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P78347

- GTF2I_HUMAN

UniProt

P78347 - GTF2I_HUMAN

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Protein
General transcription factor II-I
Gene
GTF2I, BAP135, WBSCR6
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

Functioni

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.3 Publications

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. protein binding Source: IntAct
  3. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. embryo development Source: Ensembl
  2. negative regulation of angiogenesis Source: MGI
  3. negative regulation of cytosolic calcium ion concentration Source: Ensembl
  4. signal transduction Source: ProtInc
  5. transcription from RNA polymerase II promoter Source: ProtInc
  6. transcription initiation from RNA polymerase II promoter Source: ProtInc
Complete GO annotation...

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

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
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:4659. GTF2I.

Subcellular locationi

Cytoplasm. Nucleus
Note: Colocalizes with BTK in the cytoplasm.1 Publication

GO - Cellular componenti

  1. cell projection Source: Ensembl
  2. cytoplasm Source: UniProtKB-SubCell
  3. neuronal cell body Source: Ensembl
  4. nucleus Source: HPA
Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi248 – 2481Y → 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
Mutagenesisi398 – 3981Y → 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
Mutagenesisi460 – 4601Y → F: No change on BTK-mediated transcriptional activation. 1 Publication
Mutagenesisi503 – 5031Y → 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

Keywords - Diseasei

Williams-Beuren syndrome

Organism-specific databases

Orphaneti904. Williams syndrome.
PharmGKBiPA29045.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed1 Publication
Chaini2 – 998997General transcription factor II-I
PRO_0000083872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei103 – 1031Phosphoserine3 Publications
Modified residuei130 – 1301N6-acetyllysine By similarity
Modified residuei207 – 2071Phosphoserine1 Publication
Modified residuei210 – 2101Phosphoserine2 Publications
Modified residuei248 – 2481Phosphotyrosine; by BTK2 Publications
Modified residuei318 – 3181Phosphotyrosine; by BTK Inferred
Modified residuei353 – 3531N6-acetyllysine By similarity
Modified residuei398 – 3981Phosphotyrosine; by BTK1 Publication
Modified residuei412 – 4121Phosphoserine; by PKG/PRKG11 Publication
Modified residuei450 – 4501N6-acetyllysine By similarity
Modified residuei503 – 5031Phosphotyrosine; by BTK1 Publication
Modified residuei558 – 5581Phosphothreonine3 Publications
Modified residuei668 – 6681Phosphoserine1 Publication
Modified residuei715 – 7151N6-acetyllysine By similarity
Modified residuei784 – 7841Phosphoserine; by PKG/PRKG11 Publication
Modified residuei823 – 8231Phosphoserine1 Publication

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, Phosphoprotein, Ubl conjugation

Proteomic databases

MaxQBiP78347.
PaxDbiP78347.
PRIDEiP78347.

PTM databases

PhosphoSiteiP78347.

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

ArrayExpressiP78347.
BgeeiP78347.
CleanExiHS_GTF2I.
GenevestigatoriP78347.

Organism-specific databases

HPAiCAB004595.
HPA026638.

Interactioni

Subunit structurei

Homodimer Reviewed prediction. 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 PRKG1.4 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
BRCA1P383985EBI-359622,EBI-349905
BTKQ061876EBI-359622,EBI-624835

Protein-protein interaction databases

BioGridi109224. 78 interactions.
DIPiDIP-24252N.
IntActiP78347. 27 interactions.
MINTiMINT-1138992.

Structurei

Secondary structure

Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi106 – 12823
Helixi138 – 1436
Beta strandi146 – 1527
Helixi167 – 1759
Turni176 – 1794
Beta strandi181 – 1855
Helixi361 – 37616
Helixi387 – 3926
Turni393 – 3964
Beta strandi397 – 4015
Turni411 – 4133
Helixi416 – 4249
Turni426 – 4283
Beta strandi430 – 4345
Turni437 – 4393
Helixi466 – 48217
Helixi492 – 4976
Turni499 – 5013
Beta strandi502 – 5065
Turni516 – 5183
Helixi521 – 5299
Turni530 – 5334
Beta strandi535 – 5395
Helixi541 – 5444
Turni856 – 8583
Helixi861 – 88323
Helixi894 – 8996
Beta strandi901 – 9077
Turni918 – 9203
Helixi923 – 9319
Turni932 – 9354
Beta strandi937 – 9426

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D9BNMR-A102-197[»]
2DN4NMR-A361-446[»]
2ED2NMR-A466-551[»]
2EJENMR-A854-954[»]
ProteinModelPortaliP78347.
SMRiP78347. Positions 104-197, 359-454, 466-556, 571-649, 731-823, 854-959.

Miscellaneous databases

EvolutionaryTraceiP78347.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati103 – 19795GTF2I-like 1
Add
BLAST
Repeati352 – 44695GTF2I-like 2
Add
BLAST
Repeati457 – 55195GTF2I-like 3
Add
BLAST
Repeati562 – 65695GTF2I-like 4
Add
BLAST
Repeati724 – 81895GTF2I-like 5
Add
BLAST
Repeati859 – 95395GTF2I-like 6
Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi320 – 3278Nuclear localization signal Reviewed prediction

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi692 – 6954Poly-Asn

Sequence similaritiesi

Belongs to the TFII-I family.
Contains 6 GTF2I-like repeats.

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG29608.
HOVERGENiHBG051856.
InParanoidiP78347.
KOiK03121.
OMAiMPPGVAF.
OrthoDBiEOG7RRF67.
PhylomeDBiP78347.
TreeFamiTF352524.

Family and domain databases

Gene3Di3.90.1460.10. 6 hits.
InterProiIPR004212. GTF2I.
IPR016659. TF_II-I.
[Graphical view]
PfamiPF02946. GTF2I. 6 hits.
[Graphical view]
PIRSFiPIRSF016441. TF_II-I. 1 hit.
SUPFAMiSSF117773. SSF117773. 6 hits.
PROSITEiPS51139. 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

Isoform 1 (identifier: P78347-1) [UniParc]FASTAAdd to Basket

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

« Hide

MAQVAMSTLP VEDEESSESR MVVTFLMSAL ESMCKELAKS KAEVACIAVY    50
ETDVFVVGTE RGRAFVNTRK DFQKDFVKYC VEEEEKAAEM HKMKSTTQAN 100
RMSVDAVEIE TLRKTVEDYF CFCYGKALGK STVVPVPYEK MLRDQSAVVV 150
QGLPEGVAFK HPENYDLATL KWILENKAGI SFIIKRPFLE PKKHVGGRVM 200
VTDADRSILS PGGSCGPIKV KTEPTEDSGI SLEMAAVTVK EESEDPDYYQ 250
YNIQAGPSET DDVDEKQPLS KPLQGSHHSS EGNEGTEMEV PAEDSTQHVP 300
SETSEDPEVE VTIEDDDYSP PSKRPKANEL PQPPVPEPAN AGKRKVREFN 350
FEKWNARITD LRKQVEELFE RKYAQAIKAK GPVTIPYPLF QSHVEDLYVE 400
GLPEGIPFRR PSTYGIPRLE RILLAKERIR FVIKKHELLN STREDLQLDK 450
PASGVKEEWY ARITKLRKMV DQLFCKKFAE ALGSTEAKAV PYQKFEAHPN 500
DLYVEGLPEN IPFRSPSWYG IPRLEKIIQV GNRIKFVIKR PELLTHSTTE 550
VTQPRTNTPV KEDWNVRITK LRKQVEEIFN LKFAQALGLT EAVKVPYPVF 600
ESNPEFLYVE GLPEGIPFRS PTWFGIPRLE RIVRGSNKIK FVVKKPELVI 650
SYLPPGMASK INTKALQSPK RPRSPGSNSK VPEIEVTVEG PNNNNPQTSA 700
VRTPTQTNGS NVPFKPRGRE FSFEAWNAKI TDLKQKVENL FNEKCGEALG 750
LKQAVKVPFA LFESFPEDFY VEGLPEGVPF RRPSTFGIPR LEKILRNKAK 800
IKFIIKKPEM FETAIKESTS SKSPPRKINS SPNVNTTASG VEDLNIIQVT 850
IPDDDNERLS KVEKARQLRE QVNDLFSRKF GEAIGMGFPV KVPYRKITIN 900
PGCVVVDGMP PGVSFKAPSY LEISSMRRIL DSAEFIKFTV IRPFPGLVIN 950
NQLVDQSESE GPVIQESAEP SQLEVPATEE IKETDGSSQI KQEPDPTW 998
Length:998
Mass (Da):112,416
Last modified:December 13, 2001 - v2
Checksum:i4CFA2C19002869B9
GO
Isoform 2 (identifier: P78347-2) [UniParc]FASTAAdd to Basket

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

Show »
Length:957
Mass (Da):107,970
Checksum:iE091B620FF633AC8
GO
Isoform 3 (identifier: P78347-3) [UniParc]FASTAAdd to Basket

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

Show »
Length:978
Mass (Da):110,280
Checksum:i1F006D480F0BE702
GO
Isoform 4 (identifier: P78347-4) [UniParc]FASTAAdd to Basket

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

Show »
Length:977
Mass (Da):110,106
Checksum:i418D59EC623E6141
GO
Isoform 5 (identifier: P78347-5) [UniParc]FASTAAdd to Basket

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

Note: No experimental confirmation available.

Show »
Length:274
Mass (Da):30,409
Checksum:iC693096D47E9CDC7
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti174 – 1741L → V.
Corresponds to variant rs1057896 [ dbSNP | Ensembl ].
VAR_051026

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei255 – 27420Missing in isoform 2, isoform 3 and isoform 5.
VSP_003867Add
BLAST
Alternative sequencei294 – 31421Missing in isoform 2 and isoform 4.
VSP_003868Add
BLAST
Alternative sequencei294 – 2941D → G in isoform 5.
VSP_055195
Alternative sequencei295 – 998704Missing in isoform 5.
VSP_055196Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741L → G in AAB48826. 1 Publication
Sequence conflicti178 – 1781A → G in AAB48826. 1 Publication
Sequence conflicti481 – 4811A → R in AAB70791. 1 Publication
Sequence conflicti634 – 6341R → H in AAB48826. 1 Publication
Sequence conflicti960 – 9601E → K in AAB48826. 1 Publication

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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.
CCDSiCCDS47614.1. [P78347-2]
CCDS5573.1. [P78347-1]
CCDS5574.1. [P78347-3]
CCDS5575.1. [P78347-4]
PIRiT03829.
T09492.
RefSeqiNP_001157108.1. NM_001163636.2.
NP_001267729.1. NM_001280800.1.
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]
XP_006716005.1. XM_006715942.1. [P78347-1]
UniGeneiHs.647041.
Hs.654705.
Hs.743231.

Genome annotation databases

EnsembliENST00000324896; ENSP00000322542; ENSG00000077809. [P78347-1]
ENST00000346152; ENSP00000322599; ENSG00000077809. [P78347-4]
ENST00000353920; ENSP00000322671; ENSG00000077809. [P78347-3]
ENST00000416070; ENSP00000387651; ENSG00000077809. [P78347-2]
ENST00000443166; ENSP00000404240; ENSG00000077809.
GeneIDi2969.
KEGGihsa:2969.
UCSCiuc003txo.4. human. [P78347-1]
uc003uav.3. human. [P78347-4]
uc003uaw.3. human. [P78347-3]
uc003uax.3. human. [P78347-2]

Polymorphism databases

DMDMi17865459.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 ]
PIRi T03829.
T09492.
RefSeqi NP_001157108.1. NM_001163636.2.
NP_001267729.1. NM_001280800.1.
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 ]
XP_006716005.1. XM_006715942.1. [P78347-1 ]
UniGenei Hs.647041.
Hs.654705.
Hs.743231.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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 P78347.
SMRi P78347. Positions 104-197, 359-454, 466-556, 571-649, 731-823, 854-959.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 109224. 78 interactions.
DIPi DIP-24252N.
IntActi P78347. 27 interactions.
MINTi MINT-1138992.

PTM databases

PhosphoSitei P78347.

Polymorphism databases

DMDMi 17865459.

Proteomic databases

MaxQBi P78347.
PaxDbi P78347.
PRIDEi P78347.

Protocols and materials databases

DNASUi 2969.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000324896 ; ENSP00000322542 ; ENSG00000077809 . [P78347-1 ]
ENST00000346152 ; ENSP00000322599 ; ENSG00000077809 . [P78347-4 ]
ENST00000353920 ; ENSP00000322671 ; ENSG00000077809 . [P78347-3 ]
ENST00000416070 ; ENSP00000387651 ; ENSG00000077809 . [P78347-2 ]
ENST00000443166 ; ENSP00000404240 ; ENSG00000077809 .
GeneIDi 2969.
KEGGi hsa:2969.
UCSCi uc003txo.4. human. [P78347-1 ]
uc003uav.3. human. [P78347-4 ]
uc003uaw.3. human. [P78347-3 ]
uc003uax.3. human. [P78347-2 ]

Organism-specific databases

CTDi 2969.
GeneCardsi GC07P074071.
H-InvDB HIX0023260.
HGNCi HGNC:4659. GTF2I.
HPAi CAB004595.
HPA026638.
MIMi 601679. gene.
neXtProti NX_P78347.
Orphaneti 904. Williams syndrome.
PharmGKBi PA29045.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG29608.
HOVERGENi HBG051856.
InParanoidi P78347.
KOi K03121.
OMAi MPPGVAF.
OrthoDBi EOG7RRF67.
PhylomeDBi P78347.
TreeFami TF352524.

Miscellaneous databases

ChiTaRSi GTF2I. human.
EvolutionaryTracei P78347.
GeneWikii GTF2I.
GenomeRNAii 2969.
NextBioi 11768.
PROi P78347.
SOURCEi Search...

Gene expression databases

ArrayExpressi P78347.
Bgeei P78347.
CleanExi HS_GTF2I.
Genevestigatori P78347.

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 ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  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. "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).
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  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).
    Tissue: Lymph and Ovary.
  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.
    Tissue: Colon adenocarcinoma.
  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.
  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.
  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.
  13. "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.
  14. "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.
  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.
  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].
    Tissue: Cervix carcinoma.
  17. "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.
  18. 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.
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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].
    Tissue: Leukemic T-cell.
  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].
    Tissue: Cervix carcinoma.
  22. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  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].
  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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  26. "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.

Entry informationi

Entry nameiGTF2I_HUMAN
AccessioniPrimary (citable) accession number: P78347
Secondary accession number(s): O14743
, O15359, O43546, O43588, O43589, Q75M85, Q75M86, Q75M87, Q75M88, Q86U51, Q9BSZ4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 13, 2001
Last sequence update: December 13, 2001
Last modified: September 3, 2014
This is version 149 of the entry and version 2 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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