Overview
| Uniprot ID | Q9NRL3 |
|---|
| Protein Name | Striatin-4 |
|---|
| Gene Name | STRN4 |
|---|
| Organism | Homo sapiens |
|---|
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 475 |
QKAVTAKKNAALDVE |
Function
Calmodulin-binding scaffolding protein which is the center of the striatin-interacting phosphatase and kinase (STRIPAK) complexes (PubMed:18782753, PubMed:32640226). STRIPAK complexes have critical roles in protein (de)phosphorylation and are regulators of multiple signaling pathways including Hippo, MAPK, nuclear receptor and cytoskeleton remodeling (PubMed:32640226). Different types of STRIPAK complexes are involved in a variety of biological processes such as cell growth, differentiation, apoptosis, metabolism and immune regulation (Probable). Key regulator of the expanded Hippo signaling pathway by interacting and allowing the inhibition of MAP4K kinases by the STRIPAK complex (PubMed:32640226)
Protein Sequence
10
MMEERAAAAV
20
AAAASSCRPL
30
GSGAGPGPTG
40
AAPVSAPAPG
50
PGPAGKGGGG
60
GGSPGPTAGP
70
EPLSLPGILH
80
FIQHEWARFE
90
AEKARWEAER
100
AELQAQVAFL
110
QGERKGQENL
120
KTDLVRRIKM
130
LEYALKQERA
140
KYHKLKFGTD
150
LNQGEKKADV
160
SEQVSNGPVE
170
SVTLENSPLV
180
WKEGRQLLRQ
190
YLEEVGYTDT
200
ILDMRSKRVR
210
SLLGRSLELN
220
GAVEPSEGAP
230
RAPPGPAGLS
240
GGESLLVKQI
250
EEQIKRNAAG
260
KDGKERLGGS
270
VLGQIPFLQN
280
CEDEDSDEDD
290
ELDSVQHKKQ
300
RVKLPSKALV
310
PEMEDEDEED
320
DSEDAINEFD
330
FLGSGEDGEG
340
APDPRRCTVD
350
GSPHELESRR
360
VKLQGILADL
370
RDVDGLPPKV
380
TGPPPGTPQP
390
RPHEDVFIMD
400
TIGGGEVSLG
410
DLADLTVTND
420
NDLSCDLSDS
430
KDAFKKTWNP
440
KFTLRSHYDG
450
IRSLAFHHSQ
460
SALLTASEDG
470
TLKLWNLQKA
480
VTAKKNAALD
490
VEPIHAFRAH
500
RGPVLAVAMG
510
SNSEYCYSGG
520
ADACIHSWKI
530
PDLSMDPYDG
540
YDPSVLSHVL
550
EGHGDAVWGL
560
AFSPTSQRLA
570
SCSADGTVRI
580
WDPSSSSPAC
590
LCTFPTASEH
600
GVPTSVAFTS
610
TEPAHIVASF
620
RSGDTVLYDM
630
EVGSALLTLE
640
SRGSSGPTQI
650
NQVVSHPNQP
660
LTITAHDDRG
670
IRFLDNRTGK
680
PVHSMVAHLD
690
AVTCLAVDPN
700
GAFLMSGSHD
710
CSLRLWSLDN
720
KTCVQEITAH
730
RKKHEEAIHA
740
VACHPSKALI
750
ASAGADALAK
VFV
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0005737 |
cytoplasm |
| Cellular Component |
GO:0030425 |
dendrite |
| Cellular Component |
GO:0043197 |
dendritic spine |
| Cellular Component |
GO:0090443 |
FAR/SIN/STRIPAK complex |
| Cellular Component |
GO:0098982 |
GABA-ergic synapse |
| Cellular Component |
GO:0098978 |
glutamatergic synapse |
| Cellular Component |
GO:0043025 |
neuronal cell body |
| Cellular Component |
GO:0098794 |
postsynapse |
| Molecular Function |
GO:0070016 |
armadillo repeat domain binding |
| Molecular Function |
GO:0005516 |
calmodulin binding |
| Molecular Function |
GO:0051721 |
protein phosphatase 2A binding |
| Molecular Function |
GO:0044877 |
protein-containing complex binding |
| Molecular Function |
GO:0030674 |
protein-macromolecule adaptor activity |
| Biological Process |
GO:0035331 |
negative regulation of hippo signaling |
| Biological Process |
GO:0035330 |
regulation of hippo signaling |
| Biological Process |
GO:0099159 |
regulation of modification of postsynaptic structure |
Reference
[1] Wu Q, Li Z, Gong T, Zheng X, Zhou X et al.. Porphyromonas gingivalis infection induces lysine lactylation reprogramming in human umbilical vein endothelial cells.. Front Cell Infect Microbiol 16:1706727. 2026. PMID: 41696360.