dbPTM

TMOD3_HUMAN - PTM Information in dbPTM

Basic Information of Protein

Overview of Protein Modification Sites with Functional and Structural Information
UniProt ID	TMOD3_HUMAN
UniProt AC	Q9NYL9
Protein Name	Tropomodulin-3
Gene Name	TMOD3
Organism	Homo sapiens (Human).
Sequence Length	352
Subcellular Localization	Cytoplasm, cytoskeleton.
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 (By similarity)..
Protein Sequence	MALPFRKDLEKYKDLDEDELLGNLSETELKQLETVLDDLDPENALLPAGFRQKNQTSKSTTGPFDREHLLSYLEKEALEHKDREDYVPYTGEKKGKIFIPKQKPVQTFTEEKVSLDPELEEALTSASDTELCDLAAILGMHNLITNTKFCNIMGSSNGVDQEHFSNVVKGEKILPVFDEPPNPTNVEESLKRTKENDAHLVEVNLNNIKNIPIPTLKDFAKALETNTHVKCFSLAATRSNDPVATAFAEMLKVNKTLKSLNVESNFITGVGILALIDALRDNETLAELKIDNQRQQLGTAVELEMAKMLEENTNILKFGYQFTQQGPRTRAANAITKNNDLVRKRRVEGDHQ

Experimental Post-Translational Modification Sites

* ASA = Accessible Surface Area

Locations	Modification	Substrate Peptides & Secondary Structure	ASA (%)	Reference
11	Ubiquitination	PFRKDLEKYKDLDED CCHHCHHHCCCCCHH	65.97	22817900
11	Acetylation	PFRKDLEKYKDLDED CCHHCHHHCCCCCHH	65.97	26051181
12	Phosphorylation	FRKDLEKYKDLDEDE CHHCHHHCCCCCHHH	10.60	30278072
13	Ubiquitination	RKDLEKYKDLDEDEL HHCHHHCCCCCHHHH	63.98	21906983
13	Acetylation	RKDLEKYKDLDEDEL HHCHHHCCCCCHHHH	63.98	26051181
25	Phosphorylation	DELLGNLSETELKQL HHHHCCCCHHHHHHH	46.61	19664994
27	Phosphorylation	LLGNLSETELKQLET HHCCCCHHHHHHHHH	43.15	29255136
34	Phosphorylation	TELKQLETVLDDLDP HHHHHHHHHHHHCCH	34.65	28464451
53	Ubiquitination	LPAGFRQKNQTSKST CCCCCCCCCCCCCCC	46.93	29967540
58	Ubiquitination	RQKNQTSKSTTGPFD CCCCCCCCCCCCCCC	56.03	24816145
59	Phosphorylation	QKNQTSKSTTGPFDR CCCCCCCCCCCCCCH	30.85	30576142
60	Phosphorylation	KNQTSKSTTGPFDRE CCCCCCCCCCCCCHH	39.24	21815630
61	Phosphorylation	NQTSKSTTGPFDREH CCCCCCCCCCCCHHH	50.37	28152594
71	Phosphorylation	FDREHLLSYLEKEAL CCHHHHHHHHHHHHH	33.75	28152594
72	Phosphorylation	DREHLLSYLEKEALE CHHHHHHHHHHHHHH	20.89	25394399
75	Ubiquitination	HLLSYLEKEALEHKD HHHHHHHHHHHHCCC	45.77	29967540
75	2-Hydroxyisobutyrylation	HLLSYLEKEALEHKD HHHHHHHHHHHHCCC	45.77	-
81	Ubiquitination	EKEALEHKDREDYVP HHHHHHCCCHHHCCC	49.45	33845483
86	Phosphorylation	EHKDREDYVPYTGEK HCCCHHHCCCCCCCC	9.89	28796482
89	Phosphorylation	DREDYVPYTGEKKGK CHHHCCCCCCCCCCE	19.82	28796482
90	Phosphorylation	REDYVPYTGEKKGKI HHHCCCCCCCCCCEE	32.56	28555341
93	2-Hydroxyisobutyrylation	YVPYTGEKKGKIFIP CCCCCCCCCCEEEEC	69.07	-
93	Acetylation	YVPYTGEKKGKIFIP CCCCCCCCCCEEEEC	69.07	25953088
93	Ubiquitination	YVPYTGEKKGKIFIP CCCCCCCCCCEEEEC	69.07	33845483
96	Ubiquitination	YTGEKKGKIFIPKQK CCCCCCCEEEECCCC	43.24	33845483
96	Sumoylation	YTGEKKGKIFIPKQK CCCCCCCEEEECCCC	43.24	-
96	Sumoylation	YTGEKKGKIFIPKQK CCCCCCCEEEECCCC	43.24	-
101	Ubiquitination	KGKIFIPKQKPVQTF CCEEEECCCCCCCCC	67.16	33845483
103	Ubiquitination	KIFIPKQKPVQTFTE EEEECCCCCCCCCCH	53.97	27667366
124	Phosphorylation	PELEEALTSASDTEL HHHHHHHHCCCHHHH	29.33	25159151
125	Phosphorylation	ELEEALTSASDTELC HHHHHHHCCCHHHHH	26.99	25159151
127	Phosphorylation	EEALTSASDTELCDL HHHHHCCCHHHHHHH	44.85	28464451
129	Phosphorylation	ALTSASDTELCDLAA HHHCCCHHHHHHHHH	28.50	26657352
145	Phosphorylation	LGMHNLITNTKFCNI HCHHHHHCCCCCCHH	39.75	26552605
147	Phosphorylation	MHNLITNTKFCNIMG HHHHHCCCCCCHHCC	19.49	26552605
155	Phosphorylation	KFCNIMGSSNGVDQE CCCHHCCCCCCCCHH	11.84	23401153
156	Phosphorylation	FCNIMGSSNGVDQEH CCHHCCCCCCCCHHH	31.69	30108239
165	Phosphorylation	GVDQEHFSNVVKGEK CCCHHHHHHCCCCCE	30.53	26552605
169	Sumoylation	EHFSNVVKGEKILPV HHHHHCCCCCEEEEC	58.00	-
169	Acetylation	EHFSNVVKGEKILPV HHHHHCCCCCEEEEC	58.00	25953088
169	Ubiquitination	EHFSNVVKGEKILPV HHHHHCCCCCEEEEC	58.00	32015554
172	Ubiquitination	SNVVKGEKILPVFDE HHCCCCCEEEECCCC	59.20	22817900
172	Acetylation	SNVVKGEKILPVFDE HHCCCCCEEEECCCC	59.20	25953088
191	Ubiquitination	TNVEESLKRTKENDA CCHHHHHHHHHCCCC	68.26	32015554
191	2-Hydroxyisobutyrylation	TNVEESLKRTKENDA CCHHHHHHHHHCCCC	68.26	-
194	Ubiquitination	EESLKRTKENDAHLV HHHHHHHHCCCCEEE	59.56	29967540
209	Sumoylation	EVNLNNIKNIPIPTL EEECCCCCCCCCCCH	51.45	-
209	Ubiquitination	EVNLNNIKNIPIPTL EEECCCCCCCCCCCH	51.45	32015554
217	Ubiquitination	NIPIPTLKDFAKALE CCCCCCHHHHHHHHH	53.96	33845483
221	Acetylation	PTLKDFAKALETNTH CCHHHHHHHHHCCCC	54.20	26051181
221	Ubiquitination	PTLKDFAKALETNTH CCHHHHHHHHHCCCC	54.20	33845483
230	Acetylation	LETNTHVKCFSLAAT HHCCCCCEEEEHHHH	23.20	26051181
230	Ubiquitination	LETNTHVKCFSLAAT HHCCCCCEEEEHHHH	23.20	29967540
252	Ubiquitination	TAFAEMLKVNKTLKS HHHHHHHHHCHHHHH	42.31	29967540
289	Ubiquitination	NETLAELKIDNQRQQ CCCHHEEECHHHHHH	39.25	24816145
294	Methylation	ELKIDNQRQQLGTAV EEECHHHHHHHHHHH	32.25	24377539
294	Dimethylation	ELKIDNQRQQLGTAV EEECHHHHHHHHHHH	32.25	-
307	Ubiquitination	AVELEMAKMLEENTN HHHHHHHHHHHHHCC	42.58	25015289
308	Sulfoxidation	VELEMAKMLEENTNI HHHHHHHHHHHHCCH	4.06	30846556
313	Phosphorylation	AKMLEENTNILKFGY HHHHHHHCCHHHHCC	27.24	28258704
317	Ubiquitination	EENTNILKFGYQFTQ HHHCCHHHHCCCCCC	32.71	25015289
317	Sumoylation	EENTNILKFGYQFTQ HHHCCHHHHCCCCCC	32.71	-
317	Acetylation	EENTNILKFGYQFTQ HHHCCHHHHCCCCCC	32.71	26051181
320	Phosphorylation	TNILKFGYQFTQQGP CCHHHHCCCCCCCCC	12.00	28152594
337	Acetylation	RAANAITKNNDLVRK HHHHHHHCCCHHHHH	47.87	26051181
337	Ubiquitination	RAANAITKNNDLVRK HHHHHHHCCCHHHHH	47.87	24816145
344	Ubiquitination	KNNDLVRKRRVEGDH CCCHHHHHHCCCCCC	36.76	29967540

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
Oops, there are no upstream regulatory protein records of TMOD3_HUMAN !!

Functions of PTM Sites

Modified Location	Modified Residue	Modification	Function	Reference
Oops, there are no descriptions of PTM sites of TMOD3_HUMAN !!

Disease-associated PTM Sites based on SAP

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

Modified Location	Modification	Variant Position (Distance <= 10)	Residue Change	SAP	Related Disease	Reference
Oops, there are no SNP-PTM records of TMOD3_HUMAN !!

Protein-Protein Interaction

Interacting Protein	Gene Name	Interaction Type	PPI Reference
PSMD9_HUMAN	PSMD9	physical	22863883
VATB2_HUMAN	ATP6V1B2	physical	26344197
MCFD2_HUMAN	MCFD2	physical	26344197
TIM16_HUMAN	PAM16	physical	26344197
RUVB2_HUMAN	RUVBL2	physical	26344197
SMRC1_HUMAN	SMARCC1	physical	26344197
SMRC2_HUMAN	SMARCC2	physical	26344197
SMD1_HUMAN	SNRPD1	physical	26344197
XRCC6_HUMAN	XRCC6	physical	26344197
ADSV_HUMAN	SCIN	physical	28514442
POTEI_HUMAN	POTEI	physical	28514442
MYO5B_HUMAN	MYO5B	physical	28514442
INF2_HUMAN	INF2	physical	28514442
HEM1_HUMAN	ALAS1	physical	28514442
SVIL_HUMAN	SVIL	physical	28514442
FLII_HUMAN	FLII	physical	28514442
LRRF2_HUMAN	LRRFIP2	physical	28514442
ACTA_HUMAN	ACTA2	physical	28514442
GELS_HUMAN	GSN	physical	28514442
LONP2_HUMAN	LONP2	physical	28514442
MEIS2_HUMAN	MEIS2	physical	28514442
SPIR2_HUMAN	SPIRE2	physical	28514442
COBL_HUMAN	COBL	physical	28514442
HEMH_HUMAN	FECH	physical	28514442
PHAR2_HUMAN	PHACTR2	physical	28514442
ACTBL_HUMAN	ACTBL2	physical	28514442
ACTB_HUMAN	ACTB	physical	28514442
TBCD4_HUMAN	TBC1D4	physical	28514442
DOCK7_HUMAN	DOCK7	physical	28514442
MYO5A_HUMAN	MYO5A	physical	28514442
TWF2_HUMAN	TWF2	physical	28514442
ACTC_HUMAN	ACTC1	physical	28514442
MYO5C_HUMAN	MYO5C	physical	28514442
SPIR1_HUMAN	SPIRE1	physical	28514442
PBX2_HUMAN	PBX2	physical	28514442
PRP4_HUMAN	PRPF4	physical	28514442
ENAH_HUMAN	ENAH	physical	28514442
CSR2B_HUMAN	CSRP2BP	physical	28514442
PBX3_HUMAN	PBX3	physical	28514442
BDH2_HUMAN	BDH2	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.

Regulatory Network of TMOD3_HUMAN

Related Literatures of Post-Translational Modification

Phosphorylation
Reference	PubMed
"Lys-N and trypsin cover complementary parts of the phosphoproteome ina refined SCX-based approach."; Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,Mohammed S.; Anal. Chem. 81:4493-4501(2009). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.	19413330 [Abstract]
"A quantitative atlas of mitotic phosphorylation."; Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,Elledge S.J., Gygi S.P.; Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.	18669648 [Abstract]
"Global, in vivo, and site-specific phosphorylation dynamics insignaling networks."; Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,Mann M.; Cell 127:635-648(2006). Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-25, AND MASSSPECTROMETRY.	17081983 [Abstract]