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Protein

Twist-related protein 1

Gene

TWIST1

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

Functioni

Acts as a transcriptional regulator. Inhibits myogenesis by sequestrating E proteins, inhibiting trans-activation by MEF2, and inhibiting DNA-binding by MYOD1 through physical interaction. This interaction probably involves the basic domains of both proteins. Also represses expression of proinflammatory cytokines such as TNFA and IL1B. Regulates cranial suture patterning and fusion. Activates transcription as a heterodimer with E proteins. Regulates gene expression differentially, depending on dimer composition. Homodimers induce expression of FGFR2 and POSTN while heterodimers repress FGFR2 and POSTN expression and induce THBS1 expression. Heterodimerization is also required for osteoblast differentiation. Represses the activity of the circadian transcriptional activator: NPAS2-ARNTL/BMAL1 heterodimer (By similarity).By similarity

GO - Molecular functioni

  • bHLH transcription factor binding Source: BHF-UCL
  • E-box binding Source: BHF-UCL
  • sequence-specific DNA binding RNA polymerase II transcription factor activity Source: BHF-UCL
  • transcription factor binding Source: UniProtKB

GO - Biological processi

  • aortic valve morphogenesis Source: BHF-UCL
  • cardiac neural crest cell migration involved in outflow tract morphogenesis Source: Ensembl
  • cell proliferation involved in heart valve development Source: BHF-UCL
  • cellular response to growth factor stimulus Source: Ensembl
  • cellular response to hypoxia Source: BHF-UCL
  • cranial suture morphogenesis Source: BHF-UCL
  • embryonic camera-type eye formation Source: BHF-UCL
  • embryonic cranial skeleton morphogenesis Source: BHF-UCL
  • embryonic digit morphogenesis Source: BHF-UCL
  • embryonic forelimb morphogenesis Source: Ensembl
  • embryonic hindlimb morphogenesis Source: Ensembl
  • endocardial cushion morphogenesis Source: Ensembl
  • eyelid development in camera-type eye Source: BHF-UCL
  • in utero embryonic development Source: Ensembl
  • mitral valve morphogenesis Source: Ensembl
  • muscle organ development Source: UniProtKB-KW
  • negative regulation of apoptotic process Source: Ensembl
  • negative regulation of cellular senescence Source: BHF-UCL
  • negative regulation of DNA damage response, signal transduction by p53 class mediator Source: BHF-UCL
  • negative regulation of double-strand break repair Source: BHF-UCL
  • negative regulation of histone acetylation Source: Ensembl
  • negative regulation of histone phosphorylation Source: BHF-UCL
  • negative regulation of osteoblast differentiation Source: BHF-UCL
  • negative regulation of oxidative phosphorylation uncoupler activity Source: Ensembl
  • negative regulation of peroxisome proliferator activated receptor signaling pathway Source: Ensembl
  • negative regulation of phosphatidylinositol 3-kinase signaling Source: BHF-UCL
  • negative regulation of sequence-specific DNA binding transcription factor activity Source: Ensembl
  • negative regulation of skeletal muscle tissue development Source: Ensembl
  • negative regulation of transcription, DNA-templated Source: UniProtKB
  • negative regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • negative regulation of tumor necrosis factor production Source: Ensembl
  • neural tube closure Source: Ensembl
  • neuron migration Source: Ensembl
  • odontogenesis Source: Ensembl
  • ossification Source: BHF-UCL
  • osteoblast differentiation Source: Ensembl
  • outer ear morphogenesis Source: BHF-UCL
  • palate development Source: Ensembl
  • positive regulation of angiogenesis Source: BHF-UCL
  • positive regulation of cell motility Source: BHF-UCL
  • positive regulation of DNA-templated transcription, initiation Source: CACAO
  • positive regulation of endocardial cushion to mesenchymal transition involved in heart valve formation Source: Ensembl
  • positive regulation of epithelial cell proliferation Source: Ensembl
  • positive regulation of epithelial to mesenchymal transition Source: BHF-UCL
  • positive regulation of fatty acid beta-oxidation Source: BHF-UCL
  • positive regulation of gene expression Source: BHF-UCL
  • positive regulation of interleukin-6 secretion Source: BHF-UCL
  • positive regulation of monocyte chemotactic protein-1 production Source: BHF-UCL
  • positive regulation of transcription from RNA polymerase II promoter Source: BHF-UCL
  • positive regulation of transcription regulatory region DNA binding Source: BHF-UCL
  • positive regulation of tumor necrosis factor production Source: BHF-UCL
  • regulation of bone mineralization Source: BHF-UCL
  • rhythmic process Source: UniProtKB-KW
  • transcription, DNA-templated Source: UniProtKB-KW
Complete GO annotation...

Keywords - Molecular functioni

Activator, Developmental protein, Repressor

Keywords - Biological processi

Biological rhythms, Differentiation, Myogenesis, Transcription, Transcription regulation

Keywords - Ligandi

DNA-binding

Enzyme and pathway databases

SignaLinkiQ15672.

Names & Taxonomyi

Protein namesi
Recommended name:
Twist-related protein 1
Alternative name(s):
Class A basic helix-loop-helix protein 38
Short name:
bHLHa38
H-twist
Gene namesi
Name:TWIST1
Synonyms:BHLHA38, TWIST
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 7

Organism-specific databases

HGNCiHGNC:12428. TWIST1.

Subcellular locationi

GO - Cellular componenti

  • nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Involvement in diseasei

Saethre-Chotzen syndrome (SCS)3 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA craniosynostosis syndrome characterized by coronal synostosis, brachycephaly, low frontal hairline, facial asymmetry, hypertelorism, broad halluces, and clinodactyly.

See also OMIM:101400
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti119 – 1191Q → P in SCS. 1 Publication
VAR_004495
Natural varianti131 – 1311L → P in SCS. 1 Publication
VAR_004496
Natural varianti135 – 1351I → IAALRKII in SCS.
VAR_004497
Natural varianti139 – 1391P → PKIIPTLP in SCS.
VAR_004498
Natural varianti156 – 1561I → V in SCS; variant form with features overlapping Baller-Gerold syndrome. 1 Publication
VAR_015219
Robinow-Sorauf syndrome (RSS)

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionAn autosomal dominant syndrome characterized by craniosynostosis, asymmetry of orbits, flat face, hypertelorism, a thin, long, and pointed nose, shallow orbits, strabismus, and broad great toes with a duplication of the distal phalanx. RSS is clinically similar to Saethre-Chotzen syndrome, with the most characteristic additional feature in Robinow-Sorauf syndrome being a bifid or partially duplicated hallux.

See also OMIM:180750
Craniosynostosis 1 (CRS1)1 Publication

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionA primary abnormality of skull growth involving premature fusion of one or more cranial sutures. The growth velocity of the skull often cannot match that of the developing brain resulting in an abnormal head shape and, in some cases, increased intracranial pressure, which must be treated promptly to avoid permanent neurodevelopmental disability.

See also OMIM:123100
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti186 – 1861A → T in CRS1. 1 Publication
VAR_034985
Natural varianti188 – 1881S → L in CRS1. 1 Publication
VAR_034986

Keywords - Diseasei

Craniosynostosis, Disease mutation

Organism-specific databases

MIMi101400. phenotype.
123100. phenotype.
180750. phenotype.
Orphaneti35099. Isolated brachycephaly.
35093. Isolated scaphocephaly.
794. Saethre-Chotzen syndrome.
PharmGKBiPA37088.

Polymorphism and mutation databases

BioMutaiTWIST1.
DMDMi2498009.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 202202Twist-related protein 1PRO_0000127483Add
BLAST

Proteomic databases

PaxDbiQ15672.
PRIDEiQ15672.

PTM databases

PhosphoSiteiQ15672.

Expressioni

Tissue specificityi

Subset of mesodermal cells.

Gene expression databases

BgeeiQ15672.
CleanExiHS_TWIST1.
ExpressionAtlasiQ15672. baseline and differential.
GenevisibleiQ15672. HS.

Interactioni

Subunit structurei

Efficient DNA binding requires dimerization with another bHLH protein. Homodimer or heterodimer with E proteins such as TCF3. ID1 binds preferentially to TCF3 but does not interact efficiently with TWIST1 so ID1 levels control the amount of TCF3 available to dimerize with TWIST1 and thus determine the type of dimer formed (By similarity).By similarity

Binary interactionsi

WithEntry#Exp.IntActNotes
BRD4O608857EBI-1797287,EBI-723869
BRD4O60885-19EBI-1797287,EBI-9345088
ETS2P150362EBI-1797287,EBI-1646991
KAT2BQ928312EBI-1797287,EBI-477430
KAT5Q929932EBI-1797287,EBI-399080
SETD8Q9NQR15EBI-1797287,EBI-1268946
TP53P046379EBI-1797287,EBI-366083

Protein-protein interaction databases

BioGridi113142. 27 interactions.
DIPiDIP-45974N.
IntActiQ15672. 16 interactions.
MINTiMINT-8309513.
STRINGi9606.ENSP00000242261.

Structurei

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MJVNMR-A68-79[»]
ProteinModelPortaliQ15672.
SMRiQ15672. Positions 109-167.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini108 – 15952bHLHPROSITE-ProRule annotationAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni161 – 19131Sufficient for transactivation activityBy similarityAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi80 – 9819Gly-richAdd
BLAST

Sequence similaritiesi

Contains 1 bHLH (basic helix-loop-helix) domain.PROSITE-ProRule annotation

Phylogenomic databases

eggNOGiNOG258515.
GeneTreeiENSGT00760000119097.
HOGENOMiHOG000261629.
InParanoidiQ15672.
KOiK09069.
OMAiDRQPKRC.
PhylomeDBiQ15672.
TreeFamiTF315153.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q15672-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MMQDVSSSPV SPADDSLSNS EEEPDRQQPP SGKRGGRKRR SSRRSAGGGA
60 70 80 90 100
GPGGAAGGGV GGGDEPGSPA QGKRGKKSAG CGGGGGAGGG GGSSSGGGSP
110 120 130 140 150
QSYEELQTQR VMANVRERQR TQSLNEAFAA LRKIIPTLPS DKLSKIQTLK
160 170 180 190 200
LAARYIDFLY QVLQSDELDS KMASCSYVAH ERLSYAFSVW RMEGAWSMSA

SH
Length:202
Mass (Da):20,954
Last modified:November 1, 1997 - v1
Checksum:i9394E4351BA1D081
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti32 – 321G → A in CAA67664 (PubMed:8995765).Curated
Sequence conflicti36 – 361G → A in CAA67664 (PubMed:8995765).Curated
Sequence conflicti41 – 411S → T in CAA62850 (PubMed:9073070).Curated
Sequence conflicti41 – 411S → T in CAA71821 (PubMed:9215678).Curated
Sequence conflicti45 – 451S → T in CAA62850 (PubMed:9073070).Curated
Sequence conflicti45 – 451S → T in CAA71821 (PubMed:9215678).Curated
Sequence conflicti56 – 561Missing in CAA62850 (PubMed:9073070).Curated
Sequence conflicti56 – 561Missing in CAA71821 (PubMed:9215678).Curated
Sequence conflicti59 – 591G → A in CAA67664 (PubMed:8995765).Curated
Sequence conflicti92 – 921G → GGGGG in CAA67664 (PubMed:8995765).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti31 – 311S → G.
Corresponds to variant rs1800126 [ dbSNP | Ensembl ].
VAR_014821
Natural varianti84 – 841G → S.
Corresponds to variant rs2234705 [ dbSNP | Ensembl ].
VAR_014822
Natural varianti119 – 1191Q → P in SCS. 1 Publication
VAR_004495
Natural varianti131 – 1311L → P in SCS. 1 Publication
VAR_004496
Natural varianti135 – 1351I → IAALRKII in SCS.
VAR_004497
Natural varianti139 – 1391P → PKIIPTLP in SCS.
VAR_004498
Natural varianti156 – 1561I → V in SCS; variant form with features overlapping Baller-Gerold syndrome. 1 Publication
VAR_015219
Natural varianti186 – 1861A → T in CRS1. 1 Publication
VAR_034985
Natural varianti188 – 1881S → L in CRS1. 1 Publication
VAR_034986

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91662 Genomic DNA. Translation: CAA62850.1.
X99268 mRNA. Translation: CAA67664.1.
U80998 Genomic DNA. Translation: AAC50930.1.
Y10871 Genomic DNA. Translation: CAA71821.1.
AC003986 Genomic DNA. Translation: AAC60381.2.
CH236948 Genomic DNA. Translation: EAL24279.1.
BC036704 mRNA. Translation: AAH36704.1.
CCDSiCCDS5367.1.
PIRiG01204.
RefSeqiNP_000465.1. NM_000474.3.
XP_011513798.1. XM_011515496.1.
UniGeneiHs.644998.
Hs.66744.

Genome annotation databases

EnsembliENST00000242261; ENSP00000242261; ENSG00000122691.
GeneIDi7291.
KEGGihsa:7291.
UCSCiuc003sum.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Web resourcesi

Atlas of Genetics and Cytogenetics in Oncology and Haematology

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X91662 Genomic DNA. Translation: CAA62850.1.
X99268 mRNA. Translation: CAA67664.1.
U80998 Genomic DNA. Translation: AAC50930.1.
Y10871 Genomic DNA. Translation: CAA71821.1.
AC003986 Genomic DNA. Translation: AAC60381.2.
CH236948 Genomic DNA. Translation: EAL24279.1.
BC036704 mRNA. Translation: AAH36704.1.
CCDSiCCDS5367.1.
PIRiG01204.
RefSeqiNP_000465.1. NM_000474.3.
XP_011513798.1. XM_011515496.1.
UniGeneiHs.644998.
Hs.66744.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2MJVNMR-A68-79[»]
ProteinModelPortaliQ15672.
SMRiQ15672. Positions 109-167.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi113142. 27 interactions.
DIPiDIP-45974N.
IntActiQ15672. 16 interactions.
MINTiMINT-8309513.
STRINGi9606.ENSP00000242261.

PTM databases

PhosphoSiteiQ15672.

Polymorphism and mutation databases

BioMutaiTWIST1.
DMDMi2498009.

Proteomic databases

PaxDbiQ15672.
PRIDEiQ15672.

Protocols and materials databases

DNASUi7291.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000242261; ENSP00000242261; ENSG00000122691.
GeneIDi7291.
KEGGihsa:7291.
UCSCiuc003sum.3. human.

Organism-specific databases

CTDi7291.
GeneCardsiGC07M019121.
GeneReviewsiTWIST1.
HGNCiHGNC:12428. TWIST1.
MIMi101400. phenotype.
123100. phenotype.
180750. phenotype.
601622. gene.
neXtProtiNX_Q15672.
Orphaneti35099. Isolated brachycephaly.
35093. Isolated scaphocephaly.
794. Saethre-Chotzen syndrome.
PharmGKBiPA37088.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiNOG258515.
GeneTreeiENSGT00760000119097.
HOGENOMiHOG000261629.
InParanoidiQ15672.
KOiK09069.
OMAiDRQPKRC.
PhylomeDBiQ15672.
TreeFamiTF315153.

Enzyme and pathway databases

SignaLinkiQ15672.

Miscellaneous databases

ChiTaRSiTWIST1. human.
GeneWikiiTwist_transcription_factor.
GenomeRNAii7291.
NextBioi28507.
PROiQ15672.
SOURCEiSearch...

Gene expression databases

BgeeiQ15672.
CleanExiHS_TWIST1.
ExpressionAtlasiQ15672. baseline and differential.
GenevisibleiQ15672. HS.

Family and domain databases

Gene3Di4.10.280.10. 1 hit.
InterProiIPR011598. bHLH_dom.
[Graphical view]
PfamiPF00010. HLH. 1 hit.
[Graphical view]
SMARTiSM00353. HLH. 1 hit.
[Graphical view]
SUPFAMiSSF47459. SSF47459. 1 hit.
PROSITEiPS50888. BHLH. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning of the human twist gene: its expression is retained in adult mesodermally-derived tissues."
    Wang S.M., Coljee V.W., Pignolo R.J., Rotenberg M.O., Cristofalo V.J., Sierra F.
    Gene 187:83-92(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
    Tissue: Lung.
  2. "The human H-twist gene is located at 7p21 and encodes a B-HLH protein that is 96% similar to its murine M-twist counterpart."
    Bourgeois P., Stoetzel C., Bolcato-Bellemin A.-L., Mattei M.-G., Perrin-Schmitt F.
    Mamm. Genome 7:915-917(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
    Tissue: Placenta.
  3. "Mutations in TWIST, a basic helix-loop-helix transcription factor, in Saethre-Chotzen syndrome."
    Howard T.D., Paznekas W.A., Green E.D., Chiang L.C., Ma N., Ortiz de Luna R.I., Delgado C.G., Gonzalez-Ramos M., Kline A.D., Jabs E.W.
    Nat. Genet. 15:36-41(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS SCS PRO-119; ALA-ALA-LEU-ARG-LYS-ILE-ILE-135 INS AND LYS-ILE-ILE-PRO-THR-LEU-PRO-139 INS.
  4. "Translocation breakpoint maps 5 kb 3-prime from TWIST in a patient affected with Saethre-Chotzen syndrome."
    Krebs I., Weis I., Hudler M., Rommens J.M., Roth H., Scherer S.W., Tsui L.-C., Fuchtbauer E.-M., Grzeschik K.-H., Tsuji K., Kunz J.
    Hum. Mol. Genet. 6:1079-1086(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
  5. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  7. "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].
    Tissue: Brain.
  8. "Twist regulates cytokine gene expression through a negative feedback loop that represses NF-kappaB activity."
    Sosic D., Richardson J.A., Yu K., Ornitz D.M., Olson E.N.
    Cell 112:169-180(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  9. Cited for: VARIANTS SCS PRO-131 AND LYS-ILE-ILE-PRO-THR-LEU-PRO-139 INS.
  10. Cited for: VARIANT SCS VAL-156.
  11. Cited for: VARIANTS CRS1 THR-186 AND LEU-188.

Entry informationi

Entry nameiTWST1_HUMAN
AccessioniPrimary (citable) accession number: Q15672
Secondary accession number(s): A4D128, Q92487, Q99804
Entry historyi
Integrated into UniProtKB/Swiss-Prot: November 1, 1997
Last sequence update: November 1, 1997
Last modified: July 22, 2015
This is version 162 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.