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Histone acetyltransferase type B subunit 2 (Kinetochore protein mis16)

 HAT2_SCHPO              Reviewed;         430 AA.
O94244;
21-MAR-2006, integrated into UniProtKB/Swiss-Prot.
01-MAY-1999, sequence version 1.
28-MAR-2018, entry version 141.
RecName: Full=Histone acetyltransferase type B subunit 2;
AltName: Full=Kinetochore protein mis16;
Name=mis16; Synonyms=hat2; ORFNames=SPCC1672.10;
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast).
Eukaryota; Fungi; Dikarya; Ascomycota; Taphrinomycotina;
Schizosaccharomycetes; Schizosaccharomycetales;
Schizosaccharomycetaceae; Schizosaccharomyces.
NCBI_TaxID=284812;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
STRAIN=972 / ATCC 24843;
PubMed=11859360; DOI=10.1038/nature724;
Wood V., Gwilliam R., Rajandream M.A., Lyne M.H., Lyne R., Stewart A.,
Sgouros J.G., Peat N., Hayles J., Baker S.G., Basham D., Bowman S.,
Brooks K., Brown D., Brown S., Chillingworth T., Churcher C.M.,
Collins M., Connor R., Cronin A., Davis P., Feltwell T., Fraser A.,
Gentles S., Goble A., Hamlin N., Harris D.E., Hidalgo J., Hodgson G.,
Holroyd S., Hornsby T., Howarth S., Huckle E.J., Hunt S., Jagels K.,
James K.D., Jones L., Jones M., Leather S., McDonald S., McLean J.,
Mooney P., Moule S., Mungall K.L., Murphy L.D., Niblett D., Odell C.,
Oliver K., O'Neil S., Pearson D., Quail M.A., Rabbinowitsch E.,
Rutherford K.M., Rutter S., Saunders D., Seeger K., Sharp S.,
Skelton J., Simmonds M.N., Squares R., Squares S., Stevens K.,
Taylor K., Taylor R.G., Tivey A., Walsh S.V., Warren T., Whitehead S.,
Woodward J.R., Volckaert G., Aert R., Robben J., Grymonprez B.,
Weltjens I., Vanstreels E., Rieger M., Schaefer M., Mueller-Auer S.,
Gabel C., Fuchs M., Duesterhoeft A., Fritzc C., Holzer E., Moestl D.,
Hilbert H., Borzym K., Langer I., Beck A., Lehrach H., Reinhardt R.,
Pohl T.M., Eger P., Zimmermann W., Wedler H., Wambutt R., Purnelle B.,
Goffeau A., Cadieu E., Dreano S., Gloux S., Lelaure V., Mottier S.,
Galibert F., Aves S.J., Xiang Z., Hunt C., Moore K., Hurst S.M.,
Lucas M., Rochet M., Gaillardin C., Tallada V.A., Garzon A., Thode G.,
Daga R.R., Cruzado L., Jimenez J., Sanchez M., del Rey F., Benito J.,
Dominguez A., Revuelta J.L., Moreno S., Armstrong J., Forsburg S.L.,
Cerutti L., Lowe T., McCombie W.R., Paulsen I., Potashkin J.,
Shpakovski G.V., Ussery D., Barrell B.G., Nurse P.;
"The genome sequence of Schizosaccharomyces pombe.";
Nature 415:871-880(2002).
[2]
FUNCTION, INTERACTION WITH MIS18, AND SUBCELLULAR LOCATION.
PubMed=15369671; DOI=10.1016/j.cell.2004.09.002;
Hayashi T., Fujita Y., Iwasaki O., Adachi Y., Takahashi K.,
Yanagida M.;
"Mis16 and Mis18 are required for CENP-A loading and histone
deacetylation at centromeres.";
Cell 118:715-729(2004).
[3]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
PubMed=16823372; DOI=10.1038/nbt1222;
Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S.,
Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S.,
Yoshida M.;
"ORFeome cloning and global analysis of protein localization in the
fission yeast Schizosaccharomyces pombe.";
Nat. Biotechnol. 24:841-847(2006).
[4]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-425, AND IDENTIFICATION
BY MASS SPECTROMETRY.
PubMed=18257517; DOI=10.1021/pr7006335;
Wilson-Grady J.T., Villen J., Gygi S.P.;
"Phosphoproteome analysis of fission yeast.";
J. Proteome Res. 7:1088-1097(2008).
[5]
IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
PubMed=24774534; DOI=10.1111/gtc.12152;
Hayashi T., Ebe M., Nagao K., Kokubu A., Sajiki K., Yanagida M.;
"Schizosaccharomyces pombe centromere protein Mis19 links Mis16 and
Mis18 to recruit CENP-A through interacting with NMD factors and the
SWI/SNF complex.";
Genes Cells 19:541-554(2014).
[6]
IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
PubMed=24789708; DOI=10.1098/rsob.140043;
Subramanian L., Toda N.R., Rappsilber J., Allshire R.C.;
"Eic1 links Mis18 with the CCAN/Mis6/Ctf19 complex to promote CENP-A
assembly.";
Open Biol. 4:140043-140043(2014).
[7]
IDENTIFICATION IN THE CENP-A RECRUITING COMPLEX, AND FUNCTION.
PubMed=25375240; DOI=10.1371/journal.pone.0111905;
Hirai H., Arai K., Kariyazono R., Yamamoto M., Sato M.;
"The kinetochore protein Kis1/Eic1/Mis19 ensures the integrity of
mitotic spindles through maintenance of kinetochore factors Mis6/CENP-
I and CENP-A.";
PLoS ONE 9:E111905-E111905(2014).
-!- FUNCTION: Regulatory subunit of the histone acetylase B (HAT-B)
complex (By similarity). The complex acetylates 'Lys-12' of
histone H4 which is required for telomeric silencing (By
similarity). Component of the CENP-A recruiting complex that
ensures the integrity of mitotic spindles through maintenance of
kinetochore factors mis6/CENP-I and cnp1/CENP-A (PubMed:15369671,
PubMed:24774534, PubMed:24789708, PubMed:25375240). Maintains the
deacetylated state of histones specifically in the central core of
the centromeres (PubMed:15369671). {ECO:0000250|UniProtKB:P39984,
ECO:0000269|PubMed:15369671, ECO:0000269|PubMed:24774534,
ECO:0000269|PubMed:24789708, ECO:0000269|PubMed:25375240}.
-!- SUBUNIT: Component of the HAT-B complex composed of at least hat1
and hat2. The HAT-B complex binds to histone H4 tail (By
similarity). Component of the CENP-A recruiting complex composed
of at least mis16, mis19, mis19 and mis20 (PubMed:24774534,
PubMed:24789708, PubMed:25375240). {ECO:0000250|UniProtKB:P39984,
ECO:0000269|PubMed:15369671, ECO:0000269|PubMed:24774534,
ECO:0000269|PubMed:24789708, ECO:0000269|PubMed:25375240}.
-!- INTERACTION:
Q9P802:mis18; NbExp=2; IntAct=EBI-1148703, EBI-1148763;
-!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:15369671}.
Nucleus {ECO:0000269|PubMed:15369671}. Chromosome, centromere
{ECO:0000269|PubMed:15369671}. Chromosome, centromere, kinetochore
{ECO:0000269|PubMed:15369671}.
-!- SIMILARITY: Belongs to the WD repeat RBAP46/RBAP48/MSI1 family.
{ECO:0000305}.
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EMBL; CU329672; CAA20448.1; -; Genomic_DNA.
PIR; T41054; T41054.
RefSeq; NP_587881.1; NM_001022873.2.
ProteinModelPortal; O94244; -.
SMR; O94244; -.
BioGrid; 275784; 11.
IntAct; O94244; 2.
STRING; 4896.SPCC1672.10.1; -.
iPTMnet; O94244; -.
SwissPalm; O94244; -.
MaxQB; O94244; -.
PaxDb; O94244; -.
PRIDE; O94244; -.
EnsemblFungi; SPCC1672.10.1; SPCC1672.10.1:pep; SPCC1672.10.
GeneID; 2539214; -.
KEGG; spo:SPCC1672.10; -.
EuPathDB; FungiDB:SPCC1672.10; -.
PomBase; SPCC1672.10; mis16.
HOGENOM; HOG000160330; -.
InParanoid; O94244; -.
KO; K10752; -.
OMA; TNHLADF; -.
OrthoDB; EOG092C4MBO; -.
PhylomeDB; O94244; -.
Reactome; R-SPO-3214847; HATs acetylate histones.
Reactome; R-SPO-8951664; Neddylation.
PRO; PR:O94244; -.
Proteomes; UP000002485; Chromosome III.
GO; GO:0098654; C:CENP-A recruiting complex; IDA:PomBase.
GO; GO:0000775; C:chromosome, centromeric region; IDA:PomBase.
GO; GO:0000778; C:condensed nuclear chromosome kinetochore; IDA:PomBase.
GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
GO; GO:0005634; C:nucleus; HDA:PomBase.
GO; GO:0061641; P:CENP-A containing chromatin organization; IMP:PomBase.
GO; GO:0016569; P:covalent chromatin modification; IEA:UniProtKB-KW.
GO; GO:0051382; P:kinetochore assembly; IMP:PomBase.
GO; GO:0000070; P:mitotic sister chromatid segregation; IMP:PomBase.
Gene3D; 2.130.10.10; -; 1.
InterPro; IPR020472; G-protein_beta_WD-40_rep.
InterPro; IPR022052; Histone-bd_RBBP4_N.
InterPro; IPR015943; WD40/YVTN_repeat-like_dom_sf.
InterPro; IPR001680; WD40_repeat.
InterPro; IPR019775; WD40_repeat_CS.
InterPro; IPR017986; WD40_repeat_dom.
InterPro; IPR036322; WD40_repeat_dom_sf.
Pfam; PF12265; CAF1C_H4-bd; 1.
Pfam; PF00400; WD40; 5.
PRINTS; PR00320; GPROTEINBRPT.
SMART; SM00320; WD40; 6.
SUPFAM; SSF50978; SSF50978; 1.
PROSITE; PS00678; WD_REPEATS_1; 3.
PROSITE; PS50082; WD_REPEATS_2; 3.
PROSITE; PS50294; WD_REPEATS_REGION; 1.
1: Evidence at protein level;
Centromere; Chromatin regulator; Chromosome; Complete proteome;
Cytoplasm; Kinetochore; Nucleus; Phosphoprotein; Reference proteome;
Repeat; WD repeat.
CHAIN 1 430 Histone acetyltransferase type B subunit
2.
/FTId=PRO_0000227743.
REPEAT 129 169 WD 1.
REPEAT 180 220 WD 2.
REPEAT 233 273 WD 3.
REPEAT 279 319 WD 4.
REPEAT 323 363 WD 5.
REPEAT 380 420 WD 6.
REGION 365 369 Interaction with the histone H4 N-
terminus. {ECO:0000250|UniProtKB:P39984}.
SITE 296 296 Important for interaction with HAT1.
{ECO:0000250|UniProtKB:P39984}.
MOD_RES 425 425 Phosphoserine.
{ECO:0000269|PubMed:18257517}.
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


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