TPM1_HUMAN - dbPTM
TPM1_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPM1_HUMAN
UniProt AC P09493
Protein Name Tropomyosin alpha-1 chain
Gene Name TPM1
Organism Homo sapiens (Human).
Sequence Length 284
Subcellular Localization Cytoplasm, cytoskeleton . Associates with F-actin stress fibers.
Protein Description Binds to actin filaments in muscle and non-muscle cells. [PubMed: 23170982 Plays a central role, in association with the troponin complex, in the calcium dependent regulation of vertebrate striated muscle contraction]
Protein Sequence MDAIKKKMQMLKLDKENALDRAEQAEADKKAAEDRSKQLEDELVSLQKKLKGTEDELDKYSEALKDAQEKLELAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIESRAQKDEEKMEIQEIQLKEAKHIAEDADRKYEEVARKLVIIESDLERAEERAELSEGKCAELEEELKTVTNNLKSLEAQAEKYSQKEDRYEEEIKVLSDKLKEAETRAEFAERSVTKLEKSIDDLEDELYAQKLKYKAISEELDHALNDMTSI
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
1Acetylation-------MDAIKKKM
-------CHHHHHHH		7.683548719
4 (in isoform 5)Phosphorylation-6.1521406692
5 (in isoform 5)Phosphorylation-48.3225850435
6 (in isoform 5)Phosphorylation-47.5725850435
12AcetylationKKKMQMLKLDKENAL
HHHHHHHHCCHHHHH		49.6622632959
12UbiquitinationKKKMQMLKLDKENAL
HHHHHHHHCCHHHHH		49.6619608861
15AcetylationMQMLKLDKENALDRA
HHHHHCCHHHHHHHH		64.4054426095
15UbiquitinationMQMLKLDKENALDRA
HHHHHCCHHHHHHHH		64.40-
16 (in isoform 5)Phosphorylation-47.6128258704
24 (in isoform 2)Phosphorylation-43.4428270605
29AcetylationAEQAEADKKAAEDRS
HHHHHHHHHHHHHHH		51.8923236377
29UbiquitinationAEQAEADKKAAEDRS
HHHHHHHHHHHHHHH		51.89-
30UbiquitinationEQAEADKKAAEDRSK
HHHHHHHHHHHHHHH		54.07-
30 (in isoform 3)Ubiquitination-54.07-
31 (in isoform 2)Phosphorylation-23.0921815630
37UbiquitinationKAAEDRSKQLEDELV
HHHHHHHHHHHHHHH		60.85-
37 (in isoform 3)Ubiquitination-60.85-
37MalonylationKAAEDRSKQLEDELV
HHHHHHHHHHHHHHH		60.8526320211
44 (in isoform 5)Phosphorylation-5.1628270605
45PhosphorylationQLEDELVSLQKKLKG
HHHHHHHHHHHHHCC		37.3925849741
45 (in isoform 10)Phosphorylation-37.3927251275
48AcetylationDELVSLQKKLKGTED
HHHHHHHHHHCCCHH		66.4219863131
48UbiquitinationDELVSLQKKLKGTED
HHHHHHHHHHCCCHH		66.42-
48 (in isoform 3)Ubiquitination-66.42-
48MalonylationDELVSLQKKLKGTED
HHHHHHHHHHCCCHH		66.4226320211
51 (in isoform 5)Phosphorylation-73.0721815630
53PhosphorylationLQKKLKGTEDELDKY
HHHHHCCCHHHHHHH		38.3826437602
59UbiquitinationGTEDELDKYSEALKD
CCHHHHHHHHHHHHH		64.40-
60PhosphorylationTEDELDKYSEALKDA
CHHHHHHHHHHHHHH		16.0621406692
61PhosphorylationEDELDKYSEALKDAQ
HHHHHHHHHHHHHHH		23.3321406692
62 (in isoform 2)Ubiquitination-55.7321906983
70 (in isoform 6)Phosphorylation-34.8726657352
70 (in isoform 7)Phosphorylation-34.8726657352
70 (in isoform 8)Phosphorylation-34.8726657352
76AcetylationEKLELAEKKATDAEA
HHHHHHHHHCCHHHH		41.94-
77UbiquitinationKLELAEKKATDAEAD
HHHHHHHHCCHHHHH		48.28-
79PhosphorylationELAEKKATDAEADVA
HHHHHHCCHHHHHHH		44.6223403867
82 (in isoform 5)Ubiquitination-48.4921906983
87PhosphorylationDAEADVASLNRRIQL
HHHHHHHHHHHHHHH		26.4819664994
87 (in isoform 10)Phosphorylation-26.4827251275
87 (in isoform 6)Phosphorylation-26.4827251275
87 (in isoform 7)Phosphorylation-26.4827251275
87 (in isoform 8)Phosphorylation-26.4827251275
108PhosphorylationRAQERLATALQKLEE
HHHHHHHHHHHHHHH		32.2824692096
112AcetylationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH		59.7322632949
112UbiquitinationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH		59.7319608861
118AcetylationQKLEEAEKAADESER
HHHHHHHHHHHHHHH		56.7988205
118UbiquitinationQKLEEAEKAADESER
HHHHHHHHHHHHHHH		56.7921906983
118 (in isoform 1)Ubiquitination-56.7921906983
118 (in isoform 3)Ubiquitination-56.7921906983
118 (in isoform 4)Ubiquitination-56.7921906983
118 (in isoform 6)Ubiquitination-56.7921906983
123PhosphorylationAEKAADESERGMKVI
HHHHHHHHHHHHHHH		32.8926437602
128MalonylationDESERGMKVIESRAQ
HHHHHHHHHHHHHHH		42.7726320211
132PhosphorylationRGMKVIESRAQKDEE
HHHHHHHHHHHCCHH		23.0722210691
136MalonylationVIESRAQKDEEKMEI
HHHHHHHCCHHHHHH		67.1526320211
141SulfoxidationAQKDEEKMEIQEIQL
HHCCHHHHHHHHHHH		6.5821406390
146 (in isoform 2)Phosphorylation-3.1322210691
149AcetylationEIQEIQLKEAKHIAE
HHHHHHHHHHHHHHH		38.9720167786
149 (in isoform 3)Ubiquitination-38.97-
150 (in isoform 2)Phosphorylation-72.10-
152 (in isoform 3)Ubiquitination-36.31-
152AcetylationEIQLKEAKHIAEDAD
HHHHHHHHHHHHHHH		36.3126210075
160MethylationHIAEDADRKYEEVAR
HHHHHHHHHHHHHHH		45.22115918801
161MethylationIAEDADRKYEEVARK
HHHHHHHHHHHHHHH		58.52-
161AcetylationIAEDADRKYEEVARK
HHHHHHHHHHHHHHH		58.5223749302
162PhosphorylationAEDADRKYEEVARKL
HHHHHHHHHHHHHHH		20.4428796482
168UbiquitinationKYEEVARKLVIIESD
HHHHHHHHHHHHHHH		37.05-
168 (in isoform 3)Ubiquitination-37.05-
174PhosphorylationRKLVIIESDLERAEE
HHHHHHHHHHHHHHH		36.7730266825
186PhosphorylationAEERAELSEGKCAEL
HHHHHHHCCCHHHHH		35.4926437602
196 (in isoform 2)Phosphorylation-46.3128355574
199PhosphorylationELEEELKTVTNNLKS
HHHHHHHHHHHHHHH		45.2323312004
201PhosphorylationEEELKTVTNNLKSLE
HHHHHHHHHHHHHHH		24.5023312004
205MalonylationKTVTNNLKSLEAQAE
HHHHHHHHHHHHHHH		55.9326320211
206PhosphorylationTVTNNLKSLEAQAEK
HHHHHHHHHHHHHHH		34.3126657352
213AcetylationSLEAQAEKYSQKEDR
HHHHHHHHHHCCHHH		53.90-
213UbiquitinationSLEAQAEKYSQKEDR
HHHHHHHHHHCCHHH		53.90-
213 (in isoform 2)Phosphorylation-53.9021712546
213 (in isoform 3)Acetylation-53.9019608861
213 (in isoform 3)Ubiquitination-53.90-
213 (in isoform 10)Acetylation-53.9019608861
213 (in isoform 4)Acetylation-53.9019608861
213 (in isoform 8)Acetylation-53.9019608861
214PhosphorylationLEAQAEKYSQKEDRY
HHHHHHHHHCCHHHH		14.0826657352
214 (in isoform 10)Phosphorylation-14.0828270605
214 (in isoform 3)Phosphorylation-14.0828270605
214 (in isoform 4)Phosphorylation-14.0828270605
214 (in isoform 8)Phosphorylation-14.0828270605
215PhosphorylationEAQAEKYSQKEDRYE
HHHHHHHHCCHHHHH		45.9326657352
215 (in isoform 10)Phosphorylation-45.9326657352
215 (in isoform 3)Phosphorylation-45.9326657352
215 (in isoform 4)Phosphorylation-45.9326657352
215 (in isoform 8)Phosphorylation-45.9326657352
221PhosphorylationYSQKEDRYEEEIKVL
HHCCHHHHHHHHHHH		39.7626437602
221 (in isoform 2)Phosphorylation-39.7621712546
226UbiquitinationDRYEEEIKVLSDKLK
HHHHHHHHHHHHHHH		40.16-
226 (in isoform 3)Ubiquitination-40.16-
229PhosphorylationEEEIKVLSDKLKEAE
HHHHHHHHHHHHHHH		35.3722673903
229 (in isoform 10)Phosphorylation-35.37-
231UbiquitinationEIKVLSDKLKEAETR
HHHHHHHHHHHHHHH		59.07-
233UbiquitinationKVLSDKLKEAETRAE
HHHHHHHHHHHHHHH		61.70-
237PhosphorylationDKLKEAETRAEFAER
HHHHHHHHHHHHHHH		42.0826437602
245PhosphorylationRAEFAERSVTKLEKS
HHHHHHHHHHHHHHC		26.1626437602
247PhosphorylationEFAERSVTKLEKSID
HHHHHHHHHHHHCHH		31.0326437602
248UbiquitinationFAERSVTKLEKSIDD
HHHHHHHHHHHCHHH		53.12-
251 (in isoform 3)Ubiquitination-64.25-
251AcetylationRSVTKLEKSIDDLED
HHHHHHHHCHHHHHH		64.2526051181
252PhosphorylationSVTKLEKSIDDLEDE
HHHHHHHCHHHHHHH		23.1322777824
252 (in isoform 9)Phosphorylation-23.1328355574
252 (in isoform 10)Phosphorylation-23.1327251275
252 (in isoform 3)Phosphorylation-23.1328355574
252 (in isoform 7)Phosphorylation-23.1328355574
252 (in isoform 8)Phosphorylation-23.1328355574
261PhosphorylationDDLEDELYAQKLKYK
HHHHHHHHHHHHHHH		12.6319764811
264UbiquitinationEDELYAQKLKYKAIS
HHHHHHHHHHHHHHH		38.48-
267PhosphorylationLYAQKLKYKAISEEL
HHHHHHHHHHHHHHH		18.98-
268UbiquitinationYAQKLKYKAISEELD
HHHHHHHHHHHHHHH		37.34-
269 (in isoform 3)Phosphorylation-13.8821712546
269 (in isoform 7)Phosphorylation-13.8821712546
269 (in isoform 8)Phosphorylation-13.8821712546
269 (in isoform 9)Phosphorylation-13.8821712546
271PhosphorylationKLKYKAISEELDHAL
HHHHHHHHHHHHHHH		29.8528348404
277 (in isoform 3)Phosphorylation-14.0221712546
277 (in isoform 7)Phosphorylation-14.0221712546
277 (in isoform 8)Phosphorylation-14.0221712546
277 (in isoform 9)Phosphorylation-14.0221712546
282PhosphorylationDHALNDMTSI-----
HHHHHHHCCC-----		26.5723663014
282 (in isoform 10)Phosphorylation-26.5722673903
283PhosphorylationHALNDMTSI------
HHHHHHCCC------		21.4722617229
283 (in isoform 10)Phosphorylation-21.47278975
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
61SPhosphorylationKinasePK3CAP42336
PhosphoELM
283SPhosphorylationKinaseDAPK1P53355
Uniprot
Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
283SOxidation

17895359
283SPhosphorylation

17895359
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 TPM1_HUMAN !!
Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
KXDL1_HUMANKXD1physical
16189514
TPM1_HUMANTPM1physical
7568216
TNNT2_HUMANTNNT2physical
6746613
TPM1_HUMANTPM1physical
3857586
TPM2_HUMANTPM2physical
3857586
CNN1_HUMANCNN1physical
2455687
TPM2_HUMANTPM2physical
22939629
TPM4_HUMANTPM4physical
22939629
ZYX_HUMANZYXphysical
22939629
TPM3_HUMANTPM3physical
22939629
ABI2_HUMANABI2physical
22863883
DP13B_HUMANAPPL2physical
22863883
CDC37_HUMANCDC37physical
22863883
ETFA_HUMANETFAphysical
22863883
FOXK1_HUMANFOXK1physical
22863883
ENPL_HUMANHSP90B1physical
22863883
SHOT1_HUMANKIAA1598physical
22863883
OGA_HUMANMGEA5physical
22863883
PP6R3_HUMANPPP6R3physical
22863883
CHIP_HUMANSTUB1physical
22863883
TPM4_HUMANTPM4physical
25416956
MD1L1_HUMANMAD1L1physical
25416956
TFPT_HUMANTFPTphysical
25416956
KXDL1_HUMANKXD1physical
25416956
SYCE1_HUMANSYCE1physical
25416956
CA216_HUMANC1orf216physical
25416956
CAGE1_HUMANCAGE1physical
25416956
GOGA3_HUMANGOLGA3physical
26186194
TPM3_HUMANTPM3physical
26186194
TPM4_HUMANTPM4physical
26186194
TPM2_HUMANTPM2physical
26186194
CROCC_HUMANCROCCphysical
26186194
EXOC4_HUMANEXOC4physical
26186194
NEMO_HUMANIKBKGphysical
26186194
MD1L1_HUMANMAD1L1physical
26186194
KLH21_HUMANKLHL21physical
26186194
C102A_HUMANCCDC102Aphysical
26186194
CNTLN_HUMANCNTLNphysical
26186194
RUFY2_HUMANRUFY2physical
26186194
HOME1_HUMANHOMER1physical
26186194
KXDL1_HUMANKXD1physical
26186194
JUND_HUMANJUNDphysical
26186194
DLG5_HUMANDLG5physical
26186194
NUCG_HUMANENDOGphysical
26186194
SCLT1_HUMANSCLT1physical
26186194
ACTN1_HUMANACTN1physical
26344197
KCRB_HUMANCKBphysical
26344197
COX5A_HUMANCOX5Aphysical
26344197
MYH4_HUMANMYH4physical
26344197
MYH6_HUMANMYH6physical
26344197
TPM3_HUMANTPM3physical
26344197
TPM2_HUMANTPM2physical
28514442
KLH21_HUMANKLHL21physical
28514442
KXDL1_HUMANKXD1physical
28514442
EXOC4_HUMANEXOC4physical
28514442
DLG5_HUMANDLG5physical
28514442
RUFY2_HUMANRUFY2physical
28514442
SCLT1_HUMANSCLT1physical
28514442
C102A_HUMANCCDC102Aphysical
28514442
MD1L1_HUMANMAD1L1physical
28514442
CROCC_HUMANCROCCphysical
28514442
NEMO_HUMANIKBKGphysical
28514442
CNTLN_HUMANCNTLNphysical
28514442
JUND_HUMANJUNDphysical
28514442
TPM4_HUMANTPM4physical
28514442
JIP4_HUMANSPAG9physical
28514442
HOME1_HUMANHOMER1physical
28514442
NUCG_HUMANENDOGphysical
28514442
Drug and Disease Associations
Kegg Disease
There are no disease associations of PTM sites.
OMIM Disease
115196Cardiomyopathy, familial hypertrophic 3 (CMH3)
611878Cardiomyopathy, dilated 1Y (CMD1Y)
611878Left ventricular non-compaction 9 (LVNC9)
Kegg Drug
There are no disease associations of PTM sites.
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPM1_HUMAN

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Related Literatures of Post-Translational Modification
Phosphorylation
ReferencePubMed
"DAP kinase mediates the phosphorylation of tropomyosin-1 downstreamof the ERK pathway, which regulates the formation of stress fibers inresponse to oxidative stress.";
Houle F., Poirier A., Dumaresq J., Huot J.;
J. Cell Sci. 120:3666-3677(2007).
Cited for: PHOSPHORYLATION AT SER-283, AND MUTAGENESIS OF SER-283.

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