Q6WCQ1 (MPRIP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

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

Name:	MPRIP
Synonyms:	KIAA0864, MRIP, RHOIP3

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	1025 AA.
Sequence status	Complete.
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. 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	Cytoplasm › cytoskeleton. Note: Colocalizes with F-actin. Ref.1 Ref.7
Sequence similarities	Contains 2 PH domains.

Ontologies

Keywords
Cellular component	Cytoplasm Cytoskeleton
Coding sequence diversity	Alternative splicing Polymorphism
Domain	Coiled coil Repeat
Ligand	Actin-binding
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular_component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	phospholipid binding Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

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 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	180	1	Phosphoserine By similarity
	Modified residue	186	1	Phosphoserine By similarity
	Modified residue	192	1	Phosphoserine Ref.10
	Modified residue	220	1	Phosphoserine Ref.10 Ref.12
	Modified residue	224	1	Phosphoserine Ref.10
	Modified residue	226	1	Phosphoserine Ref.10
	Modified residue	269	1	Phosphoserine Ref.12
	Modified residue	289	1	Phosphoserine Ref.10 Ref.11 Ref.12
	Modified residue	292	1	Phosphoserine Ref.10
	Modified residue	295	1	Phosphothreonine Ref.10
	Modified residue	320	1	Phosphothreonine By similarity
	Modified residue	362	1	Phosphoserine Ref.10 Ref.12
	Modified residue	365	1	Phosphoserine Ref.10 Ref.12
	Modified residue	619	1	Phosphoserine Ref.8 Ref.10 Ref.12
	Modified residue	891	1	Phosphoserine Ref.10 Ref.12
	Modified residue	977	1	Phosphoserine Ref.10 Ref.12 Ref.14
	Modified residue	993	1	Phosphoserine Ref.14
	Modified residue	1014	1	Phosphoserine By similarity
	Modified residue	1016	1	Phosphoserine Ref.14
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
	Natural variant	327	1	P → Q. Ref.3 Ref.5 Corresponds to variant rs3744137 [ dbSNP | Ensembl ].		VAR_051203
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	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

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 25, 2008. Version 3. Checksum: 5B7A30CDB3685E4E	FASTA	1,025	116,533
	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
	Isoform 2 [UniParc]. Checksum: EE674842C8133516	FASTA	1,038	118,103
	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 NIRSKSLKEG 1030 LTVQERLKLF ESRDLKKD
	Isoform 3 [UniParc]. Checksum: FCFDB3210A73EEF9	FASTA	1,000	114,049
	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 FPRKRPDLLN FKKGWLTKQY 370 380 390 400 410 420 EDGQWKKHWF VLADQSLRYY RDSVAEEAAD LDGEIDLSAC YDVTEYPVQR NYGFQIHTKE 430 440 450 460 470 480 GEFTLSAMTS GIRRNWIQTI MKHVHPTTAP DVTSSLPEEK NKSSCSFETC PRPTEKQEAE 490 500 510 520 530 540 LGEPDPEQKR SRARERRREG RSKTFDWAEF RPIQQALAQE RVGGVGPADT HEPLRPEAEP 550 560 570 580 590 600 GELERERARR REERRKRFGM LDATDGPGTE DAALRMEVDR SPGLPMSDLK THNVHVEIEQ 610 620 630 640 650 660 RWHQVETTPL REEKQVPIAP VHLSSEDGGD RLSTHELTSL LEKELEQSQK EASDLLEQNR 670 680 690 700 710 720 LLQDQLRVAL GREQSAREGY VLQATCERGF AAMEETHQKK IEDLQRQHQR ELEKLREEKD 730 740 750 760 770 780 RLLAEETAAT ISAIEAMKNA HREEMERELE KSQRSQISSV NSDVEALRRQ YLEELQSVQR 790 800 810 820 830 840 ELEVLSEQYS QKCLENAHLA QALEAERQAL RQCQRENQEL NAHNQELNNR LAAEITRLRT 850 860 870 880 890 900 LLTGDGGGEA TGSPLAQGKD AYELEVLLRV KESEIQYLKQ EISSLKDELQ TALRDKKYAS 910 920 930 940 950 960 DKYKDIYTEL SIAKAKADCD ISRLKEQLKA ATEALGEKSP DSATVSGYDI MKSKSNPDFL 970 980 990 1000 KKDRSCVTRQ LRNIRSKSLK EGLTVQERLK LFESRDLKKD

References

	« Hide 'large scale' referencesShow '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. , 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY.
+	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.
IPI	IPI00166518. IPI00295457. IPI00305344.
RefSeq	NP_055949.2. NM_015134.3. NP_958431.2. NM_201274.3.
UniGene	Hs.462341.
3D structure databases
ProteinModelPortal	Q6WCQ1.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6WCQ1. 11 interactions.
MINT	MINT-1161017.
STRING	9606.ENSP00000379156.
PTM databases
PhosphoSite	Q6WCQ1.
Polymorphism databases
DMDM	215274136.
Proteomic databases
PaxDb	Q6WCQ1.
PRIDE	Q6WCQ1.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000341712; ENSP00000342379; ENSG00000133030. ENST00000395804; ENSP00000379149; ENSG00000133030. ENST00000395811; ENSP00000379156; ENSG00000133030. ENST00000444976; ENSP00000400189; ENSG00000133030.
GeneID	23164.
KEGG	hsa:23164.
UCSC	uc002gqu.2. human. uc002gqv.2. human. uc002gqw.2. human.
Organism-specific databases
CTD	23164.
GeneCards	GC17P016946.
HGNC	HGNC:30321. MPRIP.
HPA	HPA022901.
MIM	612935. gene.
neXtProt	NX_Q6WCQ1.
PharmGKB	PA162396092.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG243797.
HOVERGEN	HBG023864.
Gene expression databases
ArrayExpress	Q6WCQ1.
Bgee	Q6WCQ1.
CleanEx	HS_MPRIP.
Genevestigator	Q6WCQ1.
GermOnline	ENSG00000133030. Homo sapiens.
Family and domain databases
Gene3D	2.30.29.30. 2 hits.
InterPro	IPR011993. PH_like_dom. IPR001849. Pleckstrin_homology. [Graphical view]
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
ChiTaRS	MPRIP. human.
GenomeRNAi	23164.
NextBio	44551.
SOURCE	Search...

Entry information

Entry name

MPRIP_HUMAN

Accession

Primary (citable) accession number: Q6WCQ1
Secondary accession number(s): Q3KQZ5 , Q5FB94, Q6DHW2, Q7Z5Y2, Q8N390, Q96G40

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 21, 2006
Last sequence update:	November 25, 2008
Last modified:	May 1, 2013
This is version 83 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.