., Fraser A.E., Galgoczy P., Gilbert J., Gill R., Gloeckner G., Gregory S.G., Gribble S., Griffiths C., Grocock R., Gu Y., Gwilliam R., Hamilton C., Hart E.A., Hawes A., Heath P.D., Heitmann K., Hennig S., Hernandez J., Hinzmann B., Ho S., Hoffs M., Howden P.J., Huckle E.J., Hume J., Hunt P.J., Hunt A.R., Isherwood J., Jacob L., Johnson D., Jones S., de Jong P.J., Joseph S.S., Keenan S., Kelly S., Kershaw J.K., Khan Z., Kioschis P., Klages S., Knights A.J., Kosiura A., Kovar-Smith C., Laird G.K., Langford C., Lawlor S., Leversha M., Lewis L., Liu W., Lloyd C., Lloyd D.M., Loulseged H., Loveland J.E., Lovell J.D., Lozado R., Lu J., Lyne R., Ma J., Maheshwari M., Matthews L.H., McDowall J., McLaren S., McMurray A., Meidl P., Meitinger T., Milne S., Miner G., Mistry S.L., Morgan M., Morris S., Mueller I., Mullikin J.C., Nguyen N., Nordsiek G., Nyakatura G., O'dell C.N., Okwuonu G., Palmer S., Pandian R., Parker D., Parrish J., Pasternak S., Patel D., Pearce A.V., Pearson D.M., Pelan S.E., Perez L., Porter K.M., Ramsey Y., Reichwald K., Rhodes S., Ridler K.A., Schlessinger D., Schueler M.G., Sehra H.K., Shaw-Smith C., Shen H., Sheridan E.M., Shownkeen R., Skuce C.D., Smith M.L., Sotheran E.C., Steingruber H.E., Steward C.A., Storey R., Swann R.M., Swarbreck D., Tabor P.E., Taudien S., Taylor T., Teague B., Thomas K., Thorpe A., Timms K., Tracey A., Trevanion S., Tromans A.C., d'Urso M., Verduzco D., Villasana D., Waldron L., Wall M., Wang Q., Warren J., Warry G.L., Wei X., West A., Whitehead S.L., Whiteley M.N., Wilkinson J.E., Willey D.L., Williams G., Williams L., Williamson A., Williamson H., Wilming L., Woodmansey R.L., Wray P.W., Yen J., Zhang J., Zhou J., Zoghbi H., Zorilla S., Buck D., Reinhardt R., Poustka A., Rosenthal A., Lehrach H., Meindl A., Minx P.J., Hillier L.W., Willard H.F., Wilson R.K., Waterston R.H., Rice C.M., Vaudin M., Coulson A., Nelson D.L., Weinstock G., Sulston J.E., Durbin R.M., Hubbard T., Gibbs R.A., Beck S., Rogers J., Bentley D.R.
    Nature 434:325-337(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT HIS-123.
    Tissue: Testis.
  5. "The NH2 tail of the novel histone variant H2BFWT exhibits properties distinct from conventional H2B with respect to the assembly of mitotic chromosomes."
    Boulard M., Gautier T., Mbele G.O., Gerson V., Hamiche A., Angelov D., Bouvet P., Dimitrov S.
    Mol. Cell. Biol. 26:1518-1526(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.

Entry informationi

Entry nameiH2BWT_HUMAN
AccessioniPrimary (citable) accession number: Q7Z2G1
Secondary accession number(s): B1AK72, Q147W3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: July 11, 2006
Last sequence update: February 10, 2009
Last modified: March 16, 2016
This is version 102 of the entry and version 2 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

In contrast to other H2B histones, it does not contain the conserved residue in C-terminus that is the target of monoubiquitination.
Ortholog in primates, but not in rodents.

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome X
    Human chromosome X: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. 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.