HAT2_SCHPO
ID HAT2_SCHPO Reviewed; 430 AA.
AC O94244;
DT 21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-1999, sequence version 1.
DT 03-AUG-2022, entry version 164.
DE RecName: Full=Histone acetyltransferase type B subunit 2;
DE AltName: Full=Kinetochore protein mis16;
GN Name=mis16; Synonyms=hat2; ORFNames=SPCC1672.10;
OS Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
OC Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
OC Schizosaccharomycetes; Schizosaccharomycetales; Schizosaccharomycetaceae;
OC Schizosaccharomyces.
OX NCBI_TaxID=284812;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=972 / ATCC 24843;
RX PubMed=11859360; DOI=10.1038/nature724;
RA Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
RA Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
RA Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M., Collins M.,
RA Connor R., Cronin A., Davis P., Feltwell T., Fraser A., Gentles S.,
RA Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G., Holroyd S.,
RA Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K., James K.D.,
RA Jones L., Jones M., Leather S., McDonald S., McLean J., Mooney P.,
RA Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C., Oliver K.,
RA O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E., Rutherford K.M.,
RA Rutter S., Saunders D., Seeger K., Sharp S., Skelton J., Simmonds M.N.,
RA Squares R., Squares S., Stevens K., Taylor K., Taylor R.G., Tivey A.,
RA Walsh S.V., Warren T., Whitehead S., Woodward J.R., Volckaert G., Aert R.,
RA Robben J., Grymonprez B., Weltjens I., Vanstreels E., Rieger M.,
RA Schaefer M., Mueller-Auer S., Gabel C., Fuchs M., Duesterhoeft A.,
RA Fritzc C., Holzer E., Moestl D., Hilbert H., Borzym K., Langer I., Beck A.,
RA Lehrach H., Reinhardt R., Pohl T.M., Eger P., Zimmermann W., Wedler H.,
RA Wambutt R., Purnelle B., Goffeau A., Cadieu E., Dreano S., Gloux S.,
RA Lelaure V., Mottier S., Galibert F., Aves S.J., Xiang Z., Hunt C.,
RA Moore K., Hurst S.M., Lucas M., Rochet M., Gaillardin C., Tallada V.A.,
RA Garzon A., Thode G., Daga R.R., Cruzado L., Jimenez J., Sanchez M.,
RA del Rey F., Benito J., Dominguez A., Revuelta J.L., Moreno S.,
RA Armstrong J., Forsburg S.L., Cerutti L., Lowe T., McCombie W.R.,
RA Paulsen I., Potashkin J., Shpakovski G.V., Ussery D., Barrell B.G.,
RA Nurse P.;
RT "The genome sequence of Schizosaccharomyces pombe.";
RL Nature 415:871-880(2002).
RN [2]
RP FUNCTION, INTERACTION WITH MIS18, AND SUBCELLULAR LOCATION.
RX PubMed=15369671; DOI=10.1016/j.cell.2004.09.002;
RA Hayashi T., Fujita Y., Iwasaki O., Adachi Y., Takahashi K., Yanagida M.;
RT "Mis16 and Mis18 are required for CENP-A loading and histone deacetylation
RT at centromeres.";
RL Cell 118:715-729(2004).
RN [3]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RX PubMed=16823372; DOI=10.1038/nbt1222;
RA Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
RA Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
RA Yoshida M.;
RT "ORFeome cloning and global analysis of protein localization in the fission
RT yeast Schizosaccharomyces pombe.";
RL Nat. Biotechnol. 24:841-847(2006).
RN [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION BY
RP MASS SPECTROMETRY.
RX PubMed=18257517; DOI=10.1021/pr7006335;
RA Wilson-Grady J.T., Villen J., Gygi S.P.;
RT "Phosphoproteome analysis of fission yeast.";
RL J. Proteome Res. 7:1088-1097(2008).
RN [5]
RP IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
RX PubMed=24774534; DOI=10.1111/gtc.12152;
RA Hayashi T., Ebe M., Nagao K., Kokubu A., Sajiki K., Yanagida M.;
RT "Schizosaccharomyces pombe centromere protein Mis19 links Mis16 and Mis18
RT to recruit CENP-A through interacting with NMD factors and the SWI/SNF
RT complex.";
RL Genes Cells 19:541-554(2014).
RN [6]
RP IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
RX PubMed=24789708; DOI=10.1098/rsob.140043;
RA Subramanian L., Toda N.R., Rappsilber J., Allshire R.C.;
RT "Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A
RT assembly.";
RL Open Biol. 4:140043-140043(2014).
RN [7]
RP IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
RX PubMed=25375240; DOI=10.1371/journal.pone.0111905;
RA Hirai H., Arai K., Kariyazono R., Yamamoto M., Sato M.;
RT "The kinetochore protein Kis1/Eic1/Mis19 ensures the integrity of mitotic
RT spindles through maintenance of kinetochore factors Mis6/CENP-I and CENP-
RT A.";
RL PLoS ONE 9:E111905-E111905(2014).
CC -!- FUNCTION: Regulatory subunit of the histone acetylase B (HAT-B) complex
CC (By similarity). The complex acetylates 'Lys-12' of histone H4 which is
CC required for telomeric silencing (By similarity). Component of the
CC CENP-A recruiting complex that ensures the integrity of mitotic
CC spindles through maintenance of kinetochore factors mis6/CENP-I and
CC cnp1/CENP-A (PubMed:15369671, PubMed:24774534, PubMed:24789708,
CC PubMed:25375240). Maintains the deacetylated state of histones
CC specifically in the central core of the centromeres (PubMed:15369671).
CC {ECO:0000250|UniProtKB:P39984, ECO:0000269|PubMed:15369671,
CC ECO:0000269|PubMed:24774534, ECO:0000269|PubMed:24789708,
CC ECO:0000269|PubMed:25375240}.
CC -!- SUBUNIT: Component of the HAT-B complex composed of at least hat1 and
CC hat2. The HAT-B complex binds to histone H4 tail (By similarity).
CC Component of the CENP-A recruiting complex composed of at least mis16,
CC mis19, mis19 and mis20 (PubMed:24774534, PubMed:24789708,
CC PubMed:25375240). {ECO:0000250|UniProtKB:P39984,
CC ECO:0000269|PubMed:15369671, ECO:0000269|PubMed:24774534,
CC ECO:0000269|PubMed:24789708, ECO:0000269|PubMed:25375240}.
CC -!- INTERACTION:
CC O94244; Q9P802: mis18; NbExp=2; IntAct=EBI-1148703, EBI-1148763;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15369671}. Nucleus
CC {ECO:0000269|PubMed:15369671}. Chromosome, centromere
CC {ECO:0000269|PubMed:15369671}. Chromosome, centromere, kinetochore
CC {ECO:0000269|PubMed:15369671}.
CC -!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
CC {ECO:0000305}.
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DR EMBL; CU329672; CAA20448.1; -; Genomic_DNA.
DR PIR; T41054; T41054.
DR RefSeq; NP_587881.1; NM_001022873.2.
DR PDB; 5WJC; X-ray; 2.30 A; A=1-430.
DR PDB; 6S1L; X-ray; 1.94 A; A=2-430.
DR PDB; 6S1R; X-ray; 1.80 A; A=2-430.
DR PDB; 6S29; X-ray; 1.99 A; A/C=2-430.
DR PDBsum; 5WJC; -.
DR PDBsum; 6S1L; -.
DR PDBsum; 6S1R; -.
DR PDBsum; 6S29; -.
DR AlphaFoldDB; O94244; -.
DR SMR; O94244; -.
DR BioGRID; 275784; 14.
DR IntAct; O94244; 2.
DR STRING; 4896.SPCC1672.10.1; -.
DR iPTMnet; O94244; -.
DR SwissPalm; O94244; -.
DR MaxQB; O94244; -.
DR PaxDb; O94244; -.
DR PRIDE; O94244; -.
DR EnsemblFungi; SPCC1672.10.1; SPCC1672.10.1:pep; SPCC1672.10.
DR GeneID; 2539214; -.
DR KEGG; spo:SPCC1672.10; -.
DR PomBase; SPCC1672.10; mis16.
DR VEuPathDB; FungiDB:SPCC1672.10; -.
DR eggNOG; KOG0264; Eukaryota.
DR HOGENOM; CLU_020445_3_1_1; -.
DR InParanoid; O94244; -.
DR OMA; PHEEGCL; -.
DR PhylomeDB; O94244; -.
DR Reactome; R-SPO-3214815; HDACs deacetylate histones.
DR Reactome; R-SPO-3214847; HATs acetylate histones.
DR Reactome; R-SPO-8951664; Neddylation.
DR PRO; PR:O94244; -.
DR Proteomes; UP000002485; Chromosome III.
DR GO; GO:0098654; C:CENP-A recruiting complex; IDA:PomBase.
DR GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0000776; C:kinetochore; IDA:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0042393; F:histone binding; IBA:GO_Central.
DR GO; GO:0034080; P:CENP-A containing chromatin assembly; IMP:PomBase.
DR GO; GO:0006338; P:chromatin remodeling; IBA:GO_Central.
DR GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
DR Gene3D; 2.130.10.10; -; 1.
DR InterPro; IPR020472; G-protein_beta_WD-40_rep.
DR InterPro; IPR022052; Histone-bd_RBBP4_N.
DR InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
DR InterPro; IPR001680; WD40_repeat.
DR InterPro; IPR019775; WD40_repeat_CS.
DR InterPro; IPR036322; WD40_repeat_dom_sf.
DR Pfam; PF12265; CAF1C_H4-bd; 1.
DR Pfam; PF00400; WD40; 5.
DR PRINTS; PR00320; GPROTEINBRPT.
DR SMART; SM00320; WD40; 6.
DR SUPFAM; SSF50978; SSF50978; 1.
DR PROSITE; PS00678; WD_REPEATS_1; 3.
DR PROSITE; PS50082; WD_REPEATS_2; 3.
DR PROSITE; PS50294; WD_REPEATS_REGION; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Centromere; Chromatin regulator; Chromosome; Cytoplasm;
KW Kinetochore; Nucleus; Phosphoprotein; Reference proteome; Repeat;
KW WD repeat.
FT CHAIN 1..430
FT /note="Histone acetyltransferase type B subunit 2"
FT /id="PRO_0000227743"
FT REPEAT 129..169
FT /note="WD 1"
FT REPEAT 180..220
FT /note="WD 2"
FT REPEAT 233..273
FT /note="WD 3"
FT REPEAT 279..319
FT /note="WD 4"
FT REPEAT 323..363
FT /note="WD 5"
FT REPEAT 380..420
FT /note="WD 6"
FT REGION 365..369
FT /note="Interaction with the histone H4 N-terminus"
FT /evidence="ECO:0000250|UniProtKB:P39984"
FT SITE 296
FT /note="Important for interaction with HAT1"
FT /evidence="ECO:0000250|UniProtKB:P39984"
FT MOD_RES 425
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT HELIX 13..40
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 41..48
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 56..64
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 68..77
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 83..85
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 87..97
FT /evidence="ECO:0007829|PDB:6S1R"
FT TURN 101..103
FT /evidence="ECO:0007829|PDB:6S29"
FT STRAND 122..132
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 136..140
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 143..150
FT /evidence="ECO:0007829|PDB:6S1R"
FT HELIX 152..154
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 156..160
FT /evidence="ECO:0007829|PDB:6S1R"
FT HELIX 161..163
FT /evidence="ECO:0007829|PDB:6S1L"
FT STRAND 166..170
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 175..178
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 185..190
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 197..202
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 207..211
FT /evidence="ECO:0007829|PDB:6S1R"
FT HELIX 214..216
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 219..221
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 223..225
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 228..231
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 238..243
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 250..255
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 260..264
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 275..277
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 284..289
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 291..293
FT /evidence="ECO:0007829|PDB:6S1L"
FT STRAND 294..301
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 306..310
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 316..321
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 328..333
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 340..345
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 350..354
FT /evidence="ECO:0007829|PDB:6S1R"
FT HELIX 355..357
FT /evidence="ECO:0007829|PDB:6S1R"
FT HELIX 364..369
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 374..378
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 385..390
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 394..396
FT /evidence="ECO:0007829|PDB:6S29"
FT STRAND 398..402
FT /evidence="ECO:0007829|PDB:6S1R"
FT STRAND 405..412
FT /evidence="ECO:0007829|PDB:6S1R"
FT HELIX 414..417
FT /evidence="ECO:0007829|PDB:6S1R"
FT TURN 418..420
FT /evidence="ECO:0007829|PDB:6S1L"
SQ SEQUENCE 430 AA; 48435 MW; 606A7D009E60EA20 CRC64;
MSEEVVQDAP LENNELNAEI DLQKTIQEEY KLWKQNVPFL YDLVITHALE WPSLTIQWLP
DKKTIPGTDY SIQRLILGTH TSGNDQNYLQ IASVQLPNFD EDTTEFTPST IRRAQATGSY
TIEISQKIPH DGDVNRARYM PQKPEIIATM GEGGNAYIFD TTCHDALTTG EALPQAVLKG
HTAEGFGLCW NPNLPGNLAT GAEDQVICLW DVQTQSFTSS ETKVISPIAK YHRHTDIVND
VQFHPQHEAL LASVSDDCTL QIHDTRLNPE EEAPKVIQAH SKAINAVAIN PFNDYLLATA
SADKTVALWD LRNPYQRLHT LEGHEDEVYG LEWSPHDEPI LASSSTDRRV CIWDLEKIGE
EQTPEDAEDG SPELLFMHGG HTNRISEFSW CPNERWVVGS LADDNILQIW SPSRVIWGRD
HVQVSPRDLE
