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Q9UHL9 (GT2D1_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 133. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
General transcription factor II-I repeat domain-containing protein 1

Short name=GTF2I repeat domain-containing protein 1
Alternative name(s):
General transcription factor III
MusTRD1/BEN
Muscle TFII-I repeat domain-containing protein 1
Slow-muscle-fiber enhancer-binding protein
USE B1-binding protein
Williams-Beuren syndrome chromosomal region 11 protein
Williams-Beuren syndrome chromosomal region 12 protein
Gene names
Name:GTF2IRD1
Synonyms:CREAM1, GTF3, MUSTRD1, RBAP2, WBSCR11, WBSCR12
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length959 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

May be a transcription regulator involved in cell-cycle progression and skeletal muscle differentiation. May repress GTF2I transcriptional functions, by preventing its nuclear residency, or by inhibiting its transcriptional activation. May contribute to slow-twitch fiber type specificity during myogenesis and in regenerating muscles. Binds troponin I slow-muscle fiber enhancer (USE B1). Binds specifically and with high affinity to the EFG sequences derived from the early enhancer of HOXC8 By similarity. Ref.9

Subunit structure

Interacts with the retinoblastoma protein (RB1) via its C-terminus. Ref.5

Subcellular location

Nucleus.

Tissue specificity

Highly expressed in adult skeletal muscle, heart, fibroblast, bone and fetal tissues. Expressed at lower levels in all other tissues tested.

Developmental stage

Highly expressed in developing and regenerating muscles, at the time of myofiber diversification.

Domain

The N-terminal half may have an activating activity.

Involvement in disease

GTF2IRD1 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 GTF2IRD1 may be the cause of certain cardiovascular and musculo-skeletal abnormalities observed in the disease.

Sequence similarities

Belongs to the TFII-I family.

Contains 5 GTF2I-like repeats.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q9UHL9-1)

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: Q9UHL9-2)

The sequence of this isoform differs from the canonical sequence as follows:
     656-670: Missing.
Note: Contains a phosphoserine at position 654.
Isoform 3 (identifier: Q9UHL9-3)

The sequence of this isoform differs from the canonical sequence as follows:
     89-89: R → LSAAQHRAATSQLEGRVVRRVLTVASRALCPTG
     656-670: Missing.
Note: Contains a phosphoserine at position 686.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 959959General transcription factor II-I repeat domain-containing protein 1
PRO_0000083870

Regions

Repeat119 – 21395GTF2I-like 1
Repeat342 – 43695GTF2I-like 2
Repeat556 – 65095GTF2I-like 3
Repeat696 – 79095GTF2I-like 4
Repeat793 – 88795GTF2I-like 5
Motif898 – 9058Nuclear localization signal Potential
Compositional bias906 – 93025Ser-rich

Amino acid modifications

Modified residue4481Phosphoserine Ref.10 Ref.12 Ref.13

Natural variations

Alternative sequence891R → LSAAQHRAATSQLEGRVVRR VLTVASRALCPTG in isoform 3.
VSP_043425
Alternative sequence656 – 67015Missing in isoform 2 and isoform 3.
VSP_003873
Natural variant6521M → V. Ref.4 Ref.5 Ref.8
Corresponds to variant rs2301895 [ dbSNP | Ensembl ].
VAR_013446

Experimental info

Mutagenesis898 – 95962Missing: Cytoplasmic localization.
Sequence conflict1111G → S in AAD14687. Ref.1
Sequence conflict1111G → S in AAD27668. Ref.2
Sequence conflict3781R → Q in AAF21796. Ref.5

Secondary structure

......................................................... 959
Helix Strand Turn

Details...

Sequences

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

Last modified May 1, 2000. Version 1.
Checksum: 7DA3097879701540

FASTA959106,057
        10         20         30         40         50         60 
MALLGKRCDV PTNGCGPDRW NSAFTRKDEI ITSLVSALDS MCSALSKLNA EVACVAVHDE 

        70         80         90        100        110        120 
SAFVVGTEKG RMFLNARKEL QSDFLRFCRG PPWKDPEAEH PKKVQRGEGG GRSLPRSSLE 

       130        140        150        160        170        180 
HGSDVYLLRK MVEEVFDVLY SEALGRASVV PLPYERLLRE PGLLAVQGLP EGLAFRRPAE 

       190        200        210        220        230        240 
YDPKALMAIL EHSHRIRFKL KRPLEDGGRD SKALVELNGV SLIPKGSRDC GLHGQAPKVP 

       250        260        270        280        290        300 
PQDLPPTATS SSMASFLYST ALPNHAIREL KQEAPSCPLA PSDLGLSRPM PEPKATGAQD 

       310        320        330        340        350        360 
FSDCCGQKPT GPGGPLIQNV HASKRILFSI VHDKSEKWDA FIKETEDINT LRECVQILFN 

       370        380        390        400        410        420 
SRYAEALGLD HMVPVPYRKI ACDPEAVEIV GIPDKIPFKR PCTYGVPKLK RILEERHSIH 

       430        440        450        460        470        480 
FIIKRMFDER IFTGNKFTKD TTKLEPASPP EDTSAEVSRA TVLDLAGNAR SDKGSMSEDC 

       490        500        510        520        530        540 
GPGTSGELGG LRPIKIEPED LDIIQVTVPD PSPTSEEMTD SMPGHLPSED SGYGMEMLTD 

       550        560        570        580        590        600 
KGLSEDARPE ERPVEDSHGD VIRPLRKQVE LLFNTRYAKA IGISEPVKVP YSKFLMHPEE 

       610        620        630        640        650        660 
LFVVGLPEGI SLRRPNCFGI AKLRKILEAS NSIQFVIKRP ELLTEGVKEP IMDSQGTASS 

       670        680        690        700        710        720 
LGFSPPALPP ERDSGDPLVD ESLKRQGFQE NYDARLSRID IANTLREQVQ DLFNKKYGEA 

       730        740        750        760        770        780 
LGIKYPVQVP YKRIKSNPGS VIIEGLPPGI PFRKPCTFGS QNLERILAVA DKIKFTVTRP 

       790        800        810        820        830        840 
FQGLIPKPDE DDANRLGEKV ILREQVKELF NEKYGEALGL NRPVLVPYKL IRDSPDAVEV 

       850        860        870        880        890        900 
TGLPDDIPFR NPNTYDIHRL EKILKAREHV RMVIINQLQP FAEICNDAKV PAKDSSIPKR 

       910        920        930        940        950 
KRKRVSEGNS VSSSSSSSSS SSSNPDSVAS ANQISLVQWP MYMVDYAGLN VQLPGPLNY 

« Hide

Isoform 2 [UniParc].

Checksum: 57E1190182D1D33F
Show »

FASTA944104,677
Isoform 3 [UniParc].

Checksum: 674D8406B5D6A618
Show »

FASTA976107,979

References

« Hide 'large scale' references
[1]"Identification of a novel slow-muscle-fiber enhancer binding protein, MUSTRD1."
O'Mahoney J.V., Guven K.L., Lin J., Joya J.E., Robinson C.S., Wade R.P., Hardeman E.C.
Mol. Cell. Biol. 18:6641-6652(1998) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Muscle.
[2]"Identification of a putative transcription factor gene (WBSCR11) that is commonly deleted in Williams-Beuren syndrome."
Osborne L.R., Campbell T., Daradich A., Scherer S.W., Tsui L.-C.
Genomics 57:279-284(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
Tissue: Colon carcinoma.
[3]"A transcription factor involved in skeletal muscle gene expression is deleted in patients with Williams syndrome."
Tassabehji M., Carette M., Wilmot C., Donnai D., Read A.P., Metcalfe K.
Eur. J. Hum. Genet. 7:737-747(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
Tissue: Fetal brain.
[4]"Identification of GTF2IRD1, a putative transcription factor within the Williams-Beuren syndrome deletion at 7q11.23."
Franke Y., Peoples R.J., Francke U.
Cytogenet. Cell Genet. 86:296-304(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT VAL-652.
[5]"Characterization and gene structure of a novel retinoblastoma-protein-associated protein similar to the transcription regulator TFII-I."
Yan X., Zhao X., Qian M., Guo N., Gong X., Zhu X.
Biochem. J. 345:749-757(2000) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RB1, MUTAGENESIS, VARIANT VAL-652.
Tissue: Cervix carcinoma, Fetal spleen and Placenta.
[6]"GTF2IRD1 represses transcription from a conserved DNA element upstream of three separate promoters."
Cunliffe P., Hart-Holden N., Hinsley T., Sharrocks A.D., Tassabehji M.
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
[7]"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].
[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 1), VARIANT VAL-652.
Tissue: Uterus.
[9]"Repression of TFII-I-dependent transcription by nuclear exclusion."
Tussie-Luna M.I., Bayarsaihan D., Ruddle F.H., Roy A.L.
Proc. Natl. Acad. Sci. U.S.A. 98:7789-7794(2001) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION.
[10]"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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"ATM and ATR substrate analysis reveals extensive protein networks responsive to DNA damage."
Matsuoka S., Ballif B.A., Smogorzewska A., McDonald E.R. III, Hurov K.E., Luo J., Bakalarski C.E., Zhao Z., Solimini N., Lerenthal Y., Shiloh Y., Gygi S.P., Elledge S.J.
Science 316:1160-1166(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-654 (ISOFORM 2), PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-686 (ISOFORM 3), IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Embryonic kidney.
[12]"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-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"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-448, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[14]"Solution structure of RSGI RUH-048 and RUH-057, a GTF2I domain in human."
RIKEN structural genomics initiative (RSGI)
Submitted (MAR-2007) to the PDB data bank
Cited for: STRUCTURE BY NMR OF 128-203 AND 565-877.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF118270 mRNA. Translation: AAD14687.2.
AF104923 mRNA. Translation: AAD27668.1.
AF151354 mRNA. Translation: AAF19786.1.
AF156489 mRNA. Translation: AAF17358.1.
AF089107 mRNA. Translation: AAF21796.1.
AY648295 mRNA. Translation: AAT68469.1.
AC004851 Genomic DNA. Translation: AAS00362.1.
AC005015 Genomic DNA. No translation available.
AC005231 Genomic DNA. Translation: AAP21877.1.
BC018136 mRNA. Translation: AAH18136.1.
RefSeqNP_001186136.1. NM_001199207.1.
NP_005676.3. NM_005685.3.
NP_057412.1. NM_016328.2.
UniGeneHs.647056.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2D99NMR-A128-203[»]
2DN5NMR-A802-877[»]
2DZQNMR-A565-650[»]
2DZRNMR-A705-790[»]
ProteinModelPortalQ9UHL9.
SMRQ9UHL9. Positions 128-203, 351-427, 565-656, 702-790, 802-880.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114939. 9 interactions.
IntActQ9UHL9. 2 interactions.
MINTMINT-1209004.
STRING9606.ENSP00000265755.

PTM databases

PhosphoSiteQ9UHL9.

Polymorphism databases

DMDM21263630.

Proteomic databases

PaxDbQ9UHL9.
PRIDEQ9UHL9.

Protocols and materials databases

DNASU9569.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000265755; ENSP00000265755; ENSG00000006704. [Q9UHL9-1]
ENST00000424337; ENSP00000408477; ENSG00000006704. [Q9UHL9-2]
ENST00000455841; ENSP00000397566; ENSG00000006704. [Q9UHL9-3]
ENST00000573381; ENSP00000460934; ENSG00000261920. [Q9UHL9-3]
ENST00000573543; ENSP00000461690; ENSG00000261920. [Q9UHL9-2]
ENST00000574416; ENSP00000458414; ENSG00000261920. [Q9UHL9-1]
GeneID9569.
KEGGhsa:9569.
UCSCuc003uap.3. human. [Q9UHL9-2]
uc003uaq.3. human. [Q9UHL9-1]
uc010lbq.3. human. [Q9UHL9-3]

Organism-specific databases

CTD9569.
GeneCardsGC07P073868.
HGNCHGNC:4661. GTF2IRD1.
HPAHPA044254.
MIM604318. gene.
neXtProtNX_Q9UHL9.
Orphanet904. Williams syndrome.
PharmGKBPA29047.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG29608.
HOGENOMHOG000112829.
HOVERGENHBG051855.
InParanoidQ9UHL9.
KOK03121.
OMASDFLRFC.
PhylomeDBQ9UHL9.
TreeFamTF352524.

Gene expression databases

ArrayExpressQ9UHL9.
BgeeQ9UHL9.
CleanExHS_GTF2IRD1.
GenevestigatorQ9UHL9.

Family and domain databases

Gene3D3.90.1460.10. 5 hits.
InterProIPR004212. GTF2I.
IPR016659. TF_II-I.
[Graphical view]
PfamPF02946. GTF2I. 5 hits.
[Graphical view]
PIRSFPIRSF016441. TF_II-I. 1 hit.
SUPFAMSSF117773. SSF117773. 5 hits.
PROSITEPS51139. GTF2I. 5 hits.
[Graphical view]
ProtoNetSearch...

Other

EvolutionaryTraceQ9UHL9.
GeneWikiGTF2IRD1.
GenomeRNAi9569.
NextBio35885.
PROQ9UHL9.
SOURCESearch...

Entry information

Entry nameGT2D1_HUMAN
AccessionPrimary (citable) accession number: Q9UHL9
Secondary accession number(s): O95444 expand/collapse secondary AC list , Q6DSU6, Q75MX7, Q86UM3, Q8WVC4, Q9UHK8, Q9UI91
Entry history
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 2000
Last modified: April 16, 2014
This is version 133 of the entry and version 1 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