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Protein

General transcription factor II-I repeat domain-containing protein 1

Gene

GTF2IRD1

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

Functioni

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).By similarity

GO - Molecular functioni

  1. DNA binding Source: UniProtKB-KW
  2. RNA polymerase II distal enhancer sequence-specific DNA binding transcription factor activity Source: UniProtKB
  3. sequence-specific DNA binding transcription factor activity Source: UniProtKB

GO - Biological processi

  1. multicellular organismal development Source: UniProtKB-KW
  2. regulation of transcription, DNA-templated Source: UniProtKB
  3. regulation of transcription from RNA polymerase II promoter Source: GOC
  4. transcription from RNA polymerase II promoter Source: GOC
  5. transition between slow and fast fiber Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Developmental protein

Keywords - Biological processi

Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Names & Taxonomyi

Protein namesi
Recommended 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 namesi
Name:GTF2IRD1
Synonyms:CREAM1, GTF3, MUSTRD1, RBAP2, WBSCR11, WBSCR12
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:4661. GTF2IRD1.

Subcellular locationi

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. nucleoplasm Source: HPA
  3. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

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.

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi898 – 95962Missing : Cytoplasmic localization. 1 PublicationAdd
BLAST

Keywords - Diseasei

Williams-Beuren syndrome

Organism-specific databases

Orphaneti904. Williams syndrome.
PharmGKBiPA29047.

Polymorphism and mutation databases

BioMutaiGTF2IRD1.
DMDMi21263630.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 959959General transcription factor II-I repeat domain-containing protein 1PRO_0000083870Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei448 – 4481Phosphoserine3 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

MaxQBiQ9UHL9.
PaxDbiQ9UHL9.
PRIDEiQ9UHL9.

PTM databases

PhosphoSiteiQ9UHL9.

Expressioni

Tissue specificityi

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

Developmental stagei

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

Gene expression databases

BgeeiQ9UHL9.
CleanExiHS_GTF2IRD1.
ExpressionAtlasiQ9UHL9. baseline and differential.
GenevestigatoriQ9UHL9.

Organism-specific databases

HPAiHPA044254.

Interactioni

Subunit structurei

Interacts with the retinoblastoma protein (RB1) via its C-terminus.1 Publication

Protein-protein interaction databases

BioGridi114939. 12 interactions.
IntActiQ9UHL9. 2 interactions.
MINTiMINT-1209004.
STRINGi9606.ENSP00000265755.

Structurei

Secondary structure

1
959
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi128 – 14417Combined sources
Helixi154 – 1596Combined sources
Turni161 – 1633Combined sources
Beta strandi164 – 1685Combined sources
Turni178 – 1803Combined sources
Helixi183 – 19210Combined sources
Turni193 – 1953Combined sources
Beta strandi197 – 2037Combined sources
Helixi565 – 58016Combined sources
Helixi591 – 5966Combined sources
Turni598 – 6003Combined sources
Beta strandi601 – 6055Combined sources
Turni615 – 6173Combined sources
Helixi620 – 6289Combined sources
Turni629 – 6324Combined sources
Beta strandi634 – 6385Combined sources
Helixi640 – 6423Combined sources
Helixi705 – 72117Combined sources
Helixi731 – 7366Combined sources
Beta strandi738 – 7458Combined sources
Helixi755 – 7573Combined sources
Helixi760 – 76910Combined sources
Turni770 – 7723Combined sources
Beta strandi774 – 7774Combined sources
Helixi802 – 81716Combined sources
Helixi828 – 8336Combined sources
Beta strandi837 – 8426Combined sources
Beta strandi852 – 8543Combined sources
Helixi857 – 8648Combined sources
Turni865 – 8695Combined sources
Beta strandi871 – 8766Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D99NMR-A128-203[»]
2DN5NMR-A802-877[»]
2DZQNMR-A565-650[»]
2DZRNMR-A705-790[»]
ProteinModelPortaliQ9UHL9.
SMRiQ9UHL9. Positions 128-203, 351-427, 565-656, 702-790, 802-880.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UHL9.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Repeati119 – 21395GTF2I-like 1Add
BLAST
Repeati342 – 43695GTF2I-like 2Add
BLAST
Repeati556 – 65095GTF2I-like 3Add
BLAST
Repeati696 – 79095GTF2I-like 4Add
BLAST
Repeati793 – 88795GTF2I-like 5Add
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi898 – 9058Nuclear localization signalSequence Analysis

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi906 – 93025Ser-richAdd
BLAST

Domaini

The N-terminal half may have an activating activity.

Sequence similaritiesi

Belongs to the TFII-I family.PROSITE-ProRule annotation
Contains 5 GTF2I-like repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat

Phylogenomic databases

eggNOGiNOG29608.
GeneTreeiENSGT00530000063863.
HOGENOMiHOG000112829.
HOVERGENiHBG051855.
InParanoidiQ9UHL9.
KOiK03121.
OMAiDCGLHGQ.
PhylomeDBiQ9UHL9.
TreeFamiTF352524.

Family and domain databases

Gene3Di3.90.1460.10. 5 hits.
InterProiIPR004212. GTF2I.
IPR016659. TF_II-I.
[Graphical view]
PfamiPF02946. GTF2I. 5 hits.
[Graphical view]
PIRSFiPIRSF016441. TF_II-I. 1 hit.
SUPFAMiSSF117773. SSF117773. 5 hits.
PROSITEiPS51139. GTF2I. 5 hits.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UHL9-1) [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
MALLGKRCDV PTNGCGPDRW NSAFTRKDEI ITSLVSALDS MCSALSKLNA
60 70 80 90 100
EVACVAVHDE SAFVVGTEKG RMFLNARKEL QSDFLRFCRG PPWKDPEAEH
110 120 130 140 150
PKKVQRGEGG GRSLPRSSLE HGSDVYLLRK MVEEVFDVLY SEALGRASVV
160 170 180 190 200
PLPYERLLRE PGLLAVQGLP EGLAFRRPAE YDPKALMAIL EHSHRIRFKL
210 220 230 240 250
KRPLEDGGRD SKALVELNGV SLIPKGSRDC GLHGQAPKVP PQDLPPTATS
260 270 280 290 300
SSMASFLYST ALPNHAIREL KQEAPSCPLA PSDLGLSRPM PEPKATGAQD
310 320 330 340 350
FSDCCGQKPT GPGGPLIQNV HASKRILFSI VHDKSEKWDA FIKETEDINT
360 370 380 390 400
LRECVQILFN SRYAEALGLD HMVPVPYRKI ACDPEAVEIV GIPDKIPFKR
410 420 430 440 450
PCTYGVPKLK RILEERHSIH FIIKRMFDER IFTGNKFTKD TTKLEPASPP
460 470 480 490 500
EDTSAEVSRA TVLDLAGNAR SDKGSMSEDC GPGTSGELGG LRPIKIEPED
510 520 530 540 550
LDIIQVTVPD PSPTSEEMTD SMPGHLPSED SGYGMEMLTD KGLSEDARPE
560 570 580 590 600
ERPVEDSHGD VIRPLRKQVE LLFNTRYAKA IGISEPVKVP YSKFLMHPEE
610 620 630 640 650
LFVVGLPEGI SLRRPNCFGI AKLRKILEAS NSIQFVIKRP ELLTEGVKEP
660 670 680 690 700
IMDSQGTASS LGFSPPALPP ERDSGDPLVD ESLKRQGFQE NYDARLSRID
710 720 730 740 750
IANTLREQVQ DLFNKKYGEA LGIKYPVQVP YKRIKSNPGS VIIEGLPPGI
760 770 780 790 800
PFRKPCTFGS QNLERILAVA DKIKFTVTRP FQGLIPKPDE DDANRLGEKV
810 820 830 840 850
ILREQVKELF NEKYGEALGL NRPVLVPYKL IRDSPDAVEV TGLPDDIPFR
860 870 880 890 900
NPNTYDIHRL EKILKAREHV RMVIINQLQP FAEICNDAKV PAKDSSIPKR
910 920 930 940 950
KRKRVSEGNS VSSSSSSSSS SSSNPDSVAS ANQISLVQWP MYMVDYAGLN

VQLPGPLNY
Length:959
Mass (Da):106,057
Last modified:May 1, 2000 - v1
Checksum:i7DA3097879701540
GO
Isoform 2 (identifier: Q9UHL9-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     656-670: Missing.

Note: Contains a phosphoserine at position 654.1 Publication

Show »
Length:944
Mass (Da):104,677
Checksum:i57E1190182D1D33F
GO
Isoform 3 (identifier: Q9UHL9-3) [UniParc]FASTAAdd to basket

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 686.1 Publication

Show »
Length:976
Mass (Da):107,979
Checksum:i674D8406B5D6A618
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti111 – 1111G → S in AAD14687 (PubMed:9774679).Curated
Sequence conflicti111 – 1111G → S in AAD27668 (PubMed:10198167).Curated
Sequence conflicti378 – 3781R → Q in AAF21796 (PubMed:10642537).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti652 – 6521M → V.3 Publications
Corresponds to variant rs2301895 [ dbSNP | Ensembl ].
VAR_013446

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei89 – 891R → LSAAQHRAATSQLEGRVVRR VLTVASRALCPTG in isoform 3. 1 PublicationVSP_043425
Alternative sequencei656 – 67015Missing in isoform 2 and isoform 3. 4 PublicationsVSP_003873Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47613.1. [Q9UHL9-2]
CCDS5571.1. [Q9UHL9-1]
CCDS56492.1. [Q9UHL9-3]
RefSeqiNP_001186136.1. NM_001199207.1. [Q9UHL9-3]
NP_005676.3. NM_005685.3. [Q9UHL9-2]
NP_057412.1. NM_016328.2. [Q9UHL9-1]
UniGeneiHs.647056.

Genome annotation databases

EnsembliENST00000265755; ENSP00000265755; ENSG00000006704. [Q9UHL9-1]
ENST00000424337; ENSP00000408477; ENSG00000006704. [Q9UHL9-2]
ENST00000455841; ENSP00000397566; ENSG00000006704. [Q9UHL9-3]
GeneIDi9569.
KEGGihsa:9569.
UCSCiuc003uap.3. human. [Q9UHL9-2]
uc003uaq.3. human. [Q9UHL9-1]
uc010lbq.3. human. [Q9UHL9-3]

Polymorphism and mutation databases

BioMutaiGTF2IRD1.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS47613.1. [Q9UHL9-2]
CCDS5571.1. [Q9UHL9-1]
CCDS56492.1. [Q9UHL9-3]
RefSeqiNP_001186136.1. NM_001199207.1. [Q9UHL9-3]
NP_005676.3. NM_005685.3. [Q9UHL9-2]
NP_057412.1. NM_016328.2. [Q9UHL9-1]
UniGeneiHs.647056.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2D99NMR-A128-203[»]
2DN5NMR-A802-877[»]
2DZQNMR-A565-650[»]
2DZRNMR-A705-790[»]
ProteinModelPortaliQ9UHL9.
SMRiQ9UHL9. Positions 128-203, 351-427, 565-656, 702-790, 802-880.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi114939. 12 interactions.
IntActiQ9UHL9. 2 interactions.
MINTiMINT-1209004.
STRINGi9606.ENSP00000265755.

PTM databases

PhosphoSiteiQ9UHL9.

Polymorphism and mutation databases

BioMutaiGTF2IRD1.
DMDMi21263630.

Proteomic databases

MaxQBiQ9UHL9.
PaxDbiQ9UHL9.
PRIDEiQ9UHL9.

Protocols and materials databases

DNASUi9569.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000265755; ENSP00000265755; ENSG00000006704. [Q9UHL9-1]
ENST00000424337; ENSP00000408477; ENSG00000006704. [Q9UHL9-2]
ENST00000455841; ENSP00000397566; ENSG00000006704. [Q9UHL9-3]
GeneIDi9569.
KEGGihsa:9569.
UCSCiuc003uap.3. human. [Q9UHL9-2]
uc003uaq.3. human. [Q9UHL9-1]
uc010lbq.3. human. [Q9UHL9-3]

Organism-specific databases

CTDi9569.
GeneCardsiGC07P073868.
HGNCiHGNC:4661. GTF2IRD1.
HPAiHPA044254.
MIMi604318. gene.
neXtProtiNX_Q9UHL9.
Orphaneti904. Williams syndrome.
PharmGKBiPA29047.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG29608.
GeneTreeiENSGT00530000063863.
HOGENOMiHOG000112829.
HOVERGENiHBG051855.
InParanoidiQ9UHL9.
KOiK03121.
OMAiDCGLHGQ.
PhylomeDBiQ9UHL9.
TreeFamiTF352524.

Miscellaneous databases

EvolutionaryTraceiQ9UHL9.
GeneWikiiGTF2IRD1.
GenomeRNAii9569.
NextBioi35885.
PROiQ9UHL9.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UHL9.
CleanExiHS_GTF2IRD1.
ExpressionAtlasiQ9UHL9. baseline and differential.
GenevestigatoriQ9UHL9.

Family and domain databases

Gene3Di3.90.1460.10. 5 hits.
InterProiIPR004212. GTF2I.
IPR016659. TF_II-I.
[Graphical view]
PfamiPF02946. GTF2I. 5 hits.
[Graphical view]
PIRSFiPIRSF016441. TF_II-I. 1 hit.
SUPFAMiSSF117773. SSF117773. 5 hits.
PROSITEiPS51139. GTF2I. 5 hits.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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.
    , 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. 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. 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.

Entry informationi

Entry nameiGT2D1_HUMAN
AccessioniPrimary (citable) accession number: Q9UHL9
Secondary accession number(s): O95444
, Q6DSU6, Q75MX7, Q86UM3, Q8WVC4, Q9UHK8, Q9UI91
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 27, 2002
Last sequence update: May 1, 2000
Last modified: April 29, 2015
This is version 142 of the entry and version 1 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, 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.