Reviewed, UniProtKB/Swiss-Prot Q6WCQ1 (MPRIP_HUMAN)

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) [Complete proteome]

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.
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 By similarity. Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent coiled coil domains. Ref.2 Ref.7 Ref.1 UniProtKB P97434
Subcellular location	Cytoplasm › cytoskeleton. Note: Colocalizes with F-actin. Ref.7 Ref.1
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
Gene Ontology (GO)
Cellular component	cytoplasm Inferred from electronic annotation. Source: UniProtKB-KW cytoskeleton Inferred from electronic annotation. Source: UniProtKB-SubCell
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 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	181	1	Phosphoserine By similarity
	Modified residue	186	1	Phosphoserine By similarity
	Modified residue	220	1	Phosphoserine Ref.8 Ref.12
	Modified residue	224	1	Phosphoserine Ref.8 Ref.12
	Modified residue	226	1	Phosphoserine Ref.12
	Modified residue	289	1	Phosphoserine Ref.12 Ref.14
	Modified residue	292	1	Phosphoserine Ref.12
	Modified residue	294	1	Phosphoserine Ref.12
	Modified residue	295	1	Phosphothreonine Ref.12 Ref.14
	Modified residue	320	1	Phosphothreonine By similarity
	Modified residue	362	1	Phosphoserine Ref.12
	Modified residue	365	1	Phosphoserine Ref.8 Ref.12 Ref.10
	Modified residue	619	1	Phosphoserine Ref.8 Ref.12 Ref.9
	Modified residue	891	1	Phosphoserine Ref.12 Ref.11
	Modified residue	977	1	Phosphoserine Ref.12
	Modified residue	993	1	Phosphoserine Ref.8 Ref.10
	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
	Natural variant	327	1	P → Q: dbSNP rs3744137. Ref.3 Ref.5		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. 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. 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: 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), 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: 16625196] [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: 17974005] [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: 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]	"Evaluation of the low-specificity protease elastase for large-scale phosphoproteome analysis." Wang B., Malik R., Nigg E.A., Korner R. Anal. Chem. 80:9526-9533(2008) [PubMed: 19007248] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-619, MASS SPECTROMETRY.
[10]	"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.
[11]	"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: 18691976] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-891, MASS SPECTROMETRY.
[12]	"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.
[13]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[14]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-289 AND THR-295, MASS SPECTROMETRY. Tissue: T-cell.
+	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. NP_958431.2.
UniGene	Hs.462341
3D structure databases
ModBase	Search...
Protein-protein interaction databases
IntAct	Q6WCQ1. 7 interactions.
STRING	Q6WCQ1.
PTM databases
PhosphoSite	Q6WCQ1.
Proteomic databases
PRIDE	Q6WCQ1.
Genome annotation databases
Ensembl	ENST00000341712; ENSP00000342379; ENSG00000133030; Homo sapiens. [Genome view] ENST00000395804; ENSP00000379149; ENSG00000133030; Homo sapiens. [Genome view]
GeneID	23164.
KEGG	hsa:23164.
Organism-specific databases
CTD	23164.
GeneCards	GC17P016888.
H-InvDB	HIX0013577.
HGNC	HGNC:30321. MPRIP.
HPA	HPA022901.
HUGE	Search...
GenAtlas	Search...
Phylogenomic databases
HOVERGEN	Q6WCQ1.
OrthoDB	EOG96MF3X.
Gene expression databases
ArrayExpress	Q6WCQ1.
Bgee	Q6WCQ1.
CleanEx	HS_MPRIP.
Genevestigator	Q6WCQ1.
GermOnline	ENSG00000133030. Homo sapiens.
Family and domain databases
InterPro	IPR011993. PH_type. IPR001849. Pleckstrin_homology. [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.

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:	November 24, 2009
This is version 55 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.