Search Results
Overview
| Uniprot ID | H0VYG3 |
|---|---|
| Protein Name | Prelamin-A/C |
| Gene Name | LMNA |
| Organism | Cavia porcellus |
Kla Sites from experimental identification
| Position | Flanking peptide |
|---|---|
| 380 | GSITKKRKLEATESR |
Function
Prelamin-A/C can accelerate smooth muscle cell senescence. It acts to disrupt mitosis and induce DNA damage in vascular smooth muscle cells (VSMCs), leading to mitotic failure, genomic instability, and premature senescence
Protein Sequence
10
METPSQRRAT
20
RSGAQATSTP
30
LSPTRITRLQ
40
EKEDLQELND
50
RLAVYIDRVR
60
SLETENAGLR
70
LRITESEEVV
80
SREVSGIKAA
90
YEAELGDARK
100
TLDSVAKERA
110
RLQLELGKVR
120
EEFKELKARN
130
TKKEGDLMAA
140
QARLKDLEAL
150
LNSKEAALST
160
ALSEKRTLES
170
ELHDLRGQVA
180
KELRETKRRH
190
ETRLVEIDNG
200
KQREFESRLA
210
DALQELRAQH
220
EDQVEQYKKE
230
LEKTYSAKLD
240
NARQSAERNS
250
NLVGAAHEEL
260
QQSRIRIDSL
270
SAQLSQLQKQ
280
LAAKEAKLRD
290
LEDSLARERD
300
TSRRLLADKE
310
REMADMRARM
320
QQQLDEYQEL
330
LDIKLALDME
340
IHAYRKLLEG
350
EEERLRLSPS
360
PTSQQRSRGR
370
TSSHSSQTHG
380
SGGSITKKRK
390
LEATESRSSF
400
SQHARTSGRV
410
AVEEVDEEGK
420
FVRLRNKSNE
430
DQSMGNWQIK
440
RQNGDDPLLT
450
YRFPPKFTLK
460
AGQVVTIWAS
470
GAGATHSPPT
480
DLVWKAQNTW
490
GCGNSLRTAL
500
INSTGEEVAM
510
RKLVRSVTVV
520
EDDEDEDGDD
530
LLHHHHGSHC
540
SSSGDPAEYN
550
LRSRTVLCGT
560
CGQPADKASA
570
SSSAAQLGGS
580
ISSGSSASSV
590
TVTRSYRSVG
600
GSGGGSFGDN
610
LVTRSYLLGN
620
SRARTQSPQN
CSIM
Gene Ontology
| Classification | GO ID | Description |
|---|---|---|
| Cellular Component | GO:0005638 | lamin filament |
| Cellular Component | GO:0016363 | nuclear matrix |
| Cellular Component | GO:0031965 | nuclear membrane |
| Cellular Component | GO:0016607 | nuclear speck |
| Cellular Component | GO:0035861 | site of double-strand break |
| Molecular Function | GO:0005200 | structural constituent of cytoskeleton |
| Molecular Function | GO:0160123 | structural constituent of nuclear lamina |
| Biological Process | GO:0071456 | cellular response to hypoxia |
| Biological Process | GO:1990683 | DNA double-strand break attachment to nuclear envelope |
| Biological Process | GO:0006303 | double-strand break repair via nonhomologous end joining |
| Biological Process | GO:0030951 | establishment or maintenance of microtubule cytoskeleton polarity |
| Biological Process | GO:0031507 | heterochromatin formation |
| Biological Process | GO:1903243 | negative regulation of cardiac muscle hypertrophy in response to stress |
| Biological Process | GO:0008285 | negative regulation of cell population proliferation |
| Biological Process | GO:0006998 | nuclear envelope organization |
| Biological Process | GO:0007097 | nuclear migration |
| Biological Process | GO:0051664 | nuclear pore localization |
| Biological Process | GO:0090435 | protein localization to nuclear envelope |
| Biological Process | GO:0030334 | regulation of cell migration |
Reference
[1] Feng J, Chen X, Li R, Xie Y, Zhang X et al.. Lactylome analysis reveals potential target modified proteins in the retina of form-deprivation myopia.. iScience 27(9):110606. 2024 Sep 20. PMID: 39246443.