Reviewed,
UniProtKB/Swiss-Prot Q6WCQ1 (MPRIP_HUMAN)
Last modified
November 25, 2008.
Version 41.
History...
Clusters with 100%,
90%,
50% identity |
Documents (3) |
Third-party data |
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Names and origin
| Protein names | Recommended name: Myosin phosphatase Rho-interacting protein Short name=M-RIP Alternative name(s): Rho-interacting protein 3 Short name=RIP3 p116Rip | ||||
| Gene names |
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| Organism | Homo sapiens (Human) | ||||
| Taxonomic identifier | 9606 [NCBI] | ||||
| Taxonomic lineage | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo |
Protein attributes
| Sequence length | 1025 AA. |
| Sequence status | Complete. |
| Sequence processing | The displayed sequence is not processed. |
| Protein existence | Evidence 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. |
| Subunit structure | Binds F-actin through its N-terminus By similarity. Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent coiled coil domains. |
| Subcellular location | Cytoplasm › cytoskeleton. Note= Colocalizes with F-actin. |
| Sequence similarities | Contains 2 PH domains. |
Ontologies
Keywords | |
|---|---|
| Cellular component | Cytoplasm Cytoskeleton |
| Coding sequence diversity | Alternative splicing |
| Domain | Coiled coil Repeat |
| Ligand | Actin-binding |
| PTM | Phosphoprotein |
Gene Ontology (GO) | |
| Cellular component | cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeletonInferred from electronic annotation. Source: UniProtKB-KW |
| Molecular function | actin binding Inferred from electronic annotation. Source: UniProtKB-KW |
| Complete GO annotation... | |
Binary interactions
With | Entry | #Exp. | IntAct | Notes |
|---|---|---|---|---|
| YWHAB | P31946 | 1 | EBI-1022605,EBI-359815 | |
| YWHAG | P61981 | 1 | EBI-1022605,EBI-359832 | |
| YWHAQ | P27348 | 1 | EBI-1022605,EBI-359854 |
Alternative products
| This entry describes 3 isoforms produced by alternative splicing. [Align] [Select] | ||||||
| Isoform 1 (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 (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 key | Position(s) | Length | Description | Graphical view | Feature identifier | ||||
Molecule processing | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Chain | 2 – 1025 | 1024 | Myosin phosphatase Rho-interacting protein | PRO_0000223930 | |||||
Regions | |||||||||
| Domain | 43 – 150 | 108 | PH 1 | ||||||
| Domain | 387 – 483 | 97 | PH 2 | ||||||
| Region | 1 – 383 | 383 | Interaction with F-actin By similarity | ||||||
| Region | 546 – 824 | 279 | Interaction with RHOA | ||||||
| Region | 824 – 879 | 56 | Interaction with PPP1R12A | ||||||
| Coiled coil | 673 – 977 | 305 | Potential | ||||||
| Compositional bias | 179 – 252 | 74 | Ser-rich | ||||||
Amino acid modifications | |||||||||
| Modified residue | 181 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 186 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 220 | 1 | Phosphoserine | ||||||
| Modified residue | 224 | 1 | Phosphoserine | ||||||
| Modified residue | 226 | 1 | Phosphoserine | ||||||
| Modified residue | 289 | 1 | Phosphoserine | ||||||
| Modified residue | 292 | 1 | Phosphoserine | ||||||
| Modified residue | 294 | 1 | Phosphoserine | ||||||
| Modified residue | 295 | 1 | Phosphothreonine | ||||||
| Modified residue | 320 | 1 | Phosphothreonine By similarity | ||||||
| Modified residue | 362 | 1 | Phosphoserine | ||||||
| Modified residue | 365 | 1 | Phosphoserine | ||||||
| Modified residue | 619 | 1 | Phosphoserine | ||||||
| Modified residue | 891 | 1 | Phosphoserine | ||||||
| Modified residue | 977 | 1 | Phosphoserine | ||||||
| Modified residue | 993 | 1 | Phosphoserine | ||||||
| Modified residue | 1014 | 1 | Phosphoserine By similarity | ||||||
| Modified residue | 1016 | 1 | Phosphoserine By similarity | ||||||
Natural variations | |||||||||
| Alternative sequence | 346 – 383 | 38 | Missing in isoform 3. | VSP_051947 | |||||
| Alternative sequence | 1017 – 1025 | 9 | VIEQVSWDT → LKEGLTVQERLKLFESRDLK KD in isoform 2 and isoform 3. | VSP_051948 | |||||
Experimental info | |||||||||
| Sequence conflict | 31 | 1 | S → P in AAQ63176. Ref.1 | ||||||
| Sequence conflict | 184 | 1 | S → R in BAD89507. Ref.2 | ||||||
| Sequence conflict | 188 – 189 | 2 | Missing in BAD89507. Ref.2 | ||||||
| Sequence conflict | 188 – 189 | 2 | Missing in AAH09982. Ref.6 | ||||||
| Sequence conflict | 189 | 1 | Missing in AAQ63176. Ref.1 | ||||||
| Sequence conflict | 189 | 1 | Missing in BAC78198. Ref.3 | ||||||
| Sequence conflict | 189 | 1 | Missing in CAD39169. Ref.5 | ||||||
| Sequence conflict | 235 | 1 | S → F in BAD89507. Ref.2 | ||||||
| Sequence conflict | 327 | 1 | P → Q in BAC78198. Ref.3 | ||||||
| Sequence conflict | 327 | 1 | P → Q in CAD39169. Ref.5 | ||||||
| Sequence conflict | 352 | 1 | P → S in BAD89507. Ref.2 | ||||||
| Sequence conflict | 528 | 1 | R → T in AAQ63176. Ref.1 | ||||||
| Sequence conflict | 550 | 1 | P → L in BAC78198. Ref.3 | ||||||
| Sequence conflict | 550 | 1 | P → L in CAD39169. Ref.5 | ||||||
| Sequence conflict | 578 | 1 | P → S in AAQ63176. Ref.1 | ||||||
Sequences
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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: 14506264] [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: 15545284] [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). |
| [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. Nusbaum C.Nature 440:1045-1049(2006) [PubMed: 16625196] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. |
| [5] | The German cDNA consortium Submitted (JUL-2002) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 38-1025 (ISOFORM 1). 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: 15489334] [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: 16257966] [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: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-224; SER-365; SER-619 AND SER-993, MASS SPECTROMETRY. Tissue: Epithelium. |
| [9] | "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-365 AND SER-993, MASS SPECTROMETRY. |
| [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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-220; SER-224; SER-226; SER-289; SER-292; SER-294; THR-295; SER-362; SER-365; SER-619; SER-891 AND SER-977, MASS SPECTROMETRY. |
| + | Additional computationally mapped references. |
Cross-references
Sequence databases | |
|---|---|
| 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. | |
| RefSeq | NP_055949.2. NP_958431.2. |
| UniGene | Hs.462341 |
3D structure databases | |
| HSSP | HSSP built from PDB template 1FAO based on UniProtKB Q9UN19. |
| ModBase | Search... |
Protein-protein interaction databases | |
| IntAct | Q6WCQ1. |
PTM databases | |
| PhosphoSite | Q6WCQ1. |
Genome annotation databases | |
| Ensembl | ENSG00000133030. Homo sapiens. [Contig view] |
| GeneID | 23164. |
| KEGG | hsa:23164. |
Organism-specific databases | |
| H-InvDB | HIX0013577. |
| HGNC | HGNC:30321. MPRIP. |
| HUGE | Search... |
| GenAtlas | Search... |
| GeneCards | Search... |
Phylogenomic databases | |
| HOVERGEN | Q6WCQ1. |
Gene expression databases | |
| ArrayExpress | Q6WCQ1. |
| GermOnline | ENSG00000133030. Homo sapiens. |
Family and domain databases | |
| InterPro | IPR001849. PH. IPR011993. PH_type. [Graphical view] |
| Gene3D | G3DSA:2.30.29.30. PH_type. 2 hits. |
| Pfam | PF00169. PH. 2 hits. [Graphical view] |
| SMART | SM00233. PH. 2 hits. [Graphical view] |
| PROSITE | PS50003. PH_DOMAIN. 2 hits. [Graphical view] |
| ProtoNet | Search... |
Other Resources | |
| NextBio | 44551. |

Clusters with