DROME:TITIN

Species (Taxon ID)	Drosophila melanogaster (Fruit fly). (7227)
Gene Name(s)	sls (synonyms: titin (ECO:0000312 with EMBL:CAB93524.1))
Protein Name(s)	Titin D-Titin Kettin
External Links
UniProt	Q9I7U4
EMBL	AB026845 AJ238575 AJ238577 AJ271740 AJ400900 AJ400901 AJ400902 AE014296 AF045775 AF045776 AF045777 AF045778 AJ245406 AJ012279 AJ012280 AF135062 AF135167 AF241648 AF241649 BK000146 AY094749
PIR	S35341
RefSeq	NP_524676.2
UniGene	Dm.2974
ProteinModelPortal	Q9I7U4
BioGrid	68776
IntAct	Q9I7U4
MINT	MINT-1723019
MEROPS	I43.001
PaxDb	Q9I7U4
PRIDE	Q9I7U4
GeneID	44013
KEGG	dme:Dmel_CG1915
CTD	44013
FlyBase	FBgn0086906
eggNOG	NOG12793
InParanoid	Q9I7U4
OrthoDB	EOG7327MW
SignaLink	Q9I7U4
ChiTaRS	sls
GenomeRNAi	44013
NextBio	836598
Proteomes	UP000000803
Bgee	Q9I7U4
GO	GO:0000794 GO:0031674 GO:0005875 GO:0030017 GO:0005863 GO:0030018 GO:0003779 GO:0008307 GO:0040011 GO:0007498 GO:0007076 GO:0016203 GO:0007517 GO:0007520 GO:0035206 GO:0045214 GO:0007062 GO:0007519 GO:0007525 GO:0007522
Gene3D	2.60.40.10
InterPro	IPR010939 IPR003961 IPR007110 IPR013783 IPR013098 IPR003599 IPR003598 IPR001452
Pfam	PF06582 PF00041 PF07679 PF00018
SMART	SM00060 SM00409 SM00408 SM00326
SUPFAM	SSF49265 SSF50044
PROSITE	PS50853 PS50835 PS50002

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Notes	Status
part_of	GO:0030018	Z disc	PMID:9548712^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007525	somatic muscle development	PMID:9548712^[1]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007522	visceral muscle development	PMID:9548712^[1]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0045214	sarcomere organization	PMID:10629221^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0040011	locomotion	PMID:10629221^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:10669599^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:9917396^[4]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030017	sarcomere	PMID:9548712^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030017	sarcomere	PMID:10629221^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0016203	muscle attachment	PMID:10629221^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0008307	structural constituent of muscle	PMID:10629221^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
involved_in	GO:0007520	myoblast fusion	PMID:10934048^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007519	skeletal muscle tissue development	PMID:10934048^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007519	skeletal muscle tissue development	PMID:10629221^[2]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007076	mitotic chromosome condensation	PMID:11062264^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007062	sister chromatid cohesion	PMID:11062264^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:10669599^[3]	ECO:0000315	mutant phenotype evidence used in manual assertion		F	Seeded From UniProt	complete
enables	GO:0003779	actin binding	PMID:9917396^[4]	ECO:0000314	direct assay evidence used in manual assertion		F	Seeded From UniProt	complete
part_of	GO:0000794	condensed nuclear chromosome	PMID:9548712^[1]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0035206	regulation of hemocyte proliferation	PMID:20688956^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:18199432^[8]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0045214	sarcomere organization	PMID:17535853^[9]	ECO:0000316	genetic interaction evidence used in manual assertion	FB:FBgn0014863	P	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:16699917^[10]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0045214	sarcomere organization	PMID:16699917^[10]	ECO:0000314	direct assay evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:16450058^[11]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:17316686^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0005863	striated muscle myosin thick filament	PMID:17316686^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0031674	I band	PMID:17316686^[12]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:15119962^[13]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007498	mesoderm development	PMID:11486054^[14]	ECO:0000270	expression pattern evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007076	mitotic chromosome condensation	PMID:11062264^[6]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
involved_in	GO:0007520	myoblast fusion	PMID:10934048^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0030017	sarcomere	PMID:10629221^[2]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:26896675^[15]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:28732005^[16]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:26251439^[17]	ECO:0000314	direct assay evidence used in manual assertion		C	Seeded From UniProt	complete
involved_in	GO:0007517	muscle organ development	PMID:12111720^[18]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P	Seeded From UniProt	complete
part_of	GO:0005737	cytoplasm	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0963 UniProtKB-SubCell:SL-0086	C	Seeded From UniProt	complete
involved_in	GO:0007275	multicellular organism development	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0217	P	Seeded From UniProt	complete
part_of	GO:0005694	chromosome	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0158 UniProtKB-SubCell:SL-0468	C	Seeded From UniProt	complete
involved_in	GO:0051301	cell division	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0132	P	Seeded From UniProt	complete
part_of	GO:0005634	nucleus	GO_REF:0000037 GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0539 UniProtKB-SubCell:SL-0191	C	Seeded From UniProt	complete
involved_in	GO:0007049	cell cycle	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0131	P	Seeded From UniProt	complete
part_of	GO:0030018	Z disc	GO_REF:0000039	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-SubCell:SL-0314	C	Seeded From UniProt	complete
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Notes

References

See Help:References for how to manage references in GONUTS.

↑ ^1.0 ^1.1 ^1.2 ^1.3 ^1.4 Machado, C et al. (1998) Human autoantibodies reveal titin as a chromosomal protein. J. Cell Biol. 141 321-33 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 Hakeda, S et al. (2000) Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila. J. Cell Biol. 148 101-14 PubMed GONUTS page
↑ ^3.0 ^3.1 Kolmerer, B et al. (2000) Sequence and expression of the kettin gene in Drosophila melanogaster and Caenorhabditis elegans. J. Mol. Biol. 296 435-48 PubMed GONUTS page
↑ ^4.0 ^4.1 van Straaten, M et al. (1999) Association of kettin with actin in the Z-disc of insect flight muscle. J. Mol. Biol. 285 1549-62 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 Zhang, Y et al. (2000) Drosophila D-titin is required for myoblast fusion and skeletal muscle striation. J. Cell. Sci. 113 ( Pt 17) 3103-15 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 Machado, C & Andrew, DJ (2000) D-Titin: a giant protein with dual roles in chromosomes and muscles. J. Cell Biol. 151 639-52 PubMed GONUTS page
↑ Sinenko, SA et al. (2010) Genetic manipulation of AML1-ETO-induced expansion of hematopoietic precursors in a Drosophila model. Blood 116 4612-20 PubMed GONUTS page
↑ Hudson, AM et al. (2008) Mononuclear muscle cells in Drosophila ovaries revealed by GFP protein traps. Dev. Biol. 314 329-40 PubMed GONUTS page
↑ Clark, KA et al. (2007) The Drosophila muscle LIM protein, Mlp84B, cooperates with D-titin to maintain muscle structural integrity. J. Cell. Sci. 120 2066-77 PubMed GONUTS page
↑ ^10.0 ^10.1 Kreisköther, N et al. (2006) Drosophila rolling pebbles colocalises and putatively interacts with alpha-Actinin and the Sls isoform Zormin in the Z-discs of the sarcomere and with Dumbfounded/Kirre, alpha-Actinin and Zormin in the terminal Z-discs. J. Muscle Res. Cell. Motil. 27 93-106 PubMed GONUTS page
↑ Bullard, B et al. (2005) The function of elastic proteins in the oscillatory contraction of insect flight muscle. J. Muscle Res. Cell. Motil. 26 479-85 PubMed GONUTS page
↑ ^12.0 ^12.1 ^12.2 Burkart, C et al. (2007) Modular proteins from the Drosophila sallimus (sls) gene and their expression in muscles with different extensibility. J. Mol. Biol. 367 953-69 PubMed GONUTS page
↑ Ayme-Southgate, A et al. (2004) Assembly of the giant protein projectin during myofibrillogenesis in Drosophila indirect flight muscles. BMC Cell Biol. 5 17 PubMed GONUTS page
↑ Furlong, EE et al. (2001) Patterns of gene expression during Drosophila mesoderm development. Science 293 1629-33 PubMed GONUTS page
↑ Sarov, M et al. (2016) A genome-wide resource for the analysis of protein localisation in Drosophila. Elife 5 e12068 PubMed GONUTS page
↑ González-Morales, N et al. (2017) Filamin actin-binding and titin-binding fulfill distinct functions in Z-disc cohesion. PLoS Genet. 13 e1006880 PubMed GONUTS page
↑ Katzemich, A et al. (2015) Binding partners of the kinase domains in Drosophila obscurin and their effect on the structure of the flight muscle. J. Cell. Sci. 128 3386-97 PubMed GONUTS page
↑ Dworak, HA & Sink, H (2002) Myoblast fusion in Drosophila. Bioessays 24 591-601 PubMed GONUTS page

[PMID:9548712-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Machado, C et al. (1998) Human autoantibodies reveal titin as a chromosomal protein. J. Cell Biol. 141 321-33 PubMed GONUTS page

[PMID:10629221-2] 2.0 ^2.1 ^2.2 ^2.3 ^2.4 ^2.5 ^2.6 Hakeda, S et al. (2000) Requirements of Kettin, a giant muscle protein highly conserved in overall structure in evolution, for normal muscle function, viability, and flight activity of Drosophila. J. Cell Biol. 148 101-14 PubMed GONUTS page

[PMID:10669599-3] 3.0 ^3.1 Kolmerer, B et al. (2000) Sequence and expression of the kettin gene in Drosophila melanogaster and Caenorhabditis elegans. J. Mol. Biol. 296 435-48 PubMed GONUTS page

[PMID:9917396-4] 4.0 ^4.1 van Straaten, M et al. (1999) Association of kettin with actin in the Z-disc of insect flight muscle. J. Mol. Biol. 285 1549-62 PubMed GONUTS page

[PMID:10934048-5] 5.0 ^5.1 ^5.2 Zhang, Y et al. (2000) Drosophila D-titin is required for myoblast fusion and skeletal muscle striation. J. Cell. Sci. 113 ( Pt 17) 3103-15 PubMed GONUTS page

[PMID:11062264-6] 6.0 ^6.1 ^6.2 Machado, C & Andrew, DJ (2000) D-Titin: a giant protein with dual roles in chromosomes and muscles. J. Cell Biol. 151 639-52 PubMed GONUTS page

[PMID:20688956-7] Sinenko, SA et al. (2010) Genetic manipulation of AML1-ETO-induced expansion of hematopoietic precursors in a Drosophila model. Blood 116 4612-20 PubMed GONUTS page

[PMID:18199432-8] Hudson, AM et al. (2008) Mononuclear muscle cells in Drosophila ovaries revealed by GFP protein traps. Dev. Biol. 314 329-40 PubMed GONUTS page

[PMID:17535853-9] Clark, KA et al. (2007) The Drosophila muscle LIM protein, Mlp84B, cooperates with D-titin to maintain muscle structural integrity. J. Cell. Sci. 120 2066-77 PubMed GONUTS page

[PMID:16699917-10] 10.0 ^10.1 Kreisköther, N et al. (2006) Drosophila rolling pebbles colocalises and putatively interacts with alpha-Actinin and the Sls isoform Zormin in the Z-discs of the sarcomere and with Dumbfounded/Kirre, alpha-Actinin and Zormin in the terminal Z-discs. J. Muscle Res. Cell. Motil. 27 93-106 PubMed GONUTS page

[PMID:16450058-11] Bullard, B et al. (2005) The function of elastic proteins in the oscillatory contraction of insect flight muscle. J. Muscle Res. Cell. Motil. 26 479-85 PubMed GONUTS page

[PMID:17316686-12] 12.0 ^12.1 ^12.2 Burkart, C et al. (2007) Modular proteins from the Drosophila sallimus (sls) gene and their expression in muscles with different extensibility. J. Mol. Biol. 367 953-69 PubMed GONUTS page

[PMID:15119962-13] Ayme-Southgate, A et al. (2004) Assembly of the giant protein projectin during myofibrillogenesis in Drosophila indirect flight muscles. BMC Cell Biol. 5 17 PubMed GONUTS page

[PMID:11486054-14] Furlong, EE et al. (2001) Patterns of gene expression during Drosophila mesoderm development. Science 293 1629-33 PubMed GONUTS page

[PMID:26896675-15] Sarov, M et al. (2016) A genome-wide resource for the analysis of protein localisation in Drosophila. Elife 5 e12068 PubMed GONUTS page

[PMID:28732005-16] González-Morales, N et al. (2017) Filamin actin-binding and titin-binding fulfill distinct functions in Z-disc cohesion. PLoS Genet. 13 e1006880 PubMed GONUTS page

[PMID:26251439-17] Katzemich, A et al. (2015) Binding partners of the kinase domains in Drosophila obscurin and their effect on the structure of the flight muscle. J. Cell. Sci. 128 3386-97 PubMed GONUTS page

[PMID:12111720-18] Dworak, HA & Sink, H (2002) Myoblast fusion in Drosophila. Bioessays 24 591-601 PubMed GONUTS page

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DROME:TITIN

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