Skip Header

You are using a version of Internet Explorer that may not display all features of this website. Please upgrade to a modern browser.
Contribute Send feedback
Read comments (?) or add your own

Q3TLD5 (RMP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 66. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Unconventional prefoldin RPB5 interactor
Alternative name(s):
Protein NNX3
Protein phosphatase 1 regulatory subunit 19
RNA polymerase II subunit 5-mediating protein
Short name=RPB5-mediating protein
Gene names
Name:Uri1
Synonyms:Nnx3, Ppp1r19, Rmp, Uri
OrganismMus musculus (Mouse) [Reference proteome]
Taxonomic identifier10090 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus

Protein attributes

Sequence length531 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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 By similarity.

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 By similarity.

Subunit structure

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-terminus region) with GTF2F1 and GTF2F2. Interacts with DMAP1, POLR2E/RPB5 and UXT By similarity.

Subcellular location

Nucleus. Cytoplasm. Mitochondrion. Cell projectiondendrite By similarity. Note: Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 in mitochondrion. Ref.1

Tissue specificity

Expressed in the spinal cord, ganglia, choroid plexus and olfactors epithelium of the developing brain. Expressed in skin, lung, kidney, testis and muscles (at protein level). Expressed strongly in brain and kidney. Expressed weakly in skeletal muscle, lung and liver. Ref.1

Developmental stage

Expressed in embryo at 6 dpc, onward. Ref.1

Post-translational modification

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-369 by RPS6KB1 in a growth factor- and rapamycin-dependent manner. S6K1-mediated mitochondrial phosphorylation at Ser-369 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 By similarity. Phosphorylated. Phosphorylation occurs essentially on serine residues. Ref.1

Sequence similarities

Belongs to the RNA polymerase II subunit 5-mediating protein family.

Ontologies

Keywords
   Biological processTranscription
Transcription regulation
   Cellular componentCell projection
Cytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
   DiseaseOncogene
   Molecular functionProtein phosphatase inhibitor
Repressor
   PTMAcetylation
Phosphoprotein
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcellular response to growth factor stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

cellular response to steroid hormone stimulus

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of phosphatase activity

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from sequence or structural similarity. Source: UniProtKB

protein folding

Inferred from electronic annotation. Source: InterPro

regulation of cell growth

Inferred from sequence or structural similarity. Source: UniProtKB

response to virus

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentDNA-directed RNA polymerase II, core complex

Inferred from electronic annotation. Source: Ensembl

cytoplasm

Inferred from sequence or structural similarity. Source: UniProtKB

dendrite

Inferred from electronic annotation. Source: UniProtKB-SubCell

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

prefoldin complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionRNA polymerase II transcription corepressor activity

Inferred from sequence or structural similarity. Source: UniProtKB

chromatin binding

Inferred from sequence or structural similarity. Source: UniProtKB

protein phosphatase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q3TLD5-1)

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 (identifier: Q3TLD5-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-74: Missing.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 531531Unconventional prefoldin RPB5 interactor
PRO_0000328753

Amino acid modifications

Modified residue11N-acetylmethionine By similarity
Modified residue3691Phosphoserine; by RPS6KB1 By similarity

Natural variations

Alternative sequence1 – 7474Missing in isoform 2.
VSP_032774

Experimental info

Sequence conflict1431T → A in BAE38857. Ref.1
Sequence conflict2011N → D in AAH23029. Ref.3
Sequence conflict3061E → D in AAH23029. Ref.3
Sequence conflict3871D → E in AAD08680. Ref.1
Sequence conflict4031R → H in AAH23029. Ref.3

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified April 8, 2008. Version 2.
Checksum: 47624F5450813693

FASTA53159,084
        10         20         30         40         50         60 
MEPPSEPEPE PQPLAEASAA APLRAPEVAR LREEQEKVVT NCQEKIQHWE KVDNDYSALQ 

        70         80         90        100        110        120 
ERLRTLPDKL SYDVMVPFGP LAFMPGKLVH TNEVTVLLGD NWFAKCSAKQ AVGLVEHRKE 

       130        140        150        160        170        180 
HVRKTIDDFK KVLKNFESRV EFTEDLQKMS DAAGDFVDIR EEIKSDFEFK GKQRIAHKPH 

       190        200        210        220        230        240 
SKPKTSDIFE ADFENGVKPK NTFDADELWA RLEELERQEE LLGELESKPD TVIANGEDRV 

       250        260        270        280        290        300 
SSEEEKEGAD TGVNVVSPVT DSSAASSCKR RAGNAGLPNG QVNSLNYSVN GSNSYHSNKD 

       310        320        330        340        350        360 
DDEEEEDDDD DDDEDDDNES DHAISADNSI PTIYFSHTVE PKRVRINTGK NTTLKFSEKK 

       370        380        390        400        410        420 
EEAKRKRKSG AGSHATHELP AIKSPADIYR VFVDVVNGEY VPRKSILKSR SRENSVCSDT 

       430        440        450        460        470        480 
SESSAADVED RRGLLRSTSS EEAVATEAGG SSLDELQENH PKKPLPSGVS EAFSGTVIEK 

       490        500        510        520        530 
EFLSPSLAPY SAIAHHALPT IPERKEVPSE VSEEPTKRVS KFRAARLQQR S 

« Hide

Isoform 2 [UniParc].

Checksum: 5BCCA41FC89E1261
Show »

FASTA45750,634

References

« Hide 'large scale' references
[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, DEVELOPMENTAL STAGE, TISSUE SPECIFICITY.
Tissue: Brain.
[2]"The transcriptional landscape of the mammalian genome."
Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J. expand/collapse author list , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
Strain: C57BL/6J.
Tissue: Testis.
[3]"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 2).
Strain: FVB/N-3.
Tissue: Mammary tumor.
[4]"Large-scale phosphorylation analysis of mouse liver."
Villen J., Beausoleil S.A., Gerber S.A., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 104:1488-1493(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Tissue: Liver.
[5]"The phagosomal proteome in interferon-gamma-activated macrophages."
Trost M., English L., Lemieux S., Courcelles M., Desjardins M., Thibault P.
Immunity 30:143-154(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AF091096 mRNA. Translation: AAD08680.1.
AK133383 mRNA. Translation: BAE21626.1.
AK166566 mRNA. Translation: BAE38857.1.
BC023029 mRNA. Translation: AAH23029.1.
RefSeqNP_035404.4. NM_011274.5.
XP_006539741.1. XM_006539678.1.
UniGeneMm.387220.

3D structure databases

ProteinModelPortalQ3TLD5.
ModBaseSearch...
MobiDBSearch...

PTM databases

PhosphoSiteQ3TLD5.

Proteomic databases

PaxDbQ3TLD5.
PRIDEQ3TLD5.

Protocols and materials databases

DNASU19777.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENSMUST00000085513; ENSMUSP00000082646; ENSMUSG00000030421. [Q3TLD5-1]
GeneID19777.
KEGGmmu:19777.
UCSCuc009gkp.2. mouse. [Q3TLD5-1]

Organism-specific databases

CTD8725.
MGIMGI:1342294. Uri1.

Phylogenomic databases

eggNOGNOG331327.
GeneTreeENSGT00390000002362.
HOGENOMHOG000154150.
HOVERGENHBG007610.
InParanoidQ3TLD5.
KOK17560.
OMAIPRKSIL.
OrthoDBEOG7PZRZV.
PhylomeDBQ3TLD5.
TreeFamTF332816.

Gene expression databases

ArrayExpressQ3TLD5.
BgeeQ3TLD5.
GenevestigatorQ3TLD5.

Family and domain databases

Gene3D1.10.287.370. 1 hit.
InterProIPR009053. Prefoldin.
IPR004127. Prefoldin_subunit_alpha.
[Graphical view]
PfamPF02996. Prefoldin. 1 hit.
[Graphical view]
SUPFAMSSF46579. SSF46579. 1 hit.
ProtoNetSearch...

Other

NextBio297242.
PROQ3TLD5.
SOURCESearch...

Entry information

Entry nameRMP_MOUSE
AccessionPrimary (citable) accession number: Q3TLD5
Secondary accession number(s): Q3V078, Q8R5C4, Q9Z243
Entry history
Integrated into UniProtKB/Swiss-Prot: April 8, 2008
Last sequence update: April 8, 2008
Last modified: April 16, 2014
This is version 66 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

MGD cross-references

Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot