HUMAN:TITIN

Species (Taxon ID)	Homo sapiens (Human). (9606)
Gene Name(s)	TTN
Protein Name(s)	Titin Connectin Rhabdomyosarcoma antigen MU-RMS-40.14
External Links
UniProt	Q8WZ42
EMBL	X90568 X90569 AJ277892 AJ277893 AJ277892 AJ277892 AJ277892 AC009948 AC010680 FJ695199 AC023270 BC013396 BC058824 BC070170 BC107797 X98114 X98115 X83270 AF058332 AF058332 AF525413 DQ248309 X64698 X64699 X64697 X69490 AL713647
CCDS	CCDS33337.1 CCDS54421.1 CCDS54422.1 CCDS54423.1 CCDS54424.1 CCDS59435.1 CCDS74610.1
PIR	I38344 I38346
RefSeq	NP_001243779.1 NP_003310.4 NP_596869.4 NP_596870.2 NP_597676.3
UniGene	Hs.134602
PDB	1BPV 1G1C 1NCT 1NCU 1TIT 1TIU 1TKI 1TNM 1TNN 1WAA 1YA5 2A38 2BK8 2F8V 2ILL 2J8H 2J8O 2NZI 2RQ8 2WP3 2WWK 2WWM 2Y9R 3B43 3KNB 3LCY 3LPW 3PUC 3Q5O 3QP3 4C4K 4JNW
PDBsum	1BPV 1G1C 1NCT 1NCU 1TIT 1TIU 1TKI 1TNM 1TNN 1WAA 1YA5 2A38 2BK8 2F8V 2ILL 2J8H 2J8O 2NZI 2RQ8 2WP3 2WWK 2WWM 2Y9R 3B43 3KNB 3LCY 3LPW 3PUC 3Q5O 3QP3 4C4K 4JNW
DisProt	DP00072
ProteinModelPortal	Q8WZ42
BioGrid	113124
DIP	DIP-33449N
IntAct	Q8WZ42
MINT	MINT-2881875
MEROPS	I43.001
PhosphoSite	Q8WZ42
MaxQB	Q8WZ42
PRIDE	Q8WZ42
Ensembl	ENST00000342992 ENST00000359218 ENST00000360870 ENST00000436599 ENST00000460472 ENST00000591111 ENST00000615779
GeneID	7273
KEGG	hsa:7273
UCSC	uc002unb.3 uc021vsy.2 uc021vsz.2 uc021vta.2 uc021vtb.2 uc031rqd.1
CTD	7273
GeneCards	GC02M179355
GeneReviews	TTN
H-InvDB	HIX0030529 HIX0161887
HGNC	HGNC:12403
HPA	CAB022682 HPA007042
MIM	188840 600334 603689 604145 608807 611705 613765
neXtProt	NX_Q8WZ42
Orphanet	178148 169186 140922 324604 289377 293899 293888 293910 154 155 178464 609
PharmGKB	PA37067
GeneTree	ENSGT00760000118877
HOGENOM	HOG000203078
HOVERGEN	HBG080473
InParanoid	Q8WZ42
KO	K12567
OMA	WFHNNRP
OrthoDB	EOG7N8ZTK
TreeFam	TF316477
Reactome	REACT_16969
SignaLink	Q8WZ42
ChiTaRS	TTN
EvolutionaryTrace	Q8WZ42
GeneWiki	Titin
GenomeRNAi	7273
NextBio	28431
PRO	PR:Q8WZ42
Proteomes	UP000005640
Bgee	Q8WZ42
ExpressionAtlas	Q8WZ42
Genevestigator	Q8WZ42
GO	GO:0000794 GO:0005737 GO:0005829 GO:0005576 GO:0070062 GO:0005794 GO:0031674 GO:0031430 GO:0005634 GO:0005865 GO:0030018 GO:0051015 GO:0042805 GO:0005524 GO:0005509 GO:0005516 GO:0019899 GO:0042802 GO:0051371 GO:0002020 GO:0019901 GO:0043621 GO:0004674 GO:0008307 GO:0097493 GO:0031433 GO:0007512 GO:0007596 GO:0060048 GO:0048739 GO:0003300 GO:0055008 GO:0055003 GO:0035995 GO:0043056 GO:0001701 GO:0007076 GO:0006936 GO:0030049 GO:0030168 GO:0002576 GO:0050790 GO:0045859 GO:1901897 GO:0051592 GO:0045214 GO:0048769 GO:0030241 GO:0030240 GO:0001756 GO:0006941
Gene3D	2.60.40.10
InterPro	IPR003961 IPR007110 IPR013783 IPR013098 IPR003599 IPR003598 IPR011009 IPR004168 IPR000719 IPR002290 IPR015129 IPR008266
Pfam	PF00041 PF07679 PF00069 PF02818 PF09042
SMART	SM00060 SM00409 SM00408 SM00220
SUPFAM	SSF49265 SSF56112
PROSITE	PS50853 PS50835 PS50011

Annotations

Qualifier	GO ID	GO term name	Reference	ECO ID	ECO term name	with/from	Aspect	Extension	Notes	Status
involved_in	GO:0010628	positive regulation of gene expression	PMID:25152160^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P52179	P	occurs_in:(CL:0000056) has_regulation_target:(UniProtKB:P05019)	Seeded From UniProt	complete
involved_in	GO:0050714	positive regulation of protein secretion	PMID:25152160^[1]	ECO:0000316	genetic interaction evidence used in manual assertion	UniProtKB:P52179	P	occurs_in:(CL:0000056) has_regulation_target:(UniProtKB:P05019)	Seeded From UniProt	complete
involved_in	GO:0010737	protein kinase A signaling	PMID:25152160^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0010628	positive regulation of gene expression	PMID:25152160^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000056) has_regulation_target:(UniProtKB:P05019)	Seeded From UniProt	complete
involved_in	GO:0050714	positive regulation of protein secretion	PMID:25152160^[1]	ECO:0000315	mutant phenotype evidence used in manual assertion		P	occurs_in:(CL:0000056) has_regulation_target:(UniProtKB:P05019)	Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	PMID:7607248^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0DP24	F		Seeded From UniProt	complete
part_of	GO:0070062	extracellular exosome	PMID:19056867^[3]	ECO:0007005	high throughput direct assay evidence used in manual assertion		C	part_of:(UBERON:0001088)	Seeded From UniProt	complete
involved_in	GO:0060048	cardiac muscle contraction	PMID:11846417^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0055008	cardiac muscle tissue morphogenesis	PMID:9817758^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0055003	cardiac myofibril assembly	PMID:11846417^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0055003	cardiac myofibril assembly	PMID:9817758^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0051592	response to calcium ion	PMID:7607248^[2]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0051371	muscle alpha-actinin binding	PMID:9501083^[6]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35609	F		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	PMID:9501083^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0050790	regulation of catalytic activity	PMID:9804419^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048769	sarcomerogenesis	PMID:9817758^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0048739	cardiac muscle fiber development	PMID:9817758^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045859	regulation of protein kinase activity	PMID:9804419^[7]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045214	sarcomere organization	PMID:11846417^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0045214	sarcomere organization	PMID:9817758^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0043621	protein self-association	PMID:9804419^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042805	actinin binding	PMID:11846417^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P35609	F		Seeded From UniProt	complete
enables	GO:0042805	actinin binding	PMID:9501083^[6]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
part_of	GO:0031674	I band	PMID:9817758^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0031433	telethonin binding	PMID:11846417^[4]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O15273	F		Seeded From UniProt	complete
enables	GO:0031433	telethonin binding	PMID:15582318^[8]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:O15273	F		Seeded From UniProt	complete
enables	GO:0031433	telethonin binding	GO_REF:0000024	ECO:0000250	sequence similarity evidence used in manual assertion	UniProtKB:O97791	F		Seeded From UniProt	complete
involved_in	GO:0030241	skeletal muscle myosin thick filament assembly	PMID:9817758^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0030240	skeletal muscle thin filament assembly	PMID:9817758^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:9817758^[5]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019901	protein kinase binding	PMID:23283722^[9]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q13557	F		Seeded From UniProt	complete
enables	GO:0008307	structural constituent of muscle	PMID:11846417^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0008307	structural constituent of muscle	PMID:9817758^[5]	ECO:0000315	mutant phenotype evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0007076	mitotic chromosome condensation	PMID:9548712^[10]	ECO:0000270	expression pattern evidence used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	PMID:7607248^[2]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P0DP23	F		Seeded From UniProt	complete
enables	GO:0005509	calcium ion binding	PMID:7607248^[2]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0003300	cardiac muscle hypertrophy	PMID:11846417^[4]	ECO:0000315	mutant phenotype evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0000794	condensed nuclear chromosome	PMID:9548712^[10]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:9501083^[6]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0019899	enzyme binding	PMID:18310072^[11]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P20807	F		Seeded From UniProt	complete
involved_in	GO:0006936	muscle contraction	PMID:10481174^[12]	ECO:0000303	author statement without traceable support used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	PMID:9804419^[7]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0002020	protease binding	PMID:9642272^[13]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:P20807	F		Seeded From UniProt	complete
involved_in	GO:0071688	striated muscle myosin thick filament assembly	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001790569 ZFIN:ZDB-GENE-030113-2 ZFIN:ZDB-GENE-030616-413	P		Seeded From UniProt	complete
involved_in	GO:0055008	cardiac muscle tissue morphogenesis	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:98864 PANTHER:PTN001790574 UniProtKB:Q8WZ42	P		Seeded From UniProt	complete
involved_in	GO:0055003	cardiac myofibril assembly	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:98864 PANTHER:PTN001790574 UniProtKB:Q8WZ42	P		Seeded From UniProt	complete
enables	GO:0051371	muscle alpha-actinin binding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001790569 UniProtKB:Q8WZ42	F		Seeded From UniProt	complete
enables	GO:0051015	actin filament binding	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001790569 UniProtKB:Q8WZ42	F		Seeded From UniProt	complete
involved_in	GO:0048739	cardiac muscle fiber development	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001790574 UniProtKB:Q8WZ42	P		Seeded From UniProt	complete
involved_in	GO:0045214	sarcomere organization	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0005666 MGI:MGI:102844 MGI:MGI:98864 PANTHER:PTN001790569 UniProtKB:Q8WZ42	P		Seeded From UniProt	complete
part_of	GO:0031430	M band	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:1328358 MGI:MGI:1341430 MGI:MGI:2685280 MGI:MGI:98864 PANTHER:PTN001790569 RGD:631436 RGD:631437 UniProtKB:A0A1D5PSF9 UniProtKB:E1BF23 UniProtKB:Q8WZ42	C		Seeded From UniProt	complete
involved_in	GO:0030241	skeletal muscle myosin thick filament assembly	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001790574 UniProtKB:Q8WZ42	P		Seeded From UniProt	complete
involved_in	GO:0030240	skeletal muscle thin filament assembly	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001790574 UniProtKB:Q8WZ42	P		Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0005666 MGI:MGI:98864 PANTHER:PTN001790569 UniProtKB:Q8WZ42	C		Seeded From UniProt	complete
part_of	GO:0030017	sarcomere	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0005666 FB:FBgn0052311 FB:FBgn0053519 MGI:MGI:102844 MGI:MGI:1328358 MGI:MGI:1341430 MGI:MGI:2685280 MGI:MGI:3045352 MGI:MGI:98864 PANTHER:PTN002492843 RGD:1305950 RGD:631436 RGD:631437 UniProtKB:A0A1D5PSF9 UniProtKB:E1BF23 UniProtKB:P16419 UniProtKB:Q05623 UniProtKB:Q14896 UniProtKB:Q8WZ42 WB:WBGene00004130 WB:WBGene00004732 WB:WBGene00006436 WB:WBGene00006759	C		Seeded From UniProt	complete
enables	GO:0008307	structural constituent of muscle	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	FB:FBgn0005666 PANTHER:PTN001790569 UniProtKB:Q14896 UniProtKB:Q8WZ42	F		Seeded From UniProt	complete
involved_in	GO:0006936	muscle contraction	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	MGI:MGI:102844 MGI:MGI:1328358 MGI:MGI:1336170 MGI:MGI:1336213 MGI:MGI:1341430 MGI:MGI:98864 PANTHER:PTN001790569 RGD:1305950 UniProtKB:Q8WZ42	P		Seeded From UniProt	complete
part_of	GO:0005865	striated muscle thin filament	PMID:21873635^[14]	ECO:0000318	biological aspect of ancestor evidence used in manual assertion	PANTHER:PTN001790569 UniProtKB:Q8WZ42	C		Seeded From UniProt	complete
involved_in	GO:0035995	detection of muscle stretch	PMID:18765796^[15]	ECO:0000314	direct assay evidence used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:19850579^[16]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0004713	protein tyrosine kinase activity	PMID:18765796^[15]	ECO:0000314	direct assay evidence used in manual assertion		F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:9804419^[7]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WZ42	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:23414517^[17]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WZ42	F		Seeded From UniProt	complete
involved_in	GO:0018108	peptidyl-tyrosine phosphorylation	GO_REF:0000108	ECO:0000364	evidence based on logical inference from manual annotation used in automatic assertion	GO:0004713	P		Seeded From UniProt	complete
enables	GO:0004672	protein kinase activity	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008266	F		Seeded From UniProt	complete
enables	GO:0005524	ATP binding	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719	F		Seeded From UniProt	complete
involved_in	GO:0006468	protein phosphorylation	GO_REF:0000002	ECO:0000256	match to sequence model evidence used in automatic assertion	InterPro:IPR000719 InterPro:IPR008266	P		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16962974^[18]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WZ42-3	F		Seeded From UniProt	complete
enables	GO:0042802	identical protein binding	PMID:16407954^[19]	ECO:0000353	physical interaction evidence used in manual assertion	UniProtKB:Q8WZ42-3	F		Seeded From UniProt	complete
part_of	GO:0031430	M band	PMID:11717165^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0030018	Z disc	PMID:11717165^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005865	striated muscle thin filament	PMID:11717165^[20]	ECO:0000314	direct assay evidence used in manual assertion		C		Seeded From UniProt	complete
enables	GO:0097493	structural molecule activity conferring elasticity	PMID:23283722^[9]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0035995	detection of muscle stretch	PMID:12507422^[21]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0008307	structural constituent of muscle	PMID:7569978^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0006941	striated muscle contraction	PMID:7569978^[22]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
involved_in	GO:0006936	muscle contraction	PMID:11911777^[23]	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	PMID:10481174^[12]	ECO:0000304	author statement supported by traceable reference used in manual assertion		F		Seeded From UniProt	complete
involved_in	GO:0030049	muscle filament sliding	Reactome:R-HSA-390522	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
part_of	GO:0005829	cytosol	Reactome:R-HSA-482772 Reactome:R-HSA-390598 Reactome:R-HSA-390597 Reactome:R-HSA-390595 Reactome:R-HSA-390593	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
part_of	GO:0005576	extracellular region	Reactome:R-HSA-482772	ECO:0000304	author statement supported by traceable reference used in manual assertion		C		Seeded From UniProt	complete
involved_in	GO:0002576	platelet degranulation	Reactome:R-HSA-114608	ECO:0000304	author statement supported by traceable reference used in manual assertion		P		Seeded From UniProt	complete
enables	GO:0000166	nucleotide binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0547	F		Seeded From UniProt	complete
enables	GO:0016740	transferase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0808	F		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
enables	GO:0005524	ATP binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0067	F		Seeded From UniProt	complete
enables	GO:0016301	kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	F		Seeded From UniProt	complete
enables	GO:0005516	calmodulin binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0112	F		Seeded From UniProt	complete
enables	GO:0004674	protein serine/threonine kinase activity	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0723	F		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:0016310	phosphorylation	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0418	P		Seeded From UniProt	complete
enables	GO:0046872	metal ion binding	GO_REF:0000037	ECO:0000322	imported manually asserted information used in automatic assertion	UniProtKB-KW:KW-0479	F		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 Kravchenko, IV et al. (2015) Induction of insulin-like growth factor 1 splice forms by subfragments of myofibrillar proteins. Mol. Cell. Endocrinol. 399 69-77 PubMed GONUTS page
↑ ^2.0 ^2.1 ^2.2 ^2.3 Gautel, M et al. (1995) A calmodulin-binding sequence in the C-terminus of human cardiac titin kinase. Eur. J. Biochem. 230 752-9 PubMed GONUTS page
↑ Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page
↑ ^4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Itoh-Satoh, M et al. (2002) Titin mutations as the molecular basis for dilated cardiomyopathy. Biochem. Biophys. Res. Commun. 291 385-93 PubMed GONUTS page
↑ ^5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 ^5.8 ^5.9 Gregorio, CC et al. (1998) The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity. J. Cell Biol. 143 1013-27 PubMed GONUTS page
↑ ^6.0 ^6.1 ^6.2 ^6.3 Young, P et al. (1998) Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin. EMBO J. 17 1614-24 PubMed GONUTS page
↑ ^7.0 ^7.1 ^7.2 ^7.3 ^7.4 Mayans, O et al. (1998) Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 395 863-9 PubMed GONUTS page
↑ Hayashi, T et al. (2004) Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy. J. Am. Coll. Cardiol. 44 2192-201 PubMed GONUTS page
↑ ^9.0 ^9.1 Hamdani, N et al. (2013) Crucial role for Ca2(+)/calmodulin-dependent protein kinase-II in regulating diastolic stress of normal and failing hearts via titin phosphorylation. Circ. Res. 112 664-74 PubMed GONUTS page
↑ ^10.0 ^10.1 Machado, C et al. (1998) Human autoantibodies reveal titin as a chromosomal protein. J. Cell Biol. 141 321-33 PubMed GONUTS page
↑ Hayashi, C et al. (2008) Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle. J. Biol. Chem. 283 14801-14 PubMed GONUTS page
↑ ^12.0 ^12.1 Trinick, J & Tskhovrebova, L (1999) Titin: a molecular control freak. Trends Cell Biol. 9 377-80 PubMed GONUTS page
↑ Ono, Y et al. (1998) Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A. J. Biol. Chem. 273 17073-8 PubMed GONUTS page
↑ ^14.00 ^14.01 ^14.02 ^14.03 ^14.04 ^14.05 ^14.06 ^14.07 ^14.08 ^14.09 ^14.10 ^14.11 ^14.12 ^14.13 ^14.14 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page
↑ ^15.0 ^15.1 Puchner, EM et al. (2008) Mechanoenzymatics of titin kinase. Proc. Natl. Acad. Sci. U.S.A. 105 13385-90 PubMed GONUTS page
↑ Mearini, G et al. (2010) Atrogin-1 and MuRF1 regulate cardiac MyBP-C levels via different mechanisms. Cardiovasc. Res. 85 357-66 PubMed GONUTS page
↑ Blandin, G et al. (2013) A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome. Skelet Muscle 3 3 PubMed GONUTS page
↑ Marino, M et al. (2006) The Ig doublet Z1Z2: a model system for the hybrid analysis of conformational dynamics in Ig tandems from titin. Structure 14 1437-47 PubMed GONUTS page
↑ Zou, P et al. (2006) Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk. Nature 439 229-33 PubMed GONUTS page
↑ ^20.0 ^20.1 ^20.2 Bang, ML et al. (2001) The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ. Res. 89 1065-72 PubMed GONUTS page
↑ Knöll, R et al. (2002) The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell 111 943-55 PubMed GONUTS page
↑ ^22.0 ^22.1 Labeit, S & Kolmerer, B (1995) Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270 293-6 PubMed GONUTS page
↑ Tskhovrebova, L & Trinick, J (2002) Role of titin in vertebrate striated muscle. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 357 199-206 PubMed GONUTS page

[PMID:25152160-1] 1.0 ^1.1 ^1.2 ^1.3 ^1.4 Kravchenko, IV et al. (2015) Induction of insulin-like growth factor 1 splice forms by subfragments of myofibrillar proteins. Mol. Cell. Endocrinol. 399 69-77 PubMed GONUTS page

[PMID:7607248-2] 2.0 ^2.1 ^2.2 ^2.3 Gautel, M et al. (1995) A calmodulin-binding sequence in the C-terminus of human cardiac titin kinase. Eur. J. Biochem. 230 752-9 PubMed GONUTS page

[PMID:19056867-3] Gonzales, PA et al. (2009) Large-scale proteomics and phosphoproteomics of urinary exosomes. J. Am. Soc. Nephrol. 20 363-79 PubMed GONUTS page

[PMID:11846417-4] 4.0 ^4.1 ^4.2 ^4.3 ^4.4 ^4.5 ^4.6 Itoh-Satoh, M et al. (2002) Titin mutations as the molecular basis for dilated cardiomyopathy. Biochem. Biophys. Res. Commun. 291 385-93 PubMed GONUTS page

[PMID:9817758-5] 5.0 ^5.1 ^5.2 ^5.3 ^5.4 ^5.5 ^5.6 ^5.7 ^5.8 ^5.9 Gregorio, CC et al. (1998) The NH2 terminus of titin spans the Z-disc: its interaction with a novel 19-kD ligand (T-cap) is required for sarcomeric integrity. J. Cell Biol. 143 1013-27 PubMed GONUTS page

[PMID:9501083-6] 6.0 ^6.1 ^6.2 ^6.3 Young, P et al. (1998) Molecular structure of the sarcomeric Z-disk: two types of titin interactions lead to an asymmetrical sorting of alpha-actinin. EMBO J. 17 1614-24 PubMed GONUTS page

[PMID:9804419-7] 7.0 ^7.1 ^7.2 ^7.3 ^7.4 Mayans, O et al. (1998) Structural basis for activation of the titin kinase domain during myofibrillogenesis. Nature 395 863-9 PubMed GONUTS page

[PMID:15582318-8] Hayashi, T et al. (2004) Tcap gene mutations in hypertrophic cardiomyopathy and dilated cardiomyopathy. J. Am. Coll. Cardiol. 44 2192-201 PubMed GONUTS page

[PMID:23283722-9] 9.0 ^9.1 Hamdani, N et al. (2013) Crucial role for Ca2(+)/calmodulin-dependent protein kinase-II in regulating diastolic stress of normal and failing hearts via titin phosphorylation. Circ. Res. 112 664-74 PubMed GONUTS page

[PMID:9548712-10] 10.0 ^10.1 Machado, C et al. (1998) Human autoantibodies reveal titin as a chromosomal protein. J. Cell Biol. 141 321-33 PubMed GONUTS page

[PMID:18310072-11] Hayashi, C et al. (2008) Multiple molecular interactions implicate the connectin/titin N2A region as a modulating scaffold for p94/calpain 3 activity in skeletal muscle. J. Biol. Chem. 283 14801-14 PubMed GONUTS page

[PMID:10481174-12] 12.0 ^12.1 Trinick, J & Tskhovrebova, L (1999) Titin: a molecular control freak. Trends Cell Biol. 9 377-80 PubMed GONUTS page

[PMID:9642272-13] Ono, Y et al. (1998) Functional defects of a muscle-specific calpain, p94, caused by mutations associated with limb-girdle muscular dystrophy type 2A. J. Biol. Chem. 273 17073-8 PubMed GONUTS page

[PMID:21873635-14] 14.00 ^14.01 ^14.02 ^14.03 ^14.04 ^14.05 ^14.06 ^14.07 ^14.08 ^14.09 ^14.10 ^14.11 ^14.12 ^14.13 ^14.14 Gaudet, P et al. (2011) Phylogenetic-based propagation of functional annotations within the Gene Ontology consortium. Brief. Bioinformatics 12 449-62 PubMed GONUTS page

[PMID:18765796-15] 15.0 ^15.1 Puchner, EM et al. (2008) Mechanoenzymatics of titin kinase. Proc. Natl. Acad. Sci. U.S.A. 105 13385-90 PubMed GONUTS page

[PMID:19850579-16] Mearini, G et al. (2010) Atrogin-1 and MuRF1 regulate cardiac MyBP-C levels via different mechanisms. Cardiovasc. Res. 85 357-66 PubMed GONUTS page

[PMID:23414517-17] Blandin, G et al. (2013) A human skeletal muscle interactome centered on proteins involved in muscular dystrophies: LGMD interactome. Skelet Muscle 3 3 PubMed GONUTS page

[PMID:16962974-18] Marino, M et al. (2006) The Ig doublet Z1Z2: a model system for the hybrid analysis of conformational dynamics in Ig tandems from titin. Structure 14 1437-47 PubMed GONUTS page

[PMID:16407954-19] Zou, P et al. (2006) Palindromic assembly of the giant muscle protein titin in the sarcomeric Z-disk. Nature 439 229-33 PubMed GONUTS page

[PMID:11717165-20] 20.0 ^20.1 ^20.2 Bang, ML et al. (2001) The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ. Res. 89 1065-72 PubMed GONUTS page

[PMID:12507422-21] Knöll, R et al. (2002) The cardiac mechanical stretch sensor machinery involves a Z disc complex that is defective in a subset of human dilated cardiomyopathy. Cell 111 943-55 PubMed GONUTS page

[PMID:7569978-22] 22.0 ^22.1 Labeit, S & Kolmerer, B (1995) Titins: giant proteins in charge of muscle ultrastructure and elasticity. Science 270 293-6 PubMed GONUTS page

[PMID:11911777-23] Tskhovrebova, L & Trinick, J (2002) Role of titin in vertebrate striated muscle. Philos. Trans. R. Soc. Lond., B, Biol. Sci. 357 199-206 PubMed GONUTS page

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HUMAN:TITIN

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