TPM3_HUMAN - dbPTM
TPM3_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPM3_HUMAN
UniProt AC P06753
Protein Name Tropomyosin alpha-3 chain
Gene Name TPM3
Organism Homo sapiens (Human).
Sequence Length 285
Subcellular Localization Cytoplasm, cytoskeleton .
Protein Description Binds to actin filaments in muscle and non-muscle cells. Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction. Smooth muscle contraction is regulated by interaction with caldesmon. In non-muscle cells is implicated in stabilizing cytoskeleton actin filaments..
Protein Sequence MMEAIKKKMQMLKLDKENALDRAEQAEAEQKQAEERSKQLEDELAAMQKKLKGTEDELDKYSEALKDAQEKLELAEKKAADAEAEVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRALKDEEKMELQEIQLKEAKHIAEEADRKYEEVARKLVIIEGDLERTEERAELAESKCSELEEELKNVTNNLKSLEAQAEKYSQKEDKYEEEIKILTDKLKEAETRAEFAERSVAKLEKTIDDLEDELYAQKLKYKAISEELDHALNDMTSI
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 Orthologous
Protein Cluster
2Acetylation------MMEAIKKKM
------CHHHHHHHH		60.13-
2 (in isoform 2)Acetylation-60.13-
2 (in isoform 3)Acetylation-60.13-
5 (in isoform 2)Phosphorylation-54.0825850435
5 (in isoform 3)Phosphorylation-54.0825850435
5 (in isoform 4)Phosphorylation-54.0825850435
5 (in isoform 5)Phosphorylation-54.0825850435
5 (in isoform 6)Phosphorylation-54.0825850435
6 (in isoform 2)Phosphorylation-47.5725850435
6 (in isoform 3)Phosphorylation-47.5725850435
6 (in isoform 4)Phosphorylation-47.5725850435
6 (in isoform 5)Phosphorylation-47.5725850435
6 (in isoform 6)Phosphorylation-47.5725850435
11 (in isoform 2)Ubiquitination-2.54-
13AcetylationKKKMQMLKLDKENAL
HHHHHHHHCCHHHHH		11.3623236377
13UbiquitinationKKKMQMLKLDKENAL
HHHHHHHHCCHHHHH		11.36-
13 (in isoform 2)Ubiquitination-11.3621890473
13MalonylationKKKMQMLKLDKENAL
HHHHHHHHCCHHHHH		11.3626320211
13 (in isoform 3)Ubiquitination-11.3621890473
16AcetylationMQMLKLDKENALDRA
HHHHHCCHHHHHHHH		47.6123749302
16UbiquitinationMQMLKLDKENALDRA
HHHHHCCHHHHHHHH		47.61-
162-HydroxyisobutyrylationMQMLKLDKENALDRA
HHHHHCCHHHHHHHH		47.61-
16MalonylationMQMLKLDKENALDRA
HHHHHCCHHHHHHHH		47.6126320211
27 (in isoform 6)Methylation-27.77-
35AcetylationAEQKQAEERSKQLED
HHHHHHHHHHHHHHH		40.4319608861
49AcetylationDELAAMQKKLKGTED
HHHHHHHHHHCCCHH		38.2430586245
50AcetylationELAAMQKKLKGTEDE
HHHHHHHHHCCCHHH		8.7819867195
51 (in isoform 4)Phosphorylation-73.0727794612
51 (in isoform 2)Phosphorylation-73.0727794612
51 (in isoform 3)Phosphorylation-73.0727794612
51 (in isoform 5)Phosphorylation-73.0727794612
51 (in isoform 6)Phosphorylation-73.0727794612
54PhosphorylationMQKKLKGTEDELDKY
HHHHHCCCHHHHHHH		59.1526437602
60UbiquitinationGTEDELDKYSEALKD
CCHHHHHHHHHHHHH		16.06-
61PhosphorylationTEDELDKYSEALKDA
CHHHHHHHHHHHHHH		23.3321406692
62PhosphorylationEDELDKYSEALKDAQ
HHHHHHHHHHHHHHH		55.7321406692
82 (in isoform 2)Ubiquitination-46.0021890473
82 (in isoform 3)Ubiquitination-46.0021890473
87PhosphorylationADAEAEVASLNRRIQ
HHHHHHHHHHHHHHH		31.21-
88PhosphorylationDAEAEVASLNRRIQL
HHHHHHHHHHHHHHH		4.1019664994
91UbiquitinationAEVASLNRRIQLVEE
HHHHHHHHHHHHHHH		21.6721906983
94AcetylationASLNRRIQLVEEELD
HHHHHHHHHHHHHHH		4.9419608861
109PhosphorylationRAQERLATALQKLEE
HHHHHHHHHHHHHHH		11.4624692096
113AcetylationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH		4.6623954790
113UbiquitinationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH		4.66-
119AcetylationQKLEEAEKAADESER
HHHHHHHHHHHHHHH		16.2020167786
119UbiquitinationQKLEEAEKAADESER
HHHHHHHHHHHHHHH		16.20-
119 (in isoform 1)Ubiquitination-16.2021906983
124PhosphorylationAEKAADESERGMKVI
HHHHHHHHHHHHHHH		51.7326437602
125 (in isoform 7)Acetylation-60.8419608861
125AcetylationEKAADESERGMKVIE
HHHHHHHHHHHHHHH		60.8419608861
125UbiquitinationEKAADESERGMKVIE
HHHHHHHHHHHHHHH		60.8421906983
126 (in isoform 7)Phosphorylation-19.0621815630
129SumoylationDESERGMKVIENRAL
HHHHHHHHHHHHHCC		5.01-
129SumoylationDESERGMKVIENRAL
HHHHHHHHHHHHHCC		5.01-
129UbiquitinationDESERGMKVIENRAL
HHHHHHHHHHHHHCC		5.01-
133UbiquitinationRGMKVIENRALKDEE
HHHHHHHHHCCCCHH		28.6221906983
137AcetylationVIENRALKDEEKMEL
HHHHHCCCCHHHHHH		70.8625953088
137UbiquitinationVIENRALKDEEKMEL
HHHHHCCCCHHHHHH		70.86-
137MalonylationVIENRALKDEEKMEL
HHHHHCCCCHHHHHH		70.8626320211
138UbiquitinationIENRALKDEEKMELQ
HHHHCCCCHHHHHHH		58.9121906983
141AcetylationRALKDEEKMELQEIQ
HCCCCHHHHHHHHHH		7.6120167786
1412-HydroxyisobutyrylationRALKDEEKMELQEIQ
HCCCCHHHHHHHHHH		7.61-
144 (in isoform 7)Phosphorylation-32.23-
150AcetylationELQEIQLKEAKHIAE
HHHHHHHHHHHHHHH		72.1023236377
150UbiquitinationELQEIQLKEAKHIAE
HHHHHHHHHHHHHHH		72.10-
150MalonylationELQEIQLKEAKHIAE
HHHHHHHHHHHHHHH		72.1026320211
151 (in isoform 7)Phosphorylation-13.7221955146
152 (in isoform 2)Phosphorylation-36.31-
152 (in isoform 3)Phosphorylation-36.31-
152 (in isoform 6)Phosphorylation-36.31-
153AcetylationEIQLKEAKHIAEEAD
HHHHHHHHHHHHHHH		31.3823749302
153UbiquitinationEIQLKEAKHIAEEAD
HHHHHHHHHHHHHHH		31.38-
161AcetylationHIAEEADRKYEEVAR
HHHHHHHHHHHHHHH		58.52-
161MethylationHIAEEADRKYEEVAR
HHHHHHHHHHHHHHH		58.52-
162PhosphorylationIAEEADRKYEEVARK
HHHHHHHHHHHHHHH		20.4418083107
162AcetylationIAEEADRKYEEVARK
HHHHHHHHHHHHHHH		20.4423954790
163PhosphorylationAEEADRKYEEVARKL
HHHHHHHHHHHHHHH		49.3728796482
169UbiquitinationKYEEVARKLVIIEGD
HHHHHHHHHHHEECC		2.52-
169 (in isoform 2)Ubiquitination-2.5221890473
169 (in isoform 3)Ubiquitination-2.5221890473
169UbiquitinationKYEEVARKLVIIEGD
HHHHHHHHHHHEECC		2.5221890473
169UbiquitinationKYEEVARKLVIIEGD
HHHHHHHHHHHEECC		2.5221890473
170S-nitrosylationYEEVARKLVIIEGDL
HHHHHHHHHHEECCH		4.6718992711
172 (in isoform 2)Phosphorylation-3.6420860994
172 (in isoform 3)Phosphorylation-3.6420860994
172 (in isoform 6)Phosphorylation-3.6420860994
177 (in isoform 2)Acetylation-63.4019608861
177 (in isoform 3)Acetylation-63.4019608861
177 (in isoform 6)Acetylation-63.4019608861
177AcetylationLVIIEGDLERTEERA
HHHEECCHHHHHHHH		63.4019608861
179MethylationIIEGDLERTEERAEL
HEECCHHHHHHHHHH		32.59115367669
179 (in isoform 2)Phosphorylation-32.5928348404
179 (in isoform 3)Phosphorylation-32.5928348404
179 (in isoform 6)Phosphorylation-32.5928348404
180PhosphorylationIEGDLERTEERAELA
EECCHHHHHHHHHHH		52.2726437602
181 (in isoform 2)Ubiquitination-57.4921890473
181 (in isoform 3)Ubiquitination-57.4921890473
184AcetylationLERTEERAELAESKC
HHHHHHHHHHHHHHH		55.5219608861
189PhosphorylationERAELAESKCSELEE
HHHHHHHHHHHHHHH		33.0326437602
191PhosphorylationAELAESKCSELEEEL
HHHHHHHHHHHHHHH		49.29-
192PhosphorylationELAESKCSELEEELK
HHHHHHHHHHHHHHH		70.4428450419
202PhosphorylationEEELKNVTNNLKSLE
HHHHHHHHHHHHHHH		47.7826437602
207PhosphorylationNVTNNLKSLEAQAEK
HHHHHHHHHHHHHHH		6.3826657352
214UbiquitinationSLEAQAEKYSQKEDK
HHHHHHHHHHCCHHH		14.08-
215PhosphorylationLEAQAEKYSQKEDKY
HHHHHHHHHCCHHHH		45.9326437602
215 (in isoform 2)Acetylation-45.9319608861
215 (in isoform 2)Ubiquitination-45.9321890473
215 (in isoform 5)Acetylation-45.9319608861
215AcetylationLEAQAEKYSQKEDKY
HHHHHHHHHCCHHHH		45.9319608861
216PhosphorylationEAQAEKYSQKEDKYE
HHHHHHHHCCHHHHH		50.4928152594
216 (in isoform 5)Phosphorylation-50.4921815630
216 (in isoform 2)Phosphorylation-50.4921815630
218UbiquitinationQAEKYSQKEDKYEEE
HHHHHHCCHHHHHHH		52.69-
218MalonylationQAEKYSQKEDKYEEE
HHHHHHCCHHHHHHH		52.6926320211
218 (in isoform 1)Ubiquitination-52.6921906983
220AcetylationEKYSQKEDKYEEEIK
HHHHCCHHHHHHHHH		56.50-
221MethylationKYSQKEDKYEEEIKI
HHHCCHHHHHHHHHH		40.6819608861
221AcetylationKYSQKEDKYEEEIKI
HHHCCHHHHHHHHHH		40.6823749302
221UbiquitinationKYSQKEDKYEEEIKI
HHHCCHHHHHHHHHH		40.6819608861
222PhosphorylationYSQKEDKYEEEIKIL
HHCCHHHHHHHHHHH		55.6928152594
223 (in isoform 2)Ubiquitination-63.0321890473
227UbiquitinationDKYEEEIKILTDKLK
HHHHHHHHHHHHHHH		6.51-
228 (in isoform 2)Acetylation-4.26-
228 (in isoform 2)Ubiquitination-4.2621890473
230PhosphorylationEEEIKILTDKLKEAE
HHHHHHHHHHHHHHH		51.3422817901
232UbiquitinationEIKILTDKLKEAETR
HHHHHHHHHHHHHHH		7.25-
2322-HydroxyisobutyrylationEIKILTDKLKEAETR
HHHHHHHHHHHHHHH		7.25-
232AcetylationEIKILTDKLKEAETR
HHHHHHHHHHHHHHH		7.2526822725
234UbiquitinationKILTDKLKEAETRAE
HHHHHHHHHHHHHHH		63.27-
234 (in isoform 2)Phosphorylation-63.27-
234 (in isoform 5)Phosphorylation-63.27-
2342-HydroxyisobutyrylationKILTDKLKEAETRAE
HHHHHHHHHHHHHHH		63.27-
235 (in isoform 4)Phosphorylation-23.1330108239
235 (in isoform 3)Phosphorylation-23.1330108239
238PhosphorylationDKLKEAETRAEFAER
HHHHHHHHHHHHHHH		24.5126437602
241 (in isoform 2)Phosphorylation-9.2621955146
241 (in isoform 5)Phosphorylation-9.2621955146
246PhosphorylationRAEFAERSVAKLEKT
HHHHHHHHHHHHHHH		7.3426437602
249AcetylationFAERSVAKLEKTIDD
HHHHHHHHHHHHHHH		6.1823749302
249UbiquitinationFAERSVAKLEKTIDD
HHHHHHHHHHHHHHH		6.18-
252PhosphorylationRSVAKLEKTIDDLED
HHHHHHHHHHHHHHH		21.9115302935
252UbiquitinationRSVAKLEKTIDDLED
HHHHHHHHHHHHHHH		21.91-
252AcetylationRSVAKLEKTIDDLED
HHHHHHHHHHHHHHH		21.9126051181
253PhosphorylationSVAKLEKTIDDLEDE
HHHHHHHHHHHHHHH		6.0124692096
262PhosphorylationDDLEDELYAQKLKYK
HHHHHHHHHHHHHHH		16.8022673903
265UbiquitinationEDELYAQKLKYKAIS
HHHHHHHHHHHHHHH		4.95-
268PhosphorylationLYAQKLKYKAISEEL
HHHHHHHHHHHHHHH		37.34-
269UbiquitinationYAQKLKYKAISEELD
HHHHHHHHHHHHHHH		13.88-
272PhosphorylationKLKYKAISEELDHAL
HHHHHHHHHHHHHHH		57.3728348404
282SulfoxidationLDHALNDMTSI----
HHHHHHHHCCC----		26.5730846556
283PhosphorylationDHALNDMTSI-----
HHHHHHHCCC-----		21.4723663014
284PhosphorylationHALNDMTSI------
HHHHHHCCC------		4.8722617229
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 TPM3_HUMAN !!
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference

Oops, there are no descriptions of PTM sites of TPM3_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 TPM3_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KXDL1_HUMANKXD1physical
16189514
TFPT_HUMANTFPTphysical
16189514
TPM3_HUMANTPM3physical
7568216
TPM4_HUMANTPM4physical
22939629
TRAP1_HUMANTRAP1physical
21988832
FAS_HUMANFASNphysical
22863883
FKBP4_HUMANFKBP4physical
22863883
FKBP5_HUMANFKBP5physical
22863883
MAGD2_HUMANMAGED2physical
22863883
TPM3_HUMANTPM3physical
25416956
TRIP6_HUMANTRIP6physical
25416956
MD1L1_HUMANMAD1L1physical
25416956
TLK1_HUMANTLK1physical
25416956
MS18B_HUMANOIP5physical
25416956
BL1S6_HUMANBLOC1S6physical
25416956
TFPT_HUMANTFPTphysical
25416956
CCHCR_HUMANCCHCR1physical
25416956
THAP1_HUMANTHAP1physical
25416956
CC146_HUMANCCDC146physical
25416956
KXDL1_HUMANKXD1physical
25416956
C102B_HUMANCCDC102Bphysical
25416956
CC114_HUMANCCDC114physical
25416956
SYCE1_HUMANSYCE1physical
25416956
IKIP_HUMANIKBIPphysical
25416956
CA216_HUMANC1orf216physical
25416956
LCA5L_HUMANLCA5Lphysical
25416956
FAM9C_HUMANFAM9Cphysical
25416956
MESH1_HUMANHDDC3physical
25416956
LURA1_HUMANLURAP1physical
25416956
ACTN2_HUMANACTN2physical
26344197
SAHH2_HUMANAHCYL1physical
26344197
AT1A1_HUMANATP1A1physical
26344197
KCRB_HUMANCKBphysical
26344197
KCRU_HUMANCKMT1Bphysical
26344197
COX5A_HUMANCOX5Aphysical
26344197
CY1_HUMANCYC1physical
26344197
OSTF1_HUMANOSTF1physical
26344197
MD1L1_HUMANMAD1L1physical
21516116
IMP3_HUMANIMP3physical
28514442
CACO1_HUMANCALCOCO1physical
28514442
JUN_HUMANJUNphysical
28514442
MET2B_HUMANMETTL2Bphysical
28514442
JIP4_HUMANSPAG9physical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
609284Nemaline myopathy 1 (NEM1)
188550Thyroid papillary carcinoma (TPC)
255310Myopathy, congenital, with fiber-type disproportion (CFTD)
609284Cap myopathy 1 (CAPM1)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPM3_HUMAN

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Related Literatures of Post-Translational Modification
Acetylation
ReferencePubMed
"Lysine acetylation targets protein complexes and co-regulates majorcellular functions.";
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.,Olsen J.V., Mann M.;
Science 325:834-840(2009).
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-12, AND MASS SPECTROMETRY.
Phosphorylation
ReferencePubMed
"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 THR-252, AND MASSSPECTROMETRY.
"Large-scale characterization of HeLa cell nuclear phosphoproteins.";
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J.,Li J., Cohn M.A., Cantley L.C., Gygi S.P.;
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-252, AND MASSSPECTROMETRY.
"Global survey of phosphotyrosine signaling identifies oncogenickinases in lung cancer.";
Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J.,Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L.,Mitchell J., Wetzel R., Macneill J., Ren J.M., Yuan J.,Bakalarski C.E., Villen J., Kornhauser J.M., Smith B., Li D., Zhou X.,Gygi S.P., Gu T.-L., Polakiewicz R.D., Rush J., Comb M.J.;
Cell 131:1190-1203(2007).
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-162, AND MASSSPECTROMETRY.

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