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O94763 (RMP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified July 9, 2014. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length535 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. 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-terminal 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 projectiondendrite 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 processTranscription
Transcription regulation
   Cellular componentCell projection
Cytoplasm
Mitochondrion
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   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 direct assay Ref.9. Source: UniProtKB

cellular response to steroid hormone stimulus

Inferred from direct assay Ref.13. Source: UniProtKB

negative regulation of intrinsic apoptotic signaling pathway

Inferred from mutant phenotype Ref.9. Source: UniProtKB

negative regulation of phosphatase activity

Inferred from mutant phenotype Ref.9. Source: UniProtKB

negative regulation of transcription from RNA polymerase II promoter

Inferred from direct assay Ref.6Ref.8Ref.13. Source: UniProtKB

protein folding

Inferred from electronic annotation. Source: InterPro

regulation of cell growth

Inferred from direct assay Ref.13. Source: UniProtKB

regulation of transcription from RNA polymerase II promoter

Inferred from mutant phenotype Ref.2. Source: UniProtKB

response to virus

Inferred from mutant phenotype Ref.2. Source: UniProtKB

   Cellular_componentDNA-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

nucleus

Inferred from direct assay Ref.8Ref.9Ref.13. Source: UniProtKB

prefoldin complex

Inferred from electronic annotation. Source: InterPro

   Molecular_functionRNA 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 binding

Inferred from physical interaction Ref.6Ref.8Ref.9Ref.13. Source: UniProtKB

protein phosphatase inhibitor activity

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

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 keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 535535Unconventional prefoldin RPB5 interactor 1
PRO_0000097365

Regions

Compositional bias299 – 31113Poly-Asp
Compositional bias314 – 3218Poly-Asp

Amino acid modifications

Modified residue11N-acetylmethionine Ref.15
Modified residue3721Phosphoserine; by RPS6KB1 Ref.9 Ref.10 Ref.12

Natural variations

Alternative sequence1 – 7676Missing in isoform 2.
VSP_032773
Alternative sequence1 – 5151MEAPT…RIQHW → MRLGNVDFTLGSNVPCVYLV FSVNR in isoform 3.
VSP_042259
Alternative sequence1 – 3939MEAPT…EEQEK → MTTWSSLQGSHVSKRALAYA L in isoform 4.
VSP_044769
Alternative sequence476 – 53560AFSGT…LQQKD → VLRLVGYSRNLAPLNVIL in isoform 4.
VSP_044770
Natural variant221L → P.
Corresponds to variant rs189187 [ dbSNP | Ensembl ].
VAR_056978

Experimental info

Mutagenesis3721S → 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 conflict71E → G in BAF84859. Ref.3
Sequence conflict2321D → N in AAH26184. Ref.5
Sequence conflict3111Missing in AAD08679. Ref.1
Sequence conflict3111Missing in BAA34781. Ref.2
Sequence conflict3111Missing in BAF84859. Ref.3
Sequence conflict3111Missing in AAH26184. Ref.5
Sequence conflict3151D → E in BAF84859. Ref.3
Sequence conflict4341R → G in BAA34781. Ref.2

Sequences

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

Last modified June 16, 2009. Version 3.
Checksum: DBB046A392E3C752

FASTA53559,832
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 5EF69C27FEB5EAFE
Show »

FASTA45951,247
Isoform 3 [UniParc].

Checksum: 5BA8E178FAE37863
Show »

FASTA50956,978
Isoform 4 [UniParc].

Checksum: 2B9B965CD25CE296
Show »

FASTA47553,447

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, 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. expand/collapse author list , 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. expand/collapse author list , 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]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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].
[15]"N-terminal acetylome analyses and functional insights of the N-terminal acetyltransferase NatB."
Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A., Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E., Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.
Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, 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.
CCDSCCDS12420.1. [O94763-1]
CCDS58658.1. [O94763-4]
RefSeqNP_001239570.1. NM_001252641.1. [O94763-4]
NP_003787.2. NM_003796.3. [O94763-1]
UniGeneHs.466391.

3D structure databases

ProteinModelPortalO94763.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid114264. 20 interactions.
IntActO94763. 19 interactions.
MINTMINT-1154170.
STRING9606.ENSP00000376097.

PTM databases

PhosphoSiteO94763.

Proteomic databases

MaxQBO94763.
PaxDbO94763.
PRIDEO94763.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000360605; ENSP00000353817; ENSG00000105176. [O94763-4]
ENST00000392271; ENSP00000376097; ENSG00000105176. [O94763-2]
ENST00000542441; ENSP00000442436; ENSG00000105176. [O94763-1]
GeneID8725.
KEGGhsa:8725.
UCSCuc002nsr.3. human. [O94763-1]

Organism-specific databases

CTD8725.
GeneCardsGC19P030415.
H-InvDBHIX0014980.
HGNCHGNC:13236. URI1.
MIM603494. gene.
neXtProtNX_O94763.
PharmGKBPA134962614.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG331327.
HOGENOMHOG000154150.
HOVERGENHBG007610.
InParanoidO94763.
KOK17560.
OMAIPRKSIL.
OrthoDBEOG7PZRZV.
PhylomeDBO94763.
TreeFamTF332816.

Gene expression databases

ArrayExpressO94763.
BgeeO94763.
CleanExHS_C19orf2.
GenevestigatorO94763.

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

ChiTaRSURI1. human.
GeneWikiC19orf2.
GenomeRNAi8725.
NextBio32727.
PROO94763.
SOURCESearch...

Entry information

Entry nameRMP_HUMAN
AccessionPrimary (citable) accession number: O94763
Secondary accession number(s): A8K805 expand/collapse secondary AC list , H7BY42, Q8TC23, Q9UNU3
Entry history
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 statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 19

Human chromosome 19: entries, gene names and cross-references to MIM