General transcription factor II-I

Complete GO annotation...

Names & Taxonomyⁱ

Protein namesⁱ	Recommended name: General transcription factor II-I Short name: GTFII-I Short name: TFII-I Alternative name(s): Bruton tyrosine kinase-associated protein 135 Short name: BAP-135 Short name: BTK-associated protein 135 SRF-Phox1-interacting protein Short name: SPIN Williams-Beuren syndrome chromosomal region 6 protein
Gene namesⁱ	Name:GTF2I Synonyms:BAP135, WBSCR6
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 7

Organism-specific databases

HGNCⁱ	HGNC:4659. GTF2I.

HGNCⁱ

HGNC:4659. GTF2I.

Subcellular locationⁱ

Cytoplasm
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase."
  Novina C.D., Kumar S., Bajpai U., Cheriyath V., Zhang K., Pillai S., Wortis H.H., Roy A.L.
  Mol. Cell. Biol. 19:5014-5024(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: INTERACTION WITH BTK, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Nucleus
PROSITE-ProRule annotation
Manual assertion according to rulesⁱ
- PROSITE-ProRule:PRU00484
1 Publication
Manual assertion based on experiment inⁱ
- Ref.10
  "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase."
  Novina C.D., Kumar S., Bajpai U., Cheriyath V., Zhang K., Pillai S., Wortis H.H., Roy A.L.
  Mol. Cell. Biol. 19:5014-5024(1999) [PubMed] [Europe PMC] [Abstract]
  Cited for: INTERACTION WITH BTK, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.

Note:

Colocalizes with BTK in the cytoplasm.

GO - Cellular componentⁱ

cell projection Source: Ensembl
cytoplasm Source: GO_Central
cytosol Source: Ensembl
membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 19946888
neuronal cell body Source: Ensembl
nucleoplasm Source: HPA
nucleus
Source: MGI
Inferred from direct assayⁱ
- 19242469

Keywords - Cellular componentⁱ

Cytoplasm, Nucleus

Pathology & Biotechⁱ

Involvement in diseaseⁱ

GTF2I is located in the Williams-Beuren syndrome (WBS) critical region. WBS results from a hemizygous deletion of several genes on chromosome 7q11.23, thought to arise as a consequence of unequal crossing over between highly homologous low-copy repeat sequences flanking the deleted region. Haploinsufficiency of GTF2I may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.

Mutagenesis

Feature key	Position(s)	Length	Description
Mutagenesisⁱ	248 – 248	1	Y → F: Abolishes BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-398 and F-503. 1 Publication Manual assertion based on experiment inⁱ Ref.11 "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I." Egloff A.M., Desiderio S. J. Biol. Chem. 276:27806-27815(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, FUNCTION, MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503.
Mutagenesisⁱ	398 – 398	1	Y → F: Abolishes BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-248 and F-503. 1 Publication Manual assertion based on experiment inⁱ Ref.11 "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I." Egloff A.M., Desiderio S. J. Biol. Chem. 276:27806-27815(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, FUNCTION, MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503.
Mutagenesisⁱ	460 – 460	1	Y → F: No change on BTK-mediated transcriptional activation. 1 Publication Manual assertion based on experiment inⁱ Ref.11 "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I." Egloff A.M., Desiderio S. J. Biol. Chem. 276:27806-27815(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, FUNCTION, MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503.
Mutagenesisⁱ	503 – 503	1	Y → F: Impairs BTK-mediated transcriptional activation. Abolishes BTK-mediated phosphorylation and impairs BTK-mediated transcriptional activation; when associated with F-248 and F-398. 1 Publication Manual assertion based on experiment inⁱ Ref.11 "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I." Egloff A.M., Desiderio S. J. Biol. Chem. 276:27806-27815(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, FUNCTION, MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503.

Keywords - Diseaseⁱ

Williams-Beuren syndrome

Organism-specific databases

MalaCardsⁱ	GTF2I.
Orphanetⁱ	904. Williams syndrome.
PharmGKBⁱ	PA29045.

Polymorphism and mutation databases

BioMutaⁱ	GTF2I.
DMDMⁱ	17865459.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Initiator methionineⁱ			RemovedCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.19 "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.24 "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features." Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C. Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.25 "N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 1 Publication Manual assertion based on experiment inⁱ Ref.9 Bienvenut W.V., Murray L., Brunton V.G., Frame M.C. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-20; 131-140; 178-185; 364-371; 444-456; 495-514; 540-555; 574-594; 620-628; 870-878; 917-927 AND 929-937, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Chainⁱ	2 – 998	997	General transcription factor II-I		PRO_0000083872	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	2 – 2	1	N-acetylalanineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.19 "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.24 "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features." Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C. Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.25 "N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB." Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R. Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 1 Publication Manual assertion based on experiment inⁱ Ref.9 Bienvenut W.V., Murray L., Brunton V.G., Frame M.C. Submitted (JUL-2007) to UniProtKB Cited for: PROTEIN SEQUENCE OF 2-20; 131-140; 178-185; 364-371; 444-456; 495-514; 540-555; 574-594; 620-628; 870-878; 917-927 AND 929-937, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
Modified residueⁱ	19 – 19	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	86 – 86		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.31 "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-86; LYS-221; LYS-456; LYS-488; LYS-561; LYS-664; LYS-816 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	94 – 94		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	103 – 103	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.18 "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-103; SER-207; SER-210 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.20 "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-103 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.21 "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-103; THR-558 AND SER-823, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.27 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome." Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H. J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-823, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	130 – 130	1	N6-acetyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9ESZ8 (GTF2I_MOUSE)
Cross-linkⁱ	130 – 130		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	207 – 207	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.18 "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-103; SER-207; SER-210 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	210 – 210	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.16 "A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-210, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.18 "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-103; SER-207; SER-210 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	214 – 214	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	221 – 221		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.29 "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-221 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	221 – 221		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.29 "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-221 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.31 "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-86; LYS-221; LYS-456; LYS-488; LYS-561; LYS-664; LYS-816 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	248 – 248	1	Phosphotyrosine; by BTK2 Publications Manual assertion based on experiment inⁱ Ref.11 "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I." Egloff A.M., Desiderio S. J. Biol. Chem. 276:27806-27815(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, FUNCTION, MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503. Ref.15 "Induction of immunoglobulin heavy-chain transcription through the transcription factor Bright requires TFII-I." Rajaiya J., Nixon J.C., Ayers N., Desgranges Z.P., Roy A.L., Webb C.F. Mol. Cell. Biol. 26:4758-4768(2006) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH ARID3A AND BTK, PHOSPHORYLATION AT TYR-248, FUNCTION.
Modified residueⁱ	318 – 318	1	Phosphotyrosine; by BTK1 Publication Manual assertion inferred by curator fromⁱ Ref.10 "Regulation of nuclear localization and transcriptional activity of TFII-I by Bruton's tyrosine kinase." Novina C.D., Kumar S., Bajpai U., Cheriyath V., Zhang K., Pillai S., Wortis H.H., Roy A.L. Mol. Cell. Biol. 19:5014-5024(1999) [PubMed] [Europe PMC] [Abstract] Cited for: INTERACTION WITH BTK, FUNCTION, SUBCELLULAR LOCATION, PHOSPHORYLATION.
Cross-linkⁱ	326 – 326		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	343 – 343		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	353 – 353	1	N6-acetyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9ESZ8 (GTF2I_MOUSE)
Cross-linkⁱ	353 – 353		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	398 – 398	1	Phosphotyrosine; by BTK1 Publication Manual assertion based on experiment inⁱ Ref.11 "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I." Egloff A.M., Desiderio S. J. Biol. Chem. 276:27806-27815(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, FUNCTION, MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503.
Modified residueⁱ	412 – 412	1	Phosphoserine; by PKG/PRKG1Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 1 Publication Manual assertion based on experiment inⁱ Ref.12 "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I." Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S., Pilz R.B. J. Biol. Chem. 277:32003-32014(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-412 AND SER-784 BY PRKG1, INTERACTION WITH PRKG1.
Modified residueⁱ	450 – 450	1	N6-acetyllysineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9ESZ8 (GTF2I_MOUSE)
Cross-linkⁱ	456 – 456		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.31 "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-86; LYS-221; LYS-456; LYS-488; LYS-561; LYS-664; LYS-816 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	488 – 488		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.31 "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-86; LYS-221; LYS-456; LYS-488; LYS-561; LYS-664; LYS-816 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	503 – 503	1	Phosphotyrosine; by BTK1 Publication Manual assertion based on experiment inⁱ Ref.11 "Identification of phosphorylation sites for Bruton's tyrosine kinase within the transcriptional regulator BAP/TFII-I." Egloff A.M., Desiderio S. J. Biol. Chem. 276:27806-27815(2001) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT TYR-248; TYR-398 AND TYR-503, INTERACTION WITH BTK, FUNCTION, MUTAGENESIS OF TYR-248; TYR-398; TYR-460 AND TYR-503.
Modified residueⁱ	517 – 517	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	556 – 556	1	PhosphothreonineBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9ESZ8 (GTF2I_MOUSE)
Modified residueⁱ	558 – 558	1	PhosphothreonineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.18 "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-103; SER-207; SER-210 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.20 "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-103 AND THR-558, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.21 "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-103; THR-558 AND SER-823, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	561 – 561		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.31 "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-86; LYS-221; LYS-456; LYS-488; LYS-561; LYS-664; LYS-816 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	660 – 660		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	664 – 664		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.31 "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-86; LYS-221; LYS-456; LYS-488; LYS-561; LYS-664; LYS-816 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	668 – 668	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.23 "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-668, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	674 – 674	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	715 – 715	1	N6-acetyllysine; alternateBy similarity Manual assertion inferred from sequence similarity toⁱ UniProtKB:Q9ESZ8 (GTF2I_MOUSE)
Cross-linkⁱ	715 – 715		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	722 – 722	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	784 – 784	1	Phosphoserine; by PKG/PRKG1Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.26 "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-19; SER-103; SER-210; SER-214; SER-412; SER-517; THR-558; SER-674; SER-722 AND SER-784, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 1 Publication Manual assertion based on experiment inⁱ Ref.12 "cGMP-dependent protein kinase I beta physically and functionally interacts with the transcriptional regulator TFII-I." Casteel D.E., Zhuang S., Gudi T., Tang J., Vuica M., Desiderio S., Pilz R.B. J. Biol. Chem. 277:32003-32014(2002) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT SER-412 AND SER-784 BY PRKG1, INTERACTION WITH PRKG1.
Cross-linkⁱ	816 – 816		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.31 "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-86; LYS-221; LYS-456; LYS-488; LYS-561; LYS-664; LYS-816 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	823 – 823	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.21 "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-103; THR-558 AND SER-823, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.27 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome." Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H. J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-823, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	991 – 991		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.29 "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-221 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Cross-linkⁱ	991 – 991		Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.28 "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-94; LYS-221; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.29 "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-221 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.30 "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-94; LYS-130; LYS-221; LYS-326; LYS-343; LYS-353; LYS-456; LYS-488; LYS-561; LYS-660; LYS-664; LYS-715 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.31 "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-86; LYS-221; LYS-456; LYS-488; LYS-561; LYS-664; LYS-816 AND LYS-991, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Isoform 2 (identifier: P78347-2)
Modified residueⁱ	278 – 278	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.27 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome." Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H. J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-823, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Isoform 4 (identifier: P78347-4)
Modified residueⁱ	298 – 298	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.27 "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome." Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H. J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-103 AND SER-823, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-278 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-298 (ISOFORM 4), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Post-translational modificationⁱ

Transiently phosphorylated on tyrosine residues by BTK in response to B-cell receptor stimulation. Phosphorylation on Tyr-248 and Tyr-398, and perhaps, on Tyr-503 contributes to BTK-mediated transcriptional activation.4 Publications

Sumoylated.1 Publication

Keywords - PTMⁱ

Acetylation, Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDⁱ	P78347.
PaxDbⁱ	P78347.
PeptideAtlasⁱ	P78347.
PRIDEⁱ	P78347.

PTM databases

iPTMnetⁱ	P78347.
PhosphoSiteⁱ	P78347.
SwissPalmⁱ	P78347.

Expressionⁱ

Tissue specificityⁱ

Ubiquitous. Isoform 1 is strongly expressed in fetal brain, weakly in adult brain, muscle, and lymphoblasts and is almost undetectable in other adult tissues, while the other isoforms are equally expressed in all adult tissues.

Gene expression databases

Bgeeⁱ	ENSG00000077809.
CleanExⁱ	HS_GTF2I.
ExpressionAtlasⁱ	P78347. baseline and differential.
Genevisibleⁱ	P78347. HS.

Organism-specific databases

HPAⁱ	CAB004595. HPA026638.

Interactionⁱ

Subunit structureⁱ

Homodimer (Potential). Interacts with SRF and PHOX1. Binds a pyrimidine-rich initiator (Inr) and a recognition site (E-box) for upstream stimulatory factor 1 (USF1). Associates with the PH domain of Bruton's tyrosine kinase (BTK). May be a component of a BHC histone deacetylase complex that contains HDAC1, HDAC2, HMG20B/BRAF35, KDM1A, RCOR1/CoREST, PHF21A/BHC80, ZMYM2, ZNF217, ZMYM3, GSE1 and GTF2I. Interacts with BTK and ARID3A. Interacts with isoform beta of PRKG1.Curated4 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
BRCA1	P38398	5	EBI-359622,EBI-349905
BTK	Q06187	6	EBI-359622,EBI-624835

With

Entry

#Exp.

IntAct

Notes

BRCA1

P38398

5

EBI-359622,EBI-349905

BTK

Q06187

6

EBI-359622,EBI-624835

Protein-protein interaction databases

BioGridⁱ	109224. 112 interactions.
DIPⁱ	DIP-24252N.
IntActⁱ	P78347. 34 interactions.
MINTⁱ	MINT-1138992.
STRINGⁱ	9606.ENSP00000322542.

Structureⁱ

Secondary structure

1

998

Legend: HelixTurnBeta strand

Show more details

Feature key	Position(s)	Length	Description
Helixⁱ	106 – 128	23	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D9B
Helixⁱ	138 – 143	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D9B
Beta strandⁱ	146 – 152	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D9B
Helixⁱ	167 – 175	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D9B
Turnⁱ	176 – 179	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D9B
Beta strandⁱ	181 – 185	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2D9B
Helixⁱ	361 – 376	16	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Helixⁱ	387 – 392	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Turnⁱ	393 – 396	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Beta strandⁱ	397 – 401	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Turnⁱ	411 – 413	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Helixⁱ	416 – 424	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Turnⁱ	426 – 428	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Beta strandⁱ	430 – 434	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Turnⁱ	437 – 439	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2DN4
Helixⁱ	466 – 482	17	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Helixⁱ	492 – 497	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Turnⁱ	499 – 501	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Beta strandⁱ	502 – 506	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Turnⁱ	516 – 518	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Helixⁱ	521 – 529	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Turnⁱ	530 – 533	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Beta strandⁱ	535 – 539	5	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Helixⁱ	541 – 544	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2ED2
Turnⁱ	856 – 858	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2EJE
Helixⁱ	861 – 883	23	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2EJE
Helixⁱ	894 – 899	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2EJE
Beta strandⁱ	901 – 907	7	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2EJE
Turnⁱ	918 – 920	3	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2EJE
Helixⁱ	923 – 931	9	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2EJE
Turnⁱ	932 – 935	4	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2EJE
Beta strandⁱ	937 – 942	6	Combined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ PDB:2EJE

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D9B	NMR	-	A	102-197	[»]
2DN4	NMR	-	A	361-446	[»]
2ED2	NMR	-	A	466-551	[»]
2EJE	NMR	-	A	854-954	[»]

ProteinModelPortalⁱ

SMRⁱ

P78347. Positions 104-197, 359-454, 466-556, 571-649, 731-823, 854-959.

ModBaseⁱ

MobiDBⁱ

Miscellaneous databases

EvolutionaryTraceⁱ	P78347.

EvolutionaryTraceⁱ

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Actions
Repeatⁱ	103 – 197	95	GTF2I-like 1	Add BLAST
Repeatⁱ	352 – 446	95	GTF2I-like 2	Add BLAST
Repeatⁱ	457 – 551	95	GTF2I-like 3	Add BLAST
Repeatⁱ	562 – 656	95	GTF2I-like 4	Add BLAST
Repeatⁱ	724 – 818	95	GTF2I-like 5	Add BLAST
Repeatⁱ	859 – 953	95	GTF2I-like 6	Add BLAST

Motif

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Motifⁱ	320 – 327	8	Nuclear localization signalSequence analysis

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Compositional biasⁱ	692 – 695	4	Poly-Asn

Sequence similaritiesⁱ

Belongs to the TFII-I family.PROSITE-ProRule annotation

Contains 6 GTF2I-like repeats.PROSITE-ProRule annotation

Keywords - Domainⁱ

Repeat

Phylogenomic databases

eggNOGⁱ	ENOG410IEPZ. Eukaryota. ENOG41100H8. LUCA.
GeneTreeⁱ	ENSGT00530000063863.
HOGENOMⁱ	HOG000147161.
HOVERGENⁱ	HBG051856.
InParanoidⁱ	P78347.
KOⁱ	K03121.
OMAⁱ	MPPGVAF.
OrthoDBⁱ	EOG091G01ZC.
PhylomeDBⁱ	P78347.
TreeFamⁱ	TF352524.

Family and domain databases

Gene3Dⁱ	3.90.1460.10. 6 hits.
InterProⁱ	IPR004212. GTF2I. IPR016659. TF_II-I. [Graphical view]
Pfamⁱ	PF02946. GTF2I. 6 hits. [Graphical view]
PIRSFⁱ	PIRSF016441. TF_II-I. 1 hit.
SUPFAMⁱ	SSF117773. SSF117773. 6 hits.
PROSITEⁱ	PS51139. GTF2I. 6 hits. [Graphical view]

Sequences (5)ⁱ

Sequence statusⁱ: Complete.

Sequence processingⁱ: The displayed sequence is further processed into a mature form.

This entry describes 5 isoformsⁱ produced by alternative splicing. Align Add to basket Added to basket

Isoform 1 (identifier: P78347-1) [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.

        10         20         30         40         50
MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY 
        60         70         80         90        100
ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN 
       110        120        130        140        150
RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV 
       160        170        180        190        200
QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM 
       210        220        230        240        250
VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ 
       260        270        280        290        300
YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDSTQHVP 
       310        320        330        340        350
SETSEDPEVE VTIEDDDYSP PSKRPKANEL PQPPVPEPAN AGKRKVREFN 
       360        370        380        390        400
FEKWNARITD LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE 
       410        420        430        440        450
GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN STREDLQLDK 
       460        470        480        490        500
PASGVKEEWY ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN 
       510        520        530        540        550
DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR PELLTHSTTE 
       560        570        580        590        600
VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF 
       610        620        630        640        650
ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVI 
       660        670        680        690        700
SYLPPGMASK INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA 
       710        720        730        740        750
VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL FNEKCGEALG 
       760        770        780        790        800
LKQAVKVPFA LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK 
       810        820        830        840        850
IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG VEDLNIIQVT 
       860        870        880        890        900
IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN 
       910        920        930        940        950
PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN 
       960        970        980        990 
NQLVDQSESE GPVIQESAEP SQLEVPATEE IKETDGSSQI KQEPDPTW

Length:998

Mass (Da):112,416

Last modified:December 13, 2001 - v2

Checksum:ⁱ4CFA2C19002869B9

Isoform 2 (identifier: P78347-2) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
255-274: Missing.
294-314: Missing.

        10         20         30         40         50
MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY 
        60         70         80         90        100
ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN 
       110        120        130        140        150
RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV 
       160        170        180        190        200
QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM 
       210        220        230        240        250
VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ 
       260        270        280        290        300
YNIQGSHHSS EGNEGTEMEV PAEDDDYSPP SKRPKANELP QPPVPEPANA 
       310        320        330        340        350
GKRKVREFNF EKWNARITDL RKQVEELFER KYAQAIKAKG PVTIPYPLFQ 
       360        370        380        390        400
SHVEDLYVEG LPEGIPFRRP STYGIPRLER ILLAKERIRF VIKKHELLNS 
       410        420        430        440        450
TREDLQLDKP ASGVKEEWYA RITKLRKMVD QLFCKKFAEA LGSTEAKAVP 
       460        470        480        490        500
YQKFEAHPND LYVEGLPENI PFRSPSWYGI PRLEKIIQVG NRIKFVIKRP 
       510        520        530        540        550
ELLTHSTTEV TQPRTNTPVK EDWNVRITKL RKQVEEIFNL KFAQALGLTE 
       560        570        580        590        600
AVKVPYPVFE SNPEFLYVEG LPEGIPFRSP TWFGIPRLER IVRGSNKIKF 
       610        620        630        640        650
VVKKPELVIS YLPPGMASKI NTKALQSPKR PRSPGSNSKV PEIEVTVEGP 
       660        670        680        690        700
NNNNPQTSAV RTPTQTNGSN VPFKPRGREF SFEAWNAKIT DLKQKVENLF 
       710        720        730        740        750
NEKCGEALGL KQAVKVPFAL FESFPEDFYV EGLPEGVPFR RPSTFGIPRL 
       760        770        780        790        800
EKILRNKAKI KFIIKKPEMF ETAIKESTSS KSPPRKINSS PNVNTTASGV 
       810        820        830        840        850
EDLNIIQVTI PDDDNERLSK VEKARQLREQ VNDLFSRKFG EAIGMGFPVK 
       860        870        880        890        900
VPYRKITINP GCVVVDGMPP GVSFKAPSYL EISSMRRILD SAEFIKFTVI 
       910        920        930        940        950
RPFPGLVINN QLVDQSESEG PVIQESAEPS QLEVPATEEI KETDGSSQIK 

QEPDPTW

Length:957

Mass (Da):107,970

Checksum:ⁱE091B620FF633AC8

Isoform 3 (identifier: P78347-3) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
255-274: Missing.

        10         20         30         40         50
MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY 
        60         70         80         90        100
ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN 
       110        120        130        140        150
RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV 
       160        170        180        190        200
QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM 
       210        220        230        240        250
VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ 
       260        270        280        290        300
YNIQGSHHSS EGNEGTEMEV PAEDSTQHVP SETSEDPEVE VTIEDDDYSP 
       310        320        330        340        350
PSKRPKANEL PQPPVPEPAN AGKRKVREFN FEKWNARITD LRKQVEELFE 
       360        370        380        390        400
RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE GLPEGIPFRR PSTYGIPRLE 
       410        420        430        440        450
RILLAKERIR FVIKKHELLN STREDLQLDK PASGVKEEWY ARITKLRKMV 
       460        470        480        490        500
DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN DLYVEGLPEN IPFRSPSWYG 
       510        520        530        540        550
IPRLEKIIQV GNRIKFVIKR PELLTHSTTE VTQPRTNTPV KEDWNVRITK 
       560        570        580        590        600
LRKQVEEIFN LKFAQALGLT EAVKVPYPVF ESNPEFLYVE GLPEGIPFRS 
       610        620        630        640        650
PTWFGIPRLE RIVRGSNKIK FVVKKPELVI SYLPPGMASK INTKALQSPK 
       660        670        680        690        700
RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA VRTPTQTNGS NVPFKPRGRE 
       710        720        730        740        750
FSFEAWNAKI TDLKQKVENL FNEKCGEALG LKQAVKVPFA LFESFPEDFY 
       760        770        780        790        800
VEGLPEGVPF RRPSTFGIPR LEKILRNKAK IKFIIKKPEM FETAIKESTS 
       810        820        830        840        850
SKSPPRKINS SPNVNTTASG VEDLNIIQVT IPDDDNERLS KVEKARQLRE 
       860        870        880        890        900
QVNDLFSRKF GEAIGMGFPV KVPYRKITIN PGCVVVDGMP PGVSFKAPSY 
       910        920        930        940        950
LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQSESE GPVIQESAEP 
       960        970 
SQLEVPATEE IKETDGSSQI KQEPDPTW

Length:978

Mass (Da):110,280

Checksum:ⁱ1F006D480F0BE702

Isoform 4 (identifier: P78347-4) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
294-314: Missing.

        10         20         30         40         50
MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY 
        60         70         80         90        100
ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN 
       110        120        130        140        150
RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV 
       160        170        180        190        200
QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM 
       210        220        230        240        250
VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ 
       260        270        280        290        300
YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDDDYSPP 
       310        320        330        340        350
SKRPKANELP QPPVPEPANA GKRKVREFNF EKWNARITDL RKQVEELFER 
       360        370        380        390        400
KYAQAIKAKG PVTIPYPLFQ SHVEDLYVEG LPEGIPFRRP STYGIPRLER 
       410        420        430        440        450
ILLAKERIRF VIKKHELLNS TREDLQLDKP ASGVKEEWYA RITKLRKMVD 
       460        470        480        490        500
QLFCKKFAEA LGSTEAKAVP YQKFEAHPND LYVEGLPENI PFRSPSWYGI 
       510        520        530        540        550
PRLEKIIQVG NRIKFVIKRP ELLTHSTTEV TQPRTNTPVK EDWNVRITKL 
       560        570        580        590        600
RKQVEEIFNL KFAQALGLTE AVKVPYPVFE SNPEFLYVEG LPEGIPFRSP 
       610        620        630        640        650
TWFGIPRLER IVRGSNKIKF VVKKPELVIS YLPPGMASKI NTKALQSPKR 
       660        670        680        690        700
PRSPGSNSKV PEIEVTVEGP NNNNPQTSAV RTPTQTNGSN VPFKPRGREF 
       710        720        730        740        750
SFEAWNAKIT DLKQKVENLF NEKCGEALGL KQAVKVPFAL FESFPEDFYV 
       760        770        780        790        800
EGLPEGVPFR RPSTFGIPRL EKILRNKAKI KFIIKKPEMF ETAIKESTSS 
       810        820        830        840        850
KSPPRKINSS PNVNTTASGV EDLNIIQVTI PDDDNERLSK VEKARQLREQ 
       860        870        880        890        900
VNDLFSRKFG EAIGMGFPVK VPYRKITINP GCVVVDGMPP GVSFKAPSYL 
       910        920        930        940        950
EISSMRRILD SAEFIKFTVI RPFPGLVINN QLVDQSESEG PVIQESAEPS 
       960        970 
QLEVPATEEI KETDGSSQIK QEPDPTW

Length:977

Mass (Da):110,106

Checksum:ⁱ418D59EC623E6141

Isoform 5 (identifier: P78347-5) [UniParc]FASTA Add to basket

The sequence of this isoform differs from the canonical sequence as follows:
     255-274: Missing.
     294-294: D → G
     295-998: Missing.

        10         20         30         40         50
MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY 
        60         70         80         90        100
ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN 
       110        120        130        140        150
RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV 
       160        170        180        190        200
QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM 
       210        220        230        240        250
VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ 
       260        270 
YNIQGSHHSS EGNEGTEMEV PAEG

Note: No experimental confirmation available.

Length:274

Mass (Da):30,409

Checksum:ⁱC693096D47E9CDC7

Alternative splicing, Polymorphism

Experimental Info

Feature key	Position(s)	Length	Description
Sequence conflictⁱ	174 – 174	1	L → G in AAB48826 (PubMed:9012831).Curated
Sequence conflictⁱ	178 – 178	1	A → G in AAB48826 (PubMed:9012831).Curated
Sequence conflictⁱ	481 – 481	1	A → R in AAB70791 (PubMed:9384587).Curated
Sequence conflictⁱ	634 – 634	1	R → H in AAB48826 (PubMed:9012831).Curated
Sequence conflictⁱ	960 – 960	1	E → K in AAB48826 (PubMed:9012831).Curated

Natural variant

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Natural variantⁱ	174 – 174	1	L → V. Corresponds to variant rs1057896 [ dbSNP \| Ensembl ].		VAR_051026

Alternative sequence

Feature key	Position(s)	Length	Description	Feature identifier	Actions
Alternative sequenceⁱ	255 – 274	20	Missing in isoform 2, isoform 3 and isoform 5. 6 Publications Manual assertion based on opinion inⁱ Ref.1 "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1." Roy A.L., Du H., Gregor P.D., Novina C.D., Martinez E., Roeder R.G. EMBO J. 16:7091-7104(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 162-171; 366-372; 646-658 AND 940-956. Ref.2 "A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I." Grueneberg D.A., Henry R.W., Brauer A., Novina C.D., Cheriyath V., Roy A.L., Gilman M. Genes Dev. 11:2482-2493(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 291-294 AND 316-333. Ref.3 "BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement." Yang W., Desiderio S. Proc. Natl. Acad. Sci. U.S.A. 94:604-609(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 144-154; 495-514 AND 681-702. Ref.4 "A duplicated gene in the breakpoint regions of the 7q11.23 Williams-Beuren syndrome deletion encodes the initiator binding protein TFII-I and BAP-135, a phosphorylation target of BTK." Perez Jurado L.A., Wang Y.-K., Peoples R., Coloma A., Cruces J., Francke U. Hum. Mol. Genet. 7:325-334(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). Ref.5 "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Ref.8 "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).	VSP_003867	Add BLAST
Alternative sequenceⁱ	294 – 314	21	Missing in isoform 2 and isoform 4. 5 Publications Manual assertion based on opinion inⁱ Ref.1 "Cloning of an inr- and E-box-binding protein, TFII-I, that interacts physically and functionally with USF1." Roy A.L., Du H., Gregor P.D., Novina C.D., Martinez E., Roeder R.G. EMBO J. 16:7091-7104(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 162-171; 366-372; 646-658 AND 940-956. Ref.2 "A multifunctional DNA-binding protein that promotes the formation of serum response factor/homeodomain complexes: identity to TFII-I." Grueneberg D.A., Henry R.W., Brauer A., Novina C.D., Cheriyath V., Roy A.L., Gilman M. Genes Dev. 11:2482-2493(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 291-294 AND 316-333. Ref.3 "BAP-135, a target for Bruton's tyrosine kinase in response to B cell receptor engagement." Yang W., Desiderio S. Proc. Natl. Acad. Sci. U.S.A. 94:604-609(1997) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PROTEIN SEQUENCE OF 144-154; 495-514 AND 681-702. Ref.4 "A duplicated gene in the breakpoint regions of the 7q11.23 Williams-Beuren syndrome deletion encodes the initiator binding protein TFII-I and BAP-135, a phosphorylation target of BTK." Perez Jurado L.A., Wang Y.-K., Peoples R., Coloma A., Cruces J., Francke U. Hum. Mol. Genet. 7:325-334(1998) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2; 3 AND 4). Ref.8 "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).	VSP_003868	Add BLAST
Alternative sequenceⁱ	294 – 294	1	D → G in isoform 5. 2 Publications Manual assertion based on opinion inⁱ Ref.5 "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Ref.8 "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).	VSP_055195
Alternative sequenceⁱ	295 – 998	704	Missing in isoform 5. 2 Publications Manual assertion based on opinion inⁱ Ref.5 "Cloning of human full-length CDSs in BD Creator(TM) system donor vector." Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S., Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y., Phelan M., Farmer A. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5). Ref.8 "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 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).	VSP_055196	Add BLAST

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF015553 mRNA. Translation: AAB70791.1. Y14946 mRNA. Translation: CAA75163.1. U77948 mRNA. Translation: AAB48826.1. AF035737 mRNA. Translation: AAC08312.1. AF038967 mRNA. Translation: AAC08313.1. AF038968 mRNA. Translation: AAC08314.1. AF038969 mRNA. Translation: AAC08315.1. BT007450 mRNA. Translation: AAP36118.1. AC005231 Genomic DNA. No translation available. AC083884 Genomic DNA. Translation: AAS07460.1. AC083884 Genomic DNA. Translation: AAS07461.1. AC083884 Genomic DNA. Translation: AAS07462.1. AC083884 Genomic DNA. Translation: AAS07463.1. AC083884 Genomic DNA. Translation: AAS07464.1. AC004883 Genomic DNA. Translation: AAL93085.1. CH471200 Genomic DNA. Translation: EAW69598.1. BC004472 mRNA. Translation: AAH04472.1. BC070484 mRNA. Translation: AAH70484.1.
CCDSⁱ	CCDS47614.1. [P78347-2] CCDS5573.1. [P78347-1] CCDS5574.1. [P78347-3] CCDS5575.1. [P78347-4] CCDS64680.1. [P78347-5]
PIRⁱ	T03829. T09492.
RefSeqⁱ	NP_001157108.1. NM_001163636.2. NP_001267729.1. NM_001280800.1. [P78347-5] NP_001509.3. NM_001518.4. [P78347-2] NP_127492.1. NM_032999.3. [P78347-1] NP_127493.1. NM_033000.3. [P78347-3] NP_127494.1. NM_033001.3. [P78347-4]
UniGeneⁱ	Hs.647041. Hs.654705. Hs.743231.

Genome annotation databases

Ensemblⁱ	ENST00000443166; ENSP00000404240; ENSG00000263001. [P78347-5] ENST00000573035; ENSP00000460070; ENSG00000263001. [P78347-1] ENST00000614986; ENSP00000484526; ENSG00000263001. [P78347-3] ENST00000620879; ENSP00000477837; ENSG00000263001. [P78347-2] ENST00000621734; ENSP00000482476; ENSG00000263001. [P78347-4]
GeneIDⁱ	2969.
KEGGⁱ	hsa:2969.
UCSCⁱ	uc003uat.5. human. [P78347-1]

Keywords - Coding sequence diversityⁱ

Cross-referencesⁱ

Sequence databases

Select the link destinations: EMBLⁱ GenBankⁱ DDBJⁱ Links Updated	AF015553 mRNA. Translation: AAB70791.1. Y14946 mRNA. Translation: CAA75163.1. U77948 mRNA. Translation: AAB48826.1. AF035737 mRNA. Translation: AAC08312.1. AF038967 mRNA. Translation: AAC08313.1. AF038968 mRNA. Translation: AAC08314.1. AF038969 mRNA. Translation: AAC08315.1. BT007450 mRNA. Translation: AAP36118.1. AC005231 Genomic DNA. No translation available. AC083884 Genomic DNA. Translation: AAS07460.1. AC083884 Genomic DNA. Translation: AAS07461.1. AC083884 Genomic DNA. Translation: AAS07462.1. AC083884 Genomic DNA. Translation: AAS07463.1. AC083884 Genomic DNA. Translation: AAS07464.1. AC004883 Genomic DNA. Translation: AAL93085.1. CH471200 Genomic DNA. Translation: EAW69598.1. BC004472 mRNA. Translation: AAH04472.1. BC070484 mRNA. Translation: AAH70484.1.
CCDSⁱ	CCDS47614.1. [P78347-2] CCDS5573.1. [P78347-1] CCDS5574.1. [P78347-3] CCDS5575.1. [P78347-4] CCDS64680.1. [P78347-5]
PIRⁱ	T03829. T09492.
RefSeqⁱ	NP_001157108.1. NM_001163636.2. NP_001267729.1. NM_001280800.1. [P78347-5] NP_001509.3. NM_001518.4. [P78347-2] NP_127492.1. NM_032999.3. [P78347-1] NP_127493.1. NM_033000.3. [P78347-3] NP_127494.1. NM_033001.3. [P78347-4]
UniGeneⁱ	Hs.647041. Hs.654705. Hs.743231.

3D structure databases

Select the link destinations:
PDBeⁱ
RCSB PDBⁱ
PDBjⁱ

Links Updated

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2D9B	NMR	-	A	102-197	[»]
2DN4	NMR	-	A	361-446	[»]
2ED2	NMR	-	A	466-551	[»]
2EJE	NMR	-	A	854-954	[»]

ProteinModelPortalⁱ

SMRⁱ

P78347. Positions 104-197, 359-454, 466-556, 571-649, 731-823, 854-959.

ModBaseⁱ

MobiDBⁱ

Protein-protein interaction databases

BioGridⁱ	109224. 112 interactions.
DIPⁱ	DIP-24252N.
IntActⁱ	P78347. 34 interactions.
MINTⁱ	MINT-1138992.
STRINGⁱ	9606.ENSP00000322542.

PTM databases

iPTMnetⁱ	P78347.
PhosphoSiteⁱ	P78347.
SwissPalmⁱ	P78347.

Polymorphism and mutation databases

BioMutaⁱ	GTF2I.
DMDMⁱ	17865459.

Proteomic databases

EPDⁱ	P78347.
PaxDbⁱ	P78347.
PeptideAtlasⁱ	P78347.
PRIDEⁱ	P78347.

Protocols and materials databases

DNASUⁱ	2969.
Structural Biology Knowledgebase	Search...

Genome annotation databases

Ensemblⁱ	ENST00000443166; ENSP00000404240; ENSG00000263001. [P78347-5] ENST00000573035; ENSP00000460070; ENSG00000263001. [P78347-1] ENST00000614986; ENSP00000484526; ENSG00000263001. [P78347-3] ENST00000620879; ENSP00000477837; ENSG00000263001. [P78347-2] ENST00000621734; ENSP00000482476; ENSG00000263001. [P78347-4]
GeneIDⁱ	2969.
KEGGⁱ	hsa:2969.
UCSCⁱ	uc003uat.5. human. [P78347-1]

Organism-specific databases

CTDⁱ	2969.
GeneCardsⁱ	GTF2I.
H-InvDB	HIX0023260.
HGNCⁱ	HGNC:4659. GTF2I.
HPAⁱ	CAB004595. HPA026638.
MalaCardsⁱ	GTF2I.
MIMⁱ	601679. gene.
neXtProtⁱ	NX_P78347.
Orphanetⁱ	904. Williams syndrome.
PharmGKBⁱ	PA29045.
GenAtlasⁱ	Search...

Phylogenomic databases

eggNOGⁱ	ENOG410IEPZ. Eukaryota. ENOG41100H8. LUCA.
GeneTreeⁱ	ENSGT00530000063863.
HOGENOMⁱ	HOG000147161.
HOVERGENⁱ	HBG051856.
InParanoidⁱ	P78347.
KOⁱ	K03121.
OMAⁱ	MPPGVAF.
OrthoDBⁱ	EOG091G01ZC.
PhylomeDBⁱ	P78347.
TreeFamⁱ	TF352524.

Enzyme and pathway databases

SIGNORⁱ	P78347.

SIGNORⁱ