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Protein

Chromatin-remodeling complexes subunit ngg1

Gene

ngg1

Organism
Schizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Transcription regulator. Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA, SLIK and ADA. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of a subset of genes. At the promoters, SAGA is required for recruitment of the basal transcription machinery. It influences RNA polymerase II transcriptional activity through different activities such as TBP interaction and promoter selectivity, interaction with transcription activators, and chromatin modification through histone acetylation and deubiquitination. SAGA acetylates nucleosomal histone H3 to some extent (to form H3K9ac, H3K14ac, H3K18ac and H3K23ac). SAGA interacts with DNA via upstream activating sequences (UASs). SALSA, an altered form of SAGA, may be involved in positive transcriptional regulation. SLIK is proposed to have partly overlapping functions with SAGA. It preferentially acetylates methylated histone H3. ADA preferentially acetylates nucleosomal histones H3 (at 'Lys-14' and 'Lys-18') and H2B.

GO - Biological processi

  1. chromatin remodeling Source: PomBase
  2. histone acetylation Source: PomBase
  3. regulation of transcription from RNA polymerase II promoter Source: PomBase
  4. transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Chromatin regulator

Keywords - Biological processi

Transcription, Transcription regulation

Names & Taxonomyi

Protein namesi
Recommended name:
Chromatin-remodeling complexes subunit ngg1
Alternative name(s):
Kinesin-associated protein 1
Gene namesi
Name:ngg1
Synonyms:ada3, kap1
ORF Names:SPBC28F2.10c
OrganismiSchizosaccharomyces pombe (strain 972 / ATCC 24843) (Fission yeast)
Taxonomic identifieri284812 [NCBI]
Taxonomic lineageiEukaryotaFungiDikaryaAscomycotaTaphrinomycotinaSchizosaccharomycetesSchizosaccharomycetalesSchizosaccharomycetaceaeSchizosaccharomyces
ProteomesiUP000002485: Chromosome II

Organism-specific databases

PomBaseiSPBC28F2.10c.

Subcellular locationi

Nucleus 1 Publication

GO - Cellular componenti

  1. nuclear chromatin Source: PomBase
  2. nucleus Source: PomBase
  3. SAGA complex Source: PomBase
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 551551Chromatin-remodeling complexes subunit ngg1PRO_0000353803Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei120 – 1201Phosphoserine1 Publication
Modified residuei144 – 1441Phosphoserine1 Publication

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9USU8.

Interactioni

Subunit structurei

Component of the SAGA complex, the SALSA complex, the ADA complex and the SLIK complex which is probably a subcomplex of SAGA.

Protein-protein interaction databases

BioGridi276964. 332 interactions.
IntActiQ9USU8. 2 interactions.
MINTiMINT-8210494.
STRINGi4896.SPBC28F2.10c-1.

Family & Domainsi

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili417 – 47660Sequence AnalysisAdd
BLAST

Sequence similaritiesi

Belongs to the NGG1 family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG265778.
InParanoidiQ9USU8.
KOiK11315.
OrthoDBiEOG7N63WV.
PhylomeDBiQ9USU8.

Family and domain databases

InterProiIPR019340. Histone_AcTrfase_su3.
[Graphical view]
PfamiPF10198. Ada3. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q9USU8-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSEQQNEAD SKPAVIPQCF KIENQYETFS RLSETSTPGV VPSVSTLWRL
60 70 80 90 100
LFELQKMIEC EPSCVEYFRQ RKEELESHVD SEIETSKDES SVNKVEEKVE
110 120 130 140 150
EFKEDNVEQE IKQKRSLSES PQESMLEKVS KKPKVSEAHN EEISPENVET
160 170 180 190 200
IENELDLPVK GKDEQTTGLV YKNANDLLTG SLLSFIVDDS FSYEQKKKLL
210 220 230 240 250
CVDSFPTSDV RSLVAGTPAT DDFSHNKPNN QISISTFYSS LDPYFRAFND
260 270 280 290 300
DDIAFLKKGF DVSSSYNIPP LGERYYDLTP EDEMTNLCAN SIYQNLQTSA
310 320 330 340 350
QGSLEAFNEA DTVSEEVRCG PLTERLMASL IPCYTQNDEE QKPSIAVGEF
360 370 380 390 400
AETDSGSEKS KIGTSIDGIE SGNNEYTEQP DIQESSLSIC EDRLRYTLKQ
410 420 430 440 450
LGILYDGDVD WSKRQDDEIS ATLRSLNARL KVVSDENEKM RNALLQMLPE
460 470 480 490 500
EMAFQEFQNV MDDLDKQIEQ AYVKRNRSLK VKKKRIVTDK IGSSATSGSF
510 520 530 540 550
PVIKSLMDKR SMWLEKLQPL FQDKLTQHLG SPTSIFNDLS DHTTSNYSTS

V
Length:551
Mass (Da):62,407
Last modified:May 1, 2000 - v1
Checksum:iF037D741B0A78403
GO

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF351206 mRNA. Translation: AAK17897.1.
CU329671 Genomic DNA. Translation: CAB57939.1.
PIRiT40053.
RefSeqiNP_595671.1. NM_001021566.2.

Genome annotation databases

EnsemblFungiiSPBC28F2.10c.1; SPBC28F2.10c.1:pep; SPBC28F2.10c.
GeneIDi2540436.
KEGGispo:SPBC28F2.10c.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF351206 mRNA. Translation: AAK17897.1.
CU329671 Genomic DNA. Translation: CAB57939.1.
PIRiT40053.
RefSeqiNP_595671.1. NM_001021566.2.

3D structure databases

ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi276964. 332 interactions.
IntActiQ9USU8. 2 interactions.
MINTiMINT-8210494.
STRINGi4896.SPBC28F2.10c-1.

Proteomic databases

MaxQBiQ9USU8.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsemblFungiiSPBC28F2.10c.1; SPBC28F2.10c.1:pep; SPBC28F2.10c.
GeneIDi2540436.
KEGGispo:SPBC28F2.10c.

Organism-specific databases

PomBaseiSPBC28F2.10c.

Phylogenomic databases

eggNOGiNOG265778.
InParanoidiQ9USU8.
KOiK11315.
OrthoDBiEOG7N63WV.
PhylomeDBiQ9USU8.

Miscellaneous databases

NextBioi20801563.
PROiQ9USU8.

Family and domain databases

InterProiIPR019340. Histone_AcTrfase_su3.
[Graphical view]
PfamiPF10198. Ada3. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "The studies of the kinesin-associated proteins in Schizosaccharomyces pombe."
    Jeong J.W., Kim H.B.
    Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Strain: 972 / ATCC 24843.
  2. "The genome sequence of Schizosaccharomyces pombe."
    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.
    Nature 415:871-880(2002) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: 972 / ATCC 24843.
  3. "ORFeome cloning and global analysis of protein localization in the fission yeast Schizosaccharomyces pombe."
    Matsuyama A., Arai R., Yashiroda Y., Shirai A., Kamata A., Sekido S., Kobayashi Y., Hashimoto A., Hamamoto M., Hiraoka Y., Horinouchi S., Yoshida M.
    Nat. Biotechnol. 24:841-847(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-120 AND SER-144, IDENTIFICATION BY MASS SPECTROMETRY.

Entry informationi

Entry nameiNGG1_SCHPO
AccessioniPrimary (citable) accession number: Q9USU8
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 4, 2008
Last sequence update: May 1, 2000
Last modified: January 7, 2015
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programFungal Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Schizosaccharomyces pombe
    Schizosaccharomyces pombe: entries and gene names
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.