TPM2_HUMAN - dbPTM
TPM2_HUMAN - PTM Information in dbPTM
Basic Information of Protein
UniProt ID TPM2_HUMAN
UniProt AC P07951
Protein Name Tropomyosin beta chain
Gene Name TPM2
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. 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. The non-muscle isoform may have a role in agonist-mediated receptor internalization..
Protein Sequence MDAIKKKMQMLKLDKENAIDRAEQAEADKKQAEDRCKQLEEEQQALQKKLKGTEDEVEKYSESVKEAQEKLEQAEKKATDAEADVASLNRRIQLVEEELDRAQERLATALQKLEEAEKAADESERGMKVIENRAMKDEEKMELQEMQLKEAKHIAEDSDRKYEEVARKLVILEGELERSEERAEVAESKCGDLEEELKIVTNNLKSLEAQADKYSTKEDKYEEEIKLLEEKLKEAETRAEFAERSVAKLEKTIDDLEDEVYAQKMKYKAISEELDNALNDITSL
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
7.68-
12AcetylationKKKMQMLKLDKENAI
HHHHHHHHCCHHHHH
49.6622632943
12UbiquitinationKKKMQMLKLDKENAI
HHHHHHHHCCHHHHH
49.66-
29AcetylationAEQAEADKKQAEDRC
HHHHHHHHHHHHHHH
54.567671341
30UbiquitinationEQAEADKKQAEDRCK
HHHHHHHHHHHHHHH
56.1121906983
30 (in isoform 1)Ubiquitination-56.1121890473
30 (in isoform 2)Ubiquitination-56.1121890473
36GlutathionylationKKQAEDRCKQLEEEQ
HHHHHHHHHHHHHHH
5.2222555962
37UbiquitinationKQAEDRCKQLEEEQQ
HHHHHHHHHHHHHHH
59.83-
37 (in isoform 2)Ubiquitination-59.83-
48AcetylationEEQQALQKKLKGTED
HHHHHHHHHHCCCHH
62.017668171
48UbiquitinationEEQQALQKKLKGTED
HHHHHHHHHHCCCHH
62.0121906983
48 (in isoform 1)Ubiquitination-62.0121890473
48 (in isoform 2)Ubiquitination-62.0121890473
51UbiquitinationQALQKKLKGTEDEVE
HHHHHHHCCCHHHHH
73.0721906983
51 (in isoform 1)Ubiquitination-73.0721890473
51 (in isoform 2)Ubiquitination-73.0721890473
53PhosphorylationLQKKLKGTEDEVEKY
HHHHHCCCHHHHHHH
38.3824692096
59UbiquitinationGTEDEVEKYSESVKE
CCHHHHHHHHHHHHH
60.29-
60PhosphorylationTEDEVEKYSESVKEA
CHHHHHHHHHHHHHH
12.2626437602
61PhosphorylationEDEVEKYSESVKEAQ
HHHHHHHHHHHHHHH
34.1726437602
63PhosphorylationEVEKYSESVKEAQEK
HHHHHHHHHHHHHHH
32.3326437602
65UbiquitinationEKYSESVKEAQEKLE
HHHHHHHHHHHHHHH
57.5221906983
65 (in isoform 1)Ubiquitination-57.5221890473
65 (in isoform 2)Ubiquitination-57.5221890473
76AcetylationEKLEQAEKKATDAEA
HHHHHHHHHHHHHHH
51.207668181
77UbiquitinationKLEQAEKKATDAEAD
HHHHHHHHHHHHHHH
48.28-
79PhosphorylationEQAEKKATDAEADVA
HHHHHHHHHHHHHHH
44.6223403867
82 (in isoform 3)Ubiquitination-48.4921890473
87PhosphorylationDAEADVASLNRRIQL
HHHHHHHHHHHHHHH
26.4819664994
108PhosphorylationRAQERLATALQKLEE
HHHHHHHHHHHHHHH
32.2824692096
112AcetylationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH
59.7322632937
112UbiquitinationRLATALQKLEEAEKA
HHHHHHHHHHHHHHH
59.73-
112 (in isoform 2)Ubiquitination-59.73-
113 (in isoform 3)Ubiquitination-4.6621890473
118AcetylationQKLEEAEKAADESER
HHHHHHHHHHHHHHH
56.7988209
118UbiquitinationQKLEEAEKAADESER
HHHHHHHHHHHHHHH
56.7921906983
118 (in isoform 1)Ubiquitination-56.7921890473
118 (in isoform 2)Ubiquitination-56.7921890473
123PhosphorylationAEKAADESERGMKVI
HHHHHHHHHHHHHHH
32.8926437602
128SumoylationDESERGMKVIENRAM
HHHHHHHHHHHHHHC
42.77-
128SumoylationDESERGMKVIENRAM
HHHHHHHHHHHHHHC
42.77-
128UbiquitinationDESERGMKVIENRAM
HHHHHHHHHHHHHHC
42.77-
128 (in isoform 2)Ubiquitination-42.77-
132 (in isoform 3)Ubiquitination-26.3621890473
136UbiquitinationVIENRAMKDEEKMEL
HHHHHHCCHHHHHHH
62.09-
140AcetylationRAMKDEEKMELQEMQ
HHCCHHHHHHHHHHH
35.317684549
149AcetylationELQEMQLKEAKHIAE
HHHHHHHHHHHHHHC
38.4423236377
149UbiquitinationELQEMQLKEAKHIAE
HHHHHHHHHHHHHHC
38.4421890473
149 (in isoform 1)Ubiquitination-38.4421890473
149 (in isoform 2)Ubiquitination-38.4421890473
152AcetylationEMQLKEAKHIAEDSD
HHHHHHHHHHHCCCC
36.3126210075
152UbiquitinationEMQLKEAKHIAEDSD
HHHHHHHHHHHCCCC
36.31-
152 (in isoform 2)Ubiquitination-36.31-
158PhosphorylationAKHIAEDSDRKYEEV
HHHHHCCCCHHHHHH
30.7124692096
162PhosphorylationAEDSDRKYEEVARKL
HCCCCHHHHHHHHHH
20.4428796482
163 (in isoform 3)Phosphorylation-49.3720068231
168UbiquitinationKYEEVARKLVILEGE
HHHHHHHHHHHHHCH
37.05-
168 (in isoform 1)Ubiquitination-37.0521890473
168 (in isoform 2)Ubiquitination-37.0521890473
170 (in isoform 3)Phosphorylation-5.4227499020
174 (in isoform 3)Phosphorylation-41.1527499020
178 (in isoform 3)Phosphorylation-63.0926657352
179PhosphorylationLEGELERSEERAEVA
HHCHHHCHHHHHHHH
34.1426437602
179 (in isoform 3)Phosphorylation-34.1426657352
188PhosphorylationERAEVAESKCGDLEE
HHHHHHHHHCCCHHH
24.4126437602
190GlutathionylationAEVAESKCGDLEEEL
HHHHHHHCCCHHHHH
7.7422555962
198UbiquitinationGDLEEELKIVTNNLK
CCHHHHHHHHHHHHH
38.11-
199 (in isoform 2)Phosphorylation-7.8420068231
201PhosphorylationEEELKIVTNNLKSLE
HHHHHHHHHHHHHHH
23.1226437602
205UbiquitinationKIVTNNLKSLEAQAD
HHHHHHHHHHHHHHH
55.932190698
205 (in isoform 1)Ubiquitination-55.9321890473
205 (in isoform 2)Ubiquitination-55.93-
206PhosphorylationIVTNNLKSLEAQADK
HHHHHHHHHHHHHHH
34.3124692096
206 (in isoform 2)Phosphorylation-34.3127499020
210 (in isoform 2)Phosphorylation-40.4927499020
213AcetylationSLEAQADKYSTKEDK
HHHHHHHHCCCHHHH
44.0823236377
213UbiquitinationSLEAQADKYSTKEDK
HHHHHHHHCCCHHHH
44.08-
214PhosphorylationLEAQADKYSTKEDKY
HHHHHHHCCCHHHHH
23.3226437602
214 (in isoform 2)Phosphorylation-23.3226657352
215PhosphorylationEAQADKYSTKEDKYE
HHHHHHCCCHHHHHH
38.4525159151
215 (in isoform 2)Phosphorylation-38.4526657352
215 (in isoform 3)Ubiquitination-38.4521890473
216PhosphorylationAQADKYSTKEDKYEE
HHHHHCCCHHHHHHH
35.0526437602
216 (in isoform 3)Phosphorylation-35.0530266825
220AcetylationKYSTKEDKYEEEIKL
HCCCHHHHHHHHHHH
56.5022632931
220MethylationKYSTKEDKYEEEIKL
HCCCHHHHHHHHHHH
56.5022632931
220UbiquitinationKYSTKEDKYEEEIKL
HCCCHHHHHHHHHHH
56.50-
221PhosphorylationYSTKEDKYEEEIKLL
CCCHHHHHHHHHHHH
40.6826437602
223 (in isoform 3)Phosphorylation-63.0330266825
226UbiquitinationDKYEEEIKLLEEKLK
HHHHHHHHHHHHHHH
50.75-
226 (in isoform 3)Phosphorylation-50.7530266825
231UbiquitinationEIKLLEEKLKEAETR
HHHHHHHHHHHHHHH
56.32-
233UbiquitinationKLLEEKLKEAETRAE
HHHHHHHHHHHHHHH
66.98-
237PhosphorylationEKLKEAETRAEFAER
HHHHHHHHHHHHHHH
42.0826437602
245PhosphorylationRAEFAERSVAKLEKT
HHHHHHHHHHHHHHH
20.2426437602
248AcetylationFAERSVAKLEKTIDD
HHHHHHHHHHHHHHH
55.8330996315
248UbiquitinationFAERSVAKLEKTIDD
HHHHHHHHHHHHHHH
55.83-
251UbiquitinationRSVAKLEKTIDDLED
HHHHHHHHHHHHHHH
62.31-
251 (in isoform 2)Ubiquitination-62.3121890473
252PhosphorylationSVAKLEKTIDDLEDE
HHHHHHHHHHHHHHH
21.9124692096
252 (in isoform 2)Phosphorylation-21.9130266825
259 (in isoform 2)Phosphorylation-28.2230266825
261PhosphorylationDDLEDEVYAQKMKYK
HHHHHHHHHHHHHHH
10.9819764811
262 (in isoform 2)Phosphorylation-14.0030266825
267PhosphorylationVYAQKMKYKAISEEL
HHHHHHHHHHHHHHH
11.36-
268UbiquitinationYAQKMKYKAISEELD
HHHHHHHHHHHHHHH
33.45-
271PhosphorylationKMKYKAISEELDNAL
HHHHHHHHHHHHHHH
29.8526437602
282PhosphorylationDNALNDITSL-----
HHHHHHHHCC-----
27.1729632367
283PhosphorylationNALNDITSL------
HHHHHHHCC------
32.2024692096

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
61SPhosphorylationKinasePIK3CGP48736
Uniprot

Functions of PTM Sites
Modified Location Modified Residue Modification Function Reference
61SPhosphorylation

-
61SPhosphorylation

-

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 TPM2_HUMAN !!

Protein-Protein Interaction
Interacting Protein Gene Name Interaction Type PPI Reference Domain-Domain Interactions
TPM2_HUMANTPM2physical
7568216
RAD_HUMANRRADphysical
8557685
TPM1_HUMANTPM1physical
3857586
TPM2_HUMANTPM2physical
3857586
ACTS_HUMANACTA1physical
17194691
TPM4_HUMANTPM4physical
22939629
TPM3_HUMANTPM3physical
22939629
HECD1_HUMANHECTD1physical
22863883
ACTN1_HUMANACTN1physical
26344197
ACTN4_HUMANACTN4physical
26344197
KCRU_HUMANCKMT1Bphysical
26344197
PSMD5_HUMANPSMD5physical
26344197

Drug and Disease Associations
Kegg Disease
OMIM Disease
609285Nemaline myopathy 4 (NEM4)
108120Arthrogryposis, distal, 1A (DA1A)
609285Cap myopathy 2 (CAPM2)
601680Arthrogryposis, distal, 2B (DA2B)
Kegg Drug
DrugBank
There are no disease associations of PTM sites.
Regulatory Network of TPM2_HUMAN

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Related Literatures of Post-Translational Modification

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