NGG1_SCHPO
ID NGG1_SCHPO Reviewed; 551 AA.
AC Q9USU8;
DT 04-NOV-2008, integrated into UniProtKB/Swiss-Prot.
DT 01-MAY-2000, sequence version 1.
DT 03-AUG-2022, entry version 111.
DE RecName: Full=Chromatin-remodeling complexes subunit ngg1;
DE AltName: Full=Kinesin-associated protein 1;
GN Name=ngg1; Synonyms=ada3, kap1; ORFNames=SPBC28F2.10c;
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 [MRNA].
RC STRAIN=972 / ATCC 24843;
RA Jeong J.W., Kim H.B.;
RT "The studies of the kinesin-associated proteins in Schizosaccharomyces
RT pombe.";
RL Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
RN [2]
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 [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-120 AND SER-144, AND
RP IDENTIFICATION BY 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).
CC -!- FUNCTION: Transcription regulator. Functions as component of the
CC transcription regulatory histone acetylation (HAT) complexes SAGA,
CC SALSA, SLIK and ADA. SAGA is involved in RNA polymerase II-dependent
CC transcriptional regulation of a subset of genes. At the promoters, SAGA
CC is required for recruitment of the basal transcription machinery. It
CC influences RNA polymerase II transcriptional activity through different
CC activities such as TBP interaction and promoter selectivity,
CC interaction with transcription activators, and chromatin modification
CC through histone acetylation and deubiquitination. SAGA acetylates
CC nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac
CC and H3K23ac). SAGA interacts with DNA via upstream activating sequences
CC (UASs). SALSA, an altered form of SAGA, may be involved in positive
CC transcriptional regulation. SLIK is proposed to have partly overlapping
CC functions with SAGA. It preferentially acetylates methylated histone
CC H3. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14'
CC and 'Lys-18') and H2B.
CC -!- SUBUNIT: Component of the SAGA complex, the SALSA complex, the ADA
CC complex and the SLIK complex which is probably a subcomplex of SAGA.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:16823372}.
CC -!- SIMILARITY: Belongs to the NGG1 family. {ECO:0000305}.
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DR EMBL; AF351206; AAK17897.1; -; mRNA.
DR EMBL; CU329671; CAB57939.1; -; Genomic_DNA.
DR PIR; T40053; T40053.
DR RefSeq; NP_595671.1; NM_001021566.2.
DR AlphaFoldDB; Q9USU8; -.
DR SMR; Q9USU8; -.
DR BioGRID; 276964; 339.
DR IntAct; Q9USU8; 2.
DR MINT; Q9USU8; -.
DR STRING; 4896.SPBC28F2.10c.1; -.
DR iPTMnet; Q9USU8; -.
DR MaxQB; Q9USU8; -.
DR PaxDb; Q9USU8; -.
DR PRIDE; Q9USU8; -.
DR EnsemblFungi; SPBC28F2.10c.1; SPBC28F2.10c.1:pep; SPBC28F2.10c.
DR GeneID; 2540436; -.
DR KEGG; spo:SPBC28F2.10c; -.
DR PomBase; SPBC28F2.10c; ngg1.
DR VEuPathDB; FungiDB:SPBC28F2.10c; -.
DR eggNOG; KOG4191; Eukaryota.
DR HOGENOM; CLU_457950_0_0_1; -.
DR InParanoid; Q9USU8; -.
DR OMA; EMAFQEF; -.
DR PhylomeDB; Q9USU8; -.
DR Reactome; R-SPO-5689880; Ub-specific processing proteases.
DR PRO; PR:Q9USU8; -.
DR Proteomes; UP000002485; Chromosome II.
DR GO; GO:0000785; C:chromatin; IC:PomBase.
DR GO; GO:0005634; C:nucleus; HDA:PomBase.
DR GO; GO:0000124; C:SAGA complex; IDA:PomBase.
DR GO; GO:0003713; F:transcription coactivator activity; IBA:GO_Central.
DR GO; GO:0006338; P:chromatin remodeling; NAS:PomBase.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IMP:PomBase.
DR InterPro; IPR019340; Histone_AcTrfase_su3.
DR PANTHER; PTHR13556; PTHR13556; 1.
DR Pfam; PF10198; Ada3; 1.
PE 1: Evidence at protein level;
KW Chromatin regulator; Coiled coil; Nucleus; Phosphoprotein;
KW Reference proteome; Transcription; Transcription regulation.
FT CHAIN 1..551
FT /note="Chromatin-remodeling complexes subunit ngg1"
FT /id="PRO_0000353803"
FT REGION 106..144
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 351..383
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COILED 417..476
FT /evidence="ECO:0000255"
FT COMPBIAS 125..144
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 357..383
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 120
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
FT MOD_RES 144
FT /note="Phosphoserine"
FT /evidence="ECO:0000269|PubMed:18257517"
SQ SEQUENCE 551 AA; 62407 MW; F037D741B0A78403 CRC64;
MSSEQQNEAD SKPAVIPQCF KIENQYETFS RLSETSTPGV VPSVSTLWRL LFELQKMIEC
EPSCVEYFRQ RKEELESHVD SEIETSKDES SVNKVEEKVE EFKEDNVEQE IKQKRSLSES
PQESMLEKVS KKPKVSEAHN EEISPENVET IENELDLPVK GKDEQTTGLV YKNANDLLTG
SLLSFIVDDS FSYEQKKKLL CVDSFPTSDV RSLVAGTPAT DDFSHNKPNN QISISTFYSS
LDPYFRAFND DDIAFLKKGF DVSSSYNIPP LGERYYDLTP EDEMTNLCAN SIYQNLQTSA
QGSLEAFNEA DTVSEEVRCG PLTERLMASL IPCYTQNDEE QKPSIAVGEF AETDSGSEKS
KIGTSIDGIE SGNNEYTEQP DIQESSLSIC EDRLRYTLKQ LGILYDGDVD WSKRQDDEIS
ATLRSLNARL KVVSDENEKM RNALLQMLPE EMAFQEFQNV MDDLDKQIEQ AYVKRNRSLK
VKKKRIVTDK IGSSATSGSF PVIKSLMDKR SMWLEKLQPL FQDKLTQHLG SPTSIFNDLS
DHTTSNYSTS V
