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Reviewed, UniProtKB/Swiss-Prot Q8N122 (RPTOR_HUMAN)

Last modified March 2, 2010. Version 75. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (3) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

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Names and origin

Protein namesRecommended name:
Regulatory-associated protein of mTOR
Short name=Raptor
Alternative name(s):
p150 target of rapamycin (TOR)-scaffold protein
Gene names
Name:RPTOR
Synonyms:KIAA1303, RAPTOR
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length1335 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

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General annotation (Comments)

Function

Involved in the control of the mammalian target of rapamycin complex 1 (mTORC1) activity which regulates cell growth and survival, and autophagy in response to nutrient and hormonal signals; functions as a scaffold for recruiting mTORC1 substrates. mTORC1 is activated in response to growth factors or amino-acids. Amino-acid-signaling to mTORC1 is mediated by Rag GTPases, which cause amino-acid-induced relocalization of mTOR within the endomembrane system. Growth factor-stimulated mTORC1 activation involves a AKT1-mediated phosphorylation of TSC1-TSC2, which leads to the activation of the RHEB GTPase that potently activates the protein kinase activity of mTORC1. Activated mTORC1 up-regulates protein synthesis by phosphorylating key regulators of mRNA translation and ribosome synthesis. mTORC1 phosphorylates EIF4EBP1 and releases it from inhibiting the elongation initiation factor 4E (eiF4E). mTORC1 phosphorylates and activates S6K1 at 'Thr-389', which then promotes protein synthesis by phosphorylating PDCD4 and targeting it for degradation. Ref.1 Ref.2

Subunit structure

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains FRAP1, MLST8, RPTOR and AKT1S1. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Binds directly to 4EBP1 and RPS6KB1 independently of its association with FRAP1. Binds preferentially to poorly or non-phosphorylated forms of EIF4EBP1, and this binding is critical to the ability of FRAP1 to catalyze phosphorylation. Forms a complex with FRAP1 under both leucine-rich and -poor conditions. Interacts with ULK1 in a nutrient-dependent manner; the interaction is reduced during starvation. Ref.1 Ref.2 Ref.7 Ref.8 Ref.13 Ref.20

Tissue specificity

Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta. Ref.1 Ref.7

Sequence similarities

Belongs to the WD repeat RAPTOR family.

Contains 7 WD repeats.

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Ontologies

Keywords
   Coding sequence diversityAlternative splicing
   DomainRepeat
WD repeat
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processcellular response to nutrient levels Ref.1

Inferred from mutant phenotype. Source: UniProtKB

positive regulation of TOR signaling pathway Ref.2

Inferred from direct assay. Source: UniProtKB

regulation of cell size Ref.1

Inferred from mutant phenotype. Source: UniProtKB

   Cellular componentTORC1 complex

Inferred from direct assay. Source: UniProtKB

cytosol

Inferred from Experiment. Source: Reactome

   Molecular functionprotein complex binding Ref.20

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

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Binary interactions

With

Entry

#Exp.

IntAct

Notes

FRAP1P423451EBI-1567928,EBI-359260
MLST8Q9BVC41EBI-1567928,EBI-1387471

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Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q8N122-1)

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: Q8N122-2)

The sequence of this isoform differs from the canonical sequence as follows:
     380-1335: Missing.

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Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 13351335Regulatory-associated protein of mTOR
PRO_0000051200

Regions

Repeat1020 – 106142WD 1
Repeat1065 – 110642WD 2
Repeat1121 – 116040WD 3
Repeat1164 – 120340WD 4
Repeat1209 – 124941WD 5
Repeat1251 – 129141WD 6
Repeat1299 – 133537WD 7
Compositional bias881 – 8877Poly-Ser

Amino acid modifications

Modified residue7191Phosphoserine Ref.15 Ref.17
Modified residue7211Phosphoserine
Modified residue7221Phosphoserine Ref.15 Ref.17 Ref.19
Modified residue8571Phosphothreonine By similarity
Modified residue8591Phosphoserine Ref.17 Ref.19 Ref.11 Ref.16 Ref.22
Modified residue8631Phosphoserine Ref.17 Ref.19 Ref.11 Ref.16 Ref.22 Ref.10 Ref.12 Ref.14
Modified residue8651Phosphothreonine Ref.14
Modified residue8771Phosphoserine Ref.17 Ref.19 Ref.16 Ref.22

Natural variations

Alternative sequence380 – 1335956Missing in isoform 2.
VSP_010174

Experimental info

Sequence conflict217 – 2182LE → RQ in BAA92541. Ref.6

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Sequences

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

Last modified October 1, 2002. Version 1.
Checksum: 688ED1943F45045A

FASTA1,335149,038
        10         20         30         40         50         60 
MESEMLQSPL LGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR MKDRMKTVSV 

        70         80         90        100        110        120 
ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE TIGANLQKQY ENWQPRARYK 

       130        140        150        160        170        180 
QSLDPTVDEV KKLCTSLRRN AKEERVLFHY NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY 

       190        200        210        220        230        240 
DLQTWMGSPS IFVYDCSNAG LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC 

       250        260        270        280        290        300 
IQLAACEATE LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG 

       310        320        330        340        350        360 
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF LLAERIMRSY 

       370        380        390        400        410        420 
NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG TAFRHSPFFA EQLTAFQVWL 

       430        440        450        460        470        480 
TMGVENRNPP EQLPIVLQVL LSQVHRLRAL DLLGRFLDLG PWAVSLALSV GIFPYVLKLL 

       490        500        510        520        530        540 
QSSARELRPL LVFIWAKILA VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA 

       550        560        570        580        590        600 
VIVNSYHTGQ EACLQGNLIA ICLEQLNDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA 

       610        620        630        640        650        660 
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ LVSDGSPMVR 

       670        680        690        700        710        720 
KELVVALSHL VVQYESNFCT VALQFIEEEK NYALPSPATT EGGSLTPVRD SPCTPRLRSV 

       730        740        750        760        770        780 
SSYGNIRAVA TARSLNKSLQ NLSLTEESGG AVAFSPGNLS TSSSASSTLG SPENEEHILS 

       790        800        810        820        830        840 
FETIDKMRRA SSYSSLNSLI GVSFNSVYTQ IWRVLLHLAA DPYPEVSDVA MKVLNSIAYK 

       850        860        870        880        890        900 
ATVNARPQRV LDTSSLTQSA PASPTNKGVH IHQAGGSPPA SSTSSSSLTN DVAKQPVSRD 

       910        920        930        940        950        960 
LPSGRPGTTG PAGAQYTPHS HQFPRTRKMF DKGPEQTADD ADDAAGHKSF ISATVQTGFC 

       970        980        990       1000       1010       1020 
DWSARYFAQP VMKIPEEHDL ESQIRKEREW RFLRNSRVRR QAQQVIQKGI TRLDDQIFLN 

      1030       1040       1050       1060       1070       1080 
RNPGVPSVVK FHPFTPCIAV ADKDSICFWD WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD 

      1090       1100       1110       1120       1130       1140 
CSLLLTATDD GAIRVWKNFA DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS 

      1150       1160       1170       1180       1190       1200 
SGDVRIVRIW DTDREMKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS 

      1210       1220       1230       1240       1250       1260 
ECRVMTYREH TAWVVKASLQ KRPDGHIVSV SVNGDVRIFD PRMPESVNVL QIVKGLTALD 

      1270       1280       1290       1300       1310       1320 
IHPQADLIAC GSVNQFTAIY NSSGELINNI KYYDGFMGQR VGAISCLAFH PHWPHLAVGS 

      1330 
NDYYISVYSV EKRVR

« Hide

Isoform 2.

Checksum: D67B01D4E68E859E
Show »

FASTA37943,256

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References

« Hide 'large scale' references
[1]"mTOR interacts with raptor to form a nutrient-sensitive complex that signals to the growth machinery."
Kim D.-H., Sarbassov D.D., Ali S.M., King J.E., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.
Cell 110:163-175(2002) [PubMed: 12150925] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, TISSUE SPECIFICITY, INTERACTION WITH 4EBP1 AND RPS6KB1.
[2]"Raptor, a binding partner of target of rapamycin (TOR), mediates TOR action."
Hara K., Maruki Y., Long X., Yoshino K., Oshiro N., Hidayat S., Tokunaga C., Avruch J., Yonezawa K.
Cell 110:177-189(2002) [PubMed: 12150926] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, INTERACTION WITH 4EBP1 AND RPS6KB1.
[3]"DNA sequence of human chromosome 17 and analysis of rearrangement in the human lineage."
Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R., Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A., Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J., Chang J.L. expand/collapse author list , Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J., DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D., Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A., Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.
Nature 440:1045-1049(2006) [PubMed: 16625196] [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: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 995-1135 (ISOFORM 1).
Tissue: Brain, Placenta and Testis.
[6]"Prediction of the coding sequences of unidentified human genes. XVI. The complete sequences of 150 new cDNA clones from brain which code for large proteins in vitro."
Nagase T., Kikuno R., Ishikawa K., Hirosawa M., Ohara O.
DNA Res. 7:65-73(2000) [PubMed: 10718198] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 217-1335.
Tissue: Brain.
[7]"Two TOR complexes, only one of which is rapamycin sensitive, have distinct roles in cell growth control."
Loewith R., Jacinto E., Wullschleger S., Lorberg A., Crespo J.L., Bonenfant D., Oppliger W., Jenoe P., Hall M.N.
Mol. Cell 10:457-468(2002) [PubMed: 12408816] [Abstract]
Cited for: INTERACTION WITH FRAP1 AND MLST8, IDENTIFICATION IN THE TORC1 COMPLEX, TISSUE SPECIFICITY.
[8]"TOS motif-mediated raptor binding regulates 4E-BP1 multisite phosphorylation and function."
Schalm S.S., Fingar D.C., Sabatini D.M., Blenis J.
Curr. Biol. 13:797-806(2003) [PubMed: 12747827] [Abstract]
Cited for: INTERACTION WITH EIF4EBP1.
[9]"Dissociation of raptor from mTOR is a mechanism of rapamycin-induced inhibition of mTOR function."
Oshiro N., Yoshino K., Hidayat S., Tokunaga C., Hara K., Eguchi S., Avruch J., Yonezawa K.
Genes Cells 9:359-366(2004) [PubMed: 15066126] [Abstract]
Cited for: DISSOCIATION OF COMPLEX BY RAPAMYCIN.
[10]"Large-scale characterization of HeLa cell nuclear phosphoproteins."
Beausoleil S.A., Jedrychowski M., Schwartz D., Elias J.E., Villen J., Li J., Cohn M.A., Cantley L.C., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 101:12130-12135(2004) [PubMed: 15302935] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, MASS SPECTROMETRY.
Tissue: Epithelium.
[11]"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
Cell 127:635-648(2006) [PubMed: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859 AND SER-863, MASS SPECTROMETRY.
Tissue: Epithelium.
[12]"A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863, MASS SPECTROMETRY.
Tissue: Epithelium.
[13]"PRAS40 is an insulin-regulated inhibitor of the mTORC1 protein kinase."
Sancak Y., Thoreen C.C., Peterson T.R., Lindquist R.A., Kang S.A., Spooner E., Carr S.A., Sabatini D.M.
Mol. Cell 25:903-915(2007) [PubMed: 17386266] [Abstract]
Cited for: INTERACTION WITH AKT1S1.
[14]"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column."
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.
Anal. Sci. 24:161-166(2008) [PubMed: 18187866] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-863 AND THR-865, MASS SPECTROMETRY.
[15]"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis."
Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III
J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719 AND SER-722, MASS SPECTROMETRY.
[16]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND SER-877, MASS SPECTROMETRY.
[17]"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: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-719; SER-722; SER-859; SER-863 AND SER-877, MASS SPECTROMETRY.
[18]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[19]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-722; SER-859; SER-863 AND SER-877, MASS SPECTROMETRY.
[20]"Nutrient-dependent mTORC1 association with the ULK1-Atg13-FIP200 complex required for autophagy."
Hosokawa N., Hara T., Kaizuka T., Kishi C., Takamura A., Miura Y., Iemura S., Natsume T., Takehana K., Yamada N., Guan J.L., Oshiro N., Mizushima N.
Mol. Biol. Cell 20:1981-1991(2009) [PubMed: 19211835] [Abstract]
Cited for: INTERACTION WITH ULK1.
[21]"Large-scale proteomics analysis of the human kinome."
Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H.
Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-721; SER-722; SER-859; SER-863 AND SER-877, MASS SPECTROMETRY.
[22]"Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
Sci. Signal. 2:RA46-RA46(2009) [PubMed: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-859; SER-863 AND SER-877, MASS SPECTROMETRY.
Tissue: T-cell.
+Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ		AY090663 mRNA. Translation: AAM09075.1.
AB082951 mRNA. Translation: BAC06490.1.
AC016245 Genomic DNA. No translation available.
AC109327 Genomic DNA. No translation available.
AC127496 Genomic DNA. No translation available.
AC133012 Genomic DNA. No translation available.
CH471099 Genomic DNA. Translation: EAW89618.1.
BC025180 mRNA. Translation: AAH25180.1.
BC033258 mRNA. Translation: AAH33258.1.
BC064515 mRNA. Translation: AAH64515.1.
BC136652 mRNA. Translation: AAI36653.1.
BC136654 mRNA. Translation: AAI36655.1.
AB037724 mRNA. Translation: BAA92541.1.
IPIIPI00166044.
IPI00410411.
RefSeqNP_065812.1.
UniGeneHs.133044

3D structure databases

SMRQ8N122. Positions 405-675.
ModBaseSearch...

Protein-protein interaction databases

IntActQ8N122. 7 interactions.
STRINGQ8N122.

PTM databases

PhosphoSiteQ8N122.

Proteomic databases

PRIDEQ8N122.

Genome annotation databases

EnsemblENST00000306801; ENSP00000307272; ENSG00000141564; Homo sapiens. [Genome view]
GeneID57521.
UCSCuc002jys.2. human.
uc002jyt.1. human.

Organism-specific databases

CTD57521.
GeneCardsGC17P076134.
H-InvDBHIX0018877.
HGNCHGNC:30287. RPTOR.
HPACAB013514.
MIM607130. gene.
HUGESearch...
GenAtlasSearch...

Phylogenomic databases

HOGENOMHBG737108.
HOVERGENHBG059496.
InParanoidQ8N122.
OMAWSAKYFA.
OrthoDBEOG951H93.
PhylomeDBQ8N122.

Enzyme and pathway databases

Pathway_Interaction_DBpi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
mtor_4pathway. mTOR signaling pathway.
ReactomeREACT_498. Signaling by Insulin receptor.

Gene expression databases

ArrayExpressQ8N122.
BgeeQ8N122.
GenevestigatorQ8N122.

Family and domain databases

InterProIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR004083. Raptor.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR011046. WD40_repeat-like_dom.
IPR017986. WD40_repeat_dom.
IPR019781. WD40_repeat_sg.
[Graphical view]
Gene3DG3DSA:1.25.10.10. ARM-like. 1 hit.
G3DSA:2.130.10.10. WD40/YVTN_repeat-like. 1 hit.
PANTHERPTHR12848. Raptor. 1 hit.
PfamPF02985. HEAT. 2 hits.
PF00400. WD40. 3 hits.
[Graphical view]
PRINTSPR01547. YEAST176DUF.
SMARTSM00320. WD40. 7 hits.
[Graphical view]
SUPFAMSSF48371. ARM-type_fold. 1 hit.
SSF50978. WD40_like. 1 hit.
PROSITEPS00678. WD_REPEATS_1. False negative.
PS50082. WD_REPEATS_2. False negative.
PS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio63899.
SOURCESearch...

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Entry information

Entry nameRPTOR_HUMAN
AccessionPrimary (citable) accession number: Q8N122
Secondary accession number(s): B2RN36 expand/collapse secondary AC list , Q8N4V9, Q8TB32, Q9P2P3
Entry history
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2002
Last modified: March 2, 2010
This is version 75 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

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Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

MIM cross-references

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

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents