TCF20

Functionⁱ

Transcriptional activator that binds to the regulatory region of MMP3 and thereby controls stromelysin expression. It stimulates the activity of various transcriptional activators such as JUN, SP1, PAX6 and ETS1, suggesting a function as a coactivator.

Regions

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
DNA bindingⁱ	1537 – 1551	15	A.T hook			Add BLAST
Zinc fingerⁱ	1884 – 1935	52	PHD-type; atypical			Add BLAST

GO - Molecular functionⁱ

DNA binding
Source: UniProtKB
Non-traceable author statementⁱ
- 10995766
poly(A) RNA binding
Source: UniProtKB
Inferred from direct assayⁱ
- 22658674
transcription coactivator activity
Source: UniProtKB
Non-traceable author statementⁱ
- 10995766
transcription factor activity, sequence-specific DNA binding Source: GO_Central
transcription regulatory region DNA binding Source: GO_Central
zinc ion binding Source: InterPro

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: Transcription factor 20 Short name: TCF-20 Alternative name(s): Nuclear factor SPBP Protein AR1 Stromelysin-1 PDGF-responsive element-binding protein Short name: SPRE-binding protein
Gene namesⁱ	Name:TCF20 Synonyms:KIAA0292, SPBP
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 22

Organism-specific databases

HGNCⁱ	HGNC:11631. TCF20.

HGNCⁱ

HGNC:11631. TCF20.

Subcellular locationⁱ

Nucleus

GO - Cellular componentⁱ

nucleoplasm Source: HPA
nucleus
Source: UniProtKB
Non-traceable author statementⁱ
- 10995766

Complete GO annotation...

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA36386.

PharmGKBⁱ

PA36386.

Polymorphism and mutation databases

BioMutaⁱ	TCF20.
DMDMⁱ	92090378.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Chainⁱ	1 – 1960	1960	Transcription factor 20		PRO_0000072448	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	419 – 419	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.8 "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions." Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K. Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-419, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	430 – 430	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	538 – 538	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	559 – 559	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	574 – 574	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	583 – 583	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	602 – 602	1	N6-acetyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9EPQ8 (TCF20_MOUSE)
Modified residueⁱ	640 – 640	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	710 – 710		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.14 "SUMO-2 orchestrates chromatin modifiers in response to DNA damage." Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C. Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-710; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	823 – 823		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "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-823; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.15 "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability." Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C. Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929; LYS-957; LYS-1137 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	844 – 844		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "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-823; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.14 "SUMO-2 orchestrates chromatin modifiers in response to DNA damage." Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C. Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-710; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.15 "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability." Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C. Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929; LYS-957; LYS-1137 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	871 – 871	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.9 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-966; SER-1053; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	929 – 929		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.13 "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli." Impens F., Radoshevich L., Cossart P., Ribet D. Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-929, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	929 – 929		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "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-823; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.13 "Mapping of SUMO sites and analysis of SUMOylation changes induced by external stimuli." Impens F., Radoshevich L., Cossart P., Ribet D. Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-929, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.14 "SUMO-2 orchestrates chromatin modifiers in response to DNA damage." Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C. Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-710; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.15 "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability." Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C. Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929; LYS-957; LYS-1137 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	957 – 957		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.15 "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability." Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C. Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929; LYS-957; LYS-1137 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	966 – 966	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.9 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-966; SER-1053; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1005 – 1005	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1053 – 1053	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.9 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-966; SER-1053; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	1137 – 1137		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.15 "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability." Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C. Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929; LYS-957; LYS-1137 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1305 – 1305	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1335 – 1335	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1361 – 1361	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	1446 – 1446		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.12 "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-823; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.14 "SUMO-2 orchestrates chromatin modifiers in response to DNA damage." Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V., Vertegaal A.C. Cell Rep. 10:1778-1791(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-710; LYS-844; LYS-929 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.15 "System-wide analysis of SUMOylation dynamics in response to replication stress reveals novel small ubiquitin-like modified target proteins and acceptor lysines relevant for genome stability." Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V., Vertegaal A.C. Mol. Cell. Proteomics 14:1419-1434(2015) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-823; LYS-844; LYS-929; LYS-957; LYS-1137 AND LYS-1446, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1522 – 1522	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.9 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-966; SER-1053; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.10 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1669 – 1669	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1671 – 1671	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.6 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-430; SER-574; SER-583; SER-871; SER-1335; SER-1361; SER-1522; SER-1669 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.9 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-871; SER-966; SER-1053; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.10 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.11 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-538; SER-559; SER-574; SER-583; SER-640; SER-871; SER-1005; SER-1305; SER-1522 AND THR-1671, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	1762 – 1762	1	PhosphothreonineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9EPQ8 (TCF20_MOUSE)
Modified residueⁱ	1764 – 1764	1	PhosphothreonineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9EPQ8 (TCF20_MOUSE)

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	Q9UGU0.
PaxDbⁱ	Q9UGU0.
PeptideAtlasⁱ	Q9UGU0.
PRIDEⁱ	Q9UGU0.

PTM databases

iPTMnetⁱ	Q9UGU0.
PhosphoSiteⁱ	Q9UGU0.

Miscellaneous databases

PMAP-CutDB	Q9UGU0.

PMAP-CutDB

Q9UGU0.

Expressionⁱ

Tissue specificityⁱ

Expressed in most tissues, except in ovary and prostate. Isoform 1 is exclusively expressed in brain, heart and testis, and this form predominates in liver and kidney. Isoform 2 predominates in lung.

Gene expression databases

Bgeeⁱ	ENSG00000100207.
CleanExⁱ	HS_TCF20.
ExpressionAtlasⁱ	Q9UGU0. baseline and differential.
Genevisibleⁱ	Q9UGU0. HS.

Organism-specific databases

HPAⁱ	CAB017849. HPA036786.

Interactionⁱ

Subunit structureⁱ

Homodimer (Probable). Interacts with RNF4 and JUN (By similarity).By similarityCurated

Protein-protein interaction databases

BioGridⁱ	112802. 37 interactions.
IntActⁱ	Q9UGU0. 28 interactions.
MINTⁱ	MINT-4541027.
STRINGⁱ	9606.ENSP00000352463.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	Q9UGU0.
SMRⁱ	Q9UGU0. Positions 1848-1932.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Regionⁱ	1170 – 1191	22	Leucine-zipper			Add BLAST

Motif

Feature key	Position(s)	Length	Description	Actions
Motifⁱ	1254 – 1268	15	Nuclear localization signalBy similarity	Add BLAST
Motifⁱ	1576 – 1600	25	Nuclear localization signalBy similarity	Add BLAST
Motifⁱ	1785 – 1792	8	Nuclear localization signalBy similarity

Compositional bias

Feature key	Position(s)	Length	Description	Actions
Compositional biasⁱ	62 – 70	9	Poly-Ala
Compositional biasⁱ	174 – 182	9	Poly-Gln
Compositional biasⁱ	203 – 262	60	Ser-rich	Add BLAST
Compositional biasⁱ	310 – 322	13	Poly-Gln	Add BLAST
Compositional biasⁱ	1556 – 1564	9	Poly-Pro

Domainⁱ

The atypical PHD domain functions as a negative modulator of cofactor binding.By similarity

Sequence similaritiesⁱ

Contains 1 A.T hook DNA-binding domain.Curated

Contains 1 PHD-type zinc finger.Curated

Zinc finger

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Zinc fingerⁱ	1884 – 1935	52	PHD-type; atypical			Add BLAST

Keywords - Domainⁱ

Zinc-finger

Phylogenomic databases

eggNOGⁱ	ENOG410IPTF. Eukaryota. ENOG410ZTQQ. LUCA.
GeneTreeⁱ	ENSGT00530000063684.
HOGENOMⁱ	HOG000026801.
HOVERGENⁱ	HBG079232.
InParanoidⁱ	Q9UGU0.
OMAⁱ	EVLQGYH.
OrthoDBⁱ	EOG091G00AM.
PhylomeDBⁱ	Q9UGU0.
TreeFamⁱ	TF331317.

Family and domain databases

InterProⁱ	IPR001965. Znf_PHD. [Graphical view]
SMARTⁱ	SM00249. PHD. 1 hit. [Graphical view]

Sequences (2)ⁱ

Sequence statusⁱ: Complete.

This entry describes 2 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: Q9UGU0-1) [UniParc]FASTA Add 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
MQSFREQSSY HGNQQSYPQE VHGSSRLEEF SPRQAQMFQN FGGTGGSSGS 
        60         70         80         90        100
SGSGSGGGRR GAAAAAAAMA SETSGHQGYQ GFRKEAGDFY YMAGNKDPVT 
       110        120        130        140        150
TGTPQPPQRR PSGPVQSYGP PQGSSFGNQY GSEGHVGQFQ AQHSGLGGVS 
       160        170        180        190        200
HYQQDYTGPF SPGSAQYQQQ ASSQQQQQQV QQLRQQLYQS HQPLPQATGQ 
       210        220        230        240        250
PASSSSHLQP MQRPSTLPSS AAGYQLRVGQ FGQHYQSSAS SSSSSSFPSP 
       260        270        280        290        300
QRFSQSGQSY DGSYNVNAGS QYEGHNVGSN AQAYGTQSNY SYQPQSMKNF 
       310        320        330        340        350
EQAKIPQGTQ QGQQQQQPQQ QQHPSQHVMQ YTNAATKLPL QSQVGQYNQP 
       360        370        380        390        400
EVPVRSPMQF HQNFSPISNP SPAASVVQSP SCSSTPSPLM QTGENLQCGQ 
       410        420        430        440        450
GSVPMGSRNR ILQLMPQLSP TPSMMPSPNS HAAGFKGFGL EGVPEKRLTD 
       460        470        480        490        500
PGLSSLSALS TQVANLPNTV QHMLLSDALT PQKKTSKRPS SSKKADSCTN 
       510        520        530        540        550
SEGSSQPEEQ LKSPMAESLD GGCSSSSEDQ GERVRQLSGQ STSSDTTYKG 
       560        570        580        590        600
GASEKAGSSP AQGAQNEPPR LNASPAAREE ATSPGAKDMP LSSDGNPKVN 
       610        620        630        640        650
EKTVGVIVSR EAMTGRVEKP GGQDKGSQED DPAATQRPPS NGGAKETSHA 
       660        670        680        690        700
SLPQPEPPGG GGSKGNKNGD NNSNHNGEGN GQSGHSAAGP GFTSRTEPSK 
       710        720        730        740        750
SPGSLRYSYK DSFGSAVPRN VSGFPQYPTG QEKGDFTGHG ERKGRNEKFP 
       760        770        780        790        800
SLLQEVLQGY HHHPDRRYSR STQEHQGMAG SLEGTTRPNV LVSQTNELAS 
       810        820        830        840        850
RGLLNKSIGS LLENPHWGPW ERKSSSTAPE MKQINLTDYP IPRKFEIEPQ 
       860        870        880        890        900
SSAHEPGGSL SERRSVICDI SPLRQIVRDP GAHSLGHMSA DTRIGRNDRL 
       910        920        930        940        950
NPTLSQSVIL PGGLVSMETK LKSQSGQIKE EDFEQSKSQA SFNNKKSGDH 
       960        970        980        990       1000
CHPPSIKHES YRGNASPGAA THDSLSDYGP QDSRPTPMRR VPGRVGGREG 
      1010       1020       1030       1040       1050
MRGRSPSQYH DFAEKLKMSP GRSRGPGGDP HHMNPHMTFS ERANRSSLHT 
      1060       1070       1080       1090       1100
PFSPNSETLA SAYHANTRAH AYGDPNAGLN SQLHYKRQMY QQQPEEYKDW 
      1110       1120       1130       1140       1150
SSGSAQGVIA AAQHRQEGPR KSPRQQQFLD RVRSPLKNDK DGMMYGPPVG 
      1160       1170       1180       1190       1200
TYHDPSAQEA GRCLMSSDGL PNKGMELKHG SQKLQESCWD LSRQTSPAKS 
      1210       1220       1230       1240       1250
SGPPGMSSQK RYGPPHETDG HGLAEATQSS KPGSVMLRLP GQEDHSSQNP 
      1260       1270       1280       1290       1300
LIMRRRVRSF ISPIPSKRQS QDVKNSSTED KGRLLHSSKE GADKAFNSYA 
      1310       1320       1330       1340       1350
HLSHSQDIKS IPKRDSSKDL PSPDSRNCPA VTLTSPAKTK ILPPRKGRGL 
      1360       1370       1380       1390       1400
KLEAIVQKIT SPNIRRSASS NSAEAGGDTV TLDDILSLKS GPPEGGSVAV 
      1410       1420       1430       1440       1450
QDADIEKRKG EVASDLVSPA NQELHVEKPL PRSSEEWRGS VDDKVKTETH 
      1460       1470       1480       1490       1500
AETVTAGKEP PGAMTSTTSQ KPGSNQGRPD GSLGGTAPLI FPDSKNVPPV 
      1510       1520       1530       1540       1550
GILAPEANPK AEEKENDTVT ISPKQEGFPP KGYFPSGKKK GRPIGSVNKQ 
      1560       1570       1580       1590       1600
KKQQQPPPPP PQPPQIPEGS ADGEPKPKKQ RQRRERRKPG AQPRKRKTKQ 
      1610       1620       1630       1640       1650
AVPIVEPQEP EIKLKYATQP LDKTDAKNKS FYPYIHVVNK CELGAVCTII 
      1660       1670       1680       1690       1700
NAEEEEQTKL VRGRKGQRSL TPPPSSTESK ALPASSFMLQ GPVVTESSVM 
      1710       1720       1730       1740       1750
GHLVCCLCGK WASYRNMGDL FGPFYPQDYA ATLPKNPPPK RATEMQSKVK 
      1760       1770       1780       1790       1800
VRHKSASNGS KTDTEEEEEQ QQQQKEQRSL AAHPRFKRRH RSEDCGGGPR 
      1810       1820       1830       1840       1850
SLSRGLPCKK AATEGSSEKT VLDSKPSVPT TSEGGPELEL QIPELPLDSN 
      1860       1870       1880       1890       1900
EFWVHEGCIL WANGIYLVCG RLYGLQEALE IAREMKCSHC QEAGATLGCY 
      1910       1920       1930       1940       1950
NKGCSFRYHY PCAIDADCLL HEENFSVRCP KHKPPLPCPL PPLQNKTAKG 
      1960
SLSTEQSERG

Length:1,960

Mass (Da):211,771

Last modified:March 7, 2006 - v3

Checksum:ⁱD3E34B1FAA6ED06F

GO

Isoform 2 (identifier: Q9UGU0-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
1934-1938: PPLPC → VRLWR
1939-1960: Missing.

« Hide

        10         20         30         40         50
MQSFREQSSY HGNQQSYPQE VHGSSRLEEF SPRQAQMFQN FGGTGGSSGS 
        60         70         80         90        100
SGSGSGGGRR GAAAAAAAMA SETSGHQGYQ GFRKEAGDFY YMAGNKDPVT 
       110        120        130        140        150
TGTPQPPQRR PSGPVQSYGP PQGSSFGNQY GSEGHVGQFQ AQHSGLGGVS 
       160        170        180        190        200
HYQQDYTGPF SPGSAQYQQQ ASSQQQQQQV QQLRQQLYQS HQPLPQATGQ 
       210        220        230        240        250
PASSSSHLQP MQRPSTLPSS AAGYQLRVGQ FGQHYQSSAS SSSSSSFPSP 
       260        270        280        290        300
QRFSQSGQSY DGSYNVNAGS QYEGHNVGSN AQAYGTQSNY SYQPQSMKNF 
       310        320        330        340        350
EQAKIPQGTQ QGQQQQQPQQ QQHPSQHVMQ YTNAATKLPL QSQVGQYNQP 
       360        370        380        390        400
EVPVRSPMQF HQNFSPISNP SPAASVVQSP SCSSTPSPLM QTGENLQCGQ 
       410        420        430        440        450
GSVPMGSRNR ILQLMPQLSP TPSMMPSPNS HAAGFKGFGL EGVPEKRLTD 
       460        470        480        490        500
PGLSSLSALS TQVANLPNTV QHMLLSDALT PQKKTSKRPS SSKKADSCTN 
       510        520        530        540        550
SEGSSQPEEQ LKSPMAESLD GGCSSSSEDQ GERVRQLSGQ STSSDTTYKG 
       560        570        580        590        600
GASEKAGSSP AQGAQNEPPR LNASPAAREE ATSPGAKDMP LSSDGNPKVN 
       610        620        630        640        650
EKTVGVIVSR EAMTGRVEKP GGQDKGSQED DPAATQRPPS NGGAKETSHA 
       660        670        680        690        700
SLPQPEPPGG GGSKGNKNGD NNSNHNGEGN GQSGHSAAGP GFTSRTEPSK 
       710        720        730        740        750
SPGSLRYSYK DSFGSAVPRN VSGFPQYPTG QEKGDFTGHG ERKGRNEKFP 
       760        770        780        790        800
SLLQEVLQGY HHHPDRRYSR STQEHQGMAG SLEGTTRPNV LVSQTNELAS 
       810        820        830        840        850
RGLLNKSIGS LLENPHWGPW ERKSSSTAPE MKQINLTDYP IPRKFEIEPQ 
       860        870        880        890        900
SSAHEPGGSL SERRSVICDI SPLRQIVRDP GAHSLGHMSA DTRIGRNDRL 
       910        920        930        940        950
NPTLSQSVIL PGGLVSMETK LKSQSGQIKE EDFEQSKSQA SFNNKKSGDH 
       960        970        980        990       1000
CHPPSIKHES YRGNASPGAA THDSLSDYGP QDSRPTPMRR VPGRVGGREG 
      1010       1020       1030       1040       1050
MRGRSPSQYH DFAEKLKMSP GRSRGPGGDP HHMNPHMTFS ERANRSSLHT 
      1060       1070       1080       1090       1100
PFSPNSETLA SAYHANTRAH AYGDPNAGLN SQLHYKRQMY QQQPEEYKDW 
      1110       1120       1130       1140       1150
SSGSAQGVIA AAQHRQEGPR KSPRQQQFLD RVRSPLKNDK DGMMYGPPVG 
      1160       1170       1180       1190       1200
TYHDPSAQEA GRCLMSSDGL PNKGMELKHG SQKLQESCWD LSRQTSPAKS 
      1210       1220       1230       1240       1250
SGPPGMSSQK RYGPPHETDG HGLAEATQSS KPGSVMLRLP GQEDHSSQNP 
      1260       1270       1280       1290       1300
LIMRRRVRSF ISPIPSKRQS QDVKNSSTED KGRLLHSSKE GADKAFNSYA 
      1310       1320       1330       1340       1350
HLSHSQDIKS IPKRDSSKDL PSPDSRNCPA VTLTSPAKTK ILPPRKGRGL 
      1360       1370       1380       1390       1400
KLEAIVQKIT SPNIRRSASS NSAEAGGDTV TLDDILSLKS GPPEGGSVAV 
      1410       1420       1430       1440       1450
QDADIEKRKG EVASDLVSPA NQELHVEKPL PRSSEEWRGS VDDKVKTETH 
      1460       1470       1480       1490       1500
AETVTAGKEP PGAMTSTTSQ KPGSNQGRPD GSLGGTAPLI FPDSKNVPPV 
      1510       1520       1530       1540       1550
GILAPEANPK AEEKENDTVT ISPKQEGFPP KGYFPSGKKK GRPIGSVNKQ 
      1560       1570       1580       1590       1600
KKQQQPPPPP PQPPQIPEGS ADGEPKPKKQ RQRRERRKPG AQPRKRKTKQ 
      1610       1620       1630       1640       1650
AVPIVEPQEP EIKLKYATQP LDKTDAKNKS FYPYIHVVNK CELGAVCTII 
      1660       1670       1680       1690       1700
NAEEEEQTKL VRGRKGQRSL TPPPSSTESK ALPASSFMLQ GPVVTESSVM 
      1710       1720       1730       1740       1750
GHLVCCLCGK WASYRNMGDL FGPFYPQDYA ATLPKNPPPK RATEMQSKVK 
      1760       1770       1780       1790       1800
VRHKSASNGS KTDTEEEEEQ QQQQKEQRSL AAHPRFKRRH RSEDCGGGPR 
      1810       1820       1830       1840       1850
SLSRGLPCKK AATEGSSEKT VLDSKPSVPT TSEGGPELEL QIPELPLDSN 
      1860       1870       1880       1890       1900
EFWVHEGCIL WANGIYLVCG RLYGLQEALE IAREMKCSHC QEAGATLGCY 
      1910       1920       1930 
NKGCSFRYHY PCAIDADCLL HEENFSVRCP KHKVRLWR

Show »

Length:1,938

Mass (Da):209,654

Checksum:ⁱDB67ACCB0AE5776C

GO

Sequence cautionⁱ

The sequence AAC36392 differs from that shown. Reason: Frameshift at position 1932. Curated

The sequence CAB42440 differs from that shown. Reason: Erroneous initiation. Curated

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Sequence conflictⁱ	122 – 122	1	Q → R (PubMed:10995766).Curated
Sequence conflictⁱ	200 – 200	1	Q → K (PubMed:10995766).Curated

Natural variant

Feature key	Position(s)	Length	Description	Feature identifier
Natural variantⁱ	405 – 405	1	M → V. Corresponds to variant rs34030679 [ dbSNP \| Ensembl ].	VAR_051419
Natural variantⁱ	485 – 485	1	T → N. Corresponds to variant rs6002656 [ dbSNP \| Ensembl ].	VAR_025427
Natural variantⁱ	722 – 722	1	S → G. Corresponds to variant rs5758651 [ dbSNP \| Ensembl ].	VAR_025428
Natural variantⁱ	1165 – 1165	1	M → I. Corresponds to variant rs17002890 [ dbSNP \| Ensembl ].	VAR_025429
Natural variantⁱ	1325 – 1325	1	S → N. Corresponds to variant rs17002888 [ dbSNP \| Ensembl ].	VAR_025430
Natural variantⁱ	1910 – 1910	1	Y → C. Corresponds to variant rs17002865 [ dbSNP \| Ensembl ].	VAR_051420

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Alternative sequenceⁱ	1934 – 1938	5	PPLPC → VRLWR in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.5 "Assignment of AR1, transcription factor 20 (TCF20), to human chromosome 22q13.3 with somatic cell hybrids and in situ hybridization." Rajadhyaksha A., Riviere M., Van Vooren P., Szpirer J., Szpirer C., Babin J., Bina M. Cytogenet. Cell Genet. 81:176-177(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1083-1938 (ISOFORM 2).		VSP_003984
Alternative sequenceⁱ	1939 – 1960	22	Missing in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.5 "Assignment of AR1, transcription factor 20 (TCF20), to human chromosome 22q13.3 with somatic cell hybrids and in situ hybridization." Rajadhyaksha A., Riviere M., Van Vooren P., Szpirer J., Szpirer C., Babin J., Bina M. Cytogenet. Cell Genet. 81:176-177(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1083-1938 (ISOFORM 2).		VSP_003985	Add BLAST

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY007595 Genomic DNA. Translation: AAG28930.1. AL031346 Genomic DNA. Translation: CAB42440.1. Different initiation. BX247885 Genomic DNA. Translation: CAI95721.1. BX247885 Genomic DNA. Translation: CAP58858.1. CH471095 Genomic DNA. Translation: EAW60495.1. AB006630 mRNA. Translation: BAA22961.1. U19345 mRNA. Translation: AAC36392.1. Frameshift.
CCDSⁱ	CCDS14032.1. [Q9UGU0-2] CCDS14033.1. [Q9UGU0-1]
RefSeqⁱ	NP_005641.1. NM_005650.3. [Q9UGU0-1] NP_852469.1. NM_181492.2. [Q9UGU0-2] XP_005261779.1. XM_005261722.3. [Q9UGU0-1] XP_006724376.1. XM_006724313.3. [Q9UGU0-1] XP_011528656.1. XM_011530354.2. [Q9UGU0-2]
UniGeneⁱ	Hs.475018.

Genome annotation databases

Ensemblⁱ	ENST00000335626; ENSP00000335561; ENSG00000100207. [Q9UGU0-2] ENST00000359486; ENSP00000352463; ENSG00000100207. [Q9UGU0-1] ENST00000574943; ENSP00000460328; ENSG00000262024. [Q9UGU0-1] ENST00000576946; ENSP00000460587; ENSG00000262024. [Q9UGU0-2] ENST00000619505; ENSP00000478503; ENSG00000276461. [Q9UGU0-2] ENST00000621408; ENSP00000483199; ENSG00000276461. [Q9UGU0-1] ENST00000626486; ENSP00000487465; ENSG00000280467. [Q9UGU0-2] ENST00000626726; ENSP00000487302; ENSG00000281897. [Q9UGU0-1] ENST00000628774; ENSP00000487296; ENSG00000280467. [Q9UGU0-1] ENST00000629538; ENSP00000486940; ENSG00000281897. [Q9UGU0-2] ENST00000634489; ENSP00000489099; ENSG00000282892. [Q9UGU0-2] ENST00000634616; ENSP00000489614; ENSG00000283026. [Q9UGU0-1] ENST00000635146; ENSP00000489215; ENSG00000282892. [Q9UGU0-1] ENST00000635421; ENSP00000489006; ENSG00000283026. [Q9UGU0-2]
GeneIDⁱ	6942.
KEGGⁱ	hsa:6942.
UCSCⁱ	uc003bck.3. human. [Q9UGU0-1]

Keywords - Coding sequence diversityⁱ

Alternative splicing, Polymorphism

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AY007595 Genomic DNA. Translation: AAG28930.1. AL031346 Genomic DNA. Translation: CAB42440.1. Different initiation. BX247885 Genomic DNA. Translation: CAI95721.1. BX247885 Genomic DNA. Translation: CAP58858.1. CH471095 Genomic DNA. Translation: EAW60495.1. AB006630 mRNA. Translation: BAA22961.1. U19345 mRNA. Translation: AAC36392.1. Frameshift.
CCDSⁱ	CCDS14032.1. [Q9UGU0-2] CCDS14033.1. [Q9UGU0-1]
RefSeqⁱ	NP_005641.1. NM_005650.3. [Q9UGU0-1] NP_852469.1. NM_181492.2. [Q9UGU0-2] XP_005261779.1. XM_005261722.3. [Q9UGU0-1] XP_006724376.1. XM_006724313.3. [Q9UGU0-1] XP_011528656.1. XM_011530354.2. [Q9UGU0-2]
UniGeneⁱ	Hs.475018.

3D structure databases

ProteinModelPortalⁱ	Q9UGU0.
SMRⁱ	Q9UGU0. Positions 1848-1932.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	112802. 37 interactions.
IntActⁱ	Q9UGU0. 28 interactions.
MINTⁱ	MINT-4541027.
STRINGⁱ	9606.ENSP00000352463.

PTM databases

iPTMnetⁱ	Q9UGU0.
PhosphoSiteⁱ	Q9UGU0.

Polymorphism and mutation databases

BioMutaⁱ	TCF20.
DMDMⁱ	92090378.

Proteomic databases

EPDⁱ	Q9UGU0.
PaxDbⁱ	Q9UGU0.
PeptideAtlasⁱ	Q9UGU0.
PRIDEⁱ	Q9UGU0.

Protocols and materials databases

Structural Biology Knowledgebase	Search...

Structural Biology Knowledgebase

Search...

Genome annotation databases

Ensemblⁱ	ENST00000335626; ENSP00000335561; ENSG00000100207. [Q9UGU0-2] ENST00000359486; ENSP00000352463; ENSG00000100207. [Q9UGU0-1] ENST00000574943; ENSP00000460328; ENSG00000262024. [Q9UGU0-1] ENST00000576946; ENSP00000460587; ENSG00000262024. [Q9UGU0-2] ENST00000619505; ENSP00000478503; ENSG00000276461. [Q9UGU0-2] ENST00000621408; ENSP00000483199; ENSG00000276461. [Q9UGU0-1] ENST00000626486; ENSP00000487465; ENSG00000280467. [Q9UGU0-2] ENST00000626726; ENSP00000487302; ENSG00000281897. [Q9UGU0-1] ENST00000628774; ENSP00000487296; ENSG00000280467. [Q9UGU0-1] ENST00000629538; ENSP00000486940; ENSG00000281897. [Q9UGU0-2] ENST00000634489; ENSP00000489099; ENSG00000282892. [Q9UGU0-2] ENST00000634616; ENSP00000489614; ENSG00000283026. [Q9UGU0-1] ENST00000635146; ENSP00000489215; ENSG00000282892. [Q9UGU0-1] ENST00000635421; ENSP00000489006; ENSG00000283026. [Q9UGU0-2]
GeneIDⁱ	6942.
KEGGⁱ	hsa:6942.
UCSCⁱ	uc003bck.3. human. [Q9UGU0-1]

Organism-specific databases

CTDⁱ	6942.
GeneCardsⁱ	TCF20.
H-InvDB	HIX0016540.
HGNCⁱ	HGNC:11631. TCF20.
HPAⁱ	CAB017849. HPA036786.
MIMⁱ	603107. gene.
neXtProtⁱ	NX_Q9UGU0.
PharmGKBⁱ	PA36386.
HUGEⁱ	Search...
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IPTF. Eukaryota. ENOG410ZTQQ. LUCA.
GeneTreeⁱ	ENSGT00530000063684.
HOGENOMⁱ	HOG000026801.
HOVERGENⁱ	HBG079232.
InParanoidⁱ	Q9UGU0.
OMAⁱ	EVLQGYH.
OrthoDBⁱ	EOG091G00AM.
PhylomeDBⁱ	Q9UGU0.
TreeFamⁱ	TF331317.

Miscellaneous databases

ChiTaRSⁱ	TCF20. human.
GeneWikiⁱ	TCF20.
GenomeRNAiⁱ	6942.
PMAP-CutDB	Q9UGU0.
PROⁱ	Q9UGU0.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000100207.
CleanExⁱ	HS_TCF20.
ExpressionAtlasⁱ	Q9UGU0. baseline and differential.
Genevisibleⁱ	Q9UGU0. HS.

Family and domain databases

InterProⁱ	IPR001965. Znf_PHD. [Graphical view]
SMARTⁱ	SM00249. PHD. 1 hit. [Graphical view]
ProtoNetⁱ	Search...

Entry informationⁱ

Entry nameⁱ

TCF20_HUMAN

Accessionⁱ

Primary (citable) accession number: Q9UGU0
Secondary accession number(s): A9JX12

Q9H4M0

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	August 2, 2002
Last sequence update:	March 7, 2006
Last modified:	September 7, 2016
This is version 134 of the entry and version 3 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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, Reference proteome

Documents

Human chromosome 22
Human chromosome 22: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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.

UniProtKB

UniParc

Help

UniRef

Proteomes

Annotation systems

Supporting data

UniProtKB - Q9UGU0 (TCF20_HUMAN)

UniProt

Q9UGU0 - TCF20_HUMAN

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Transcription factor 20

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

Miscellaneous databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Motif

Compositional bias

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Zinc finger

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (2)i

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (2)ⁱ

Sequence cautionⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ