O94763 (RMP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	URI1
Synonyms:	C19orf2, NNX3, PPP1R19, RMP, URI

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	535 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. Antagonizes transcriptional modulation via hepatitis B virus X protein. Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13 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. Ref.6 Ref.7 Ref.8 Ref.9 Ref.12 Ref.13
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. Ref.2 Ref.6 Ref.7 Ref.8 Ref.12 Ref.13
Subcellular location	Nucleus. Cytoplasm. Mitochondrion. Cell projection › dendrite By similarity. Note: Colocalizes with PFDN2, PFDN4, PPP1CC, RPS6KB1 and STAP1 at mitochondrion. Ref.1 Ref.8 Ref.9
Tissue specificity	Ubiquitous. Expressed in ovarian cancers (at protein level). Expressed strongly in skeletal muscle. Expressed weakly in brain, heart, pancreas and in prostate epithelial cells. Ref.1 Ref.2 Ref.12 Ref.13
Post-translational modification	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. Ref.1 Ref.9 Ref.12 Ref.13
Sequence similarities	Belongs to the RNA polymerase II subunit 5-mediating protein family.
Sequence caution	The sequence AAH26184.2 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

Ontologies

Keywords
Biological process	Transcription Transcription regulation
Cellular component	Cell projection Cytoplasm Mitochondrion Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
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 direct assay Ref.9. Source: UniProtKB cellular response to steroid hormone stimulus Inferred from direct assay Ref.13. Source: UniProtKB negative regulation of phosphatase activity Inferred from mutant phenotype Ref.9. Source: UniProtKB protein folding Inferred from electronic annotation. Source: InterPro regulation of apoptotic process Inferred from mutant phenotype Ref.9. Source: UniProtKB regulation of cell growth Inferred from direct assay Ref.13. Source: UniProtKB response to virus Inferred from mutant phenotype Ref.2. Source: UniProtKB
Cellular_component	DNA-directed RNA polymerase II, core complex Inferred from direct assay Ref.2. Source: UniProtKB cytoplasm Inferred from direct assay Ref.8Ref.9Ref.13. Source: UniProtKB dendrite Inferred from electronic annotation. Source: UniProtKB-SubCell mitochondrion Inferred from electronic annotation. Source: UniProtKB-SubCell prefoldin complex Inferred from electronic annotation. Source: InterPro
Molecular_function	RNA polymerase II transcription corepressor activity Inferred from direct assay Ref.6Ref.8Ref.13. Source: UniProtKB chromatin binding Inferred from direct assay Ref.13. Source: UniProtKB protein phosphatase inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
GTF2F1	P35269	3	EBI-357067,EBI-457886
GTF2F2	P13984	4	EBI-357067,EBI-1030560
POLR2E	P19388	2	EBI-357067,EBI-395189
PPP1CC	P36873	5	EBI-357067,EBI-356283

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: O94763-1)

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: O94763-2)

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

Isoform 3 (identifier: O94763-3)

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

Note: No experimental confirmation available.

Isoform 4 (identifier: O94763-4)

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.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 535	535	Unconventional prefoldin RPB5 interactor 1		PRO_0000097365
Regions
	Compositional bias	299 – 311	13	Poly-Asp
	Compositional bias	314 – 321	8	Poly-Asp
Amino acid modifications
	Modified residue	244	1	Phosphoserine By similarity
	Modified residue	372	1	Phosphoserine; by RPS6KB1 Ref.9 Ref.10 Ref.12
	Modified residue	440	1	Phosphoserine By similarity
Natural variations
	Alternative sequence	1 – 76	76	Missing in isoform 2.		VSP_032773
	Alternative sequence	1 – 51	51	MEAPT…RIQHW → MRLGNVDFTLGSNVPCVYLV FSVNR in isoform 3.		VSP_042259
	Alternative sequence	1 – 39	39	MEAPT…EEQEK → MTTWSSLQGSHVSKRALAYA L in isoform 4.		VSP_044769
	Alternative sequence	476 – 535	60	AFSGT…LQQKD → VLRLVGYSRNLAPLNVIL in isoform 4.		VSP_044770
	Natural variant	22	1	L → P. Corresponds to variant rs189187 [ dbSNP | Ensembl ].		VAR_056978
Experimental info
	Mutagenesis	372	1	S → A: Does not lead to dissociation of the URI1-PPP1CC complex. Enhances phosphorylation of RPS6KB1 after IGF1 stimulation. Confers a cell survival increase. Ref.9 Ref.12
	Sequence conflict	7	1	E → G in BAF84859. Ref.3
	Sequence conflict	232	1	D → N in AAH26184. Ref.5
	Sequence conflict	311	1	Missing in AAD08679. Ref.1
	Sequence conflict	311	1	Missing in BAA34781. Ref.2
	Sequence conflict	311	1	Missing in BAF84859. Ref.3
	Sequence conflict	311	1	Missing in AAH26184. Ref.5
	Sequence conflict	315	1	D → E in BAF84859. Ref.3
	Sequence conflict	434	1	R → G in BAA34781. Ref.2

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified June 16, 2009. Version 3. Checksum: DBB046A392E3C752	FASTA	535	59,832
	10 20 30 40 50 60 MEAPTVETPP DPSPPSAPAP ALVPLRAPDV ARLREEQEKV VTNCQERIQH WKKVDNDYNA 70 80 90 100 110 120 LRERLSTLPD KLSYNIMVPF GPFAFMPGKL VHTNEVTVLL GDNWFAKCSA KQAVGLVEHR 130 140 150 160 170 180 KEHVRKTIDD LKKVMKNFES RVEFTEDLQK MSDAAGDIVD IREEIKCDFE FKAKHRIAHK 190 200 210 220 230 240 PHSKPKTSDI FEADIANDVK SKDLLADKEL WARLEELERQ EELLGELDSK PDTVIANGED 250 260 270 280 290 300 TTSSEEEKED RNTNVNAMHQ VTDSHTPCHK DVASSEPFSG QVNSQLNCSV NGSSSYHSDD 310 320 330 340 350 360 DDDDDDDDDD DNIDDDDGDN DHEALGVGDN SIPTIYFSHT VEPKRVRINT GKNTTLKFSE 370 380 390 400 410 420 KKEEAKRKRK NSTGSGHSAQ ELPTIRTPAD IYRAFVDVVN GEYVPRKSIL KSRSRENSVC 430 440 450 460 470 480 SDTSESSAAE FDDRRGVLRS ISCEEATCSD TSESILEEEP QENQKKLLPL SVTPEAFSGT 490 500 510 520 530 VIEKEFVSPS LTPPPAIAHP ALPTIPERKE VLLEASEETG KRVSKFKAAR LQQKD
	Isoform 2 [UniParc]. Checksum: 5EF69C27FEB5EAFE	FASTA	459	51,247
	10 20 30 40 50 60 MVPFGPFAFM PGKLVHTNEV TVLLGDNWFA KCSAKQAVGL VEHRKEHVRK TIDDLKKVMK 70 80 90 100 110 120 NFESRVEFTE DLQKMSDAAG DIVDIREEIK CDFEFKAKHR IAHKPHSKPK TSDIFEADIA 130 140 150 160 170 180 NDVKSKDLLA DKELWARLEE LERQEELLGE LDSKPDTVIA NGEDTTSSEE EKEDRNTNVN 190 200 210 220 230 240 AMHQVTDSHT PCHKDVASSE PFSGQVNSQL NCSVNGSSSY HSDDDDDDDD DDDDDNIDDD 250 260 270 280 290 300 DGDNDHEALG VGDNSIPTIY FSHTVEPKRV RINTGKNTTL KFSEKKEEAK RKRKNSTGSG 310 320 330 340 350 360 HSAQELPTIR TPADIYRAFV DVVNGEYVPR KSILKSRSRE NSVCSDTSES SAAEFDDRRG 370 380 390 400 410 420 VLRSISCEEA TCSDTSESIL EEEPQENQKK LLPLSVTPEA FSGTVIEKEF VSPSLTPPPA 430 440 450 IAHPALPTIP ERKEVLLEAS EETGKRVSKF KAARLQQKD
	Isoform 3 [UniParc]. Checksum: 5BA8E178FAE37863	FASTA	509	56,978
	10 20 30 40 50 60 MRLGNVDFTL GSNVPCVYLV FSVNRKKVDN DYNALRERLS TLPDKLSYNI MVPFGPFAFM 70 80 90 100 110 120 PGKLVHTNEV TVLLGDNWFA KCSAKQAVGL VEHRKEHVRK TIDDLKKVMK NFESRVEFTE 130 140 150 160 170 180 DLQKMSDAAG DIVDIREEIK CDFEFKAKHR IAHKPHSKPK TSDIFEADIA NDVKSKDLLA 190 200 210 220 230 240 DKELWARLEE LERQEELLGE LDSKPDTVIA NGEDTTSSEE EKEDRNTNVN AMHQVTDSHT 250 260 270 280 290 300 PCHKDVASSE PFSGQVNSQL NCSVNGSSSY HSDDDDDDDD DDDDDNIDDD DGDNDHEALG 310 320 330 340 350 360 VGDNSIPTIY FSHTVEPKRV RINTGKNTTL KFSEKKEEAK RKRKNSTGSG HSAQELPTIR 370 380 390 400 410 420 TPADIYRAFV DVVNGEYVPR KSILKSRSRE NSVCSDTSES SAAEFDDRRG VLRSISCEEA 430 440 450 460 470 480 TCSDTSESIL EEEPQENQKK LLPLSVTPEA FSGTVIEKEF VSPSLTPPPA IAHPALPTIP 490 500 ERKEVLLEAS EETGKRVSKF KAARLQQKD
	Isoform 4 [UniParc]. Checksum: 2B9B965CD25CE296	FASTA	475	53,447
	10 20 30 40 50 60 MTTWSSLQGS HVSKRALAYA LVVTNCQERI QHWKKVDNDY NALRERLSTL PDKLSYNIMV 70 80 90 100 110 120 PFGPFAFMPG KLVHTNEVTV LLGDNWFAKC SAKQAVGLVE HRKEHVRKTI DDLKKVMKNF 130 140 150 160 170 180 ESRVEFTEDL QKMSDAAGDI VDIREEIKCD FEFKAKHRIA HKPHSKPKTS DIFEADIAND 190 200 210 220 230 240 VKSKDLLADK ELWARLEELE RQEELLGELD SKPDTVIANG EDTTSSEEEK EDRNTNVNAM 250 260 270 280 290 300 HQVTDSHTPC HKDVASSEPF SGQVNSQLNC SVNGSSSYHS DDDDDDDDDD DDDNIDDDDG 310 320 330 340 350 360 DNDHEALGVG DNSIPTIYFS HTVEPKRVRI NTGKNTTLKF SEKKEEAKRK RKNSTGSGHS 370 380 390 400 410 420 AQELPTIRTP ADIYRAFVDV VNGEYVPRKS ILKSRSRENS VCSDTSESSA AEFDDRRGVL 430 440 450 460 470 RSISCEEATC SDTSESILEE EPQENQKKLL PLSVTPEVLR LVGYSRNLAP LNVIL

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, 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 SPECTROMETRY.
[10]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-372, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[11]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[12]	"URI is an oncogene amplified in ovarian cancer cells and is required for their survival." Theurillat J.P., Metzler S.C., Henzi N., Djouder N., Helbling M., Zimmermann A.K., Jacob F., Soltermann A., Caduff R., Heinzelmann-Schwarz V., Moch H., Krek W. Cancer Cell 19:317-332(2011) [PubMed] [Europe PMC] [Abstract] Cited for: FUNCTION, INTERACTION WITH PPP1CC, PHOSPHORYLATION AT SER-372, MUTAGENESIS OF SER-372, TISSUE SPECIFICITY.
[13]	"Regulation of androgen receptor-mediated transcription by RPB5 binding protein URI/RMP." Mita P., Savas J.N., Djouder N., Yates J.R. III, Ha S., Ruoff R., Schafler E.D., Nwachukwu J.C., Tanese N., Cowan N.J., Zavadil J., Garabedian M.J., Logan S.K. Mol. Cell. Biol. 31:3639-3652(2011) [PubMed] [Europe PMC] [Abstract] 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].
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
IPI	IPI00477619. IPI00939535. IPI01015668.
RefSeq	NP_001239570.1. NM_001252641.1. NP_003787.2. NM_003796.3.
UniGene	Hs.466391.
3D structure databases
ProteinModelPortal	O94763.
ModBase	Search...
Protein-protein interaction databases
IntAct	O94763. 19 interactions.
MINT	MINT-1154170.
STRING	9606.ENSP00000376097.
PTM databases
PhosphoSite	O94763.
Proteomic databases
PaxDb	O94763.
PRIDE	O94763.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360605; ENSP00000353817; ENSG00000105176. ENST00000392271; ENSP00000376097; ENSG00000105176. ENST00000542441; ENSP00000442436; ENSG00000105176.
GeneID	8725.
KEGG	hsa:8725.
UCSC	uc002nsq.3. human.
Organism-specific databases
CTD	8725.
GeneCards	GC19P030415.
H-InvDB	HIX0014980.
HGNC	HGNC:13236. URI1.
MIM	603494. gene.
neXtProt	NX_O94763.
PharmGKB	PA134962614.
GenAtlas	Search...
Phylogenomic databases
eggNOG	NOG331327.
HOGENOM	HOG000154150.
HOVERGEN	HBG007610.
InParanoid	O94763.
OMA	IPRKSIL.
PhylomeDB	O94763.
Gene expression databases
ArrayExpress	O94763.
Bgee	O94763.
CleanEx	HS_C19orf2.
Genevestigator	O94763.
GermOnline	ENSG00000105176. Homo sapiens.
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
ChiTaRS	URI1. human.
GenomeRNAi	8725.
NextBio	32727.
SOURCE	Search...

Entry information

Entry name

RMP_HUMAN

Accession

Primary (citable) accession number: O94763
Secondary accession number(s): A8K805 , H7BY42, Q8TC23, Q9UNU3

Entry history

Integrated into UniProtKB/Swiss-Prot:	March 27, 2002
Last sequence update:	June 16, 2009
Last modified:	May 1, 2013
This is version 102 of the entry and version 3 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.