Q3TLD5 (RMP_MOUSE) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended 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

Organism

Mus musculus (Mouse) [Reference proteome]

Taxonomic identifier

10090 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Glires › Rodentia › Sciurognathi › Muroidea › Muridae › Murinae › Mus › Mus

Protein attributes

Sequence length	531 AA.
Sequence status	Complete.
Protein existence	Evidence 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 projection › dendrite 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 process	Transcription Transcription regulation
Cellular component	Cell projection Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing
Disease	Oncogene
Molecular function	Protein phosphatase inhibitor Repressor
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	cellular 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 phosphatase activity Inferred from sequence or structural similarity. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro regulation of apoptotic process Inferred from sequence or structural similarity. Source: UniProtKB regulation of cell growth Inferred from sequence or structural similarity. Source: UniProtKB response to virus Inferred from electronic annotation. Source: Compara
Cellular_component	DNA-directed RNA polymerase II, core complex Inferred from electronic annotation. Source: Compara 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_function	RNA 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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 531	531	Unconventional prefoldin RPB5 interactor		PRO_0000328753
Amino acid modifications
	Modified residue	242	1	Phosphoserine Ref.4
	Modified residue	369	1	Phosphoserine; by RPS6KB1 By similarity
	Modified residue	437	1	Phosphoserine Ref.4
Natural variations
	Alternative sequence	1 – 74	74	Missing in isoform 2.		VSP_032774
Experimental info
	Sequence conflict	143	1	T → A in BAE38857. Ref.1
	Sequence conflict	201	1	N → D in AAH23029. Ref.3
	Sequence conflict	306	1	E → D in AAH23029. Ref.3
	Sequence conflict	387	1	D → E in AAD08680. Ref.1
	Sequence conflict	403	1	R → H in AAH23029. Ref.3

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified April 8, 2008. Version 2. Checksum: 47624F5450813693	FASTA	531	59,084
	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
	Isoform 2 [UniParc]. Checksum: 5BCCA41FC89E1261	FASTA	457	50,634
	10 20 30 40 50 60 MVPFGPLAFM PGKLVHTNEV TVLLGDNWFA KCSAKQAVGL VEHRKEHVRK TIDDFKKVLK 70 80 90 100 110 120 NFESRVEFTE DLQKMSDAAG DFVDIREEIK SDFEFKGKQR IAHKPHSKPK TSDIFEADFE 130 140 150 160 170 180 NGVKPKNTFD ADELWARLEE LERQEELLGE LESKPDTVIA NGEDRVSSEE EKEGADTGVN 190 200 210 220 230 240 VVSPVTDSSA ASSCKRRAGN AGLPNGQVNS LNYSVNGSNS YHSNKDDDEE EEDDDDDDDE 250 260 270 280 290 300 DDDNESDHAI SADNSIPTIY FSHTVEPKRV RINTGKNTTL KFSEKKEEAK RKRKSGAGSH 310 320 330 340 350 360 ATHELPAIKS PADIYRVFVD VVNGEYVPRK SILKSRSREN SVCSDTSESS AADVEDRRGL 370 380 390 400 410 420 LRSTSSEEAV ATEAGGSSLD ELQENHPKKP LPSGVSEAFS GTVIEKEFLS PSLAPYSAIA 430 440 450 HHALPTIPER KEVPSEVSEE PTKRVSKFRA ARLQQRS

References

	« Hide 'large scale' referencesShow '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. , 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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-242 AND SER-437, MASS SPECTROMETRY. Tissue: Liver.
+	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.
IPI	IPI00331656. IPI00890211.
RefSeq	NP_035404.4. NM_011274.5.
UniGene	Mm.387220.
3D structure databases
ProteinModelPortal	Q3TLD5.
ModBase	Search...
PTM databases
PhosphoSite	Q3TLD5.
Proteomic databases
PaxDb	Q3TLD5.
PRIDE	Q3TLD5.
Protocols and materials databases
DNASU	19777.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENSMUST00000085513; ENSMUSP00000082646; ENSMUSG00000030421.
GeneID	19777.
KEGG	mmu:19777.
UCSC	uc009gkp.2. mouse. uc009gkq.2. mouse.
Organism-specific databases
CTD	8725.
MGI	MGI:1342294. Uri1.
Phylogenomic databases
eggNOG	NOG331327.
GeneTree	ENSGT00390000002362.
HOGENOM	HOG000154150.
HOVERGEN	HBG007610.
InParanoid	Q3TLD5.
OMA	IPRKSIL.
OrthoDB	EOG461444.
Gene expression databases
ArrayExpress	Q3TLD5.
Bgee	Q3TLD5.
Genevestigator	Q3TLD5.
Family and domain databases
InterPro	IPR009053. Prefoldin. IPR004127. Prefoldin_subunit. [Graphical view]
Pfam	PF02996. Prefoldin. 1 hit. [Graphical view]
SUPFAM	SSF46579. Prefoldin. 1 hit.
ProtoNet	Search...
Other
NextBio	297242.
SOURCE	Search...

Entry information

Entry name

RMP_MOUSE

Accession

Primary (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 3, 2013
This is version 57 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program