Full text data of H2AFV
H2AFV
(H2AV)
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Histone H2A.V (H2A.F/Z)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Histone H2A.V (H2A.F/Z)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00018278
IPI00018278 Histone H2A.F/Z variant, isoform 1 DNA binding, chromosome organization and biogenesis, nucleosome assembly soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nucleus n/a expected molecular weight found in band found in band around 25 kDa
IPI00018278 Histone H2A.F/Z variant, isoform 1 DNA binding, chromosome organization and biogenesis, nucleosome assembly soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a nucleus n/a expected molecular weight found in band found in band around 25 kDa
UniProt
Q71UI9
ID H2AV_HUMAN Reviewed; 128 AA.
AC Q71UI9; A6NFA8; A6NKY0; A6NN01; A8MQC5; Q59GV8; Q6PK98;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Histone H2A.V;
DE AltName: Full=H2A.F/Z;
GN Name=H2AFV; Synonyms=H2AV;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Groitl P., Wolf H., Niller H.H.;
RT "Novel human member of the variant histone family.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Kidney, Ovarian adenocarcinoma, Prostatic carcinoma, Skin, and
RC Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP MASS SPECTROMETRY.
RX PubMed=16457589; DOI=10.1021/pr050269n;
RA Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.;
RT "Precise characterization of human histones in the H2A gene family by
RT top down mass spectrometry.";
RL J. Proteome Res. 5:248-253(2006).
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. Nucleosomes wrap and compact DNA into
CC chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central
CC role in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a
CC complex set of post-translational modifications of histones, also
CC called histone code, and nucleosome remodeling. May be involved in
CC the formation of constitutive heterochromatin. May be required for
CC chromosome segregation during cell division (By similarity).
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC approximately 147 bp of DNA. H2A or its variant H2AFV forms a
CC heterodimer with H2B (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q71UI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q71UI9-2; Sequence=VSP_042855;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q71UI9-3; Sequence=VSP_044633;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q71UI9-4; Sequence=VSP_045232;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q71UI9-5; Sequence=VSP_046783;
CC Note=No experimental confirmation available;
CC -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for
CC epigenetic transcriptional repression (By similarity).
CC -!- PTM: Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.
CC Acetylation disappears at mitosis (By similarity).
CC -!- MASS SPECTROMETRY: Mass=13369.4; Method=Electrospray; Range=2-128;
CC Note=Monoisotopic, not modified; Source=PubMed:16457589;
CC -!- SIMILARITY: Belongs to the histone H2A family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92238.1; Type=Erroneous initiation;
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DR EMBL; AF081192; AAC31938.1; -; mRNA.
DR EMBL; AK023973; BAG51243.1; -; mRNA.
DR EMBL; AB209001; BAD92238.1; ALT_INIT; mRNA.
DR EMBL; AC004854; AAS00365.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61075.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61077.1; -; Genomic_DNA.
DR EMBL; BC000098; AAH00098.1; -; mRNA.
DR EMBL; BC004274; AAH04274.3; -; mRNA.
DR EMBL; BC014885; AAH14885.1; -; mRNA.
DR EMBL; BC070169; AAH70169.1; -; mRNA.
DR EMBL; BE742590; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU543626; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_036544.1; NM_012412.4.
DR RefSeq; NP_619541.1; NM_138635.3.
DR RefSeq; NP_958844.1; NM_201436.2.
DR RefSeq; NP_958924.1; NM_201516.2.
DR RefSeq; NP_958925.1; NM_201517.2.
DR UniGene; Hs.488189; -.
DR ProteinModelPortal; Q71UI9; -.
DR SMR; Q71UI9; 17-123.
DR IntAct; Q71UI9; 3.
DR MINT; MINT-4828370; -.
DR STRING; 9606.ENSP00000308405; -.
DR PhosphoSite; Q71UI9; -.
DR DMDM; 74749787; -.
DR PaxDb; Q71UI9; -.
DR PRIDE; Q71UI9; -.
DR DNASU; 94239; -.
DR Ensembl; ENST00000222690; ENSP00000222690; ENSG00000105968.
DR Ensembl; ENST00000308153; ENSP00000308405; ENSG00000105968.
DR Ensembl; ENST00000349299; ENSP00000342714; ENSG00000105968.
DR Ensembl; ENST00000350771; ENSP00000340708; ENSG00000105968.
DR Ensembl; ENST00000381124; ENSP00000370516; ENSG00000105968.
DR GeneID; 94239; -.
DR KEGG; hsa:94239; -.
DR UCSC; uc003tmd.2; human.
DR CTD; 94239; -.
DR GeneCards; GC07M044833; -.
DR HGNC; HGNC:20664; H2AFV.
DR HPA; HPA045242; -.
DR neXtProt; NX_Q71UI9; -.
DR PharmGKB; PA134895050; -.
DR eggNOG; COG5262; -.
DR HOGENOM; HOG000234652; -.
DR HOVERGEN; HBG009342; -.
DR InParanoid; Q71UI9; -.
DR KO; K11251; -.
DR OMA; GNASKDM; -.
DR PhylomeDB; Q71UI9; -.
DR ChiTaRS; H2AFV; human.
DR GeneWiki; H2AFV; -.
DR GenomeRNAi; 94239; -.
DR NextBio; 78481; -.
DR PRO; PR:Q71UI9; -.
DR ArrayExpress; Q71UI9; -.
DR Bgee; Q71UI9; -.
DR CleanEx; HS_H2AFV; -.
DR Genevestigator; Q71UI9; -.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_core_D.
DR InterPro; IPR002119; Histone_H2A.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; Complete proteome;
KW DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 128 Histone H2A.V.
FT /FTId=PRO_0000239068.
FT MOD_RES 5 5 N6-acetyllysine (By similarity).
FT MOD_RES 8 8 N6-acetyllysine (By similarity).
FT MOD_RES 12 12 N6-acetyllysine (By similarity).
FT CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin) (By
FT similarity).
FT VAR_SEQ 1 27 MAGGKAGKDSGKAKAKAVSRSQRAGLQ -> M (in
FT isoform 4).
FT /FTId=VSP_045232.
FT VAR_SEQ 28 65 Missing (in isoform 3).
FT /FTId=VSP_044633.
FT VAR_SEQ 67 128 Missing (in isoform 5).
FT /FTId=VSP_046783.
FT VAR_SEQ 109 128 GVIPHIHKSLIGKKGQQKTA -> EKRRCS (in
FT isoform 2).
FT /FTId=VSP_042855.
FT VARIANT 125 125 Q -> R (in dbSNP:rs1802437).
FT /FTId=VAR_059312.
SQ SEQUENCE 128 AA; 13509 MW; 1F3C388F6854041C CRC64;
MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTA
//
ID H2AV_HUMAN Reviewed; 128 AA.
AC Q71UI9; A6NFA8; A6NKY0; A6NN01; A8MQC5; Q59GV8; Q6PK98;
DT 30-MAY-2006, integrated into UniProtKB/Swiss-Prot.
read moreDT 23-JAN-2007, sequence version 3.
DT 22-JAN-2014, entry version 100.
DE RecName: Full=Histone H2A.V;
DE AltName: Full=H2A.F/Z;
GN Name=H2AFV; Synonyms=H2AV;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RA Groitl P., Wolf H., Niller H.H.;
RT "Novel human member of the variant histone family.";
RL Submitted (JUL-1998) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Brain;
RA Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S.,
RA Ohara O., Nagase T., Kikuno R.F.;
RL Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12853948; DOI=10.1038/nature01782;
RA Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R.,
RA Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H.,
RA Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A.,
RA Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J.,
RA Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A.,
RA Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S.,
RA Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M.,
RA Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C.,
RA Latreille P., Miller N., Johnson D., Murray J., Woessner J.P.,
RA Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J.,
RA Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L.,
RA Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R.,
RA Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K.,
RA Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S.,
RA Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M.,
RA Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R.,
RA Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D.,
RA Waterston R.H., Wilson R.K.;
RT "The DNA sequence of human chromosome 7.";
RL Nature 424:157-164(2003).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1; 3 AND 4).
RC TISSUE=Kidney, Ovarian adenocarcinoma, Prostatic carcinoma, Skin, and
RC Uterus;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP MASS SPECTROMETRY.
RX PubMed=16457589; DOI=10.1021/pr050269n;
RA Boyne M.T. II, Pesavento J.J., Mizzen C.A., Kelleher N.L.;
RT "Precise characterization of human histones in the H2A gene family by
RT top down mass spectrometry.";
RL J. Proteome Res. 5:248-253(2006).
CC -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC subset of nucleosomes. Nucleosomes wrap and compact DNA into
CC chromatin, limiting DNA accessibility to the cellular machineries
CC which require DNA as a template. Histones thereby play a central
CC role in transcription regulation, DNA repair, DNA replication and
CC chromosomal stability. DNA accessibility is regulated via a
CC complex set of post-translational modifications of histones, also
CC called histone code, and nucleosome remodeling. May be involved in
CC the formation of constitutive heterochromatin. May be required for
CC chromosome segregation during cell division (By similarity).
CC -!- SUBUNIT: The nucleosome is a histone octamer containing two
CC molecules each of H2A, H2B, H3 and H4 assembled in one H3-H4
CC heterotetramer and two H2A-H2B heterodimers. The octamer wraps
CC approximately 147 bp of DNA. H2A or its variant H2AFV forms a
CC heterodimer with H2B (By similarity).
CC -!- SUBCELLULAR LOCATION: Nucleus (By similarity). Chromosome (By
CC similarity).
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=5;
CC Name=1;
CC IsoId=Q71UI9-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q71UI9-2; Sequence=VSP_042855;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=Q71UI9-3; Sequence=VSP_044633;
CC Note=No experimental confirmation available;
CC Name=4;
CC IsoId=Q71UI9-4; Sequence=VSP_045232;
CC Note=No experimental confirmation available;
CC Name=5;
CC IsoId=Q71UI9-5; Sequence=VSP_046783;
CC Note=No experimental confirmation available;
CC -!- PTM: Monoubiquitination of Lys-122 gives a specific tag for
CC epigenetic transcriptional repression (By similarity).
CC -!- PTM: Acetylated on Lys-5, Lys-8 and Lys-12 during interphase.
CC Acetylation disappears at mitosis (By similarity).
CC -!- MASS SPECTROMETRY: Mass=13369.4; Method=Electrospray; Range=2-128;
CC Note=Monoisotopic, not modified; Source=PubMed:16457589;
CC -!- SIMILARITY: Belongs to the histone H2A family.
CC -!- SEQUENCE CAUTION:
CC Sequence=BAD92238.1; Type=Erroneous initiation;
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DR EMBL; AF081192; AAC31938.1; -; mRNA.
DR EMBL; AK023973; BAG51243.1; -; mRNA.
DR EMBL; AB209001; BAD92238.1; ALT_INIT; mRNA.
DR EMBL; AC004854; AAS00365.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61075.1; -; Genomic_DNA.
DR EMBL; CH471128; EAW61077.1; -; Genomic_DNA.
DR EMBL; BC000098; AAH00098.1; -; mRNA.
DR EMBL; BC004274; AAH04274.3; -; mRNA.
DR EMBL; BC014885; AAH14885.1; -; mRNA.
DR EMBL; BC070169; AAH70169.1; -; mRNA.
DR EMBL; BE742590; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BU543626; -; NOT_ANNOTATED_CDS; mRNA.
DR RefSeq; NP_036544.1; NM_012412.4.
DR RefSeq; NP_619541.1; NM_138635.3.
DR RefSeq; NP_958844.1; NM_201436.2.
DR RefSeq; NP_958924.1; NM_201516.2.
DR RefSeq; NP_958925.1; NM_201517.2.
DR UniGene; Hs.488189; -.
DR ProteinModelPortal; Q71UI9; -.
DR SMR; Q71UI9; 17-123.
DR IntAct; Q71UI9; 3.
DR MINT; MINT-4828370; -.
DR STRING; 9606.ENSP00000308405; -.
DR PhosphoSite; Q71UI9; -.
DR DMDM; 74749787; -.
DR PaxDb; Q71UI9; -.
DR PRIDE; Q71UI9; -.
DR DNASU; 94239; -.
DR Ensembl; ENST00000222690; ENSP00000222690; ENSG00000105968.
DR Ensembl; ENST00000308153; ENSP00000308405; ENSG00000105968.
DR Ensembl; ENST00000349299; ENSP00000342714; ENSG00000105968.
DR Ensembl; ENST00000350771; ENSP00000340708; ENSG00000105968.
DR Ensembl; ENST00000381124; ENSP00000370516; ENSG00000105968.
DR GeneID; 94239; -.
DR KEGG; hsa:94239; -.
DR UCSC; uc003tmd.2; human.
DR CTD; 94239; -.
DR GeneCards; GC07M044833; -.
DR HGNC; HGNC:20664; H2AFV.
DR HPA; HPA045242; -.
DR neXtProt; NX_Q71UI9; -.
DR PharmGKB; PA134895050; -.
DR eggNOG; COG5262; -.
DR HOGENOM; HOG000234652; -.
DR HOVERGEN; HBG009342; -.
DR InParanoid; Q71UI9; -.
DR KO; K11251; -.
DR OMA; GNASKDM; -.
DR PhylomeDB; Q71UI9; -.
DR ChiTaRS; H2AFV; human.
DR GeneWiki; H2AFV; -.
DR GenomeRNAi; 94239; -.
DR NextBio; 78481; -.
DR PRO; PR:Q71UI9; -.
DR ArrayExpress; Q71UI9; -.
DR Bgee; Q71UI9; -.
DR CleanEx; HS_H2AFV; -.
DR Genevestigator; Q71UI9; -.
DR GO; GO:0000786; C:nucleosome; IEA:UniProtKB-KW.
DR GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR GO; GO:0003677; F:DNA binding; IEA:UniProtKB-KW.
DR GO; GO:0006334; P:nucleosome assembly; IEA:InterPro.
DR Gene3D; 1.10.20.10; -; 1.
DR InterPro; IPR009072; Histone-fold.
DR InterPro; IPR007125; Histone_core_D.
DR InterPro; IPR002119; Histone_H2A.
DR Pfam; PF00125; Histone; 1.
DR PRINTS; PR00620; HISTONEH2A.
DR SMART; SM00414; H2A; 1.
DR SUPFAM; SSF47113; SSF47113; 1.
DR PROSITE; PS00046; HISTONE_H2A; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Chromosome; Complete proteome;
KW DNA-binding; Isopeptide bond; Nucleosome core; Nucleus; Polymorphism;
KW Reference proteome; Ubl conjugation.
FT CHAIN 1 128 Histone H2A.V.
FT /FTId=PRO_0000239068.
FT MOD_RES 5 5 N6-acetyllysine (By similarity).
FT MOD_RES 8 8 N6-acetyllysine (By similarity).
FT MOD_RES 12 12 N6-acetyllysine (By similarity).
FT CROSSLNK 122 122 Glycyl lysine isopeptide (Lys-Gly)
FT (interchain with G-Cter in ubiquitin) (By
FT similarity).
FT VAR_SEQ 1 27 MAGGKAGKDSGKAKAKAVSRSQRAGLQ -> M (in
FT isoform 4).
FT /FTId=VSP_045232.
FT VAR_SEQ 28 65 Missing (in isoform 3).
FT /FTId=VSP_044633.
FT VAR_SEQ 67 128 Missing (in isoform 5).
FT /FTId=VSP_046783.
FT VAR_SEQ 109 128 GVIPHIHKSLIGKKGQQKTA -> EKRRCS (in
FT isoform 2).
FT /FTId=VSP_042855.
FT VARIANT 125 125 Q -> R (in dbSNP:rs1802437).
FT /FTId=VAR_059312.
SQ SEQUENCE 128 AA; 13509 MW; 1F3C388F6854041C CRC64;
MAGGKAGKDS GKAKAKAVSR SQRAGLQFPV GRIHRHLKTR TTSHGRVGAT AAVYSAAILE
YLTAEVLELA GNASKDLKVK RITPRHLQLA IRGDEELDSL IKATIAGGGV IPHIHKSLIG
KKGQQKTA
//