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Q6WCQ1

- MPRIP_HUMAN

UniProt

Q6WCQ1 - MPRIP_HUMAN

Protein

Myosin phosphatase Rho-interacting protein

Gene

MPRIP

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 96 (01 Oct 2014)
      Sequence version 3 (25 Nov 2008)
      Previous versions | rss
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    Functioni

    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.By similarity2 Publications

    GO - Molecular functioni

    1. protein binding Source: IntAct

    Keywords - Ligandi

    Actin-binding

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Myosin phosphatase Rho-interacting protein
    Short name:
    M-RIP
    Alternative name(s):
    Rho-interacting protein 3
    Short name:
    RIP3
    p116Rip
    Gene namesi
    Name:MPRIP
    Synonyms:KIAA0864, MRIP, RHOIP3Imported
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 17

    Organism-specific databases

    HGNCiHGNC:30321. MPRIP.

    Subcellular locationi

    Cytoplasmcytoskeleton 2 Publications
    Note: Colocalizes with F-actin.

    GO - Cellular componenti

    1. actin cytoskeleton Source: HPA
    2. cytoplasm Source: HPA

    Keywords - Cellular componenti

    Cytoplasm, Cytoskeleton

    Pathology & Biotechi

    Organism-specific databases

    PharmGKBiPA162396092.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini2 – 10251024Myosin phosphatase Rho-interacting proteinPRO_0000223930Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei192 – 1921Phosphoserine1 Publication
    Modified residuei220 – 2201Phosphoserine2 Publications
    Modified residuei224 – 2241Phosphoserine1 Publication
    Modified residuei226 – 2261Phosphoserine1 Publication
    Modified residuei269 – 2691Phosphoserine1 Publication
    Modified residuei289 – 2891Phosphoserine3 Publications
    Modified residuei292 – 2921Phosphoserine1 Publication
    Modified residuei295 – 2951Phosphothreonine1 Publication
    Modified residuei362 – 3621Phosphoserine2 Publications
    Modified residuei365 – 3651Phosphoserine2 Publications
    Modified residuei619 – 6191Phosphoserine3 Publications
    Modified residuei891 – 8911Phosphoserine2 Publications
    Modified residuei977 – 9771Phosphoserine3 Publications
    Modified residuei993 – 9931Phosphoserine1 Publication
    Modified residuei1016 – 10161Phosphoserine1 Publication

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ6WCQ1.
    PaxDbiQ6WCQ1.
    PRIDEiQ6WCQ1.

    PTM databases

    PhosphoSiteiQ6WCQ1.

    Expressioni

    Gene expression databases

    ArrayExpressiQ6WCQ1.
    BgeeiQ6WCQ1.
    CleanExiHS_MPRIP.
    GenevestigatoriQ6WCQ1.

    Organism-specific databases

    HPAiHPA022901.

    Interactioni

    Subunit structurei

    Binds F-actin through its N-terminus. Interacts with MYZAP By similarity. Binds RHOA, PPP1R12A/MBS and PPP1R12C/MBS85 through adjacent coiled coil domains.By similarity3 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    Ppp1r12aQ107286EBI-1022605,EBI-918263From a different organism.

    Protein-protein interaction databases

    BioGridi116776. 28 interactions.
    IntActiQ6WCQ1. 16 interactions.
    MINTiMINT-1161017.
    STRINGi9606.ENSP00000379156.

    Structurei

    3D structure databases

    ProteinModelPortaliQ6WCQ1.
    SMRiQ6WCQ1. Positions 390-482.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini43 – 150108PH 1PROSITE-ProRule annotationAdd
    BLAST
    Domaini387 – 48397PH 2PROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 383383Interaction with F-actinBy similarityAdd
    BLAST
    Regioni546 – 824279Interaction with RHOAAdd
    BLAST
    Regioni824 – 87956Interaction with PPP1R12AAdd
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili673 – 977305Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi179 – 25274Ser-richAdd
    BLAST

    Sequence similaritiesi

    Contains 2 PH domains.PROSITE-ProRule annotation

    Keywords - Domaini

    Coiled coil, Repeat

    Phylogenomic databases

    eggNOGiNOG243797.
    HOVERGENiHBG023864.
    OrthoDBiEOG773XKP.
    PhylomeDBiQ6WCQ1.
    TreeFamiTF329258.

    Family and domain databases

    Gene3Di2.30.29.30. 2 hits.
    InterProiIPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view]
    PfamiPF00169. PH. 2 hits.
    [Graphical view]
    SMARTiSM00233. PH. 2 hits.
    [Graphical view]
    PROSITEiPS50003. PH_DOMAIN. 2 hits.
    [Graphical view]

    Sequences (3)i

    Sequence statusi: Complete.

    This entry describes 3 isoformsi produced by alternative splicing. Align

    Isoform 11 Publication (identifier: Q6WCQ1-1) [UniParc]FASTAAdd to Basket

    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.

    « Hide

    MSAAKENPCR KFQANIFNKS KCQNCFKPRE SHLLNDEDLT QAKPIYGGWL     50
    LLAPDGTDFD NPVHRSRKWQ RRFFILYEHG LLRYALDEMP TTLPQGTINM 100
    NQCTDVVDGE GRTGQKFSLC ILTPEKEHFI RAETKEIVSG WLEMLMVYPR 150
    TNKQNQKKKR KVEPPTPQEP GPAKVAVTSS SSSSSSSSSI PSAEKVPTTK 200
    STLWQEEMRT KDQPDGSSLS PAQSPSQSQP PAASSLREPG LESKEEESAM 250
    SSDRMDCGRK VRVESGYFSL EKTKQDLKAE EQQLPPPLSP PSPSTPNHRR 300
    SQVIEKFEAL DIEKAEHMET NAVGPSPSSD TRQGRSEKRA FPRKRDFTNE 350
    APPAPLPDAS ASPLSPHRRA KSLDRRSTEP SVTPDLLNFK KGWLTKQYED 400
    GQWKKHWFVL ADQSLRYYRD SVAEEAADLD GEIDLSACYD VTEYPVQRNY 450
    GFQIHTKEGE FTLSAMTSGI RRNWIQTIMK HVHPTTAPDV TSSLPEEKNK 500
    SSCSFETCPR PTEKQEAELG EPDPEQKRSR ARERRREGRS KTFDWAEFRP 550
    IQQALAQERV GGVGPADTHE PLRPEAEPGE LERERARRRE ERRKRFGMLD 600
    ATDGPGTEDA ALRMEVDRSP GLPMSDLKTH NVHVEIEQRW HQVETTPLRE 650
    EKQVPIAPVH LSSEDGGDRL STHELTSLLE KELEQSQKEA SDLLEQNRLL 700
    QDQLRVALGR EQSAREGYVL QATCERGFAA MEETHQKKIE DLQRQHQREL 750
    EKLREEKDRL LAEETAATIS AIEAMKNAHR EEMERELEKS QRSQISSVNS 800
    DVEALRRQYL EELQSVQREL EVLSEQYSQK CLENAHLAQA LEAERQALRQ 850
    CQRENQELNA HNQELNNRLA AEITRLRTLL TGDGGGEATG SPLAQGKDAY 900
    ELEVLLRVKE SEIQYLKQEI SSLKDELQTA LRDKKYASDK YKDIYTELSI 950
    AKAKADCDIS RLKEQLKAAT EALGEKSPDS ATVSGYDIMK SKSNPDFLKK 1000
    DRSCVTRQLR NIRSKSVIEQ VSWDT 1025
    Length:1,025
    Mass (Da):116,533
    Last modified:November 25, 2008 - v3
    Checksum:i5B7A30CDB3685E4E
    GO
    Isoform 21 Publication (identifier: Q6WCQ1-2) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,038
    Mass (Da):118,103
    Checksum:iEE674842C8133516
    GO
    Isoform 3Curated (identifier: Q6WCQ1-3) [UniParc]FASTAAdd to Basket

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

    Show »
    Length:1,000
    Mass (Da):114,049
    Checksum:iFCFDB3210A73EEF9
    GO

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti31 – 311S → P in AAQ63176. (PubMed:14506264)Curated
    Sequence conflicti184 – 1841S → R in BAD89507. (PubMed:15545284)Curated
    Sequence conflicti188 – 1892Missing in BAD89507. (PubMed:15545284)Curated
    Sequence conflicti188 – 1892Missing in AAH09982. (PubMed:15489334)Curated
    Sequence conflicti189 – 1891Missing in AAQ63176. (PubMed:14506264)Curated
    Sequence conflicti189 – 1891Missing in BAC78198. 1 PublicationCurated
    Sequence conflicti189 – 1891Missing in CAD39169. (PubMed:17974005)Curated
    Sequence conflicti235 – 2351S → F in BAD89507. (PubMed:15545284)Curated
    Sequence conflicti352 – 3521P → S in BAD89507. (PubMed:15545284)Curated
    Sequence conflicti528 – 5281R → T in AAQ63176. (PubMed:14506264)Curated
    Sequence conflicti550 – 5501P → L in BAC78198. 1 PublicationCurated
    Sequence conflicti550 – 5501P → L in CAD39169. (PubMed:17974005)Curated
    Sequence conflicti578 – 5781P → S in AAQ63176. (PubMed:14506264)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti327 – 3271P → Q.2 Publications
    Corresponds to variant rs3744137 [ dbSNP | Ensembl ].
    VAR_051203

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei346 – 38338Missing in isoform 3. 1 PublicationVSP_051947Add
    BLAST
    Alternative sequencei1017 – 10259VIEQVSWDT → LKEGLTVQERLKLFESRDLK KD in isoform 2 and isoform 3. 3 PublicationsVSP_051948

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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.
    CCDSiCCDS32578.1. [Q6WCQ1-1]
    CCDS42268.1. [Q6WCQ1-2]
    RefSeqiNP_055949.2. NM_015134.3. [Q6WCQ1-2]
    NP_958431.2. NM_201274.3. [Q6WCQ1-1]
    UniGeneiHs.462341.

    Genome annotation databases

    EnsembliENST00000341712; ENSP00000342379; ENSG00000133030. [Q6WCQ1-1]
    ENST00000395811; ENSP00000379156; ENSG00000133030. [Q6WCQ1-2]
    GeneIDi23164.
    KEGGihsa:23164.
    UCSCiuc002gqu.2. human. [Q6WCQ1-1]
    uc002gqv.2. human. [Q6WCQ1-2]

    Polymorphism databases

    DMDMi215274136.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    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 .
    CCDSi CCDS32578.1. [Q6WCQ1-1 ]
    CCDS42268.1. [Q6WCQ1-2 ]
    RefSeqi NP_055949.2. NM_015134.3. [Q6WCQ1-2 ]
    NP_958431.2. NM_201274.3. [Q6WCQ1-1 ]
    UniGenei Hs.462341.

    3D structure databases

    ProteinModelPortali Q6WCQ1.
    SMRi Q6WCQ1. Positions 390-482.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116776. 28 interactions.
    IntActi Q6WCQ1. 16 interactions.
    MINTi MINT-1161017.
    STRINGi 9606.ENSP00000379156.

    PTM databases

    PhosphoSitei Q6WCQ1.

    Polymorphism databases

    DMDMi 215274136.

    Proteomic databases

    MaxQBi Q6WCQ1.
    PaxDbi Q6WCQ1.
    PRIDEi Q6WCQ1.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000341712 ; ENSP00000342379 ; ENSG00000133030 . [Q6WCQ1-1 ]
    ENST00000395811 ; ENSP00000379156 ; ENSG00000133030 . [Q6WCQ1-2 ]
    GeneIDi 23164.
    KEGGi hsa:23164.
    UCSCi uc002gqu.2. human. [Q6WCQ1-1 ]
    uc002gqv.2. human. [Q6WCQ1-2 ]

    Organism-specific databases

    CTDi 23164.
    GeneCardsi GC17P016946.
    HGNCi HGNC:30321. MPRIP.
    HPAi HPA022901.
    MIMi 612935. gene.
    neXtProti NX_Q6WCQ1.
    PharmGKBi PA162396092.
    HUGEi Search...
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG243797.
    HOVERGENi HBG023864.
    OrthoDBi EOG773XKP.
    PhylomeDBi Q6WCQ1.
    TreeFami TF329258.

    Miscellaneous databases

    ChiTaRSi MPRIP. human.
    GeneWikii M-RIP.
    GenomeRNAii 23164.
    NextBioi 44551.
    PROi Q6WCQ1.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q6WCQ1.
    Bgeei Q6WCQ1.
    CleanExi HS_MPRIP.
    Genevestigatori Q6WCQ1.

    Family and domain databases

    Gene3Di 2.30.29.30. 2 hits.
    InterProi IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    [Graphical view ]
    Pfami PF00169. PH. 2 hits.
    [Graphical view ]
    SMARTi SM00233. PH. 2 hits.
    [Graphical view ]
    PROSITEi PS50003. PH_DOMAIN. 2 hits.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    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: AortaImported.
    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. 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: BrainImported, LymphImported and MuscleImported.
    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. 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. 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].

    Entry informationi

    Entry nameiMPRIP_HUMAN
    AccessioniPrimary (citable) accession number: Q6WCQ1
    Secondary accession number(s): Q3KQZ5
    , Q5FB94, Q6DHW2, Q7Z5Y2, Q8N390, Q96G40
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: February 21, 2006
    Last sequence update: November 25, 2008
    Last modified: October 1, 2014
    This is version 96 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (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.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 17
      Human chromosome 17: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3