Reviewed, UniProtKB/Swiss-Prot P10627 (TWIST_DROME)

Names and origin

Protein names

Recommended name:
    Protein twist

Gene names

Name:	twi
ORF Names:	CG2956

Organism

Drosophila melanogaster (Fruit fly) [Complete proteome]

Taxonomic identifier

7227 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Arthropoda › Hexapoda › Insecta › Pterygota › Neoptera › Endopterygota › Diptera › Brachycera › Muscomorpha › Ephydroidea › Drosophilidae › Drosophila › Sophophora

Protein attributes

Sequence length	490 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Involved in the establishment and dorsoventral patterning of germ layers in the embryo. Ref.1
Subunit structure	Efficient DNA binding requires dimerization with another bHLH protein. Homodimer.
Subcellular location	Nucleus. Ref.1
Tissue specificity	Expressed in embryonic abdomen; a single cell ventrally, pairs of cells laterally and three cells dorsally in each hemisegment. In the thorax, there are patches of cells associated with the imaginal disks. During larval development, cells proliferate and, in the abdomen, they form ventral, lateral and dorsal clusters, which are the precursors of the adult abdominal muscles. In the thorax, they form populations of cells in the imaginal disks that correspond to the adepithelial cells. Ref.5
Developmental stage	Expressed throughout development.
Disruption phenotype	Embryos fail to form the ventral furrow at gastrulation and lack mesoderm and all internal organs. Ref.1
Sequence similarities	Contains 1 basic helix-loop-helix (bHLH) domain.

Ontologies

Keywords
Biological process	Differentiation Transcription Transcription regulation
Cellular component	Nucleus
Ligand	DNA-binding
Molecular function	Developmental protein
PTM	Phosphoprotein
Technical term	Complete proteome
Gene Ontology (GO)
Biological process	Malpighian tubule morphogenesis Inferred from mutant phenotype. Source: FlyBase dorsal/ventral axis specification Traceable author statement. Source: FlyBase ectoderm and mesoderm interaction Non-traceable author statement. Source: FlyBase heart development Traceable author statement. Source: FlyBase mesodermal cell fate determination Traceable author statement. Source: FlyBase mesodermal cell fate specification Traceable author statement. Source: FlyBase muscle fiber development Inferred from mutant phenotype. Source: FlyBase positive regulation of transcription from RNA polymerase II promoter Non-traceable author statement. Source: FlyBase regulation of striated muscle development Inferred from mutant phenotype. Source: UniProtKB salivary gland morphogenesis Inferred from mutant phenotype. Source: FlyBase transcription Inferred from electronic annotation. Source: UniProtKB-KW ventral furrow formation Ref.1 Inferred from mutant phenotype. Source: UniProtKB
Cellular component	nucleus Ref.1 Inferred from direct assay. Source: UniProtKB
Molecular function	DNA binding Inferred from direct assay. Source: UniProtKB protein heterodimerization activity Inferred from physical interaction. Source: UniProtKB protein homodimerization activity Inferred from physical interaction. Source: UniProtKB specific transcriptional repressor activity Inferred from mutant phenotype. Source: FlyBase transcription activator activity Non-traceable author statement. Source: FlyBase
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 490	490	Protein twist		PRO_0000127478
Regions
	Domain	375 – 414	40	Helix-loop-helix motif
	DNA binding	362 – 374	13	Basic motif
	Compositional bias	48 – 70	23	Gln/His-rich
	Compositional bias	178 – 189	12	Gln-rich
	Compositional bias	244 – 263	20	Gln-rich
Amino acid modifications
	Modified residue	325	1	Phosphoserine Ref.6
	Modified residue	328	1	Phosphoserine Ref.6
Experimental info
	Sequence conflict	44	1	Q → H in CAA31024. Ref.1
	Sequence conflict	44	1	Q → H in CAA32707. Ref.1
	Sequence conflict	112	1	T → A in CAA31024. Ref.1
	Sequence conflict	112	1	T → A in CAA32707. Ref.1
	Sequence conflict	112	1	T → A in AAL68080. Ref.4
	Sequence conflict	251	1	L → Q in CAA31024. Ref.1
	Sequence conflict	251	1	L → Q in CAA32707. Ref.1
	Sequence conflict	251	1	Missing in AAL68080. Ref.4
	Sequence conflict	251	1	Missing in AAM49823. Ref.4
	Sequence conflict	453	1	A → G in CAA31024. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	P10627-1 [UniParc]. Last modified February 21, 2001. Version 2. Checksum: AEB0D4D4EEE97DB7	FASTA	490	54,422
	10 20 30 40 50 60 MMSARSVSPK VLLDISYKPT LPNIMELQNN VIKLIQVEQQ AYMQSGYQLQ HQQQHLHSHQ 70 80 90 100 110 120 HHQQHHQQQH AQYAPLPSEY AAYGITELED TDYNIPSNEV LSTSSNQSAQ STSLELNNNN 130 140 150 160 170 180 TSSNTNSSGN NPSGFDGQAS SGSSWNEHGK RARSSGDYDC QTGGSLVMQP EHKKLIHQQQ 190 200 210 220 230 240 QQQQQHQQQI YVDYLPTTVD EVASAQSCPG VQSTCTSPQS HFDFPDEELP EHKAQVFLPL 250 260 270 280 290 300 YNNQQQQSQQ LQQQQPHQQS HAQMHFQNAY RQSFEGYEPA NSLNGSAYSS SDRDDMEYAR 310 320 330 340 350 360 HNALSSVSDL NGGVMSPACL ADDGSAGSLL DGSDAGGKAF RKPRRRLKRK PSKTEETDEF 370 380 390 400 410 420 SNQRVMANVR ERQRTQSLND AFKSLQQIIP TLPSDKLSKI QTLKLATRYI DFLCRMLSSS 430 440 450 460 470 480 DISLLKALEA QGSPSAYGSA SSLLSAAANG AEADLKCLRK ANGAPIIPPE KLSYLFGVWR 490 MEGDAQHQKA

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Sequence of the twist gene and nuclear localization of its protein in endomesodermal cells of early Drosophila embryos." Thisse B., Stoetzel C., Gorostiza-Thisse C., Perrin-Schmitt F. EMBO J. 7:2175-2183(1988) [PubMed: 3416836] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA / MRNA], FUNCTION, SUBCELLULAR LOCATION, DISRUPTION PHENOTYPE. Strain: Oregon-R.
[2]	"The genome sequence of Drosophila melanogaster." Adams M.D., Celniker S.E., Holt R.A., Evans C.A., Gocayne J.D., Amanatides P.G., Scherer S.E., Li P.W., Hoskins R.A., Galle R.F., George R.A., Lewis S.E., Richards S., Ashburner M., Henderson S.N., Sutton G.G., Wortman J.R., Yandell M.D. , Zhang Q., Chen L.X., Brandon R.C., Rogers Y.-H.C., Blazej R.G., Champe M., Pfeiffer B.D., Wan K.H., Doyle C., Baxter E.G., Helt G., Nelson C.R., Miklos G.L.G., Abril J.F., Agbayani A., An H.-J., Andrews-Pfannkoch C., Baldwin D., Ballew R.M., Basu A., Baxendale J., Bayraktaroglu L., Beasley E.M., Beeson K.Y., Benos P.V., Berman B.P., Bhandari D., Bolshakov S., Borkova D., Botchan M.R., Bouck J., Brokstein P., Brottier P., Burtis K.C., Busam D.A., Butler H., Cadieu E., Center A., Chandra I., Cherry J.M., Cawley S., Dahlke C., Davenport L.B., Davies P., de Pablos B., Delcher A., Deng Z., Mays A.D., Dew I., Dietz S.M., Dodson K., Doup L.E., Downes M., Dugan-Rocha S., Dunkov B.C., Dunn P., Durbin K.J., Evangelista C.C., Ferraz C., Ferriera S., Fleischmann W., Fosler C., Gabrielian A.E., Garg N.S., Gelbart W.M., Glasser K., Glodek A., Gong F., Gorrell J.H., Gu Z., Guan P., Harris M., Harris N.L., Harvey D.A., Heiman T.J., Hernandez J.R., Houck J., Hostin D., Houston K.A., Howland T.J., Wei M.-H., Ibegwam C., Jalali M., Kalush F., Karpen G.H., Ke Z., Kennison J.A., Ketchum K.A., Kimmel B.E., Kodira C.D., Kraft C.L., Kravitz S., Kulp D., Lai Z., Lasko P., Lei Y., Levitsky A.A., Li J.H., Li Z., Liang Y., Lin X., Liu X., Mattei B., McIntosh T.C., McLeod M.P., McPherson D., Merkulov G., Milshina N.V., Mobarry C., Morris J., Moshrefi A., Mount S.M., Moy M., Murphy B., Murphy L., Muzny D.M., Nelson D.L., Nelson D.R., Nelson K.A., Nixon K., Nusskern D.R., Pacleb J.M., Palazzolo M., Pittman G.S., Pan S., Pollard J., Puri V., Reese M.G., Reinert K., Remington K., Saunders R.D.C., Scheeler F., Shen H., Shue B.C., Siden-Kiamos I., Simpson M., Skupski M.P., Smith T.J., Spier E., Spradling A.C., Stapleton M., Strong R., Sun E., Svirskas R., Tector C., Turner R., Venter E., Wang A.H., Wang X., Wang Z.-Y., Wassarman D.A., Weinstock G.M., Weissenbach J., Williams S.M., Woodage T., Worley K.C., Wu D., Yang S., Yao Q.A., Ye J., Yeh R.-F., Zaveri J.S., Zhan M., Zhang G., Zhao Q., Zheng L., Zheng X.H., Zhong F.N., Zhong W., Zhou X., Zhu S.C., Zhu X., Smith H.O., Gibbs R.A., Myers E.W., Rubin G.M., Venter J.C. Science 287:2185-2195(2000) [PubMed: 10731132] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. Strain: Berkeley.
[3]	"Annotation of the Drosophila melanogaster euchromatic genome: a systematic review." Misra S., Crosby M.A., Mungall C.J., Matthews B.B., Campbell K.S., Hradecky P., Huang Y., Kaminker J.S., Millburn G.H., Prochnik S.E., Smith C.D., Tupy J.L., Whitfield E.J., Bayraktaroglu L., Berman B.P., Bettencourt B.R., Celniker S.E., de Grey A.D.N.J. , Drysdale R.A., Harris N.L., Richter J., Russo S., Schroeder A.J., Shu S.Q., Stapleton M., Yamada C., Ashburner M., Gelbart W.M., Rubin G.M., Lewis S.E. Genome Biol. 3:RESEARCH0083.1-RESEARCH0083.22(2002) [PubMed: 12537572] [Abstract] Cited for: GENOME REANNOTATION.
[4]	"A Drosophila full-length cDNA resource." Stapleton M., Carlson J.W., Brokstein P., Yu C., Champe M., George R.A., Guarin H., Kronmiller B., Pacleb J.M., Park S., Wan K.H., Rubin G.M., Celniker S.E. Genome Biol. 3:RESEARCH0080.1-RESEARCH0080.8(2002) [PubMed: 12537569] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Strain: Berkeley. Tissue: Testis.
[5]	"Cells with persistent twist expression are the embryonic precursors of adult muscles in Drosophila." Bate M., Rushton E., Currie D.A. Development 113:79-89(1991) [PubMed: 1765010] [Abstract] Cited for: TISSUE SPECIFICITY.
[6]	"Phosphoproteome analysis of Drosophila melanogaster embryos." Zhai B., Villen J., Beausoleil S.A., Mintseris J., Gygi S.P. J. Proteome Res. 7:1675-1682(2008) [PubMed: 18327897] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-325 AND SER-328, MASS SPECTROMETRY. Tissue: Embryo.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBLGenBankDDBJ	X12506 Genomic DNA. Translation: CAA31024.1. X14569 mRNA. Translation: CAA32707.1. AE013599 Genomic DNA. Translation: AAF46941.1. AY075213 mRNA. Translation: AAL68080.1. AY118454 mRNA. Translation: AAM49823.1.
PIR	S00995.
RefSeq	NP_001033967.1. NP_523816.2.
UniGene	Dm.5605
3D structure databases
HSSP	HSSP built from PDB template 1NLW based on UniProtKB P25912.
ModBase	Search...
Protein-protein interaction databases
IntAct	P10627. 3 interactions.
Proteomic databases
PRIDE	P10627.
Genome annotation databases
Ensembl	FBgn0003900. Drosophila melanogaster. [Contig view]
GeneID	37655.
KEGG	dme:Dmel_CG2956.
Organism-specific databases
FlyBase	FBgn0003900. twi.
Phylogenomic databases
HOGENOM	P10627.
OMA	P10627. TELEDTD.
Enzyme and pathway databases
BioCyc	DMEL-XXX-02:DMEL-XXX-02-006137-MON.
Gene expression databases
ArrayExpress	P10627.
GermOnline	CG2956. Drosophila melanogaster.
Family and domain databases
InterPro	IPR001092. HLH_basic. IPR011598. HLH_DNA_bd. IPR015789. Twist. [Graphical view]
Gene3D	G3DSA:4.10.280.10. HLH_DNA_bd. 1 hit.
PANTHER	PTHR23349:SF6. Twist. 1 hit.
Pfam	PF00010. HLH. 1 hit. [Graphical view]
SMART	SM00353. HLH. 1 hit. [Graphical view]
PROSITE	PS50888. HLH. 1 hit. [Graphical view]
ProtoNet	Search...
Other Resources
NextBio	804759.

Entry information

Entry name

TWIST_DROME

Accession

Primary (citable) accession number: P10627
Secondary accession number(s): Q8MT07, Q8T8Y9, Q9W1W1

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 1, 1989
Last sequence update:	February 21, 2001
Last modified:	June 16, 2009
This is version 95 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

Drosophila annotation project