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P78347 (GTF2I_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 145. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length998 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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.

Binary interactions

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 998997General transcription factor II-I
PRO_0000083872

Regions

Repeat103 – 19795GTF2I-like 1
Repeat352 – 44695GTF2I-like 2
Repeat457 – 55195GTF2I-like 3
Repeat562 – 65695GTF2I-like 4
Repeat724 – 81895GTF2I-like 5
Repeat859 – 95395GTF2I-like 6
Motif320 – 3278Nuclear localization signal Potential
Compositional bias692 – 6954Poly-Asn

Amino acid modifications

Modified residue21N-acetylalanine Ref.7 Ref.17 Ref.22 Ref.23
Modified residue1031Phosphoserine Ref.16 Ref.18 Ref.19
Modified residue1301N6-acetyllysine By similarity
Modified residue2071Phosphoserine Ref.16
Modified residue2101Phosphoserine Ref.14 Ref.16
Modified residue2481Phosphotyrosine; by BTK Ref.9 Ref.13
Modified residue3181Phosphotyrosine; by BTK Probable
Modified residue3531N6-acetyllysine By similarity
Modified residue3981Phosphotyrosine; by BTK Ref.9
Modified residue4121Phosphoserine; by PKG/PRKG1 Ref.10
Modified residue4501N6-acetyllysine By similarity
Modified residue5031Phosphotyrosine; by BTK Ref.9
Modified residue5581Phosphothreonine Ref.16 Ref.18 Ref.19
Modified residue6681Phosphoserine Ref.21
Modified residue7151N6-acetyllysine By similarity
Modified residue7841Phosphoserine; by PKG/PRKG1 Ref.10
Modified residue8231Phosphoserine Ref.19

Natural variations

Alternative sequence255 – 27420Missing in isoform 2 and isoform 3.
VSP_003867
Alternative sequence294 – 31421Missing in isoform 2 and isoform 4.
VSP_003868
Natural variant1741L → V.
Corresponds to variant rs1057896 [ dbSNP | Ensembl ].
VAR_051026

Experimental info

Mutagenesis2481Y → 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
Mutagenesis3981Y → 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
Mutagenesis4601Y → F: No change on BTK-mediated transcriptional activation. Ref.9
Mutagenesis5031Y → 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 conflict1741L → G in AAB48826. Ref.3
Sequence conflict1781A → G in AAB48826. Ref.3
Sequence conflict2941D → G in AAH04472. Ref.6
Sequence conflict4811A → R in AAB70791. Ref.1
Sequence conflict6341R → H in AAB48826. Ref.3
Sequence conflict9601E → K in AAB48826. Ref.3

Secondary structure

........................................................... 998
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified December 13, 2001. Version 2.
Checksum: 4CFA2C19002869B9

FASTA998112,416
        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 

« Hide

Isoform 2 [UniParc].

Checksum: E091B620FF633AC8
Show »

FASTA957107,970
Isoform 3 [UniParc].

Checksum: 1F006D480F0BE702
Show »

FASTA978110,280
Isoform 4 [UniParc].

Checksum: 418D59EC623E6141
Show »

FASTA977110,106

References

« Hide '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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[22]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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.
PIRT03829.
T09492.
RefSeqNP_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.
UniGeneHs.647041.
Hs.654705.
Hs.743231.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9BNMR-A102-197[»]
2DN4NMR-A361-446[»]
2ED2NMR-A466-551[»]
2EJENMR-A854-954[»]
ProteinModelPortalP78347.
SMRP78347. Positions 104-197, 359-454, 466-556, 571-649, 731-823, 854-959.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid109224. 73 interactions.
DIPDIP-24252N.
IntActP78347. 26 interactions.
MINTMINT-1138992.

PTM databases

PhosphoSiteP78347.

Polymorphism databases

DMDM17865459.

Proteomic databases

PaxDbP78347.
PRIDEP78347.

Protocols and materials databases

DNASU2969.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000324896; ENSP00000322542; ENSG00000077809. [P78347-1]
ENST00000346152; ENSP00000322599; ENSG00000077809. [P78347-4]
ENST00000353920; ENSP00000322671; ENSG00000077809. [P78347-3]
ENST00000416070; ENSP00000387651; ENSG00000077809. [P78347-2]
GeneID2969.
KEGGhsa:2969.
UCSCuc003txo.4. human. [P78347-1]
uc003uav.3. human. [P78347-4]
uc003uaw.3. human. [P78347-3]
uc003uax.3. human. [P78347-2]

Organism-specific databases

CTD2969.
GeneCardsGC07P074071.
H-InvDBHIX0023260.
HGNCHGNC:4659. GTF2I.
HPACAB004595.
HPA026638.
MIM601679. gene.
neXtProtNX_P78347.
Orphanet904. Williams syndrome.
PharmGKBPA29045.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG29608.
HOVERGENHBG051856.
InParanoidP78347.
KOK03121.
OMAFLEPKKQ.
OrthoDBEOG7RRF67.
PhylomeDBP78347.
TreeFamTF352524.

Gene expression databases

ArrayExpressP78347.
BgeeP78347.
CleanExHS_GTF2I.
GenevestigatorP78347.

Family and domain databases

Gene3D3.90.1460.10. 6 hits.
InterProIPR004212. GTF2I.
IPR016659. TF_II-I.
[Graphical view]
PfamPF02946. GTF2I. 6 hits.
[Graphical view]
PIRSFPIRSF016441. TF_II-I. 1 hit.
SUPFAMSSF117773. SSF117773. 6 hits.
PROSITEPS51139. GTF2I. 6 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSGTF2I. human.
EvolutionaryTraceP78347.
GeneWikiGTF2I.
GenomeRNAi2969.
NextBio11768.
PROP78347.
SOURCESearch...

Entry information

Entry nameGTF2I_HUMAN
AccessionPrimary (citable) accession number: P78347
Secondary accession number(s): O14743 expand/collapse secondary AC list , 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: April 16, 2014
This is version 145 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 7

Human chromosome 7: entries, gene names and cross-references to MIM