Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

P78347

- GTF2I_HUMAN

UniProt

P78347 - GTF2I_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein

General transcription factor II-I

Gene

GTF2I

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (5)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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. sequence-specific DNA binding transcription factor activity Source: ProtInc

GO - Biological processi

  1. negative regulation of angiogenesis Source: MGI
  2. signal transduction Source: ProtInc
  3. transcription from RNA polymerase II promoter Source: ProtInc
  4. 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 lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:4659. GTF2I.

Subcellular locationi

Cytoplasm 1 Publication. Nucleus 1 PublicationPROSITE-ProRule annotation
Note: Colocalizes with BTK in the cytoplasm.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB-SubCell
  2. membrane Source: UniProtKB
  3. 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 – 11Removed4 Publications
Chaini2 – 998997General transcription factor II-IPRO_0000083872Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei103 – 1031Phosphoserine3 Publications
Modified residuei130 – 1301N6-acetyllysineBy similarity
Modified residuei207 – 2071Phosphoserine1 Publication
Modified residuei210 – 2101Phosphoserine2 Publications
Modified residuei248 – 2481Phosphotyrosine; by BTK2 Publications
Modified residuei318 – 3181Phosphotyrosine; by BTK1 Publication
Modified residuei353 – 3531N6-acetyllysineBy similarity
Modified residuei398 – 3981Phosphotyrosine; by BTK1 Publication
Modified residuei412 – 4121Phosphoserine; by PKG/PRKG11 Publication
Modified residuei450 – 4501N6-acetyllysineBy similarity
Modified residuei503 – 5031Phosphotyrosine; by BTK1 Publication
Modified residuei558 – 5581Phosphothreonine3 Publications
Modified residuei668 – 6681Phosphoserine1 Publication
Modified residuei715 – 7151N6-acetyllysineBy 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.9 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

BgeeiP78347.
CleanExiHS_GTF2I.
ExpressionAtlasiP78347. baseline and differential.
GenevestigatoriP78347.

Organism-specific databases

HPAiCAB004595.
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 PRKG1.4 PublicationsCurated

Binary interactionsi

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

Protein-protein interaction databases

BioGridi109224. 92 interactions.
DIPiDIP-24252N.
IntActiP78347. 26 interactions.
MINTiMINT-1138992.

Structurei

Secondary structure

1
998
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi106 – 12823Combined sources
Helixi138 – 1436Combined sources
Beta strandi146 – 1527Combined sources
Helixi167 – 1759Combined sources
Turni176 – 1794Combined sources
Beta strandi181 – 1855Combined sources
Helixi361 – 37616Combined sources
Helixi387 – 3926Combined sources
Turni393 – 3964Combined sources
Beta strandi397 – 4015Combined sources
Turni411 – 4133Combined sources
Helixi416 – 4249Combined sources
Turni426 – 4283Combined sources
Beta strandi430 – 4345Combined sources
Turni437 – 4393Combined sources
Helixi466 – 48217Combined sources
Helixi492 – 4976Combined sources
Turni499 – 5013Combined sources
Beta strandi502 – 5065Combined sources
Turni516 – 5183Combined sources
Helixi521 – 5299Combined sources
Turni530 – 5334Combined sources
Beta strandi535 – 5395Combined sources
Helixi541 – 5444Combined sources
Turni856 – 8583Combined sources
Helixi861 – 88323Combined sources
Helixi894 – 8996Combined sources
Beta strandi901 – 9077Combined sources
Turni918 – 9203Combined sources
Helixi923 – 9319Combined sources
Turni932 – 9354Combined sources
Beta strandi937 – 9426Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
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.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP78347.

Family & Domainsi

Domains and Repeats

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

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi320 – 3278Nuclear localization signalSequence Analysis

Compositional bias

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

eggNOGiNOG29608.
GeneTreeiENSGT00530000063863.
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

        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
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

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti174 – 1741L → G in AAB48826. (PubMed:9012831)Curated
Sequence conflicti178 – 1781A → G in AAB48826. (PubMed:9012831)Curated
Sequence conflicti481 – 4811A → R in AAB70791. (PubMed:9384587)Curated
Sequence conflicti634 – 6341R → H in AAB48826. (PubMed:9012831)Curated
Sequence conflicti960 – 9601E → K in AAB48826. (PubMed:9012831)Curated

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. 6 PublicationsVSP_003867Add
BLAST
Alternative sequencei294 – 31421Missing in isoform 2 and isoform 4. 5 PublicationsVSP_003868Add
BLAST
Alternative sequencei294 – 2941D → G in isoform 5. 2 PublicationsVSP_055195
Alternative sequencei295 – 998704Missing in isoform 5. 2 PublicationsVSP_055196Add
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.
CCDSiCCDS47614.1. [P78347-2]
CCDS5573.1. [P78347-1]
CCDS5574.1. [P78347-3]
CCDS5575.1. [P78347-4]
CCDS64680.1. [P78347-5]
PIRiT03829.
T09492.
RefSeqiNP_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]
XP_006716005.1. XM_006715942.1. [P78347-1]
UniGeneiHs.647041.
Hs.654705.
Hs.743231.

Genome annotation databases

EnsembliENST00000443166; ENSP00000404240; ENSG00000263001. [P78347-5]
ENST00000573035; ENSP00000460070; ENSG00000263001. [P78347-1]
ENST00000614986; ENSP00000484526; ENSG00000263001. [P78347-3]
ENST00000620879; ENSP00000477837; ENSG00000263001. [P78347-2]
ENST00000621734; ENSP00000482476; ENSG00000263001. [P78347-4]
GeneIDi2969.
KEGGihsa:2969.
UCSCiuc003txo.4. human. [P78347-1]
uc003uat.3. human.
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:
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 ]
XP_006716005.1. XM_006715942.1. [P78347-1 ]
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 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. 92 interactions.
DIPi DIP-24252N.
IntActi P78347. 26 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 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 uc003txo.4. human. [P78347-1 ]
uc003uat.3. human.
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.
GeneTreei ENSGT00530000063863.
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

Bgeei P78347.
CleanExi HS_GTF2I.
ExpressionAtlasi P78347. baseline and differential.
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.
+Additional computationally mapped references.

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: January 7, 2015
This is version 153 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.
© 2002– 2015 UniProt Consortium | License & Disclaimer