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H2AV1_DICDI
ID   H2AV1_DICDI             Reviewed;         260 AA.
AC   Q54HW2;
DT   24-NOV-2009, integrated into UniProtKB/Swiss-Prot.
DT   24-MAY-2005, sequence version 1.
DT   03-AUG-2022, entry version 100.
DE   RecName: Full=Histone H2A.v1;
GN   Name=H2Av1; ORFNames=DDB_G0289187;
OS   Dictyostelium discoideum (Slime mold).
OC   Eukaryota; Amoebozoa; Evosea; Eumycetozoa; Dictyostelia; Dictyosteliales;
OC   Dictyosteliaceae; Dictyostelium.
OX   NCBI_TaxID=44689;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC   STRAIN=AX4;
RX   PubMed=15875012; DOI=10.1038/nature03481;
RA   Eichinger L., Pachebat J.A., Gloeckner G., Rajandream M.A., Sucgang R.,
RA   Berriman M., Song J., Olsen R., Szafranski K., Xu Q., Tunggal B.,
RA   Kummerfeld S., Madera M., Konfortov B.A., Rivero F., Bankier A.T.,
RA   Lehmann R., Hamlin N., Davies R., Gaudet P., Fey P., Pilcher K., Chen G.,
RA   Saunders D., Sodergren E.J., Davis P., Kerhornou A., Nie X., Hall N.,
RA   Anjard C., Hemphill L., Bason N., Farbrother P., Desany B., Just E.,
RA   Morio T., Rost R., Churcher C.M., Cooper J., Haydock S., van Driessche N.,
RA   Cronin A., Goodhead I., Muzny D.M., Mourier T., Pain A., Lu M., Harper D.,
RA   Lindsay R., Hauser H., James K.D., Quiles M., Madan Babu M., Saito T.,
RA   Buchrieser C., Wardroper A., Felder M., Thangavelu M., Johnson D.,
RA   Knights A., Loulseged H., Mungall K.L., Oliver K., Price C., Quail M.A.,
RA   Urushihara H., Hernandez J., Rabbinowitsch E., Steffen D., Sanders M.,
RA   Ma J., Kohara Y., Sharp S., Simmonds M.N., Spiegler S., Tivey A.,
RA   Sugano S., White B., Walker D., Woodward J.R., Winckler T., Tanaka Y.,
RA   Shaulsky G., Schleicher M., Weinstock G.M., Rosenthal A., Cox E.C.,
RA   Chisholm R.L., Gibbs R.A., Loomis W.F., Platzer M., Kay R.R.,
RA   Williams J.G., Dear P.H., Noegel A.A., Barrell B.G., Kuspa A.;
RT   "The genome of the social amoeba Dictyostelium discoideum.";
RL   Nature 435:43-57(2005).
CC   -!- SIMILARITY: Belongs to the histone H2A family. {ECO:0000305}.
CC   -!- CAUTION: In contrast to other members of the histone H2A family, this
CC       protein is much longer and has a highly divergent N-terminus. It is
CC       therefore unclear whether it is a real histone. {ECO:0000305}.
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DR   EMBL; AAFI02000131; EAL62827.1; -; Genomic_DNA.
DR   RefSeq; XP_636327.1; XM_631235.1.
DR   AlphaFoldDB; Q54HW2; -.
DR   SMR; Q54HW2; -.
DR   STRING; 44689.DDB0220641; -.
DR   PaxDb; Q54HW2; -.
DR   EnsemblProtists; EAL62827; EAL62827; DDB_G0289187.
DR   GeneID; 8627000; -.
DR   KEGG; ddi:DDB_G0289187; -.
DR   dictyBase; DDB_G0289187; H2Av1.
DR   eggNOG; KOG1756; Eukaryota.
DR   HOGENOM; CLU_1071291_0_0_1; -.
DR   InParanoid; Q54HW2; -.
DR   Reactome; R-DDI-2299718; Condensation of Prophase Chromosomes.
DR   Reactome; R-DDI-2559580; Oxidative Stress Induced Senescence.
DR   Reactome; R-DDI-3214815; HDACs deacetylate histones.
DR   Reactome; R-DDI-3214858; RMTs methylate histone arginines.
DR   Reactome; R-DDI-427359; SIRT1 negatively regulates rRNA expression.
DR   Reactome; R-DDI-5689880; Ub-specific processing proteases.
DR   Reactome; R-DDI-5693565; Recruitment and ATM-mediated phosphorylation of repair and signaling proteins at DNA double strand breaks.
DR   Reactome; R-DDI-68616; Assembly of the ORC complex at the origin of replication.
DR   Reactome; R-DDI-73772; RNA Polymerase I Promoter Escape.
DR   PRO; PR:Q54HW2; -.
DR   Proteomes; UP000002195; Chromosome 5.
DR   GO; GO:0000786; C:nucleosome; IEA:InterPro.
DR   GO; GO:0003677; F:DNA binding; IBA:GO_Central.
DR   GO; GO:0046982; F:protein heterodimerization activity; IEA:InterPro.
DR   GO; GO:0030527; F:structural constituent of chromatin; IEA:InterPro.
DR   Gene3D; 1.10.20.10; -; 1.
DR   InterPro; IPR009072; Histone-fold.
DR   InterPro; IPR002119; Histone_H2A.
DR   InterPro; IPR007125; Histone_H2A/H2B/H3.
DR   InterPro; IPR032454; Histone_H2A_C.
DR   PANTHER; PTHR23430; PTHR23430; 1.
DR   Pfam; PF00125; Histone; 1.
DR   Pfam; PF16211; Histone_H2A_C; 1.
DR   PRINTS; PR00620; HISTONEH2A.
DR   SMART; SM00414; H2A; 1.
DR   SUPFAM; SSF47113; SSF47113; 1.
PE   3: Inferred from homology;
KW   Reference proteome.
FT   CHAIN           1..260
FT                   /note="Histone H2A.v1"
FT                   /id="PRO_0000389155"
FT   REGION          65..122
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          236..260
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        65..103
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        107..122
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   260 AA;  29478 MW;  DC7404D60108B051 CRC64;
     MVKGKSKKVV TSTIQEENVS KEPLAPIVPI VPDILRNEEE LVFIEIEKRD KNEIVNVPIT
     QTNPVVQTNN KTNNKNNINN NNNNNNNNNN NNINNNNKNN KVKKTTTTTK KNNEKSNEKQ
     KSVKFANKIN ESRSARADLT FPVSRIEKMI REGRFTKRCS SDAPVFLAAV LEYLTLEILE
     LSITYANQKN KTRITPQHIH LSICCDAELN DLLKNVTIAN GGVPKFIHPI LLDTPKKKGH
     QQNMNENDIS KEKDIKSSKN
 
 
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