Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q6WCQ1 (MPRIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 91. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Myosin phosphatase Rho-interacting protein

Short name=M-RIP
Alternative name(s):
Rho-interacting protein 3
Short name=RIP3
p116Rip
Gene names
Name:MPRIP
Synonyms:KIAA0864, MRIP, RHOIP3
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1025 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

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. Ref.2 Ref.7 UniProtKB P97434

Subunit structure

Binds F-actin through its N-terminus. Interacts with MYZAP By similarity. Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent coiled coil domains. Ref.1 Ref.2 Ref.7

Subcellular location

Cytoplasmcytoskeleton. Note: Colocalizes with F-actin. Ref.1 Ref.7

Sequence similarities

Contains 2 PH domains.

Ontologies

Keywords
   Cellular componentCytoplasm
Cytoskeleton
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainCoiled coil
Repeat
   LigandActin-binding
   PTMPhosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Cellular_componentactin cytoskeleton

Inferred from direct assay. Source: HPA

cytoplasm

Inferred from direct assay. Source: HPA

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Ppp1r12aQ107286EBI-1022605,EBI-918263From a different organism.

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 Ref.2 (identifier: Q6WCQ1-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 Ref.1 (identifier: Q6WCQ1-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1017-1025: VIEQVSWDT → LKEGLTVQERLKLFESRDLKKD
Isoform 3 (identifier: Q6WCQ1-3)

The sequence of this isoform differs from the canonical sequence as follows:
     346-383: Missing.
     1017-1025: VIEQVSWDT → LKEGLTVQERLKLFESRDLKKD

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain2 – 10251024Myosin phosphatase Rho-interacting protein
PRO_0000223930

Regions

Domain43 – 150108PH 1
Domain387 – 48397PH 2
Region1 – 383383Interaction with F-actin By similarity
Region546 – 824279Interaction with RHOA
Region824 – 87956Interaction with PPP1R12A
Coiled coil673 – 977305 Potential
Compositional bias179 – 25274Ser-rich

Amino acid modifications

Modified residue1921Phosphoserine Ref.10
Modified residue2201Phosphoserine Ref.10 Ref.12
Modified residue2241Phosphoserine Ref.10
Modified residue2261Phosphoserine Ref.10
Modified residue2691Phosphoserine Ref.12
Modified residue2891Phosphoserine Ref.10 Ref.11 Ref.12
Modified residue2921Phosphoserine Ref.10
Modified residue2951Phosphothreonine Ref.10
Modified residue3621Phosphoserine Ref.10 Ref.12
Modified residue3651Phosphoserine Ref.10 Ref.12
Modified residue6191Phosphoserine Ref.8 Ref.10 Ref.12
Modified residue8911Phosphoserine Ref.10 Ref.12
Modified residue9771Phosphoserine Ref.10 Ref.12 Ref.14
Modified residue9931Phosphoserine Ref.14
Modified residue10161Phosphoserine Ref.14

Natural variations

Alternative sequence346 – 38338Missing in isoform 3.
VSP_051947
Alternative sequence1017 – 10259VIEQVSWDT → LKEGLTVQERLKLFESRDLK KD in isoform 2 and isoform 3.
VSP_051948
Natural variant3271P → Q. Ref.3 Ref.5
Corresponds to variant rs3744137 [ dbSNP | Ensembl ].
VAR_051203

Experimental info

Sequence conflict311S → P in AAQ63176. Ref.1
Sequence conflict1841S → R in BAD89507. Ref.2
Sequence conflict188 – 1892Missing in BAD89507. Ref.2
Sequence conflict188 – 1892Missing in AAH09982. Ref.6
Sequence conflict1891Missing in AAQ63176. Ref.1
Sequence conflict1891Missing in BAC78198. Ref.3
Sequence conflict1891Missing in CAD39169. Ref.5
Sequence conflict2351S → F in BAD89507. Ref.2
Sequence conflict3521P → S in BAD89507. Ref.2
Sequence conflict5281R → T in AAQ63176. Ref.1
Sequence conflict5501P → L in BAC78198. Ref.3
Sequence conflict5501P → L in CAD39169. Ref.5
Sequence conflict5781P → S in AAQ63176. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 25, 2008. Version 3.
Checksum: 5B7A30CDB3685E4E

FASTA1,025116,533
        10         20         30         40         50         60 
MSAAKENPCR KFQANIFNKS KCQNCFKPRE SHLLNDEDLT QAKPIYGGWL LLAPDGTDFD 

        70         80         90        100        110        120 
NPVHRSRKWQ RRFFILYEHG LLRYALDEMP TTLPQGTINM NQCTDVVDGE GRTGQKFSLC 

       130        140        150        160        170        180 
ILTPEKEHFI RAETKEIVSG WLEMLMVYPR TNKQNQKKKR KVEPPTPQEP GPAKVAVTSS 

       190        200        210        220        230        240 
SSSSSSSSSI PSAEKVPTTK STLWQEEMRT KDQPDGSSLS PAQSPSQSQP PAASSLREPG 

       250        260        270        280        290        300 
LESKEEESAM SSDRMDCGRK VRVESGYFSL EKTKQDLKAE EQQLPPPLSP PSPSTPNHRR 

       310        320        330        340        350        360 
SQVIEKFEAL DIEKAEHMET NAVGPSPSSD TRQGRSEKRA FPRKRDFTNE APPAPLPDAS 

       370        380        390        400        410        420 
ASPLSPHRRA KSLDRRSTEP SVTPDLLNFK KGWLTKQYED GQWKKHWFVL ADQSLRYYRD 

       430        440        450        460        470        480 
SVAEEAADLD GEIDLSACYD VTEYPVQRNY GFQIHTKEGE FTLSAMTSGI RRNWIQTIMK 

       490        500        510        520        530        540 
HVHPTTAPDV TSSLPEEKNK SSCSFETCPR PTEKQEAELG EPDPEQKRSR ARERRREGRS 

       550        560        570        580        590        600 
KTFDWAEFRP IQQALAQERV GGVGPADTHE PLRPEAEPGE LERERARRRE ERRKRFGMLD 

       610        620        630        640        650        660 
ATDGPGTEDA ALRMEVDRSP GLPMSDLKTH NVHVEIEQRW HQVETTPLRE EKQVPIAPVH 

       670        680        690        700        710        720 
LSSEDGGDRL STHELTSLLE KELEQSQKEA SDLLEQNRLL QDQLRVALGR EQSAREGYVL 

       730        740        750        760        770        780 
QATCERGFAA MEETHQKKIE DLQRQHQREL EKLREEKDRL LAEETAATIS AIEAMKNAHR 

       790        800        810        820        830        840 
EEMERELEKS QRSQISSVNS DVEALRRQYL EELQSVQREL EVLSEQYSQK CLENAHLAQA 

       850        860        870        880        890        900 
LEAERQALRQ CQRENQELNA HNQELNNRLA AEITRLRTLL TGDGGGEATG SPLAQGKDAY 

       910        920        930        940        950        960 
ELEVLLRVKE SEIQYLKQEI SSLKDELQTA LRDKKYASDK YKDIYTELSI AKAKADCDIS 

       970        980        990       1000       1010       1020 
RLKEQLKAAT EALGEKSPDS ATVSGYDIMK SKSNPDFLKK DRSCVTRQLR NIRSKSVIEQ 


VSWDT 

« Hide

Isoform 2 [UniParc].

Checksum: EE674842C8133516
Show »

FASTA1,038118,103
Isoform 3 [UniParc].

Checksum: FCFDB3210A73EEF9
Show »

FASTA1,000114,049

References

« Hide 'large scale' references
[1]"Myosin phosphatase-Rho interacting protein. A new member of the myosin phosphatase complex that directly binds RhoA."
Surks H.K., Richards C.T., Mendelsohn M.E.
J. Biol. Chem. 278:51484-51493(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), SUBCELLULAR LOCATION, INTERACTION WITH PPP1R12A AND RHOA.
Tissue: Aorta.
[2]"p116Rip decreases myosin II phosphorylation by activating myosin light chain phosphatase and by inactivating RhoA."
Koga Y., Ikebe M.
J. Biol. Chem. 280:4983-4991(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, INTERACTION WITH PPP1R12A.
[3]"Cloning of human orthologue RHOIP3 of Mus Rhoip3."
Inazawa J., Imoto I.
Submitted (DEC-2002) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), VARIANT GLN-327.
[4]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[5]"The full-ORF clone resource of the German cDNA consortium."
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1025 (ISOFORM 1), VARIANT GLN-327.
Tissue: Melanoma.
[6]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 157-1025 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 194-1025 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 377-1025 (ISOFORM 2).
Tissue: Brain, Lymph and Muscle.
[7]"M-RIP targets myosin phosphatase to stress fibers to regulate myosin light chain phosphorylation in vascular smooth muscle cells."
Surks H.K., Riddick N., Ohtani K.
J. Biol. Chem. 280:42543-42551(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, INTERACTION WITH PPP1R12A AND F-ACTIN.
[8]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[9]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[10]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-192; SER-220; SER-224; SER-226; SER-289; SER-292; THR-295; SER-362; SER-365; SER-619; SER-891 AND SER-977, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[11]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Leukemic T-cell.
[12]"Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-269; SER-289; SER-362; SER-365; SER-619; SER-891 AND SER-977, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Cervix carcinoma.
[13]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[14]"System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-977; SER-993 AND SER-1016, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AY296247 mRNA. Translation: AAQ63176.1.
AB189741 mRNA. Translation: BAD89507.1.
AB098507 mRNA. Translation: BAC78198.1.
AC079111 Genomic DNA. No translation available.
AC055811 Genomic DNA. No translation available.
AL834513 mRNA. Translation: CAD39169.1.
BC009982 mRNA. Translation: AAH09982.2.
BC075847 mRNA. Translation: AAH75847.1.
BC105987 mRNA. Translation: AAI05988.1.
RefSeqNP_055949.2. NM_015134.3.
NP_958431.2. NM_201274.3.
UniGeneHs.462341.

3D structure databases

ProteinModelPortalQ6WCQ1.
SMRQ6WCQ1. Positions 43-146, 388-482.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116776. 25 interactions.
IntActQ6WCQ1. 16 interactions.
MINTMINT-1161017.
STRING9606.ENSP00000379156.

PTM databases

PhosphoSiteQ6WCQ1.

Polymorphism databases

DMDM215274136.

Proteomic databases

PaxDbQ6WCQ1.
PRIDEQ6WCQ1.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000341712; ENSP00000342379; ENSG00000133030. [Q6WCQ1-1]
ENST00000395804; ENSP00000379149; ENSG00000133030. [Q6WCQ1-1]
ENST00000395811; ENSP00000379156; ENSG00000133030. [Q6WCQ1-2]
ENST00000444976; ENSP00000400189; ENSG00000133030. [Q6WCQ1-3]
GeneID23164.
KEGGhsa:23164.
UCSCuc002gqu.2. human. [Q6WCQ1-1]
uc002gqv.2. human. [Q6WCQ1-2]

Organism-specific databases

CTD23164.
GeneCardsGC17P016946.
HGNCHGNC:30321. MPRIP.
HPAHPA022901.
MIM612935. gene.
neXtProtNX_Q6WCQ1.
PharmGKBPA162396092.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG243797.
HOVERGENHBG023864.
OrthoDBEOG773XKP.
PhylomeDBQ6WCQ1.
TreeFamTF329258.

Gene expression databases

ArrayExpressQ6WCQ1.
BgeeQ6WCQ1.
CleanExHS_MPRIP.
GenevestigatorQ6WCQ1.

Family and domain databases

Gene3D2.30.29.30. 2 hits.
InterProIPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
[Graphical view]
PfamPF00169. PH. 2 hits.
[Graphical view]
SMARTSM00233. PH. 2 hits.
[Graphical view]
PROSITEPS50003. PH_DOMAIN. 2 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSMPRIP. human.
GeneWikiM-RIP.
GenomeRNAi23164.
NextBio44551.
PROQ6WCQ1.
SOURCESearch...

Entry information

Entry nameMPRIP_HUMAN
AccessionPrimary (citable) accession number: Q6WCQ1
Secondary accession number(s): Q3KQZ5 expand/collapse secondary AC list , Q5FB94, Q6DHW2, Q7Z5Y2, Q8N390, Q96G40
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2006
Last sequence update: November 25, 2008
Last modified: April 16, 2014
This is version 91 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM