Search Results
Overview
| Uniprot ID | Q9NZR1 |
|---|---|
| Protein Name | Tropomodulin-2 |
| Gene Name | TMOD2 |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 101 | KGRVFIPKEKPIETR |
| 13 | QKELEKYKNIDEDEL |
| 171 | RNVVKGEKVKPVFEE |
| 336 | RVAAAITKNNDLVRK |
| 81 | EKEALEQKDREDFVP |
Function
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
10
MALPFQKELE
20
KYKNIDEDEL
30
LGKLSEEELK
40
QLENVLDDLD
50
PESAMLPAGF
60
RQKDQTQKAA
70
TGPFDREHLL
80
MYLEKEALEQ
90
KDREDFVPFT
100
GEKKGRVFIP
110
KEKPIETRKE
120
EKVTLDPELE
130
EALASASDTE
140
LYDLAAVLGV
150
HNLLNNPKFD
160
EETANNKGGK
170
GPVRNVVKGE
180
KVKPVFEEPP
190
NPTNVEISLQ
200
QMKANDPSLQ
210
EVNLNNIKNI
220
PIPTLREFAK
230
ALETNTHVKK
240
FSLAATRSND
250
PVAIAFADML
260
KVNKTLTSLN
270
IESNFITGTG
280
ILALVEALKE
290
NDTLTEIKID
300
NQRQQLGTAV
310
EMEIAQMLEE
320
NSRILKFGYQ
330
FTKQGPRTRV
340
AAAITKNNDL
350
VRKKRVEADR
R
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005856 | cytoskeleton |
| Cellular Component | GO:0030016 | myofibril |
| Cellular Component | GO:0005865 | striated muscle thin filament |
| Molecular Function | GO:0003779 | actin binding |
| Molecular Function | GO:0005523 | tropomyosin binding |
| Biological Process | GO:0007015 | actin filament organization |
| Biological Process | GO:0006936 | muscle contraction |
| Biological Process | GO:0030239 | myofibril assembly |
| Biological Process | GO:0007399 | nervous system development |
| Biological Process | GO:0051694 | pointed-end actin filament capping |
Reference
[1] Shi CM, Wang QC, Li XL, Yang YH, Tang XY et al.. Global Profiling of Protein Lactylation in Human Hippocampi.. Proteomics Clin Appl 19(2):e202400061. 2025 Mar. PMID: 39610256.