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Protein

Transcription initiation protein SPT3 homolog

Gene

SUPT3H

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Probable transcriptional activator.1 Publication

GO - Molecular functioni

  • DNA binding Source: GO_Central
  • transcription coactivator activity Source: UniProtKB

GO - Biological processi

  • histone deubiquitination Source: UniProtKB
  • histone H3 acetylation Source: UniProtKB
  • mitophagy in response to mitochondrial depolarization Source: ParkinsonsUK-UCL
  • positive regulation of defense response to virus by host Source: ParkinsonsUK-UCL
  • positive regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription, DNA-templated Source: UniProtKB
  • regulation of transcription from RNA polymerase II promoter Source: ProtInc
  • transcription from RNA polymerase II promoter Source: ProtInc
  • xenophagy Source: ParkinsonsUK-UCL
Complete GO annotation...

Keywords - Molecular functioni

Activator

Keywords - Biological processi

Transcription, Transcription regulation

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Names & Taxonomyi

Protein namesi
Recommended name:
Transcription initiation protein SPT3 homolog
Alternative name(s):
SPT3-like protein
Gene namesi
Name:SUPT3H
Synonyms:SPT3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 6

Organism-specific databases

HGNCiHGNC:11466. SUPT3H.

Subcellular locationi

GO - Cellular componenti

  • nucleoplasm Source: HPA
  • nucleus Source: UniProtKB
  • SAGA complex Source: GO_Central
  • STAGA complex Source: UniProtKB
  • transcription factor TFTC complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA36252.

Polymorphism and mutation databases

BioMutaiSUPT3H.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 399399Transcription initiation protein SPT3 homologPRO_0000072313Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Cross-linki205 – 205Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources
Isoform 2 (identifier: O75486-2)
Modified residuei1 – 11N-acetylmethionineCombined sources

Keywords - PTMi

Acetylation, Isopeptide bond, Ubl conjugation

Proteomic databases

EPDiO75486.
MaxQBiO75486.
PaxDbiO75486.
PeptideAtlasiO75486.
PRIDEiO75486.

PTM databases

iPTMnetiO75486.
PhosphoSiteiO75486.

Expressioni

Tissue specificityi

Expressed in all tissues tested including pancreas, kidney, skeletal muscle, liver, lung, placenta, brain and heart.

Gene expression databases

BgeeiO75486.
CleanExiHS_SUPT3H.
ExpressionAtlasiO75486. baseline and differential.
GenevisibleiO75486. HS.

Organism-specific databases

HPAiHPA024371.

Interactioni

Subunit structurei

Component of the PCAF complex, at least composed of TADA2L/ADA2, SUPT3H, TADA3L/ADA3, TAF5L/PAF65-beta, TAF6L/PAF65-alpha, TAF10/TAFII30, TAF12/TAFII20, TAF9/TAFII31 and TRRAP. Associates with TAFII31 and GCN5L2. Component of the TFTC-HAT complex, at least composed of TAF5L, TAF6L, TADA3L, SUPT3H/SPT3, TAF2/TAFII150, TAF4/TAFII135, TAF5/TAFII100, GCN5L2/GCN5, TAF10 and TRRAP. Component of the STAGA transcription coactivator-HAT complex, at least composed of SUPT3H, GCN5L2, TAF5L, TAF6L, SUPT7L, TADA3L, TAD1L, TAF10, TAF12, TRRAP and TAF9. The STAGA core complex is associated with a subcomplex required for histone deubiquitination composed of ATXN7L3, ENY2 and USP22.4 Publications

Protein-protein interaction databases

BioGridi114042. 35 interactions.
DIPiDIP-28148N.
IntActiO75486. 6 interactions.
STRINGi9606.ENSP00000360515.

Structurei

3D structure databases

ProteinModelPortaliO75486.
SMRiO75486. Positions 107-151.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Sequence similaritiesi

Belongs to the SPT3 family.Curated

Phylogenomic databases

eggNOGiKOG3902. Eukaryota.
ENOG410Z86C. LUCA.
GeneTreeiENSGT00390000010738.
HOGENOMiHOG000294119.
HOVERGENiHBG058560.
InParanoidiO75486.
KOiK11313.
OMAiHPVKIAR.
OrthoDBiEOG738052.
PhylomeDBiO75486.
TreeFamiTF323574.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR003195. TFIID-18.
[Graphical view]
PANTHERiPTHR11380. PTHR11380. 1 hit.
PfamiPF02269. TFIID-18kDa. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: O75486-1) [UniParc]FASTAAdd to basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MYSPRGSQGR GTAEATANSP SPPIAPSHSR VTFSLSTLHT LSPPPRPFPS
60 70 80 90 100
VSRAAAQKPH HLHPHILLAG SAAVPPRVLK AEMNNTAASP MSTATSSSGR
110 120 130 140 150
STGKSISFAT ELQSMMYSLG DARRPLHETA VLVEDVVHTQ LINLLQQAAE
160 170 180 190 200
VSQLRGARVI TPEDLLFLMR KDKKKLRRLL KYMFIRDYKS KIVKGIDEDD
210 220 230 240 250
LLEDKLSGSN NANKRQKIAQ DFLNSIDQTG ELLAMFEDDE IDEVKQERME
260 270 280 290 300
RAERQTRIMD SAQYAEFCES RQLSFSKKAS KFRDWLDCSS MEIKPNVVAM
310 320 330 340 350
EILAYLAYET VAQLVDLALL VRQDMVTKAG DPFSHAISAT FIQYHNSAES
360 370 380 390
TAACGVEAHS DAIQPCHIRE AIRRYSHRIG PLSPFTNAYR RNGMAFLAC
Length:399
Mass (Da):44,362
Last modified:May 15, 2002 - v2
Checksum:i06CD35E28A301F35
GO
Isoform 2 (identifier: O75486-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-82: Missing.

Show »
Length:317
Mass (Da):35,793
Checksum:iAF339954A57DB5A6
GO
Isoform 3 (identifier: O75486-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-116: MYSPRGSQGR...SFATELQSMM → MVVFGTTFFN...ILPLLNDSGR

Show »
Length:328
Mass (Da):37,427
Checksum:i3E2B1193CD0C5393
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti124 – 1285RPLHE → SLFMR in AAC70014 (PubMed:9787080).Curated
Sequence conflicti255 – 2573QTR → HNS in AAC70014 (PubMed:9787080).Curated
Sequence conflicti306 – 3061L → S in BAG36602 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti324 – 3241D → A.
Corresponds to variant rs16872923 [ dbSNP | Ensembl ].
VAR_057000

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 116116MYSPR…LQSMM → MVVFGTTFFNFDSFIGKTDS IEIIGKSVFPYCYHNILPLL NDSGR in isoform 3. 1 PublicationVSP_035878Add
BLAST
Alternative sequencei1 – 8282Missing in isoform 2. 3 PublicationsVSP_003975Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064804 mRNA. Translation: AAC70014.1.
AF069734 mRNA. Translation: AAC39904.1.
AF073930 mRNA. Translation: AAC36098.1.
AK313874 mRNA. Translation: BAG36602.1.
AL096865
, AL138880, AL161905, AL360272 Genomic DNA. Translation: CAI19927.1.
AL138880
, AL096865, AL161905, AL360272 Genomic DNA. Translation: CAI14627.1.
AL161905
, AL096865, AL138880, AL360272 Genomic DNA. Translation: CAI15666.1.
AL360272
, AL096865, AL138880, AL161905 Genomic DNA. Translation: CAH70848.1.
AL360272
, AL138880, AL161905, AL499610 Genomic DNA. Translation: CAH70846.1.
AL499610
, AL138880, AL161905, AL360272 Genomic DNA. Translation: CAH73344.1.
AL138880
, AL161905, AL360272, AL499610 Genomic DNA. Translation: CAI14625.1.
AL161905
, AL138880, AL360272, AL499610 Genomic DNA. Translation: CAI15664.1.
CH471081 Genomic DNA. Translation: EAX04274.1.
CH471081 Genomic DNA. Translation: EAX04275.1.
BC050384 mRNA. Translation: AAH50384.1.
CCDSiCCDS34465.1. [O75486-2]
CCDS34466.1. [O75486-3]
RefSeqiNP_003590.1. NM_003599.3. [O75486-2]
NP_852001.1. NM_181356.2. [O75486-3]
UniGeneiHs.368325.

Genome annotation databases

EnsembliENST00000371459; ENSP00000360514; ENSG00000196284. [O75486-2]
ENST00000371460; ENSP00000360515; ENSG00000196284. [O75486-3]
ENST00000475057; ENSP00000436411; ENSG00000196284. [O75486-2]
GeneIDi8464.
KEGGihsa:8464.
UCSCiuc003oxn.3. human. [O75486-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF064804 mRNA. Translation: AAC70014.1.
AF069734 mRNA. Translation: AAC39904.1.
AF073930 mRNA. Translation: AAC36098.1.
AK313874 mRNA. Translation: BAG36602.1.
AL096865
, AL138880, AL161905, AL360272 Genomic DNA. Translation: CAI19927.1.
AL138880
, AL096865, AL161905, AL360272 Genomic DNA. Translation: CAI14627.1.
AL161905
, AL096865, AL138880, AL360272 Genomic DNA. Translation: CAI15666.1.
AL360272
, AL096865, AL138880, AL161905 Genomic DNA. Translation: CAH70848.1.
AL360272
, AL138880, AL161905, AL499610 Genomic DNA. Translation: CAH70846.1.
AL499610
, AL138880, AL161905, AL360272 Genomic DNA. Translation: CAH73344.1.
AL138880
, AL161905, AL360272, AL499610 Genomic DNA. Translation: CAI14625.1.
AL161905
, AL138880, AL360272, AL499610 Genomic DNA. Translation: CAI15664.1.
CH471081 Genomic DNA. Translation: EAX04274.1.
CH471081 Genomic DNA. Translation: EAX04275.1.
BC050384 mRNA. Translation: AAH50384.1.
CCDSiCCDS34465.1. [O75486-2]
CCDS34466.1. [O75486-3]
RefSeqiNP_003590.1. NM_003599.3. [O75486-2]
NP_852001.1. NM_181356.2. [O75486-3]
UniGeneiHs.368325.

3D structure databases

ProteinModelPortaliO75486.
SMRiO75486. Positions 107-151.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114042. 35 interactions.
DIPiDIP-28148N.
IntActiO75486. 6 interactions.
STRINGi9606.ENSP00000360515.

PTM databases

iPTMnetiO75486.
PhosphoSiteiO75486.

Polymorphism and mutation databases

BioMutaiSUPT3H.

Proteomic databases

EPDiO75486.
MaxQBiO75486.
PaxDbiO75486.
PeptideAtlasiO75486.
PRIDEiO75486.

Protocols and materials databases

DNASUi8464.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000371459; ENSP00000360514; ENSG00000196284. [O75486-2]
ENST00000371460; ENSP00000360515; ENSG00000196284. [O75486-3]
ENST00000475057; ENSP00000436411; ENSG00000196284. [O75486-2]
GeneIDi8464.
KEGGihsa:8464.
UCSCiuc003oxn.3. human. [O75486-1]

Organism-specific databases

CTDi8464.
GeneCardsiSUPT3H.
HGNCiHGNC:11466. SUPT3H.
HPAiHPA024371.
MIMi602947. gene.
neXtProtiNX_O75486.
PharmGKBiPA36252.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3902. Eukaryota.
ENOG410Z86C. LUCA.
GeneTreeiENSGT00390000010738.
HOGENOMiHOG000294119.
HOVERGENiHBG058560.
InParanoidiO75486.
KOiK11313.
OMAiHPVKIAR.
OrthoDBiEOG738052.
PhylomeDBiO75486.
TreeFamiTF323574.

Enzyme and pathway databases

ReactomeiR-HSA-3214847. HATs acetylate histones.

Miscellaneous databases

ChiTaRSiSUPT3H. human.
GeneWikiiTranscription_initiation_protein_SPT3_homolog.
GenomeRNAii8464.
PROiO75486.
SOURCEiSearch...

Gene expression databases

BgeeiO75486.
CleanExiHS_SUPT3H.
ExpressionAtlasiO75486. baseline and differential.
GenevisibleiO75486. HS.

Family and domain databases

Gene3Di1.10.20.10. 1 hit.
InterProiIPR009072. Histone-fold.
IPR003195. TFIID-18.
[Graphical view]
PANTHERiPTHR11380. PTHR11380. 1 hit.
PfamiPF02269. TFIID-18kDa. 1 hit.
[Graphical view]
SUPFAMiSSF47113. SSF47113. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of a human homologue of the Saccharomyces cerevisiae transcription factor Spt3 (SUPT3H)."
    Yu J., Madison J.M., Mundlos S., Winston F., Olsen B.R.
    Genomics 53:90-96(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION.
    Tissue: Craniofacial.
  2. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 159-170 AND 379-390.
    Tissue: Cervix carcinoma.
  3. "A human SPT3-TAFII31-GCN5-L acetylase complex distinct from transcription factor IID."
    Martinez E., Kundu T.K., Fu J., Roeder R.G.
    J. Biol. Chem. 273:23781-23785(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, INTERACTION WITH TAFII31 AND GCN5L2.
    Tissue: Cervix carcinoma.
  4. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
    Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
    , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
    Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
    Tissue: Testis.
  5. "The DNA sequence and analysis of human chromosome 6."
    Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D.
    , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
    Nature 425:805-811(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
    Tissue: Colon.
  8. "The 400 kDa subunit of the PCAF histone acetylase complex belongs to the ATM superfamily."
    Vassilev A., Yamauchi J., Kotani T., Prives C., Avantaggiati M.L., Qin J., Nakatani Y.
    Mol. Cell 2:869-875(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE PCAF COMPLEX WITH TADA2L; TADA3L; TAF5L; TAF6L; TAF10; TAF12; TRRAP AND TAF9.
    Tissue: Fetal heart.
  9. "Identification of TATA-binding protein-free TAFII-containing complex subunits suggests a role in nucleosome acetylation and signal transduction."
    Brand M., Yamamoto K., Staub A., Tora L.
    J. Biol. Chem. 274:18285-18289(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE TFTC-HAT COMPLEX WITH TAF5L; TAF6L; TADA3L; TAF2; TAF4; TAF5; TRRAP; GCN5L2 AND TAF10.
  10. "Human STAGA complex is a chromatin-acetylating transcription coactivator that interacts with pre-mRNA splicing and DNA damage-binding factors in vivo."
    Martinez E., Palhan V.B., Tjernberg A., Lymar E.S., Gamper A.M., Kundu T.K., Chait B.T., Roeder R.G.
    Mol. Cell. Biol. 21:6782-6795(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE STAGA COMPLEX, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
  11. "A TFTC/STAGA module mediates histone H2A and H2B deubiquitination, coactivates nuclear receptors, and counteracts heterochromatin silencing."
    Zhao Y., Lang G., Ito S., Bonnet J., Metzger E., Sawatsubashi S., Suzuki E., Le Guezennec X., Stunnenberg H.G., Krasnov A., Georgieva S.G., Schuele R., Takeyama K., Kato S., Tora L., Devys D.
    Mol. Cell 29:92-101(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN STAGA COMPLEX.
  12. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1 (ISOFORM 2), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-205, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiSUPT3_HUMAN
AccessioniPrimary (citable) accession number: O75486
Secondary accession number(s): A6NKG9
, B2R9Q5, O76066, Q5TAV9, Q86VN7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 15, 2002
Last sequence update: May 15, 2002
Last modified: July 6, 2016
This is version 139 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. SIMILARITY comments
    Index of protein domains and families

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 one 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.