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O94763

- RMP_HUMAN

UniProt

O94763 - RMP_HUMAN

Protein

Unconventional prefoldin RPB5 interactor 1

Gene

URI1

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 116 (01 Oct 2014)
      Sequence version 3 (16 Jun 2009)
      Previous versions | rss
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    Functioni

    Involved in gene transcription regulation. Acts as a transcriptional repressor in concert with the corepressor UXT to regulate androgen receptor (AR) transcription. May act as a tumor suppressor to repress AR-mediated gene transcription and to inhibit anchorage-independent growth in prostate cancer cells. Required for cell survival in ovarian cancer cells. Together with UXT, associates with chromatin to the NKX3-1 promoter region. Antagonizes transcriptional modulation via hepatitis B virus X protein.
    Plays a central role in maintaining S6K1 signaling and BAD phosphorylation under normal growth conditions thereby protecting cells from potential deleterious effects of sustained S6K1 signaling. The URI1-PPP1CC complex acts as a central component of a negative feedback mechanism that counteracts excessive S6K1 survival signaling to BAD in response to growth factors. Mediates inhibition of PPP1CC phosphatase activity in mitochondria. Coordinates the regulation of nutrient-sensitive gene expression availability in a mTOR-dependent manner. Seems to be a scaffolding protein able to assemble a prefoldin-like complex that contains PFDs and proteins with roles in transcription and ubiquitination.

    GO - Molecular functioni

    1. chromatin binding Source: UniProtKB
    2. protein binding Source: UniProtKB
    3. protein phosphatase inhibitor activity Source: UniProtKB-KW
    4. RNA polymerase II transcription corepressor activity Source: UniProtKB

    GO - Biological processi

    1. cellular response to growth factor stimulus Source: UniProtKB
    2. cellular response to steroid hormone stimulus Source: UniProtKB
    3. negative regulation of intrinsic apoptotic signaling pathway Source: UniProtKB
    4. negative regulation of phosphatase activity Source: UniProtKB
    5. negative regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    6. protein folding Source: InterPro
    7. regulation of cell growth Source: UniProtKB
    8. regulation of transcription from RNA polymerase II promoter Source: UniProtKB
    9. response to virus Source: UniProtKB

    Keywords - Molecular functioni

    Protein phosphatase inhibitor, Repressor

    Keywords - Biological processi

    Transcription, Transcription regulation

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Unconventional prefoldin RPB5 interactor 1
    Alternative name(s):
    Protein NNX3
    Protein phosphatase 1 regulatory subunit 19
    RNA polymerase II subunit 5-mediating protein
    Short name:
    RPB5-mediating protein
    Gene namesi
    Name:URI1
    Synonyms:C19orf2, NNX3, PPP1R19, RMP, URI
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 19

    Organism-specific databases

    HGNCiHGNC:13236. URI1.

    Subcellular locationi

    Nucleus. Cytoplasm. Mitochondrion. Cell projectiondendrite By similarity
    Note: Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 at mitochondrion.

    GO - Cellular componenti

    1. cytoplasm Source: UniProtKB
    2. dendrite Source: UniProtKB-SubCell
    3. DNA-directed RNA polymerase II, core complex Source: UniProtKB
    4. mitochondrion Source: UniProtKB-SubCell
    5. nucleus Source: UniProtKB
    6. prefoldin complex Source: InterPro

    Keywords - Cellular componenti

    Cell projection, Cytoplasm, Mitochondrion, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi372 – 3721S → A: Does not lead to dissociation of the URI1-PPP1CC complex. Enhances phosphorylation of RPS6KB1 after IGF1 stimulation. Confers a cell survival increase. 2 Publications

    Keywords - Diseasei

    Oncogene

    Organism-specific databases

    PharmGKBiPA134962614.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 535535Unconventional prefoldin RPB5 interactor 1PRO_0000097365Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei1 – 11N-acetylmethionine1 Publication
    Modified residuei372 – 3721Phosphoserine; by RPS6KB13 Publications

    Post-translational modificationi

    Phosphorylated. Phosphorylation occurs essentially on serine residues. Phosphorylation occurs in response to androgen treatment in prostate cancer cells in a mTOR-dependent manner. Phosphorylated; hyperhosphorylated in mitochondria in a mTORC-dependent signaling pathway. Phosphorylated at Ser-372 by RPS6KB1 in a growth factor- and rapamycin-dependent manner. S6K1-mediated mitochondrial phosphorylation at Ser-372 disrupts the URI1-PPP1CC complex in the mitochondrion, relieves PPP1CC phosphatase inhibition activity and hence engages a negative feedback diminishing RPS6KB1 kinase activity, preventing sustained S6K1-dependent signaling.5 Publications

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiO94763.
    PaxDbiO94763.
    PRIDEiO94763.

    PTM databases

    PhosphoSiteiO94763.

    Expressioni

    Tissue specificityi

    Ubiquitous. Expressed in ovarian cancers (at protein level). Expressed strongly in skeletal muscle. Expressed weakly in brain, heart, pancreas and in prostate epithelial cells.4 Publications

    Gene expression databases

    ArrayExpressiO94763.
    BgeeiO94763.
    CleanExiHS_C19orf2.
    GenevestigatoriO94763.

    Interactioni

    Subunit structurei

    Homodimer. Component of the URI complex that contains PFDN2, POLR2E/RPB5, RUVBL2, RUVBL1 and URI1. Interacts with PPP1CC; the interaction is phosphorylation-dependent and occurs in a growth factor-dependent manner. Interacts with PFDN2, PFDN4 and STAP1; the interactions are phosphorylation-dependent and occur in a growth-dependent manner in the mitochondrion. Interacts (via the middle C-terminal region) with GTF2F1 and GTF2F2. Interacts with DMAP1, POLR2E/RPB5 and UXT.6 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    GTF2F1P352693EBI-357067,EBI-457886
    GTF2F2P139844EBI-357067,EBI-1030560
    PFDN2Q9UHV92EBI-357067,EBI-359873
    POLR2EP193882EBI-357067,EBI-395189
    PPP1CCP368736EBI-357067,EBI-356283
    RPAP3Q9H6T32EBI-357067,EBI-356928

    Protein-protein interaction databases

    BioGridi114264. 20 interactions.
    IntActiO94763. 32 interactions.
    MINTiMINT-1154170.
    STRINGi9606.ENSP00000376097.

    Structurei

    3D structure databases

    ProteinModelPortaliO94763.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi299 – 31113Poly-AspAdd
    BLAST
    Compositional biasi314 – 3218Poly-Asp

    Sequence similaritiesi

    Phylogenomic databases

    eggNOGiNOG331327.
    HOGENOMiHOG000154150.
    HOVERGENiHBG007610.
    InParanoidiO94763.
    KOiK17560.
    OMAiIPRKSIL.
    OrthoDBiEOG7PZRZV.
    PhylomeDBiO94763.
    TreeFamiTF332816.

    Family and domain databases

    Gene3Di1.10.287.370. 1 hit.
    InterProiIPR009053. Prefoldin.
    IPR004127. Prefoldin_subunit_alpha.
    [Graphical view]
    PfamiPF02996. Prefoldin. 1 hit.
    [Graphical view]
    SUPFAMiSSF46579. SSF46579. 1 hit.

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: O94763-1) [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

    MEAPTVETPP DPSPPSAPAP ALVPLRAPDV ARLREEQEKV VTNCQERIQH    50
    WKKVDNDYNA LRERLSTLPD KLSYNIMVPF GPFAFMPGKL VHTNEVTVLL 100
    GDNWFAKCSA KQAVGLVEHR KEHVRKTIDD LKKVMKNFES RVEFTEDLQK 150
    MSDAAGDIVD IREEIKCDFE FKAKHRIAHK PHSKPKTSDI FEADIANDVK 200
    SKDLLADKEL WARLEELERQ EELLGELDSK PDTVIANGED TTSSEEEKED 250
    RNTNVNAMHQ VTDSHTPCHK DVASSEPFSG QVNSQLNCSV NGSSSYHSDD 300
    DDDDDDDDDD DNIDDDDGDN DHEALGVGDN SIPTIYFSHT VEPKRVRINT 350
    GKNTTLKFSE KKEEAKRKRK NSTGSGHSAQ ELPTIRTPAD IYRAFVDVVN 400
    GEYVPRKSIL KSRSRENSVC SDTSESSAAE FDDRRGVLRS ISCEEATCSD 450
    TSESILEEEP QENQKKLLPL SVTPEAFSGT VIEKEFVSPS LTPPPAIAHP 500
    ALPTIPERKE VLLEASEETG KRVSKFKAAR LQQKD 535
    Length:535
    Mass (Da):59,832
    Last modified:June 16, 2009 - v3
    Checksum:iDBB046A392E3C752
    GO
    Isoform 2 (identifier: O94763-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-76: Missing.

    Show »
    Length:459
    Mass (Da):51,247
    Checksum:i5EF69C27FEB5EAFE
    GO
    Isoform 3 (identifier: O94763-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-51: MEAPTVETPP...TNCQERIQHW → MRLGNVDFTLGSNVPCVYLVFSVNR

    Note: No experimental confirmation available.

    Show »
    Length:509
    Mass (Da):56,978
    Checksum:i5BA8E178FAE37863
    GO
    Isoform 4 (identifier: O94763-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-39: MEAPTVETPPDPSPPSAPAPALVPLRAPDVARLREEQEK → MTTWSSLQGSHVSKRALAYAL
         476-535: AFSGTVIEKE...FKAARLQQKD → VLRLVGYSRNLAPLNVIL

    Note: No experimental confirmation available.

    Show »
    Length:475
    Mass (Da):53,447
    Checksum:i2B9B965CD25CE296
    GO

    Sequence cautioni

    The sequence AAH26184.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti7 – 71E → G in BAF84859. (PubMed:14702039)Curated
    Sequence conflicti232 – 2321D → N in AAH26184. (PubMed:15489334)Curated
    Sequence conflicti311 – 3111Missing in AAD08679. (PubMed:9878255)Curated
    Sequence conflicti311 – 3111Missing in BAA34781. (PubMed:9819440)Curated
    Sequence conflicti311 – 3111Missing in BAF84859. (PubMed:14702039)Curated
    Sequence conflicti311 – 3111Missing in AAH26184. (PubMed:15489334)Curated
    Sequence conflicti315 – 3151D → E in BAF84859. (PubMed:14702039)Curated
    Sequence conflicti434 – 4341R → G in BAA34781. (PubMed:9819440)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti22 – 221L → P.
    Corresponds to variant rs189187 [ dbSNP | Ensembl ].
    VAR_056978

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 7676Missing in isoform 2. 1 PublicationVSP_032773Add
    BLAST
    Alternative sequencei1 – 5151MEAPT…RIQHW → MRLGNVDFTLGSNVPCVYLV FSVNR in isoform 3. 1 PublicationVSP_042259Add
    BLAST
    Alternative sequencei1 – 3939MEAPT…EEQEK → MTTWSSLQGSHVSKRALAYA L in isoform 4. 1 PublicationVSP_044769Add
    BLAST
    Alternative sequencei476 – 53560AFSGT…LQQKD → VLRLVGYSRNLAPLNVIL in isoform 4. 1 PublicationVSP_044770Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091095 mRNA. Translation: AAD08679.1.
    AB006572 mRNA. Translation: BAA34781.1.
    AK292170 mRNA. Translation: BAF84859.1.
    AC008507 mRNA. No translation available.
    BC026184 mRNA. Translation: AAH26184.2. Different initiation.
    CCDSiCCDS12420.1. [O94763-1]
    CCDS58658.1. [O94763-4]
    RefSeqiNP_001239570.1. NM_001252641.1. [O94763-4]
    NP_003787.2. NM_003796.3. [O94763-1]
    UniGeneiHs.466391.

    Genome annotation databases

    EnsembliENST00000360605; ENSP00000353817; ENSG00000105176. [O94763-4]
    ENST00000392271; ENSP00000376097; ENSG00000105176. [O94763-2]
    GeneIDi8725.
    KEGGihsa:8725.
    UCSCiuc002nsr.3. human. [O94763-1]

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF091095 mRNA. Translation: AAD08679.1 .
    AB006572 mRNA. Translation: BAA34781.1 .
    AK292170 mRNA. Translation: BAF84859.1 .
    AC008507 mRNA. No translation available.
    BC026184 mRNA. Translation: AAH26184.2 . Different initiation.
    CCDSi CCDS12420.1. [O94763-1 ]
    CCDS58658.1. [O94763-4 ]
    RefSeqi NP_001239570.1. NM_001252641.1. [O94763-4 ]
    NP_003787.2. NM_003796.3. [O94763-1 ]
    UniGenei Hs.466391.

    3D structure databases

    ProteinModelPortali O94763.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 114264. 20 interactions.
    IntActi O94763. 32 interactions.
    MINTi MINT-1154170.
    STRINGi 9606.ENSP00000376097.

    PTM databases

    PhosphoSitei O94763.

    Proteomic databases

    MaxQBi O94763.
    PaxDbi O94763.
    PRIDEi O94763.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000360605 ; ENSP00000353817 ; ENSG00000105176 . [O94763-4 ]
    ENST00000392271 ; ENSP00000376097 ; ENSG00000105176 . [O94763-2 ]
    GeneIDi 8725.
    KEGGi hsa:8725.
    UCSCi uc002nsr.3. human. [O94763-1 ]

    Organism-specific databases

    CTDi 8725.
    GeneCardsi GC19P030415.
    H-InvDB HIX0014980.
    HGNCi HGNC:13236. URI1.
    MIMi 603494. gene.
    neXtProti NX_O94763.
    PharmGKBi PA134962614.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG331327.
    HOGENOMi HOG000154150.
    HOVERGENi HBG007610.
    InParanoidi O94763.
    KOi K17560.
    OMAi IPRKSIL.
    OrthoDBi EOG7PZRZV.
    PhylomeDBi O94763.
    TreeFami TF332816.

    Miscellaneous databases

    ChiTaRSi URI1. human.
    GeneWikii C19orf2.
    GenomeRNAii 8725.
    NextBioi 32727.
    PROi O94763.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi O94763.
    Bgeei O94763.
    CleanExi HS_C19orf2.
    Genevestigatori O94763.

    Family and domain databases

    Gene3Di 1.10.287.370. 1 hit.
    InterProi IPR009053. Prefoldin.
    IPR004127. Prefoldin_subunit_alpha.
    [Graphical view ]
    Pfami PF02996. Prefoldin. 1 hit.
    [Graphical view ]
    SUPFAMi SSF46579. SSF46579. 1 hit.
    ProtoNeti Search...

    Publicationsi

    1. "Molecular cloning of a gene on chromosome 19q12 coding for a novel intracellular protein: analysis of expression in human and mouse tissues and in human tumor cells, particularly Reed-Sternberg cells in Hodgkin disease."
      Van Leuven F., Torrekens S., Moechars D., Hilliker C., Buellens M., Bollen M., Delabie J.
      Genomics 54:511-520(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), PHOSPHORYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY.
      Tissue: Liver.
    2. "RMP, a novel RNA polymerase II subunit 5-interacting protein, counteracts transactivation by hepatitis B virus X protein."
      Dorjsuren D., Lin Y., Wei W., Yamashita T., Nomura T., Hayashi N., Murakami S.
      Mol. Cell. Biol. 18:7546-7555(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), INTERACTION WITH POLR2E, TISSUE SPECIFICITY.
      Tissue: Hepatoma.
    3. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    4. "The DNA sequence and biology of human chromosome 19."
      Grimwood J., Gordon L.A., Olsen A.S., Terry A., Schmutz J., Lamerdin J.E., Hellsten U., Goodstein D., Couronne O., Tran-Gyamfi M., Aerts A., Altherr M., Ashworth L., Bajorek E., Black S., Branscomb E., Caenepeel S., Carrano A.V.
      , Caoile C., Chan Y.M., Christensen M., Cleland C.A., Copeland A., Dalin E., Dehal P., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Garcia C., Georgescu A.M., Glavina T., Gomez M., Gonzales E., Groza M., Hammon N., Hawkins T., Haydu L., Ho I., Huang W., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Larionov V., Leem S.-H., Lopez F., Lou Y., Lowry S., Malfatti S., Martinez D., McCready P.M., Medina C., Morgan J., Nelson K., Nolan M., Ovcharenko I., Pitluck S., Pollard M., Popkie A.P., Predki P., Quan G., Ramirez L., Rash S., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., She X., Smith D., Slezak T., Solovyev V., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wagner M., Wheeler J., Wu K., Xie G., Yang J., Dubchak I., Furey T.S., DeJong P., Dickson M., Gordon D., Eichler E.E., Pennacchio L.A., Richardson P., Stubbs L., Rokhsar D.S., Myers R.M., Rubin E.M., Lucas S.M.
      Nature 428:529-535(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    5. "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] (ISOFORM 4).
      Tissue: Testis.
    6. "Interaction with general transcription factor IIF (TFIIF) is required for the suppression of activated transcription by RPB5-mediating protein (RMP)."
      Wei W., Gu J.X., Zhu C.Q., Sun F.Y., Dorjsuren D., Lin Y., Murakami S.
      Cell Res. 13:111-120(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH GTF2F1 AND GTF2F2.
    7. "Control of nutrient-sensitive transcription programs by the unconventional prefoldin URI."
      Gstaiger M., Luke B., Hess D., Oakeley E.J., Wirbelauer C., Blondel M., Vigneron M., Peter M., Krek W.
      Science 302:1208-1212(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, IDENTIFICATION IN THE URI COMPLEX.
    8. "Subcellular localization of RPB5-mediating protein and its putative functional partner."
      Delgermaa L., Hayashi N., Dorjsuren D., Nomura T., Thuy le T.T., Murakami S.
      Mol. Cell. Biol. 24:8556-8566(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH DMAP1, SUBCELLULAR LOCATION.
    9. "S6K1-mediated disassembly of mitochondrial URI/PP1gamma complexes activates a negative feedback program that counters S6K1 survival signaling."
      Djouder N., Metzler S.C., Schmidt A., Wirbelauer C., Gstaiger M., Aebersold R., Hess D., Krek W.
      Mol. Cell 28:28-40(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN DEPHOSPHORYLATION OF PPP1CC, PHOSPHORYLATION AT SER-372 BY RPS6KB1, MUTAGENESIS OF SER-372, SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY.
    10. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    11. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    12. Cited for: FUNCTION, INTERACTION WITH PPP1CC, PHOSPHORYLATION AT SER-372, MUTAGENESIS OF SER-372, TISSUE SPECIFICITY.
    13. Cited for: FUNCTION IN TRANSCRIPTIONAL REGULATION, INTERACTION WITH UXT, PHOSPHORYLATION, TISSUE SPECIFICITY.
    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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    15. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

    Entry informationi

    Entry nameiRMP_HUMAN
    AccessioniPrimary (citable) accession number: O94763
    Secondary accession number(s): A8K805
    , H7BY42, Q8TC23, Q9UNU3
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: March 27, 2002
    Last sequence update: June 16, 2009
    Last modified: October 1, 2014
    This is version 116 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 19
      Human chromosome 19: 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