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P85299 (PRR5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified May 29, 2013. Version 52. 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·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order
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:
Proline-rich protein 5
Alternative name(s):
Protein observed with Rictor-1
Short name=Protor-1
Gene names
Name:PRR5
Synonyms:PROTOR1
ORF Names:PP610
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length388 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Subunit of mTORC2, which regulates cell growth and survival in response to hormonal signals. mTORC2 is activated by growth factors, but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2 seems to function upstream of Rho GTPases to regulate the actin cytoskeleton, probably by activating one or more Rho-type guanine nucleotide exchange factors. mTORC2 promotes the serum-induced formation of stress-fibers or F-actin. mTORC2 plays a critical role in AKT1 'Ser-473' phosphorylation, which may facilitate the phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1 which is a prerequisite for full activation. mTORC2 regulates the phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the phosphorylation of PRKCA on 'Ser-657'. PRR5 plays an important role in regulation of PDGFRB expression and in modulation of platelet-derived growth factor signaling. May act as a tumor suppressor in breast cancer. Ref.6 Ref.8

Subunit structure

Part of the mammalian target of rapamycin complex 2 (mTORC2) which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR. Contrary to mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to MTOR and RICTOR within the TORC2 complex. Ref.7 Ref.8

Tissue specificity

Most abundant in kidney and liver. Also highly expressed in brain, spleen, testis and placenta. Overexpressed in several colorectal tumors. Ref.6 Ref.8

Sequence similarities

Belongs to the PROTOR family.

Ontologies

Keywords
   Biological processCell cycle
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseTumor suppressor
   Technical termComplete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

Complete GO annotation...

Alternative products

This entry describes 5 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P85299-1)

Also known as: alpha;

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: P85299-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-101: Missing.
     102-107: KIRFYE → MAPMPT
Isoform 3 (identifier: P85299-3)

Also known as: beta;

The sequence of this isoform differs from the canonical sequence as follows:
     1-9: Missing.
Note: Derived from EST data. No experimental confirmation available.
Isoform 4 (identifier: P85299-4)

Also known as: gamma;

The sequence of this isoform differs from the canonical sequence as follows:
     1-95: Missing.
Note: Derived from EST data. No experimental confirmation available.
Isoform 5 (identifier: P85299-5)

The sequence of this isoform differs from the canonical sequence as follows:
     1-5: MRTLR → MVCLELSQREAWGSGSPEKMPAQPEGLY
Note: No experimental confirmation available.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 388388Proline-rich protein 5
PRO_0000308162

Regions

Region10 – 9586Interaction with RICTOR
Region188 – 21831Interaction with RICTOR
Compositional bias24 – 274Poly-Ala

Natural variations

Alternative sequence1 – 101101Missing in isoform 2.
VSP_001646
Alternative sequence1 – 9595Missing in isoform 4.
VSP_028884
Alternative sequence1 – 99Missing in isoform 3.
VSP_028885
Alternative sequence1 – 55MRTLR → MVCLELSQREAWGSGSPEKM PAQPEGLY in isoform 5.
VSP_045883
Alternative sequence102 – 1076KIRFYE → MAPMPT in isoform 2.
VSP_001648
Natural variant2431V → M.
Corresponds to variant rs36082900 [ dbSNP | Ensembl ].
VAR_062230

Experimental info

Sequence conflict2801R → W in BAA90999. Ref.1

Sequences

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

Last modified October 23, 2007. Version 1.
Checksum: FA6B90495623EF3F

FASTA38842,753
        10         20         30         40         50         60 
MRTLRRLKFM SSPSLSDLGK REPAAAADER GTQQRRACAN ATWNSIHNGV IAVFQRKGLP 

        70         80         90        100        110        120 
DQELFSLNEG VRQLLKTELG SFFTEYLQNQ LLTKGMVILR DKIRFYEGQK LLDSLAETWD 

       130        140        150        160        170        180 
FFFSDVLPML QAIFYPVQGK EPSVRQLALL HFRNAITLSV KLEDALARAH ARVPPAIVQM 

       190        200        210        220        230        240 
LLVLQGVHES RGVTEDYLRL ETLVQKVVSP YLGTYGLHSS EGPFTHSCIL EKRLLRRSRS 

       250        260        270        280        290        300 
GDVLAKNPVV RSKSYNTPLL NPVQEHEAEG AAAGGTSIRR HSVSEMTSCP EPQGFSDPPG 

       310        320        330        340        350        360 
QGPTGTFRSS PAPHSGPCPS RLYPTTQPPE QGLDPTRSSL PRSSPENLVD QILESVDSDS 

       370        380 
EGIFIDFGRG RGSGMSDLEG SGGRQSVV

« Hide

Isoform 2 [UniParc] [UniParc].

Checksum: 24E46CD123CA100E
Show »

FASTA28731,125
Isoform 3 (beta) [UniParc].

Checksum: 1A0E3E17802AFD85
Show »

FASTA37941,551
Isoform 4 (gamma) [UniParc].

Checksum: 63D42183C35C9A0B
Show »

FASTA29332,061
Isoform 5 [UniParc].

Checksum: 85B5B9159AB9350B
Show »

FASTA41145,172

References

« Hide 'large scale' references
[1]"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] (ISOFORMS 2 AND 5).
Tissue: Colon mucosa and Kidney.
[2]"Large-scale cDNA transfection screening for genes related to cancer development and progression."
Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X., Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X. expand/collapse author list , Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.
Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
[3]"The DNA sequence of human chromosome 22."
Dunham I., Hunt A.R., Collins J.E., Bruskiewich R., Beare D.M., Clamp M., Smink L.J., Ainscough R., Almeida J.P., Babbage A.K., Bagguley C., Bailey J., Barlow K.F., Bates K.N., Beasley O.P., Bird C.P., Blakey S.E., Bridgeman A.M. expand/collapse author list , Buck D., Burgess J., Burrill W.D., Burton J., Carder C., Carter N.P., Chen Y., Clark G., Clegg S.M., Cobley V.E., Cole C.G., Collier R.E., Connor R., Conroy D., Corby N.R., Coville G.J., Cox A.V., Davis J., Dawson E., Dhami P.D., Dockree C., Dodsworth S.J., Durbin R.M., Ellington A.G., Evans K.L., Fey J.M., Fleming K., French L., Garner A.A., Gilbert J.G.R., Goward M.E., Grafham D.V., Griffiths M.N.D., Hall C., Hall R.E., Hall-Tamlyn G., Heathcott R.W., Ho S., Holmes S., Hunt S.E., Jones M.C., Kershaw J., Kimberley A.M., King A., Laird G.K., Langford C.F., Leversha M.A., Lloyd C., Lloyd D.M., Martyn I.D., Mashreghi-Mohammadi M., Matthews L.H., Mccann O.T., Mcclay J., Mclaren S., McMurray A.A., Milne S.A., Mortimore B.J., Odell C.N., Pavitt R., Pearce A.V., Pearson D., Phillimore B.J.C.T., Phillips S.H., Plumb R.W., Ramsay H., Ramsey Y., Rogers L., Ross M.T., Scott C.E., Sehra H.K., Skuce C.D., Smalley S., Smith M.L., Soderlund C., Spragon L., Steward C.A., Sulston J.E., Swann R.M., Vaudin M., Wall M., Wallis J.M., Whiteley M.N., Willey D.L., Williams L., Williams S.A., Williamson H., Wilmer T.E., Wilming L., Wright C.L., Hubbard T., Bentley D.R., Beck S., Rogers J., Shimizu N., Minoshima S., Kawasaki K., Sasaki T., Asakawa S., Kudoh J., Shintani A., Shibuya K., Yoshizaki Y., Aoki N., Mitsuyama S., Roe B.A., Chen F., Chu L., Crabtree J., Deschamps S., Do A., Do T., Dorman A., Fang F., Fu Y., Hu P., Hua A., Kenton S., Lai H., Lao H.I., Lewis J., Lewis S., Lin S.-P., Loh P., Malaj E., Nguyen T., Pan H., Phan S., Qi S., Qian Y., Ray L., Ren Q., Shaull S., Sloan D., Song L., Wang Q., Wang Y., Wang Z., White J., Willingham D., Wu H., Yao Z., Zhan M., Zhang G., Chissoe S., Murray J., Miller N., Minx P., Fulton R., Johnson D., Bemis G., Bentley D., Bradshaw H., Bourne S., Cordes M., Du Z., Fulton L., Goela D., Graves T., Hawkins J., Hinds K., Kemp K., Latreille P., Layman D., Ozersky P., Rohlfing T., Scheet P., Walker C., Wamsley A., Wohldmann P., Pepin K., Nelson J., Korf I., Bedell J.A., Hillier L.W., Mardis E., Waterston R., Wilson R., Emanuel B.S., Shaikh T., Kurahashi H., Saitta S., Budarf M.L., McDermid H.E., Johnson A., Wong A.C.C., Morrow B.E., Edelmann L., Kim U.J., Shizuya H., Simon M.I., Dumanski J.P., Peyrard M., Kedra D., Seroussi E., Fransson I., Tapia I., Bruder C.E., O'Brien K.P., Wilkinson P., Bodenteich A., Hartman K., Hu X., Khan A.S., Lane L., Tilahun Y., Wright H.
Nature 402:489-495(1999) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. expand/collapse author list , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.
Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases
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 2).
Tissue: Liver.
[6]"PRR5 encodes a conserved proline-rich protein predominant in kidney: analysis of genomic organization, expression, and mutation status in breast and colorectal carcinomas."
Johnstone C.N., Castellvi-Bel S., Chang L.M., Sung R.K., Bowser M.J., Pique J.M., Castells A., Rustgi A.K.
Genomics 85:338-351(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION (ISOFORMS 1; 3 AND 4), FUNCTION, TISSUE SPECIFICITY.
[7]"Identification of Protor as a novel Rictor-binding component of mTOR complex-2."
Pearce L.R., Huang X., Boudeau J., Pawlowski R., Wullschleger S., Deak M., Ibrahim A.F.M., Gourlay R., Magnuson M.A., Alessi D.R.
Biochem. J. 405:513-522(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH RICTOR.
[8]"PRR5, a novel component of mTOR complex 2, regulates platelet-derived growth factor receptor beta expression and signaling."
Woo S.-Y., Kim D.-H., Jun C.-B., Kim Y.-M., Haar E.V., Lee S.-I., Hegg J.W., Bandhakavi S., Griffin T.J., Kim D.-H.
J. Biol. Chem. 282:25604-25612(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH MTOR AND RICTOR, TISSUE SPECIFICITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AK000192 mRNA. Translation: BAA90999.1.
AK055848 mRNA. Translation: BAG51585.1.
AF177331 mRNA. Translation: AAG17975.1.
Z93244, Z98743 Genomic DNA. Translation: CAQ06711.1.
Z93244, Z98743 Genomic DNA. Translation: CAQ06720.1.
Z98743, Z93244 Genomic DNA. Translation: CAQ09256.1.
Z98743, Z93244 Genomic DNA. Translation: CAQ09263.1.
CH471138 Genomic DNA. Translation: EAW73353.1.
CH471138 Genomic DNA. Translation: EAW73355.1.
BC016921 mRNA. Translation: AAH16921.1.
BK005635 mRNA. Translation: DAA05654.1.
BK005636 mRNA. Translation: DAA05655.1.
BK005637 mRNA. Translation: DAA05656.1.
BK005638 mRNA. Translation: DAA05657.1.
BK005639 mRNA. Translation: DAA05658.1.
IPIIPI00216061.
IPI00396352.
IPI00604678.
IPI00869329.
IPI00878190.
RefSeqNP_001017528.1. NM_001017528.2.
NP_001017529.1. NM_001017529.2.
NP_001017530.1. NM_001017530.1.
NP_001185650.1. NM_001198721.1.
NP_056181.2. NM_015366.3.
NP_851850.1. NM_181333.3.
UniGeneHs.102336.

3D structure databases

ProteinModelPortalP85299.
ModBaseSearch...

Protein-protein interaction databases

IntActP85299. 13 interactions.

PTM databases

PhosphoSiteP85299.

Polymorphism databases

DMDM160016058.

Proteomic databases

PaxDbP85299.
PRIDEP85299.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000006251; ENSP00000006251; ENSG00000186654.
ENST00000336985; ENSP00000337464; ENSG00000186654.
ENST00000403581; ENSP00000384848; ENSG00000186654.
GeneID55615.
KEGGhsa:55615.
UCSCuc003bew.2. human.
uc003bfh.1. human.
uc010gzt.1. human.

Organism-specific databases

CTD55615.
GeneCardsGC22P045064.
HGNCHGNC:31682. PRR5.
HPAHPA054072.
MIM609406. gene.
neXtProtNX_P85299.
PharmGKBPA144596392.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG46045.
HOVERGENHBG067971.

Gene expression databases

ArrayExpressP85299.
BgeeP85299.
GenevestigatorP85299.

Family and domain databases

InterProIPR013745. HbrB.
[Graphical view]
PfamPF08539. HbrB. 1 hit.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSPRR5. human.
GenomeRNAi55615.
NextBio60196.
SOURCESearch...

Entry information

Entry namePRR5_HUMAN
AccessionPrimary (citable) accession number: P85299
Secondary accession number(s): B1AHF6 expand/collapse secondary AC list , B1AHG5, B3KP73, O75983, O95695, Q5BIW2, Q5EAJ8, Q5EAJ9, Q5XKJ6, Q96RW1, Q96RW2, Q9HA49, Q9HC46, Q9NSG0, Q9NVX8, Q9NXL1, Q9UH20
Entry history
Integrated into UniProtKB/Swiss-Prot: October 23, 2007
Last sequence update: October 23, 2007
Last modified: May 29, 2013
This is version 52 of the entry and version 1 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

Human chromosome 22

Human chromosome 22: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

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