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O94763

- RMP_HUMAN

UniProt

O94763 - RMP_HUMAN

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Protein
Unconventional prefoldin RPB5 interactor 1
Gene
URI1, C19orf2, NNX3, PPP1R19, RMP, URI
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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.6 Publications
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.6 Publications

GO - Molecular functioni

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

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
Complete GO annotation...

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.3 Publications

GO - Cellular componenti

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

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 1
PRO_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.4 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
POLR2EP193882EBI-357067,EBI-395189
PPP1CCP368736EBI-357067,EBI-356283

Protein-protein interaction databases

BioGridi114264. 20 interactions.
IntActiO94763. 19 interactions.
MINTiMINT-1154170.
STRINGi9606.ENSP00000376097.

Structurei

3D structure databases

ProteinModelPortaliO94763.

Family & Domainsi

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi299 – 31113Poly-Asp
Add
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.

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.
VSP_032773Add
BLAST
Alternative sequencei1 – 5151MEAPT…RIQHW → MRLGNVDFTLGSNVPCVYLV FSVNR in isoform 3.
VSP_042259Add
BLAST
Alternative sequencei1 – 3939MEAPT…EEQEK → MTTWSSLQGSHVSKRALAYA L in isoform 4.
VSP_044769Add
BLAST
Alternative sequencei476 – 53560AFSGT…LQQKD → VLRLVGYSRNLAPLNVIL in isoform 4.
VSP_044770Add
BLAST

Sequence conflict

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti7 – 71E → G in BAF84859. 1 Publication
Sequence conflicti232 – 2321D → N in AAH26184. 1 Publication
Sequence conflicti311 – 3111Missing in AAD08679. 1 Publication
Sequence conflicti311 – 3111Missing in BAA34781. 1 Publication
Sequence conflicti311 – 3111Missing in BAF84859. 1 Publication
Sequence conflicti311 – 3111Missing in AAH26184. 1 Publication
Sequence conflicti315 – 3151D → E in BAF84859. 1 Publication
Sequence conflicti434 – 4341R → G in BAA34781. 1 Publication

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]
ENST00000542441; ENSP00000442436; ENSG00000105176. [O94763-1]
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. 19 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 ]
ENST00000542441 ; ENSP00000442436 ; ENSG00000105176 . [O94763-1 ]
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

« Hide 'large scale' publications
  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: July 9, 2014
This is version 115 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

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