P78347 (GTF2I_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	GTF2I
Synonyms:	BAP135, WBSCR6

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	998 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Interacts with the basal transcription machinery by coordinating the formation of a multiprotein complex at the C-FOS promoter, and linking specific signal responsive activator complexes. Promotes the formation of stable high-order complexes of SRF and PHOX1 and interacts cooperatively with PHOX1 to promote serum-inducible transcription of a reporter gene deriven by the C-FOS serum response element (SRE). Acts as a coregulator for USF1 by binding independently two promoter elements, a pyrimidine-rich initiator (Inr) and an upstream E-box. Required for the formation of functional ARID3A DNA-binding complexes and for activation of immunoglobulin heavy-chain transcription upon B-lymphocyte activation. Ref.8 Ref.9 Ref.13
Subunit structure	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 betaof PRKG1. Ref.8 Ref.9 Ref.10 Ref.13
Subcellular location	Cytoplasm. Nucleus. Note: Colocalizes with BTK in the cytoplasm. Ref.8
Tissue specificity	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.
Post-translational modification	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. Ref.8 Ref.9 Ref.10 Ref.13 Sumoylated. Ref.11
Involvement in disease	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.
Sequence similarities	Belongs to the TFII-I family. Contains 6 GTF2I-like repeats.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cytoplasm Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Williams-Beuren syndrome
Domain	Repeat
Ligand	DNA-binding
PTM	Acetylation Phosphoprotein Ubl conjugation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	embryo development Inferred from electronic annotation. Source: Ensembl negative regulation of angiogenesis Inferred from direct assay PubMed 19242469. Source: MGI negative regulation of cytosolic calcium ion concentration Inferred from electronic annotation. Source: Ensembl signal transduction Traceable author statement Ref.3. Source: ProtInc transcription initiation from RNA polymerase II promoter Traceable author statement Ref.2. Source: ProtInc
Cellular_component	cell projection Inferred from electronic annotation. Source: Ensembl cytoplasm Inferred from electronic annotation. Source: UniProtKB-SubCell neuronal cell body Inferred from electronic annotation. Source: Ensembl nucleus Inferred from direct assay. Source: HPA
Molecular_function	DNA binding Inferred from electronic annotation. Source: UniProtKB-KW sequence-specific DNA binding transcription factor activity Non-traceable author statement Ref.2. Source: ProtInc
Complete GO annotation...

Binary interactions

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

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P78347-1)

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.

Isoform 2 (identifier: P78347-2)

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

Isoform 3 (identifier: P78347-3)

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

Isoform 4 (identifier: P78347-4)

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

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.7

Chain

2 – 998

997

General transcription factor II-I

PRO_0000083872

Regions

Repeat

103 – 197

95

GTF2I-like 1

Repeat

352 – 446

95

GTF2I-like 2

Repeat

457 – 551

95

GTF2I-like 3

Repeat

562 – 656

95

GTF2I-like 4

Repeat

724 – 818

95

GTF2I-like 5

Repeat

859 – 953

95

GTF2I-like 6

Motif

320 – 327

8

Nuclear localization signal Potential

Compositional bias

692 – 695

4

Poly-Asn

Amino acid modifications

Modified residue

2

1

N-acetylalanine Ref.7 Ref.17 Ref.22

Modified residue

103

1

Phosphoserine Ref.16 Ref.18 Ref.19

Modified residue

207

1

Phosphoserine Ref.16

Modified residue

210

1

Phosphoserine Ref.14 Ref.16

Modified residue

248

1

Phosphotyrosine; by BTK Ref.9 Ref.13

Modified residue

318

1

Phosphotyrosine; by BTK Probable

Modified residue

398

1

Phosphotyrosine; by BTK Ref.9

Modified residue

412

1

Phosphoserine; by PKG/PRKG1 Ref.10

Modified residue

503

1

Phosphotyrosine; by BTK Ref.9

Modified residue

558

1

Phosphothreonine Ref.16 Ref.18 Ref.19

Modified residue

668

1

Phosphoserine Ref.21

Modified residue

784

1

Phosphoserine; by PKG/PRKG1 Ref.10

Modified residue

823

1

Phosphoserine Ref.19

Natural variations

Alternative sequence

255 – 274

20

Missing in isoform 2 and isoform 3.

VSP_003867

Alternative sequence

294 – 314

21

Missing in isoform 2 and isoform 4.

VSP_003868

Natural variant

174

1

L → V.
Corresponds to variant rs1057896 [ dbSNP | Ensembl ].

VAR_051026

Experimental info

Mutagenesis

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. Ref.9

Mutagenesis

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. Ref.9

Mutagenesis

460

1

Y → F: No change on BTK-mediated transcriptional activation. Ref.9

Mutagenesis

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. Ref.9

Sequence conflict

174

1

L → G in AAB48826. Ref.3

Sequence conflict

178

1

A → G in AAB48826. Ref.3

Sequence conflict

294

1

D → G in AAH04472. Ref.6

Sequence conflict

481

1

A → R in AAB70791. Ref.1

Sequence conflict

634

1

R → H in AAB48826. Ref.3

Sequence conflict

960

1

E → K in AAB48826. Ref.3

Secondary structure

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998

Helix Strand Turn

Details...

Helix

106 – 128

23

Helix

138 – 143

6

Beta strand

146 – 152

7

Helix

167 – 175

9

Turn

176 – 179

4

Beta strand

181 – 185

5

Helix

361 – 376

16

Helix

387 – 392

6

Turn

393 – 396

4

Beta strand

397 – 401

5

Turn

411 – 413

3

Helix

416 – 424

9

Turn

426 – 428

3

Beta strand

430 – 434

5

Turn

437 – 439

3

Helix

466 – 482

17

Helix

492 – 497

6

Turn

499 – 501

3

Beta strand

502 – 506

5

Turn

516 – 518

3

Helix

521 – 529

9

Turn

530 – 533

4

Beta strand

535 – 539

5

Helix

541 – 544

4

Turn

856 – 858

3

Helix

861 – 883

23

Helix

894 – 899

6

Beta strand

901 – 907

7

Turn

918 – 920

3

Helix

923 – 931

9

Turn

932 – 935

4

Beta strand

937 – 942

6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified December 13, 2001. Version 2. Checksum: 4CFA2C19002869B9	FASTA	998	112,416
	10 20 30 40 50 60 MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE 70 80 90 100 110 120 RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF 130 140 150 160 170 180 CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI 190 200 210 220 230 240 SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK 250 260 270 280 290 300 EESEDPDYYQ YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDSTQHVP 310 320 330 340 350 360 SETSEDPEVE VTIEDDDYSP PSKRPKANEL PQPPVPEPAN AGKRKVREFN FEKWNARITD 370 380 390 400 410 420 LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE GLPEGIPFRR PSTYGIPRLE 430 440 450 460 470 480 RILLAKERIR FVIKKHELLN STREDLQLDK PASGVKEEWY ARITKLRKMV DQLFCKKFAE 490 500 510 520 530 540 ALGSTEAKAV PYQKFEAHPN DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR 550 560 570 580 590 600 PELLTHSTTE VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF 610 620 630 640 650 660 ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVI SYLPPGMASK 670 680 690 700 710 720 INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA VRTPTQTNGS NVPFKPRGRE 730 740 750 760 770 780 FSFEAWNAKI TDLKQKVENL FNEKCGEALG LKQAVKVPFA LFESFPEDFY VEGLPEGVPF 790 800 810 820 830 840 RRPSTFGIPR LEKILRNKAK IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG 850 860 870 880 890 900 VEDLNIIQVT IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN 910 920 930 940 950 960 PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQSESE 970 980 990 GPVIQESAEP SQLEVPATEE IKETDGSSQI KQEPDPTW
	Isoform 2 [UniParc]. Checksum: E091B620FF633AC8	FASTA	957	107,970
	10 20 30 40 50 60 MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE 70 80 90 100 110 120 RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF 130 140 150 160 170 180 CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI 190 200 210 220 230 240 SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK 250 260 270 280 290 300 EESEDPDYYQ YNIQGSHHSS EGNEGTEMEV PAEDDDYSPP SKRPKANELP QPPVPEPANA 310 320 330 340 350 360 GKRKVREFNF EKWNARITDL RKQVEELFER KYAQAIKAKG PVTIPYPLFQ SHVEDLYVEG 370 380 390 400 410 420 LPEGIPFRRP STYGIPRLER ILLAKERIRF VIKKHELLNS TREDLQLDKP ASGVKEEWYA 430 440 450 460 470 480 RITKLRKMVD QLFCKKFAEA LGSTEAKAVP YQKFEAHPND LYVEGLPENI PFRSPSWYGI 490 500 510 520 530 540 PRLEKIIQVG NRIKFVIKRP ELLTHSTTEV TQPRTNTPVK EDWNVRITKL RKQVEEIFNL 550 560 570 580 590 600 KFAQALGLTE AVKVPYPVFE SNPEFLYVEG LPEGIPFRSP TWFGIPRLER IVRGSNKIKF 610 620 630 640 650 660 VVKKPELVIS YLPPGMASKI NTKALQSPKR PRSPGSNSKV PEIEVTVEGP NNNNPQTSAV 670 680 690 700 710 720 RTPTQTNGSN VPFKPRGREF SFEAWNAKIT DLKQKVENLF NEKCGEALGL KQAVKVPFAL 730 740 750 760 770 780 FESFPEDFYV EGLPEGVPFR RPSTFGIPRL EKILRNKAKI KFIIKKPEMF ETAIKESTSS 790 800 810 820 830 840 KSPPRKINSS PNVNTTASGV EDLNIIQVTI PDDDNERLSK VEKARQLREQ VNDLFSRKFG 850 860 870 880 890 900 EAIGMGFPVK VPYRKITINP GCVVVDGMPP GVSFKAPSYL EISSMRRILD SAEFIKFTVI 910 920 930 940 950 RPFPGLVINN QLVDQSESEG PVIQESAEPS QLEVPATEEI KETDGSSQIK QEPDPTW
	Isoform 3 [UniParc]. Checksum: 1F006D480F0BE702	FASTA	978	110,280
	10 20 30 40 50 60 MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE 70 80 90 100 110 120 RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF 130 140 150 160 170 180 CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI 190 200 210 220 230 240 SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK 250 260 270 280 290 300 EESEDPDYYQ YNIQGSHHSS EGNEGTEMEV PAEDSTQHVP SETSEDPEVE VTIEDDDYSP 310 320 330 340 350 360 PSKRPKANEL PQPPVPEPAN AGKRKVREFN FEKWNARITD LRKQVEELFE RKYAQAIKAK 370 380 390 400 410 420 GPVTIPYPLF QSHVEDLYVE GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN 430 440 450 460 470 480 STREDLQLDK PASGVKEEWY ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN 490 500 510 520 530 540 DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR PELLTHSTTE VTQPRTNTPV 550 560 570 580 590 600 KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF ESNPEFLYVE GLPEGIPFRS 610 620 630 640 650 660 PTWFGIPRLE RIVRGSNKIK FVVKKPELVI SYLPPGMASK INTKALQSPK RPRSPGSNSK 670 680 690 700 710 720 VPEIEVTVEG PNNNNPQTSA VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL 730 740 750 760 770 780 FNEKCGEALG LKQAVKVPFA LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK 790 800 810 820 830 840 IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG VEDLNIIQVT IPDDDNERLS 850 860 870 880 890 900 KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN PGCVVVDGMP PGVSFKAPSY 910 920 930 940 950 960 LEISSMRRIL DSAEFIKFTV IRPFPGLVIN NQLVDQSESE GPVIQESAEP SQLEVPATEE 970 IKETDGSSQI KQEPDPTW
	Isoform 4 [UniParc]. Checksum: 418D59EC623E6141	FASTA	977	110,106
	10 20 30 40 50 60 MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY ETDVFVVGTE 70 80 90 100 110 120 RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN RMSVDAVEIE TLRKTVEDYF 130 140 150 160 170 180 CFCYGKALGK STVVPVPYEK MLRDQSAVVV QGLPEGVAFK HPENYDLATL KWILENKAGI 190 200 210 220 230 240 SFIIKRPFLE PKKHVGGRVM VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK 250 260 270 280 290 300 EESEDPDYYQ YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDDDYSPP 310 320 330 340 350 360 SKRPKANELP QPPVPEPANA GKRKVREFNF EKWNARITDL RKQVEELFER KYAQAIKAKG 370 380 390 400 410 420 PVTIPYPLFQ SHVEDLYVEG LPEGIPFRRP STYGIPRLER ILLAKERIRF VIKKHELLNS 430 440 450 460 470 480 TREDLQLDKP ASGVKEEWYA RITKLRKMVD QLFCKKFAEA LGSTEAKAVP YQKFEAHPND 490 500 510 520 530 540 LYVEGLPENI PFRSPSWYGI PRLEKIIQVG NRIKFVIKRP ELLTHSTTEV TQPRTNTPVK 550 560 570 580 590 600 EDWNVRITKL RKQVEEIFNL KFAQALGLTE AVKVPYPVFE SNPEFLYVEG LPEGIPFRSP 610 620 630 640 650 660 TWFGIPRLER IVRGSNKIKF VVKKPELVIS YLPPGMASKI NTKALQSPKR PRSPGSNSKV 670 680 690 700 710 720 PEIEVTVEGP NNNNPQTSAV RTPTQTNGSN VPFKPRGREF SFEAWNAKIT DLKQKVENLF 730 740 750 760 770 780 NEKCGEALGL KQAVKVPFAL FESFPEDFYV EGLPEGVPFR RPSTFGIPRL EKILRNKAKI 790 800 810 820 830 840 KFIIKKPEMF ETAIKESTSS KSPPRKINSS PNVNTTASGV EDLNIIQVTI PDDDNERLSK 850 860 870 880 890 900 VEKARQLREQ VNDLFSRKFG EAIGMGFPVK VPYRKITINP GCVVVDGMPP GVSFKAPSYL 910 920 930 940 950 960 EISSMRRILD SAEFIKFTVI RPFPGLVINN QLVDQSESEG PVIQESAEPS QLEVPATEEI 970 KETDGSSQIK QEPDPTW

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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.
[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. Tissue: Cervix carcinoma.
[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.
[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).
[5]	"The DNA sequence of human chromosome 7." Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L. , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K. Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]	"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] OF 1-294 (ISOFORM 3). Tissue: Lymph and Ovary.
[7]	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, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma.
[8]	"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.
[9]	"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.
[10]	"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.
[11]	"Systematic identification and analysis of mammalian small ubiquitin-like modifier substrates." Gocke C.B., Yu H., Kang J. J. Biol. Chem. 280:5004-5012(2005) [PubMed] [Europe PMC] [Abstract] Cited for: SUMOYLATION.
[12]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[13]	"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.
[14]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[15]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Tissue: Cervix carcinoma.
[16]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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, MASS SPECTROMETRY.
[18]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[19]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[20]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[21]	"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, MASS SPECTROMETRY.
[22]	"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, MASS SPECTROMETRY.
[23]	"Solution structure of RSGI RUH-052, a GTF2I domain in human." RIKEN structural genomics initiative (RSGI) Submitted (AUG-2007) to the PDB data bank Cited for: STRUCTURE BY NMR OF 102-197 AND 361-554.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

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.
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.
BC004472 mRNA. Translation: AAH04472.1.
BC070484 mRNA. Translation: AAH70484.1.

PIR

T03829.
T09492.

RefSeq

NP_001157108.1. NM_001163636.2.
NP_001267729.1. NM_001280800.1.
NP_001509.3. NM_001518.4.
NP_127492.1. NM_032999.3.
NP_127493.1. NM_033000.3.
NP_127494.1. NM_033001.3.

UniGene

Hs.647041.

3D structure databases

PDBe
RCSB PDB
PDBj

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	[»]

ProteinModelPortal

P78347.

SMR

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

ModBase

Search...

MobiDB

Search...

Protein-protein interaction databases

BioGrid

109224. 64 interactions.

DIP

DIP-24252N.

IntAct

P78347. 26 interactions.

MINT

MINT-1138992.

PTM databases

PhosphoSite

P78347.

Polymorphism databases

DMDM

17865459.

Proteomic databases

PaxDb

P78347.

PRIDE

P78347.

Protocols and materials databases

DNASU

2969.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000324896; ENSP00000322542; ENSG00000077809.
ENST00000346152; ENSP00000322599; ENSG00000077809.
ENST00000353920; ENSP00000322671; ENSG00000077809.
ENST00000416070; ENSP00000387651; ENSG00000077809.

GeneID

2969.

KEGG

hsa:2969.

UCSC

uc003txo.4. human.

Organism-specific databases

CTD

2969.

GeneCards

GC07P074071.

H-InvDB

HIX0023260.

HGNC

HGNC:4659. GTF2I.

HPA

CAB004595.
HPA026638.

MIM

601679. gene.

neXtProt

NX_P78347.

Orphanet

904. Williams syndrome.

PharmGKB

PA29045.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG29608.

HOVERGEN

HBG051856.

InParanoid

P78347.

KO

K03121.

OMA

FLEPKKQ.

OrthoDB

EOG7RRF67.

PhylomeDB

P78347.

TreeFam

TF352524.

Gene expression databases

ArrayExpress

P78347.

Bgee

P78347.

CleanEx

HS_GTF2I.

Genevestigator

P78347.

Family and domain databases

Gene3D

3.90.1460.10. 6 hits.

InterPro

IPR004212. GTF2I.
IPR016659. TF_II-I.
[Graphical view]

Pfam

PF02946. GTF2I. 6 hits.
[Graphical view]

PIRSF

PIRSF016441. TF_II-I. 1 hit.

SUPFAM

SSF117773. SSF117773. 6 hits.

PROSITE

PS51139. GTF2I. 6 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

GTF2I. human.

EvolutionaryTrace

P78347.

GeneWiki

GTF2I.

GenomeRNAi

2969.

NextBio

11768.

PRO

P78347.

SOURCE

Search...

Entry information

Entry name

GTF2I_HUMAN

Accession

Primary (citable) accession number: P78347
Secondary accession number(s): O14743 , O15359, O43546, O43588, O43589, Q75M85, Q75M86, Q75M87, Q75M88, Q9BSZ4

Entry history

Integrated into UniProtKB/Swiss-Prot:	December 13, 2001
Last sequence update:	December 13, 2001
Last modified:	February 19, 2014
This is version 143 of the entry and version 2 of the sequence. [Complete history]

Entry status

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.