| Tag | Content |
|---|
| CPLM ID | CPLM-006418 |
UniProt Accession | |
Genbank Protein ID | |
Genbank Nucleotide ID | |
Protein Name | Transcriptional activator SPT7 |
Protein Synonyms/Alias | |
Gene Name | SPT7 |
Gene Synonyms/Alias | YBR081C; YBR0739 |
Created Date | July 27, 2013 |
Organism | Saccharomyces cerevisiae (strain ATCC 204508 / S288c) (Baker's yeast) |
NCBI Taxa ID | 559292 |
Lysine Modification | Position | Peptide | Type | References |
|---|
| 379 | TFSDTGNKRPKQSNL | acetylation | [1, 2] | | 400 | GIENLSLKHLLSSIQ | acetylation | [1] | | 410 | LSSIQQKKSQLGISD | acetylation | [1] | | 469 | HSTPFLNKVSKREAP | acetylation | [2] | | 584 | EVAGSGRKGLNMGAH | acetylation | [1, 2] | | 595 | MGAHMLAKENGKVSE | acetylation | [2] | | 599 | MLAKENGKVSEKDSS | acetylation | [1] | | 603 | ENGKVSEKDSSKTVK | acetylation | [1, 2] | | 607 | VSEKDSSKTVKDEAP | acetylation | [1, 2] | | 610 | KDSSKTVKDEAPTND | acetylation | [1] | | 629 | SVIPEGEKEKDKTAS | acetylation | [1, 2] | | 633 | EGEKEKDKTASSTVT | acetylation | [1, 2] | | 647 | TVHENVNKNEIKENG | acetylation | [1, 2] | | 655 | NEIKENGKNEEQDMV | acetylation | [2] | | 667 | DMVEESSKTEDSSKD | acetylation | [1, 2] | | 679 | SKDADAAKKDTEDGL | acetylation | [2] | | 680 | KDADAAKKDTEDGLQ | acetylation | [1, 2] | | 897 | QSRFLANKDLGLTPK | acetylation | [2] |
|
Reference | [1] In-depth profiling of post-translational modifications on the related transcription factor complexes TFIID and SAGA. Mischerikow N, Spedale G, Altelaar AF, Timmers HT, Pijnappel WW, Heck AJ. J Proteome Res. 2009 Nov;8(11):5020-30. [ PMID: 19731963] [2] Proteome-wide analysis of lysine acetylation suggests its broad regulatory scope in Saccharomyces cerevisiae. Henriksen P, Wagner SA, Weinert BT, Sharma S, Bacinskaja G, Rehman M, Juffer AH, Walther TC, Lisby M, Choudhary C. Mol Cell Proteomics. 2012 Nov;11(11):1510-22. [ PMID: 22865919] |
Functional Description | Functions as component of the transcription regulatory histone acetylation (HAT) complexes SAGA, SALSA and SLIK. SAGA is involved in RNA polymerase II-dependent transcriptional regulation of approximately 10% of yeast 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 (SPT3, SPT8 and SPT20) and promoter selectivity, interaction with transcription activators (GCN5, ADA2, ADA3 and TRA1), and chromatin modification through histone acetylation (GCN5) and deubiquitination (UBP8). 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, at least after activation at the GAL1-10 locus. SPT7 is transcriptional activator of TY elements and other genes. |
Sequence Annotation | DOMAIN 458 528 Bromo.
MOD_RES 78 78 Phosphothreonine; by ATM or ATR.
MOD_RES 88 88 Phosphoserine.
MOD_RES 1293 1293 Phosphoserine. |
Keyword | Activator; Bromodomain; Complete proteome; Nucleus; Phosphoprotein; Reference proteome; Transcription; Transcription regulation. |
Sequence Source | UniProt (SWISSPROT/TrEMBL); GenBank; EMBL |
Protein Length | 1332 AA |
Protein Sequence | MTERIPIKNY QRTNAKALLK LTEKLFNKNF FDLYLTSQQL VVLEYLLSIS SEEDKLKAWD 60
YFLKGNIALN VEKSFPLTQE EEHHGAVSPA VDTRSDDVSS QTIKDNNNTN TNTSISNENH 120
VENEIEDKGD NAIANEDNFV NNDESDNVEE DLFKLDLEDL KQQISGTRFI GNLSLKIRYV 180
LWQCAIDYIY CDRNEFGDEN DTEYTLLDVE EKEEEEIGKN EKPQNKEGIS KFAEDEDYDD 240
EDENYDEDST DVKNVDDPPK NLDSISSSNI EIDDERRLVL NISISKETLS KLKTNNVEEI 300
MGNWNKIYHS FEYDKETMIK RLKLEESDKM IEKGKKKRSR SDLEAATDEQ DRENTNDEPD 360
TNQKLPTPEG STFSDTGNKR PKQSNLDLTV NLGIENLSLK HLLSSIQQKK SQLGISDYEL 420
KHLIMDVRKN RSKWTSDERI GQEELYEACE KVVLELRNYT EHSTPFLNKV SKREAPNYHQ 480
IIKKSMDLNT VLKKLKSFQY DSKQEFVDDI MLIWKNCLTY NSDPSHFLRG HAIAMQKKSL 540
QLIRMIPNIT IRNRADLEKE IEDMEKDKDY ELDEEEEVAG SGRKGLNMGA HMLAKENGKV 600
SEKDSSKTVK DEAPTNDDKL TSVIPEGEKE KDKTASSTVT VHENVNKNEI KENGKNEEQD 660
MVEESSKTED SSKDADAAKK DTEDGLQDKT AENKEAGENN EEEEDDDDED EDEDMVDSQS 720
YLLEKDDDRD DLEISVWKTV TAKVRAEICL KRTEYFKNGK LNSDSEAFLK NPQRMKRFDQ 780
LFLEYKEQKA LESYRQKIEQ NSIMKNGFGT VLKQEDDDQL QFHNDHSLNG NEAFEKQPND 840
IELDDTRFLQ EYDISNAIPD IVYEGVNTKT LDKMEDASVD RMLQNGINKQ SRFLANKDLG 900
LTPKMNQNIT LIQQIRHICH KISLIRMLQS PLSAQNSRSN PNAFLNNHIY NYTIIDDSLD 960
IDPVSQLPTH DYKNNRELIW KFMHKNISKV AMANGFETAH PSAINMLTEI AGDYLSNLIK 1020
TLKLHHETNS LNRGTNVEML QTTLLENGIN RPDDLFSYVE SEFGKKTKKL QDIKQKLESF 1080
LRALLRPTLQ ELSERNFEDE SQSFFTGDFA SELTGEDFFG FRELGLEKEF GVLSSSVPLQ 1140
LLTTQFQTVD GETKVQAKKI QPEESDSIVY KKITKGMLDA GSFWNTLLPL LQKDYERSKA 1200
YIAKQSKSSA NDKTSMTSTE DNSFALLEED QFVSKKTATK ARLPPTGKIS TTYKKKPIAS 1260
AFILPEEDLE NDVKADPTTT VNAKVGAEND GDSSLFLRTP QPLDPLDMDD AFDDTNMGSN 1320
SSFSLSLPRL NQ 1332 |
Gene Ontology | GO:0005739; C:mitochondrion; IDA:SGD. GO:0000124; C:SAGA complex; IDA:SGD. GO:0046695; C:SLIK (SAGA-like) complex; IDA:SGD. GO:0005198; F:structural molecule activity; IDA:SGD. GO:0000747; P:conjugation with cellular fusion; IMP:SGD. GO:0016573; P:histone acetylation; IDA:SGD. GO:0006461; P:protein complex assembly; IMP:SGD. GO:0006355; P:regulation of transcription, DNA-dependent; IEA:UniProtKB-KW. GO:0006351; P:transcription, DNA-dependent; IEA:UniProtKB-KW. |
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