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Database: UniProt
Entry: U3CRN5_CALJA
LinkDB: U3CRN5_CALJA
Original site: U3CRN5_CALJA 
ID   U3CRN5_CALJA            Unreviewed;       372 AA.
AC   U3CRN5; F7BSD8;
DT   13-NOV-2013, integrated into UniProtKB/TrEMBL.
DT   13-NOV-2013, sequence version 1.
DT   24-JAN-2024, entry version 47.
DE   RecName: Full=Core histone macro-H2A {ECO:0000256|PIRNR:PIRNR037942};
GN   Name=H2AFY2 {ECO:0000313|EMBL:JAB03811.1};
GN   Synonyms=MACROH2A2 {ECO:0000313|Ensembl:ENSCJAP00000030220.3};
OS   Callithrix jacchus (White-tufted-ear marmoset).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Platyrrhini; Cebidae;
OC   Callitrichinae; Callithrix; Callithrix.
OX   NCBI_TaxID=9483 {ECO:0000313|EMBL:JAB03811.1};
RN   [1] {ECO:0000313|Ensembl:ENSCJAP00000030220.3}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA   Warren W., Ye L., Minx P., Worley K., Gibbs R., Wilson R.K.;
RL   Submitted (MAR-2009) to the EMBL/GenBank/DDBJ databases.
RN   [2] {ECO:0000313|EMBL:JAB03811.1}
RP   NUCLEOTIDE SEQUENCE.
RC   TISSUE=Bladder {ECO:0000313|EMBL:JAB03811.1}, Cerebellum
RC   {ECO:0000313|EMBL:JAB47023.1}, Cerebral cortex
RC   {ECO:0000313|EMBL:JAB27128.1}, Hippocampus
RC   {ECO:0000313|EMBL:JAB16967.1}, and Skeletal muscle
RC   {ECO:0000313|EMBL:JAB37726.1};
RX   PubMed=25243066; DOI=10.1186/2047-217X-3-14;
RA   Maudhoo M.D., Ren D., Gradnigo J.S., Gibbs R.M., Lubker A.C.,
RA   Moriyama E.N., French J.A., Norgren R.B.Jr.;
RT   "De novo assembly of the common marmoset transcriptome from NextGen mRNA
RT   sequences.";
RL   Gigascience 3:14-14(2014).
RN   [3] {ECO:0000313|Ensembl:ENSCJAP00000030220.3}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (JUL-2023) to UniProtKB.
CC   -!- FUNCTION: Variant histone H2A which replaces conventional H2A in a
CC       subset of nucleosomes. {ECO:0000256|PIRNR:PIRNR037942}.
CC   -!- SUBUNIT: The nucleosome is a histone octamer containing two molecules
CC       each of H2A, H2B, H3 and H4 assembled in one H3-H4 heterotetramer and
CC       two H2A-H2B heterodimers. {ECO:0000256|PIRNR:PIRNR037942}.
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000256|PIRNR:PIRNR037942}.
CC       Chromosome {ECO:0000256|PIRNR:PIRNR037942}.
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DR   EMBL; GAMT01008050; JAB03811.1; -; mRNA.
DR   EMBL; GAMS01006169; JAB16967.1; -; mRNA.
DR   EMBL; GAMR01006804; JAB27128.1; -; mRNA.
DR   EMBL; GAMQ01004125; JAB37726.1; -; mRNA.
DR   EMBL; GAMP01005732; JAB47023.1; -; mRNA.
DR   STRING; 9483.ENSCJAP00000030220; -.
DR   Ensembl; ENSCJAT00000031934.5; ENSCJAP00000030220.3; ENSCJAG00000016412.5.
DR   GeneTree; ENSGT00940000158120; -.
DR   OMA; LVLGQKX; -.
DR   OrthoDB; 235643at2759; -.
DR   Proteomes; UP000008225; Chromosome 12.
DR   Bgee; ENSCJAG00000016412; Expressed in ovary and 6 other cell types or tissues.
DR   GO; GO:0001740; C:Barr body; IEA:Ensembl.
DR   GO; GO:0005654; C:nucleoplasm; IEA:Ensembl.
DR   GO; GO:0000786; C:nucleosome; IEA:UniProtKB-UniRule.
DR   GO; GO:0031490; F:chromatin DNA binding; IEA:UniProtKB-UniRule.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0000977; F:RNA polymerase II transcription regulatory region sequence-specific DNA binding; IEA:Ensembl.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   GO; GO:0007420; P:brain development; IEA:Ensembl.
DR   GO; GO:0071169; P:establishment of protein localization to chromatin; IEA:Ensembl.
DR   GO; GO:0045814; P:negative regulation of gene expression, epigenetic; IEA:Ensembl.
DR   GO; GO:0000122; P:negative regulation of transcription by RNA polymerase II; IEA:Ensembl.
DR   GO; GO:1901837; P:negative regulation of transcription of nucleolar large rRNA by RNA polymerase I; IEA:Ensembl.
DR   GO; GO:0006334; P:nucleosome assembly; IEA:UniProtKB-UniRule.
DR   GO; GO:0045618; P:positive regulation of keratinocyte differentiation; IEA:Ensembl.
DR   GO; GO:0007549; P:sex-chromosome dosage compensation; IEA:Ensembl.
DR   CDD; cd00074; H2A; 1.
DR   CDD; cd02904; Macro_H2A-like; 1.
DR   Gene3D; 1.10.20.10; Histone, subunit A; 1.
DR   Gene3D; 3.40.220.10; Leucine Aminopeptidase, subunit E, domain 1; 1.
DR   InterPro; IPR021171; Core_histone_macro-H2A.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   InterPro; IPR002589; Macro_dom.
DR   InterPro; IPR043472; Macro_dom-like.
DR   InterPro; IPR035796; Macro_H2A.
DR   PANTHER; PTHR23430:SF37; CORE HISTONE MACRO-H2A.2; 1.
DR   PANTHER; PTHR23430; HISTONE H2A; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   Pfam; PF01661; Macro; 1.
DR   PIRSF; PIRSF037942; Core_histone_macro-H2A; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00506; A1pp; 1.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; Histone-fold; 1.
DR   SUPFAM; SSF52949; Macro domain-like; 1.
DR   PROSITE; PS51154; MACRO; 1.
PE   2: Evidence at transcript level;
KW   Chromatin regulator {ECO:0000256|ARBA:ARBA00022853,
KW   ECO:0000256|PIRNR:PIRNR037942}; Chromosome {ECO:0000256|ARBA:ARBA00022454};
KW   DNA-binding {ECO:0000256|ARBA:ARBA00023125, ECO:0000256|PIRNR:PIRNR037942};
KW   Nucleosome core {ECO:0000256|ARBA:ARBA00023269,
KW   ECO:0000256|PIRNR:PIRNR037942};
KW   Nucleus {ECO:0000256|ARBA:ARBA00023242, ECO:0000256|PIRNR:PIRNR037942};
KW   Reference proteome {ECO:0000313|Proteomes:UP000008225};
KW   Ubl conjugation {ECO:0000256|ARBA:ARBA00022843}.
FT   DOMAIN          184..370
FT                   /note="Macro"
FT                   /evidence="ECO:0000259|PROSITE:PS51154"
FT   REGION          115..182
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        115..139
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        140..157
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   CROSSLNK        116
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin); alternate"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037942-1"
FT   CROSSLNK        117
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in ubiquitin)"
FT                   /evidence="ECO:0000256|PIRSR:PIRSR037942-1"
SQ   SEQUENCE   372 AA;  40072 MW;  C4B35CD156031C2A CRC64;
     MSGRSGKKKM SKLSRSARAG VIFPVGRLMR YLKKGTFKYR ISVGAPVYMA AVIEYLAAEI
     LELAGNAARD NKKARIAPRH ILLAVANDEE LNQLLKGVTI ASGGVLPRIH PELLAKKRGT
     KGKSETILSP PPEKRGRKAT SGKKGGKKSK AAKPRTSKKS KPKDSDKEGT SNSTSEDGPG
     DGFTILSSKS LVLGQKLSLT QSDISHIGSM RVEGIVHPTT AEIDLKEDIG KALEKAGGKE
     FLETVKELRK SQGPLEVAEA AVSQSSGLAA KFVIHCHIPQ WGSDKCEEQL EETIKNCLSA
     AEDKKLKSVA FPPFPSGRNC FPKQTAAQVT LKAISAHFDD SSASSLKNVY FLLFDSETIG
     IYVQEMAKLD AK
//
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