TMOD1_HUMAN - PTM Information in dbPTM

Basic Information of Protein

• UniProt ID: TMOD1_HUMAN
• UniProt AC: P28289
• Protein Name: Tropomodulin-1
• Gene Name: TMOD1
• Organism: Homo sapiens (Human).
• Sequence Length: 359
• Subcellular Localization: Cytoplasm, cytoskeleton . In myofibrils with sarcomeric structure, localizes to the pointed end of actin thin filaments (PubMed:25250574).
• Protein Description: Blocks the elongation and depolymerization of the actin filaments at the pointed end. The Tmod/TM complex contributes to the formation of the short actin protofilament, which in turn defines the geometry of the membrane skeleton. May play an important role in regulating the organization of actin filaments by preferentially binding to a specific tropomyosin isoform at its N-terminus..
• Protein Sequence: MSYRRELEKYRDLDEDEILGALTEEELRTLENELDELDPDNALLPAGLRQKDQTTKAPTGPFKREELLDHLEKQAKEFKDREDLVPYTGEKRGKVWVPKQKPLDPVLESVTLEPELEEALANASDAELCDIAAILGMHTLMSNQQYYQALSSSSIMNKEGLNSVIKPTQYKPVPDEEPNSTDVEETLERIKNNDPKLEEVNLNNIRNIPIPTLKAYAEALKENSYVKKFSIVGTRSNDPVAYALAEMLKENKVLKTLNVESNFISGAGILRLVEALPYNTSLVEMKIDNQSQPLGNKVEMEIVSMLEKNATLLKFGYHFTQQGPRLRASNAMMNNNDLVRKRRLADLTGPIIPKCRSGV

Overview of Protein Modification Sites with Functional and Structural Information

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
2	Phosphorylation	------MSYRRELEK ------CCHHHHHHH	27.61	19137675
3	Phosphorylation	-----MSYRRELEKY -----CCHHHHHHHH	16.64	-
10	Phosphorylation	YRRELEKYRDLDEDE HHHHHHHHCCCCHHH	10.45	-
23	Phosphorylation	DEILGALTEEELRTL HHHHHHCCHHHHHHH	40.59	-
54	Phosphorylation	GLRQKDQTTKAPTGP HHCCCCCCCCCCCCC	40.16	19137675
87	Phosphorylation	DREDLVPYTGEKRGK CHHHCCCCCCCCCCE	21.65	17081983
88	Phosphorylation	REDLVPYTGEKRGKV HHHCCCCCCCCCCEE	32.56	17081983
225	Phosphorylation	EALKENSYVKKFSIV HHHHHCCCEEEEEEE	28.06	-
234	Phosphorylation	KKFSIVGTRSNDPVA EEEEEECCCCCCHHH	21.74	18452278
236	Phosphorylation	FSIVGTRSNDPVAYA EEEECCCCCCHHHHH	45.48	18452278
242	Phosphorylation	RSNDPVAYALAEMLK CCCCHHHHHHHHHHH	11.46	-
278	Phosphorylation	RLVEALPYNTSLVEM HHHHHCCCCCCEEEE	31.74	20068231
280	Phosphorylation	VEALPYNTSLVEMKI HHHCCCCCCEEEEEE	20.00	20068231
281	Phosphorylation	EALPYNTSLVEMKID HHCCCCCCEEEEEEC	27.12	20068231
304	Phosphorylation	KVEMEIVSMLEKNAT HHHHHHHHHHHHCCH	24.26	29759185
329	Phosphorylation	QGPRLRASNAMMNNN CCCHHHHHHHHCCCC	20.77	-

Upstream regulatory proteins (kinases for phosphorylation sites, E3 ubiquitin ligases of ubiquitination sites, ...)

Modified Location	Modified Residue	Modification	Type of Upstream Proteins	Gene Name of Upstream Proteins	UniProt AC of Upstream Proteins	Sources
2	S	Phosphorylation	Kinase	TRPM7	Q96QT4	GPS
54	T	Phosphorylation	Kinase	TRPM7	Q96QT4	GPS

Functions of PTM Sites

Oops, there are no descriptions of PTM sites of TMOD1_HUMAN !!

Disease-associated PTM Sites based on SAP

* Distance = the distance between SAP position and PTM sites.

Oops, there are no SNP-PTM records of TMOD1_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
GELS_HUMAN	GSN	physical	26186194
MYO5C_HUMAN	MYO5C	physical	26186194
MYO5B_HUMAN	MYO5B	physical	26186194
FLII_HUMAN	FLII	physical	26186194
LRRF1_HUMAN	LRRFIP1	physical	26186194
LRRF2_HUMAN	LRRFIP2	physical	26186194
TBCD4_HUMAN	TBC1D4	physical	26186194
SNX1_HUMAN	SNX1	physical	26186194
ADSV_HUMAN	SCIN	physical	26186194
CBPC1_HUMAN	AGTPBP1	physical	26186194
NIN_HUMAN	NIN	physical	26186194
SYWC_HUMAN	WARS	physical	26344197
MYO5B_HUMAN	MYO5B	physical	28514442
ADSV_HUMAN	SCIN	physical	28514442
LRRF2_HUMAN	LRRFIP2	physical	28514442
FLII_HUMAN	FLII	physical	28514442
MYO5C_HUMAN	MYO5C	physical	28514442
CBPC1_HUMAN	AGTPBP1	physical	28514442
NIN_HUMAN	NIN	physical	28514442
GELS_HUMAN	GSN	physical	28514442
SNX1_HUMAN	SNX1	physical	28514442
TBCD4_HUMAN	TBC1D4	physical	28514442

Drug and Disease Associations

• Kegg Disease
• There are no disease associations of PTM sites.
• OMIM Disease
• There are no disease associations of PTM sites.
• Kegg Drug
• There are no disease associations of PTM sites.
• DrugBank
• There are no disease associations of PTM sites.