Overview
| Uniprot ID | Q6WCQ1 |
| Protein Name | Myosin phosphatase Rho-interacting protein |
| Gene Name | MPRIP |
| Organism | Homo sapiens |
Kla Sites from experimental identification
| Position |
Flanking peptide |
| 161 |
QNQKKKRKVEPPTPQ |
| 200 |
AEKVPTTKSTLWQEE |
| 306 |
RRSQVIEKFEALDIE |
| 541 |
RRREGRSKTFDWAEF |
Function
Targets myosin phosphatase to the actin cytoskeleton. Required for the regulation of the actin cytoskeleton by RhoA and ROCK1. Depletion leads to an increased number of stress fibers in smooth muscle cells through stabilization of actin fibers by phosphorylated myosin. Overexpression of MRIP as well as its F-actin-binding region leads to disassembly of stress fibers in neuronal cells
Protein Sequence
10
MSAAKENPCR
20
KFQANIFNKS
30
KCQNCFKPRE
40
SHLLNDEDLT
50
QAKPIYGGWL
60
LLAPDGTDFD
70
NPVHRSRKWQ
80
RRFFILYEHG
90
LLRYALDEMP
100
TTLPQGTINM
110
NQCTDVVDGE
120
GRTGQKFSLC
130
ILTPEKEHFI
140
RAETKEIVSG
150
WLEMLMVYPR
160
TNKQNQKKKR
170
KVEPPTPQEP
180
GPAKVAVTSS
190
SSSSSSSSSI
200
PSAEKVPTTK
210
STLWQEEMRT
220
KDQPDGSSLS
230
PAQSPSQSQP
240
PAASSLREPG
250
LESKEEESAM
260
SSDRMDCGRK
270
VRVESGYFSL
280
EKTKQDLKAE
290
EQQLPPPLSP
300
PSPSTPNHRR
310
SQVIEKFEAL
320
DIEKAEHMET
330
NAVGPSPSSD
340
TRQGRSEKRA
350
FPRKRDFTNE
360
APPAPLPDAS
370
ASPLSPHRRA
380
KSLDRRSTEP
390
SVTPDLLNFK
400
KGWLTKQYED
410
GQWKKHWFVL
420
ADQSLRYYRD
430
SVAEEAADLD
440
GEIDLSACYD
450
VTEYPVQRNY
460
GFQIHTKEGE
470
FTLSAMTSGI
480
RRNWIQTIMK
490
HVHPTTAPDV
500
TSSLPEEKNK
510
SSCSFETCPR
520
PTEKQEAELG
530
EPDPEQKRSR
540
ARERRREGRS
550
KTFDWAEFRP
560
IQQALAQERV
570
GGVGPADTHE
580
PLRPEAEPGE
590
LERERARRRE
600
ERRKRFGMLD
610
ATDGPGTEDA
620
ALRMEVDRSP
630
GLPMSDLKTH
640
NVHVEIEQRW
650
HQVETTPLRE
660
EKQVPIAPVH
670
LSSEDGGDRL
680
STHELTSLLE
690
KELEQSQKEA
700
SDLLEQNRLL
710
QDQLRVALGR
720
EQSAREGYVL
730
QATCERGFAA
740
MEETHQKKIE
750
DLQRQHQREL
760
EKLREEKDRL
770
LAEETAATIS
780
AIEAMKNAHR
790
EEMERELEKS
800
QRSQISSVNS
810
DVEALRRQYL
820
EELQSVQREL
830
EVLSEQYSQK
840
CLENAHLAQA
850
LEAERQALRQ
860
CQRENQELNA
870
HNQELNNRLA
880
AEITRLRTLL
890
TGDGGGEATG
900
SPLAQGKDAY
910
ELEVLLRVKE
920
SEIQYLKQEI
930
SSLKDELQTA
940
LRDKKYASDK
950
YKDIYTELSI
960
AKAKADCDIS
970
RLKEQLKAAT
980
EALGEKSPDS
990
ATVSGYDIMK
1000
SKSNPDFLKK
1010
DRSCVTRQLR
1020
NIRSKSVIEQ
VSWDT
Gene Ontology
| Classification |
GO ID |
Description |
| Cellular Component |
GO:0015629 |
actin cytoskeleton |
| Cellular Component |
GO:0005925 |
focal adhesion |
| Molecular Function |
GO:0051015 |
actin filament binding |
| Molecular Function |
GO:0045296 |
cadherin binding |
| Molecular Function |
GO:0042802 |
identical protein binding |
Reference
[1] He J, Lai T, Zhou Z, Yang H, Lei Z et al.. Multiomics profiling reveals the involvement of protein lactylation in nonhomologous end joining pathway conferring radioresistance in lung adenocarcinoma cell.. Sci Rep 15(1):24651. 2025 Jul 9. PMID: 40634431.
[2] 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.