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O75367

- H2AY_HUMAN

UniProt

O75367 - H2AY_HUMAN

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Protein
Core histone macro-H2A.1
Gene
H2AFY, MACROH2A1
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

Variant histone H2A which replaces conventional H2A in a subset of nucleosomes where it represses transcription. 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. Involved in stable X chromosome inactivation. Inhibits the binding of transcription factors and interferes with the activity of remodeling SWI/SNF complexes. Inhibits histone acetylation by EP300 and recruits class I HDACs, which induces a hypoacetylated state of chromatin. In addition, isoform 1, but not isoform 2, binds ADP-ribose and O-acetyl-ADP-ribose, and may be involved in ADP-ribose-mediated chromatin modulation.5 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB
  2. chromatin DNA binding Source: UniProt
  3. double-stranded methylated DNA binding Source: UniProt
  4. protein binding Source: IntAct
  5. protein kinase binding Source: UniProt
  6. protein serine/threonine kinase inhibitor activity Source: UniProt
  7. rDNA binding Source: UniProt
  8. transcription regulatory region DNA binding Source: UniProt

GO - Biological processi

  1. chromatin modification Source: UniProtKB-KW
  2. dosage compensation Source: MGI
  3. establishment of protein localization to chromatin Source: UniProt
  4. negative regulation of cell cycle G2/M phase transition Source: UniProt
  5. negative regulation of gene expression, epigenetic Source: UniProt
  6. negative regulation of histone phosphorylation Source: UniProt
  7. negative regulation of protein serine/threonine kinase activity Source: UniProt
  8. negative regulation of transcription from RNA polymerase II promoter Source: UniProt
  9. negative regulation of transcription of nuclear large rRNA transcript from RNA polymerase I promoter Source: UniProt
  10. nucleosome assembly Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Core histone macro-H2A.1
Short name:
Histone macroH2A1
Short name:
mH2A1
Alternative name(s):
Histone H2A.y
Short name:
H2A/y
Medulloblastoma antigen MU-MB-50.205
Gene namesi
Name:H2AFY
Synonyms:MACROH2A1
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 5

Organism-specific databases

HGNCiHGNC:4740. H2AFY.

Subcellular locationi

Nucleus. Chromosome
Note: Enriched in inactive X chromosome chromatin and in senescence-associated heterochromatin.3 Publications

GO - Cellular componenti

  1. Barr body Source: MGI
  2. condensed chromosome Source: Ensembl
  3. extracellular vesicular exosome Source: UniProt
  4. nuclear chromatin Source: UniProt
  5. nucleolus Source: UniProt
  6. nucleosome Source: UniProtKB
  7. nucleus Source: UniProt
  8. sex chromatin Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Chromosome, Nucleosome core, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA29117.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 372372Core histone macro-H2A.1
PRO_0000055318Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei18 – 181N6-methyllysine1 Publication
Modified residuei116 – 1161N6-acetyllysine; alternate By similarity
Cross-linki116 – 116Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin); alternate1 Publication
Cross-linki117 – 117Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei123 – 1231N6,N6-dimethyllysine; alternate Inferred
Modified residuei123 – 1231N6-acetyllysine; alternate By similarity
Modified residuei129 – 1291Phosphothreonine6 Publications
Modified residuei170 – 1701Phosphoserine3 Publications
Modified residuei173 – 1731Phosphoserine1 Publication
Modified residuei178 – 1781Phosphothreonine4 Publications

Post-translational modificationi

Monoubiquitinated at either Lys-116 or Lys-117. May also be polyubiquitinated. Ubiquitination is mediated by the CUL3/SPOP E3 complex and does not promote proteasomal degradation. Instead, it is required for enrichment in inactive X chromosome chromatin.

Keywords - PTMi

Acetylation, Isopeptide bond, Methylation, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiO75367.
PaxDbiO75367.
PRIDEiO75367.

2D gel databases

SWISS-2DPAGEO75367.

PTM databases

PhosphoSiteiO75367.

Miscellaneous databases

PMAP-CutDBO75367.

Expressioni

Tissue specificityi

Ubiquitous.1 Publication

Gene expression databases

ArrayExpressiO75367.
BgeeiO75367.
CleanExiHS_H2AFY.
GenevestigatoriO75367.

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. Interacts with HDAC1 and HDAC2 By similarity. Interacts with SPOP. Part of a complex consisting of H2AFY, CUL3 and SPOP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
ERBB2P046266EBI-2868511,EBI-641062

Protein-protein interaction databases

BioGridi114927. 37 interactions.
DIPiDIP-44283N.
IntActiO75367. 6 interactions.
MINTiMINT-2866965.
STRINGi9606.ENSP00000353806.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi15 – 195
Helixi25 – 3511
Beta strandi36 – 383
Beta strandi39 – 413
Helixi44 – 7027
Beta strandi74 – 763
Helixi78 – 869
Helixi89 – 946
Turni95 – 973
Beta strandi98 – 1003
Helixi111 – 1133
Beta strandi174 – 1774
Beta strandi185 – 1906
Beta strandi196 – 2027
Helixi204 – 2063
Beta strandi213 – 2197
Helixi227 – 25226
Beta strandi260 – 2645
Beta strandi268 – 27710
Helixi286 – 30318
Beta strandi307 – 3115
Beta strandi315 – 3195
Helixi323 – 34018
Beta strandi341 – 3433
Beta strandi348 – 3558
Helixi356 – 36712

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1U35X-ray3.00C/G1-120[»]
1ZR3X-ray1.66A/B/C/D162-372[»]
1ZR5X-ray2.92A/B161-372[»]
2F8NX-ray2.90G1-120[»]
2FXKX-ray2.54A/B162-372[»]
3HQHX-ray2.30M167-181[»]
3HSVX-ray1.43M172-186[»]
3IIDX-ray1.90A162-372[»]
3IIFX-ray2.10A/B/C162-372[»]
3IVBX-ray1.75M167-181[»]
ProteinModelPortaliO75367.
SMRiO75367. Positions 10-117, 181-369.

Miscellaneous databases

EvolutionaryTraceiO75367.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini2 – 117116Histone H2A
Add
BLAST
Domaini184 – 370187Macro
Add
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi118 – 16245Lys-rich
Add
BLAST

Sequence similaritiesi

Contains 1 histone H2A domain.
Contains 1 Macro domain.

Phylogenomic databases

eggNOGiCOG2110.
HOVERGENiHBG009342.
InParanoidiO75367.
KOiK11251.
OMAiQVVQADI.
OrthoDBiEOG71G9VP.
PhylomeDBiO75367.
TreeFamiTF332276.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR021171. Core_histone_macro-H2A.
IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
IPR002589. Macro_dom.
[Graphical view]
PfamiPF00125. Histone. 1 hit.
PF01661. Macro. 1 hit.
[Graphical view]
PIRSFiPIRSF037942. Core_histone_macro-H2A. 1 hit.
PRINTSiPR00620. HISTONEH2A.
SMARTiSM00506. A1pp. 1 hit.
SM00414. H2A. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
PROSITEiPS51154. MACRO. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 2 (identifier: O75367-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

MSSRGGKKKS TKTSRSAKAG VIFPVGRMLR YIKKGHPKYR IGVGAPVYMA    50
AVLEYLTAEI LELAGNAARD NKKGRVTPRH ILLAVANDEE LNQLLKGVTI 100
ASGGVLPNIH PELLAKKRGS KGKLEAIITP PPAKKAKSPS QKKPVSKKAG 150
GKKGARKSKK KQGEVSKAAS ADSTTEGTPA DGFTVLSTKS LFLGQKLNLI 200
HSEISNLAGF EVEAIINPTN ADIDLKDDLG NTLEKKGGKE FVEAVLELRK 250
KNGPLEVAGA AVSAGHGLPA KFVIHCNSPV WGADKCEELL EKTVKNCLAL 300
ADDKKLKSIA FPSIGSGRNG FPKQTAAQLI LKAISSYFVS TMSSSIKTVY 350
FVLFDSESIG IYVQEMAKLD AN 372
Length:372
Mass (Da):39,617
Last modified:January 23, 2007 - v4
Checksum:i37DED989EF7E69DC
GO
Isoform 1 (identifier: O75367-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     198-229: NLIHSEISNLAGFEVEAIINPTNADIDLKDDL → QVVQADIASIDSDAVVHPTNTDFYIGGEV

Note: Specifically binds ADP-ribose and O-acetyl-ADP-ribose. Important residues for binding are Asp-203, Gly-224, Gly-314 and Phe-348.

Show »
Length:369
Mass (Da):39,184
Checksum:iD21A4CE6C7AA3BB1
GO
Isoform 3 (identifier: O75367-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     159-159: Missing.

Show »
Length:371
Mass (Da):39,489
Checksum:i54320BFD118454D1
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei159 – 1591Missing in isoform 3.
VSP_038379
Alternative sequencei198 – 22932NLIHS…LKDDL → QVVQADIASIDSDAVVHPTN TDFYIGGEV in isoform 1.
VSP_002056Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti186 – 1861L → F in BAB14565. 1 Publication
Sequence conflicti210 – 2101F → S in BAB14565. 1 Publication
Sequence conflicti225 – 2251L → P in AAC33433. 1 Publication
Sequence conflicti291 – 2911E → G in AAH95406. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF041483 mRNA. Translation: AAC33433.1.
AF044286 mRNA. Translation: AAC33434.1.
AF054174 mRNA. Translation: AAC39908.1.
AK023409 mRNA. Translation: BAB14565.1.
AC026691 Genomic DNA. No translation available.
BC013331 mRNA. Translation: AAH13331.1.
BC095406 mRNA. Translation: AAH95406.1.
AY134746 mRNA. Translation: AAN08620.1.
CCDSiCCDS4183.1. [O75367-3]
CCDS4184.1. [O75367-2]
CCDS4185.1. [O75367-1]
RefSeqiNP_001035248.1. NM_001040158.1. [O75367-3]
NP_004884.1. NM_004893.2. [O75367-3]
NP_613075.1. NM_138609.2. [O75367-2]
NP_613258.2. NM_138610.2. [O75367-1]
UniGeneiHs.420272.
Hs.599225.

Genome annotation databases

EnsembliENST00000304332; ENSP00000302572; ENSG00000113648. [O75367-3]
ENST00000312469; ENSP00000310169; ENSG00000113648. [O75367-2]
ENST00000510038; ENSP00000424971; ENSG00000113648. [O75367-1]
ENST00000511689; ENSP00000423563; ENSG00000113648. [O75367-1]
GeneIDi9555.
KEGGihsa:9555.
UCSCiuc003lam.1. human. [O75367-1]
uc003lan.1. human. [O75367-2]
uc003lao.1. human. [O75367-3]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AF041483 mRNA. Translation: AAC33433.1 .
AF044286 mRNA. Translation: AAC33434.1 .
AF054174 mRNA. Translation: AAC39908.1 .
AK023409 mRNA. Translation: BAB14565.1 .
AC026691 Genomic DNA. No translation available.
BC013331 mRNA. Translation: AAH13331.1 .
BC095406 mRNA. Translation: AAH95406.1 .
AY134746 mRNA. Translation: AAN08620.1 .
CCDSi CCDS4183.1. [O75367-3 ]
CCDS4184.1. [O75367-2 ]
CCDS4185.1. [O75367-1 ]
RefSeqi NP_001035248.1. NM_001040158.1. [O75367-3 ]
NP_004884.1. NM_004893.2. [O75367-3 ]
NP_613075.1. NM_138609.2. [O75367-2 ]
NP_613258.2. NM_138610.2. [O75367-1 ]
UniGenei Hs.420272.
Hs.599225.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1U35 X-ray 3.00 C/G 1-120 [» ]
1ZR3 X-ray 1.66 A/B/C/D 162-372 [» ]
1ZR5 X-ray 2.92 A/B 161-372 [» ]
2F8N X-ray 2.90 G 1-120 [» ]
2FXK X-ray 2.54 A/B 162-372 [» ]
3HQH X-ray 2.30 M 167-181 [» ]
3HSV X-ray 1.43 M 172-186 [» ]
3IID X-ray 1.90 A 162-372 [» ]
3IIF X-ray 2.10 A/B/C 162-372 [» ]
3IVB X-ray 1.75 M 167-181 [» ]
ProteinModelPortali O75367.
SMRi O75367. Positions 10-117, 181-369.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 114927. 37 interactions.
DIPi DIP-44283N.
IntActi O75367. 6 interactions.
MINTi MINT-2866965.
STRINGi 9606.ENSP00000353806.

PTM databases

PhosphoSitei O75367.

2D gel databases

SWISS-2DPAGE O75367.

Proteomic databases

MaxQBi O75367.
PaxDbi O75367.
PRIDEi O75367.

Protocols and materials databases

DNASUi 9555.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000304332 ; ENSP00000302572 ; ENSG00000113648 . [O75367-3 ]
ENST00000312469 ; ENSP00000310169 ; ENSG00000113648 . [O75367-2 ]
ENST00000510038 ; ENSP00000424971 ; ENSG00000113648 . [O75367-1 ]
ENST00000511689 ; ENSP00000423563 ; ENSG00000113648 . [O75367-1 ]
GeneIDi 9555.
KEGGi hsa:9555.
UCSCi uc003lam.1. human. [O75367-1 ]
uc003lan.1. human. [O75367-2 ]
uc003lao.1. human. [O75367-3 ]

Organism-specific databases

CTDi 9555.
GeneCardsi GC05M134669.
HGNCi HGNC:4740. H2AFY.
MIMi 610054. gene.
neXtProti NX_O75367.
PharmGKBi PA29117.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG2110.
HOVERGENi HBG009342.
InParanoidi O75367.
KOi K11251.
OMAi QVVQADI.
OrthoDBi EOG71G9VP.
PhylomeDBi O75367.
TreeFami TF332276.

Miscellaneous databases

ChiTaRSi H2AFY. human.
EvolutionaryTracei O75367.
GeneWikii H2AFY.
GenomeRNAii 9555.
NextBioi 35835.
PMAP-CutDB O75367.
PROi O75367.
SOURCEi Search...

Gene expression databases

ArrayExpressi O75367.
Bgeei O75367.
CleanExi HS_H2AFY.
Genevestigatori O75367.

Family and domain databases

Gene3Di 1.10.20.10. 1 hit.
InterProi IPR021171. Core_histone_macro-H2A.
IPR009072. Histone-fold.
IPR007125. Histone_core_D.
IPR002119. Histone_H2A.
IPR002589. Macro_dom.
[Graphical view ]
Pfami PF00125. Histone. 1 hit.
PF01661. Macro. 1 hit.
[Graphical view ]
PIRSFi PIRSF037942. Core_histone_macro-H2A. 1 hit.
PRINTSi PR00620. HISTONEH2A.
SMARTi SM00506. A1pp. 1 hit.
SM00414. H2A. 1 hit.
[Graphical view ]
SUPFAMi SSF47113. SSF47113. 1 hit.
PROSITEi PS51154. MACRO. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Isolation of cDNA clones encoding human histone macroH2A1 subtypes."
    Lee Y., Hong M., Kim J.W., Hong Y.M., Choe Y.-K., Chang S.Y., Lee K.S., Choe I.S.
    Biochim. Biophys. Acta 1399:73-77(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2), TISSUE SPECIFICITY.
    Tissue: Liver.
  2. "Identification of genes expressed in human CD34(+) hematopoietic stem/progenitor cells by expressed sequence tags and efficient full-length cDNA cloning."
    Mao M., Fu G., Wu J.-S., Zhang Q.-H., Zhou J., Kan L.-X., Huang Q.-H., He K.-L., Gu B.-W., Han Z.-G., Shen Y., Gu J., Yu Y.-P., Xu S.-H., Wang Y.-X., Chen S.-J., Chen Z.
    Proc. Natl. Acad. Sci. U.S.A. 95:8175-8180(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 2 AND 3).
    Tissue: Umbilical cord blood.
  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] (ISOFORM 2).
    Tissue: Ovary.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. "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] (ISOFORM 2).
    Tissue: Bone marrow and Placenta.
  6. Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 6-372 (ISOFORM 3).
    Tissue: Medulloblastoma.
  7. "Histone macroH2A1 is concentrated in the inactive X chromosome of female mammals."
    Costanzi C., Pehrson J.R.
    Nature 393:599-601(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION.
  8. "The histone variant macroH2A interferes with transcription factor binding and SWI/SNF nucleosome remodeling."
    Angelov D., Molla A., Perche P.-Y., Hans F., Cote J., Khochbin S., Bouvet P., Dimitrov S.
    Mol. Cell 11:1033-1041(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. "Histone variant macroH2A1.2 is mono-ubiquitinated at its histone domain."
    Ogawa Y., Ono T., Wakata Y., Okawa K., Tagami H., Shibahara K.
    Biochem. Biophys. Res. Commun. 336:204-209(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION AT LYS-116 AND LYS-117, IDENTIFICATION BY MASS SPECTROMETRY.
  10. "Formation of MacroH2A-containing senescence-associated heterochromatin foci and senescence driven by ASF1a and HIRA."
    Zhang R., Poustovoitov M.V., Ye X., Santos H.A., Chen W., Daganzo S.M., Erzberger J.P., Serebriiskii I.G., Canutescu A.A., Dunbrack R.L., Pehrson J.R., Berger J.M., Kaufman P.D., Adams P.D.
    Dev. Cell 8:19-30(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  11. Cited for: BINDING TO ADP-RIBOSE (ISOFORM 1).
  12. "Stable X chromosome inactivation involves the PRC1 Polycomb complex and requires histone MACROH2A1 and the CULLIN3/SPOP ubiquitin E3 ligase."
    Hernandez-Munoz I., Lund A.H., van der Stoop P., Boutsma E., Muijrers I., Verhoeven E., Nusinow D.A., Panning B., Marahrens Y., van Lohuizen M.
    Proc. Natl. Acad. Sci. U.S.A. 102:7635-7640(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN A COMPLEX WITH CULLIN3 AND SPOP, UBIQUITINATION, SUBCELLULAR LOCATION, FUNCTION.
  13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  14. "Mechanism of polymerase II transcription repression by the histone variant macroH2A."
    Doyen C.-M., An W., Angelov D., Bondarenko V., Mietton F., Studitsky V.M., Hamiche A., Roeder R.G., Bouvet P., Dimitrov S.
    Mol. Cell. Biol. 26:1156-1164(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  15. "Mapping post-translational modifications of the histone variant MacroH2A1 using tandem mass spectrometry."
    Chu F., Nusinow D.A., Chalkley R.J., Plath K., Panning B., Burlingame A.L.
    Mol. Cell. Proteomics 5:194-203(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: METHYLATION AT LYS-18 AND LYS-123, PHOSPHORYLATION AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY.
  16. "Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra."
    Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D.
    J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  17. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-170 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  19. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129; SER-170; SER-173 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND THR-178, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-129 AND SER-170, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS) OF 1-120 IN COMPLEX WITH THE NUCLEOSOME CORE PARTICLE, FUNCTION.
  23. Cited for: X-RAY CRYSTALLOGRAPHY (2.54 ANGSTROMS) OF 162-372 (ISOFORM 1), X-RAY CRYSTALLOGRAPHY (2.92 ANGSTROMS) OF 161-372 (ISOFORM 2), BINDING TO ADP-RIBOSE AND O-ACETYL-ADP-RIBOSE (ISOFORM 1).
  24. "Structures of SPOP-substrate complexes: insights into molecular architectures of BTB-Cul3 ubiquitin ligases."
    Zhuang M., Calabrese M.F., Liu J., Waddell M.B., Nourse A., Hammel M., Miller D.J., Walden H., Duda D.M., Seyedin S.N., Hoggard T., Harper J.W., White K.P., Schulman B.A.
    Mol. Cell 36:39-50(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.43 ANGSTROMS) OF 172-186 IN COMPLEXES WITH SPOP, SUBUNIT, UBIQUITINATION.

Entry informationi

Entry nameiH2AY_HUMAN
AccessioniPrimary (citable) accession number: O75367
Secondary accession number(s): O75377
, Q503A8, Q7Z5E3, Q96D41, Q9H8P3, Q9UP96
Entry historyi
Integrated into UniProtKB/Swiss-Prot: January 24, 2001
Last sequence update: January 23, 2007
Last modified: September 3, 2014
This is version 148 of the entry and version 4 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 number of individuals with antibodies against this antigen is 2-fold higher in pediatric patients with cancer compared to healthy controls.

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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