Q7Z2G1 (H2BWT_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2B type W-T

Alternative name(s):
H2B histone family member W testis-specific

Gene names

Name:

H2BFWT

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	175 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.5
Subunit structure	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.
Subcellular location	Nucleus membrane. Chromosome Ref.1.
Tissue specificity	Testis-specific. Present in sperm cells (at protein level). Ref.1
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.
Sequence similarities	Belongs to the histone H2B family.

Ontologies

Keywords
Cellular component	Chromosome Membrane Nucleosome core Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	nuclear membrane Inferred from electronic annotation. Source: UniProtKB-SubCell nucleosome Inferred from electronic annotation. Source: UniProtKB-KW
Molecular function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 175	175	Histone H2B type W-T		PRO_0000244828
Natural variations
	Natural variant	87	1	R → W. Corresponds to variant rs17332043 [ dbSNP | Ensembl ].		VAR_049315
	Natural variant	123	1	R → H. Ref.1 Ref.4 Corresponds to variant rs553509 [ dbSNP | Ensembl ].		VAR_054318

Sequences

	Sequence		Length	Mass (Da)
	Q7Z2G1 [UniParc]. Last modified February 10, 2009. Version 2. Checksum: C47C922CBBE96BCC	FASTA	175	19,618
	10 20 30 40 50 60 MLRTEVPRLP RSTTAIVWSC HLMATASAMA GPSSETTSEE QLITQEPKEA NSTTSQKQSK 70 80 90 100 110 120 QRKRGRHGPR RCHSNCRGDS FATYFRRVLK QVHQGLSLSR EAVSVMDSLV HDILDRIATE 130 140 150 160 170 AGRLARSTKR QTITAWETRM AVRLLLPGQM GKLAESEGTK AVLRTSLYAI QQQRK

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 15475252] [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: 15772651] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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: 15489334] [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: 16449661] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00873035.
RefSeq	NP_001002916.2. NM_001002916.3.
UniGene	Hs.127778.
3D structure databases
ProteinModelPortal	Q7Z2G1.
SMR	Q7Z2G1. Positions 76-168.
ModBase	Search...
Protein-protein interaction databases
STRING	Q7Z2G1.
Polymorphism databases
DMDM	223590216.
Proteomic databases
PRIDE	Q7Z2G1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000217926; ENSP00000354723; ENSG00000123569.
GeneID	158983.
KEGG	hsa:158983.
UCSC	uc004elr.1. human.
Organism-specific databases
CTD	158983.
GeneCards	GC0XM103265.
H-InvDB	HIX0016960.
HGNC	HGNC:27252. H2BFWT.
MIM	300507. gene.
neXtProt	NX_Q7Z2G1.
PharmGKB	PA134930988.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG10958.
GeneTree	ENSGT00530000064214.
OMA	SAMAGPS.
OrthoDB	EOG4G7C0J.
PhylomeDB	Q7Z2G1.
Gene expression databases
ArrayExpress	Q7Z2G1.
Bgee	Q7Z2G1.
CleanEx	HS_H2BFWT.
Genevestigator	Q7Z2G1.
Family and domain databases
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR000558. Histone_H2B. [Graphical view]
Gene3D	G3DSA:1.10.20.10. Histone-fold. 1 hit.
KO	K11252.
PANTHER	PTHR23428. Histone_H2B. 1 hit.
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00621. HISTONEH2B.
SMART	SM00427. H2B. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00357. HISTONE_H2B. False negative. [Graphical view]
ProtoNet	Search...
Other
NextBio	87858.
SOURCE	Search...

Entry information

Entry name

H2BWT_HUMAN

Accession

Primary (citable) accession number: Q7Z2G1
Secondary accession number(s): B1AK72, Q147W3

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 11, 2006
Last sequence update:	February 10, 2009
Last modified:	January 25, 2012
This is version 69 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.