Q71UI9 (H2AV_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Histone H2A.V

Alternative name(s):
H2A.F/Z

Gene names

Name:	H2AFV
Synonyms:	H2AV

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	128 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Variant histone H2A which replaces conventional H2A in a subset of nucleosomes. 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. May be involved in the formation of constitutive heterochromatin. May be required for chromosome segregation during cell division By similarity.
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. H2A or its variant H2AFV forms an heterodimer with H2B By similarity.
Subcellular location	Nucleus By similarity. Chromosome By similarity.
Post-translational modification	Monoubiquitination of Lys-122 gives a specific tag for epigenetic transcriptional repression By similarity. Acetylated on Lys-5, Lys-8 and Lys-12 during interphase. Acetylation disappears at mitosis By similarity.
Sequence similarities	Belongs to the histone H2A family.
Mass spectrometry	Molecular mass is 13369.4 Da from positions 2 - 128. Determined by ESI. Monoisotopic, not modified. Ref.5
Sequence caution	The sequence BAD92238.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Chromosome Nucleosome core Nucleus
Coding sequence diversity	Polymorphism
Ligand	DNA-binding
PTM	Acetylation Isopeptide bond Ubl conjugation
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	nucleosome assembly Inferred from electronic annotation. Source: InterPro
Cellular component	nucleosome Inferred from electronic annotation. Source: UniProtKB-KW nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
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
	Initiator methionine	1	1	Removed By similarity
	Chain	2 – 128	127	Histone H2A.V		PRO_0000239068
Amino acid modifications
	Modified residue	5	1	N6-acetyllysine Ref.6
	Modified residue	8	1	N6-acetyllysine Ref.6
	Modified residue	12	1	N6-acetyllysine Ref.6
	Modified residue	14	1	N6-acetyllysine Ref.6
	Cross-link	122		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin) By similarity
Natural variations
	Natural variant	125	1	Q → R. Corresponds to variant rs1802437 [ dbSNP | Ensembl ].		VAR_059312

Sequences

	Sequence		Length	Mass (Da)
	Q71UI9 [UniParc]. Last modified January 23, 2007. Version 3. Checksum: 1F3C388F6854041C	FASTA	128	13,509
	10 20 30 40 50 60 MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT AAVYSAAILE 70 80 90 100 110 120 YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG KKGQQKTA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Novel human member of the variant histone family." Groitl P., Wolf H., Niller H.H. Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F. Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain.
[3]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed: 12853948] [Abstract] 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]. Tissue: Kidney, Skin and Uterus.
[5]	"Precise characterization of human histones in the H2A gene family by top down mass spectrometry." Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L. J. Proteome Res. 5:248-253(2006) [PubMed: 16457589] [Abstract] Cited for: MASS SPECTROMETRY.
[6]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T., Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y. Mol. Cell 23:607-618(2006) [PubMed: 16916647] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-5; LYS-8; LYS-12 AND LYS-14, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AF081192 mRNA. Translation: AAC31938.1. AB209001 mRNA. Translation: BAD92238.1. Different initiation. AC004854 Genomic DNA. Translation: AAS00365.1. BC000098 mRNA. Translation: AAH00098.1. BC004274 mRNA. Translation: AAH04274.3. BC014885 mRNA. Translation: AAH14885.1. BC070169 mRNA. Translation: AAH70169.1.
IPI	IPI00018278.
RefSeq	NP_036544.1. NM_012412.4. NP_619541.1. NM_138635.3. NP_958844.1. NM_201436.2. NP_958924.1. NM_201516.2. NP_958925.1. NM_201517.2.
UniGene	Hs.488189.
3D structure databases
ProteinModelPortal	Q71UI9.
SMR	Q71UI9. Positions 17-123.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q71UI9. 2 interactions.
STRING	Q71UI9.
PTM databases
PhosphoSite	Q71UI9.
Polymorphism databases
DMDM	74749787.
Proteomic databases
PRIDE	Q71UI9.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000308153; ENSP00000308405; ENSG00000105968. ENST00000421098; ENSP00000415202; ENSG00000105968.
GeneID	94239.
KEGG	hsa:94239.
UCSC	uc003tma.2. human.
Organism-specific databases
CTD	94239.
GeneCards	GC07M044833.
HGNC	HGNC:20664. H2AFV.
neXtProt	NX_Q71UI9.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG20323.
GeneTree	ENSGT00540000069960.
HOGENOM	HBG610736.
HOVERGEN	HBG009342.
InParanoid	Q71UI9.
PhylomeDB	Q71UI9.
Gene expression databases
ArrayExpress	Q71UI9.
Bgee	Q71UI9.
CleanEx	HS_H2AFV.
Genevestigator	Q71UI9.
GermOnline	ENSG00000105968. Homo sapiens.
Family and domain databases
InterPro	IPR009072. Histone-fold. IPR007125. Histone_core_D. IPR002119. Histone_H2A. [Graphical view]
Gene3D	G3DSA:1.10.20.10. Histone-fold. 1 hit.
KO	K11251.
Pfam	PF00125. Histone. 1 hit. [Graphical view]
PRINTS	PR00620. HISTONEH2A.
SMART	SM00414. H2A. 1 hit. [Graphical view]
SUPFAM	SSF47113. Histone-fold. 1 hit.
PROSITE	PS00046. HISTONE_H2A. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	78481.

Entry information

Entry name

H2AV_HUMAN

Accession

Primary (citable) accession number: Q71UI9
Secondary accession number(s): Q59GV8, Q6PK98

Entry history

Integrated into UniProtKB/Swiss-Prot:	May 30, 2006
Last sequence update:	January 23, 2007
Last modified:	January 25, 2012
This is version 82 of the entry and version 3 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.