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Protein

Regulatory-associated protein of mTOR

Gene

RPTOR

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

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. 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. Amino acid-signaling to mTORC1 requires its relocalization to the lysosomes mediated by the Ragulator complex and the Rag GTPases. 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. Involved in ciliogenesis.3 Publications

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • protein binding, bridging Source: WormBase
  • protein complex binding Source: UniProtKB
  • protein kinase activator activity Source: WormBase
  • protein kinase binding Source: UniProtKB
  • RNA polymerase III type 1 promoter DNA binding Source: UniProtKB
  • RNA polymerase III type 2 promoter DNA binding Source: UniProtKB
  • RNA polymerase III type 3 promoter DNA binding Source: UniProtKB
  • TFIIIC-class transcription factor binding Source: UniProtKB

GO - Biological processi

  • cell cycle arrest Source: Reactome
  • cell growth Source: UniProtKB
  • cellular response to amino acid stimulus Source: UniProtKB
  • cellular response to nutrient levels Source: UniProtKB
  • macroautophagy Source: Reactome
  • positive regulation of cell growth Source: ParkinsonsUK-UCL
  • positive regulation of endothelial cell proliferation Source: Ensembl
  • positive regulation of G1/S transition of mitotic cell cycle Source: ParkinsonsUK-UCL
  • positive regulation of peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of peptidyl-threonine phosphorylation Source: ParkinsonsUK-UCL
  • positive regulation of protein serine/threonine kinase activity Source: UniProtKB
  • positive regulation of TOR signaling Source: UniProtKB
  • positive regulation of transcription from RNA polymerase III promoter Source: UniProtKB
  • regulation of cell size Source: UniProtKB
  • regulation of cellular response to heat Source: Reactome
  • TOR signaling Source: UniProtKB
Complete GO annotation...

Enzyme and pathway databases

ReactomeiR-HSA-1632852. Macroautophagy.
R-HSA-165159. mTOR signalling.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-3371571. HSF1-dependent transactivation.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
SignaLinkiQ8N122.
SIGNORiQ8N122.

Names & Taxonomyi

Protein namesi
Recommended name:
Regulatory-associated protein of mTOR
Short name:
Raptor
Alternative name(s):
p150 target of rapamycin (TOR)-scaffold protein
Gene namesi
Name:RPTOR
Synonyms:KIAA1303, RAPTOR
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 17

Organism-specific databases

HGNCiHGNC:30287. RPTOR.

Subcellular locationi

  • Cytoplasm
  • Lysosome
  • Cytoplasmic granule

  • Note: Targeting to lysosomes depends on amino acid availability. In arsenite-stressed cells, accumulates in stress granules when associated with SPAG5 and association with lysosomes is drastically decreased.

GO - Cellular componenti

  • cytoplasm Source: UniProtKB
  • cytosol Source: Reactome
  • dendrite Source: Ensembl
  • intracellular membrane-bounded organelle Source: HPA
  • lysosomal membrane Source: UniProtKB
  • lysosome Source: UniProtKB
  • neuronal cell body Source: Ensembl
  • nucleoplasm Source: HPA
  • TORC1 complex Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Lysosome

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Mutagenesisi722S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-792. 1 Publication1
Mutagenesisi792S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-722. 1 Publication1

Organism-specific databases

DisGeNETi57521.
OpenTargetsiENSG00000141564.
PharmGKBiPA165432629.

Chemistry databases

ChEMBLiCHEMBL3120040.

Polymorphism and mutation databases

BioMutaiRPTOR.
DMDMi46577501.

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00000512001 – 1335Regulatory-associated protein of mTORAdd BLAST1335

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei696Phosphoserine; by MAPK8Combined sources2 Publications1
Modified residuei706Phosphothreonine; by MAPK82 Publications1
Modified residuei719Phosphoserine; by RPS6KA1Combined sources1 Publication1
Modified residuei721Phosphoserine; by RPS6KA11 Publication1
Modified residuei722Phosphoserine; by AMPK and RPS6KA1Combined sources2 Publications1
Modified residuei738PhosphoserineCombined sources1
Modified residuei792Phosphoserine; by AMPK1 Publication1
Modified residuei855Phosphoserine1 Publication1
Modified residuei859Phosphoserine; by MTORCombined sources1 Publication1
Modified residuei863Phosphoserine; by MAPK8 and MTORCombined sources2 Publications1
Modified residuei865PhosphothreonineCombined sources1
Modified residuei877PhosphoserineCombined sources1 Publication1

Post-translational modificationi

Insulin-stimulated phosphorylation at Ser-863 by MTOR and MAPK8 up-regulates mTORC1 activity. Osmotic stress also induces phosphorylation at Ser-696, Thr-706 and Ser-863 by MAPK8. Ser-863 phosphorylation is required for phosphorylation at Ser-855 and Ser-859. In response to nutrient limitation, phosphorylated by AMPK; phosphorylation promotes interaction with 14-3-3 proteins, leading to negative regulation of the mTORC1 complex. In response to growth factors, phosphorylated at Ser-719, Ser-721 and Ser-722 by RPS6KA1, which stimulates mTORC1 activity.4 Publications

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ8N122.
MaxQBiQ8N122.
PaxDbiQ8N122.
PeptideAtlasiQ8N122.
PRIDEiQ8N122.

PTM databases

iPTMnetiQ8N122.
PhosphoSitePlusiQ8N122.

Expressioni

Tissue specificityi

Highly expressed in skeletal muscle, and in a lesser extent in brain, lung, small intestine, kidney and placenta. Isoform 3 is widely expressed, with highest levels in nasal mucosa and pituitary and lowest in spleen.2 Publications

Gene expression databases

BgeeiENSG00000141564.
ExpressionAtlasiQ8N122. baseline and differential.
GenevisibleiQ8N122. HS.

Organism-specific databases

HPAiCAB013514.
HPA029821.
HPA064306.

Interactioni

Subunit structurei

Part of the mammalian target of rapamycin complex 1 (mTORC1) which contains MTOR, MLST8, RPTOR, AKT1S1/PRAS40 and DEPTOR. mTORC1 binds to and is inhibited by FKBP12-rapamycin. Binds directly to 4EBP1 and RPS6KB1 independently of its association with MTOR. Binds preferentially to poorly or non-phosphorylated forms of EIF4EBP1, and this binding is critical to the ability of MTOR to catalyze phosphorylation. Forms a complex with MTOR under both leucine-rich and -poor conditions. Interacts with ULK1 in a nutrient-dependent manner; the interaction is reduced during starvation. Interacts (when phosphorylated by AMPK) with 14-3-3 protein, leading to inhibit its activity. Interacts with SPAG5; SPAG5 competes with MTOR for RPTOR-binding, resulting in decreased mTORC1 formation. Interacts with G3BP1. The complex formed with G3BP1 AND SPAG5 is increased by oxidative stress. Interacts with HTR6 (PubMed:23027611). Interacts with PIH1D1 (PubMed:24036451). Interacts with BRAT1.11 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
EIF4EBP1Q135415EBI-1567928,EBI-74090
G3BP1Q132834EBI-1567928,EBI-1047359
LARSQ9P2J53EBI-1567928,EBI-356077
MLST8Q9BVC43EBI-1567928,EBI-1387471
MTMR3Q136153EBI-1567928,EBI-371938
MTORP4234532EBI-1567928,EBI-359260
MtorQ9JLN95EBI-1567928,EBI-1571628From a different organism.
PREX1Q8TCU62EBI-1567928,EBI-1046542
RAB1AP628204EBI-1567928,EBI-716845
Rps6kb1P679992EBI-1567928,EBI-2639458From a different organism.
RRAGCQ9HB905EBI-1567928,EBI-752390
SIRT1Q96EB63EBI-1567928,EBI-1802965
SPAG5Q96R069EBI-1567928,EBI-413317

GO - Molecular functioni

  • 14-3-3 protein binding Source: UniProtKB
  • protein binding, bridging Source: WormBase
  • protein complex binding Source: UniProtKB
  • protein kinase binding Source: UniProtKB
  • TFIIIC-class transcription factor binding Source: UniProtKB

Protein-protein interaction databases

BioGridi121582. 97 interactors.
DIPiDIP-39482N.
IntActiQ8N122. 35 interactors.
MINTiMINT-3038940.
STRINGi9606.ENSP00000307272.

Structurei

3D structure databases

ProteinModelPortaliQ8N122.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Repeati1020 – 1061WD 1Add BLAST42
Repeati1065 – 1106WD 2Add BLAST42
Repeati1121 – 1160WD 3Add BLAST40
Repeati1164 – 1203WD 4Add BLAST40
Repeati1209 – 1249WD 5Add BLAST41
Repeati1251 – 1291WD 6Add BLAST41
Repeati1299 – 1335WD 7Add BLAST37

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi881 – 887Poly-Ser7

Sequence similaritiesi

Belongs to the WD repeat RAPTOR family.Curated
Contains 7 WD repeats.PROSITE-ProRule annotation

Keywords - Domaini

Repeat, WD repeat

Phylogenomic databases

eggNOGiKOG1517. Eukaryota.
ENOG410XQKJ. LUCA.
GeneTreeiENSGT00640000091541.
HOGENOMiHOG000184479.
HOVERGENiHBG059496.
InParanoidiQ8N122.
KOiK07204.
OMAiEPGGHRN.
OrthoDBiEOG091G00H9.
PhylomeDBiQ8N122.
TreeFamiTF105729.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
2.130.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR004083. Raptor.
IPR029347. Raptor_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR12848. PTHR12848. 1 hit.
PfamiPF02985. HEAT. 1 hit.
PF14538. Raptor_N. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM01302. Raptor_N. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 1 hit.
PROSITEiPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q8N122-1) [UniParc]FASTAAdd to basket

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.

« Hide

        10         20         30         40         50
MESEMLQSPL LGLGEEDEAD LTDWNLPLAF MKKRHCEKIE GSKSLAQSWR
60 70 80 90 100
MKDRMKTVSV ALVLCLNVGV DPPDVVKTTP CARLECWIDP LSMGPQKALE
110 120 130 140 150
TIGANLQKQY ENWQPRARYK QSLDPTVDEV KKLCTSLRRN AKEERVLFHY
160 170 180 190 200
NGHGVPRPTV NGEVWVFNKN YTQYIPLSIY DLQTWMGSPS IFVYDCSNAG
210 220 230 240 250
LIVKSFKQFA LQREQELEVA AINPNHPLAQ MPLPPSMKNC IQLAACEATE
260 270 280 290 300
LLPMIPDLPA DLFTSCLTTP IKIALRWFCM QKCVSLVPGV TLDLIEKIPG
310 320 330 340 350
RLNDRRTPLG ELNWIFTAIT DTIAWNVLPR DLFQKLFRQD LLVASLFRNF
360 370 380 390 400
LLAERIMRSY NCTPVSSPRL PPTYMHAMWQ AWDLAVDICL SQLPTIIEEG
410 420 430 440 450
TAFRHSPFFA EQLTAFQVWL TMGVENRNPP EQLPIVLQVL LSQVHRLRAL
460 470 480 490 500
DLLGRFLDLG PWAVSLALSV GIFPYVLKLL QSSARELRPL LVFIWAKILA
510 520 530 540 550
VDSSCQADLV KDNGHKYFLS VLADPYMPAE HRTMTAFILA VIVNSYHTGQ
560 570 580 590 600
EACLQGNLIA ICLEQLNDPH PLLRQWVAIC LGRIWQNFDS ARWCGVRDSA
610 620 630 640 650
HEKLYSLLSD PIPEVRCAAV FALGTFVGNS AERTDHSTTI DHNVAMMLAQ
660 670 680 690 700
LVSDGSPMVR KELVVALSHL VVQYESNFCT VALQFIEEEK NYALPSPATT
710 720 730 740 750
EGGSLTPVRD SPCTPRLRSV SSYGNIRAVA TARSLNKSLQ NLSLTEESGG
760 770 780 790 800
AVAFSPGNLS TSSSASSTLG SPENEEHILS FETIDKMRRA SSYSSLNSLI
810 820 830 840 850
GVSFNSVYTQ IWRVLLHLAA DPYPEVSDVA MKVLNSIAYK ATVNARPQRV
860 870 880 890 900
LDTSSLTQSA PASPTNKGVH IHQAGGSPPA SSTSSSSLTN DVAKQPVSRD
910 920 930 940 950
LPSGRPGTTG PAGAQYTPHS HQFPRTRKMF DKGPEQTADD ADDAAGHKSF
960 970 980 990 1000
ISATVQTGFC DWSARYFAQP VMKIPEEHDL ESQIRKEREW RFLRNSRVRR
1010 1020 1030 1040 1050
QAQQVIQKGI TRLDDQIFLN RNPGVPSVVK FHPFTPCIAV ADKDSICFWD
1060 1070 1080 1090 1100
WEKGEKLDYF HNGNPRYTRV TAMEYLNGQD CSLLLTATDD GAIRVWKNFA
1110 1120 1130 1140 1150
DLEKNPEMVT AWQGLSDMLP TTRGAGMVVD WEQETGLLMS SGDVRIVRIW
1160 1170 1180 1190 1200
DTDREMKVQD IPTGADSCVT SLSCDSHRSL IVAGLGDGSI RVYDRRMALS
1210 1220 1230 1240 1250
ECRVMTYREH TAWVVKASLQ KRPDGHIVSV SVNGDVRIFD PRMPESVNVL
1260 1270 1280 1290 1300
QIVKGLTALD IHPQADLIAC GSVNQFTAIY NSSGELINNI KYYDGFMGQR
1310 1320 1330
VGAISCLAFH PHWPHLAVGS NDYYISVYSV EKRVR
Length:1,335
Mass (Da):149,038
Last modified:October 1, 2002 - v1
Checksum:i688ED1943F45045A
GO
Isoform 2 (identifier: Q8N122-2) [UniParc]FASTAAdd to basket

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

Show »
Length:379
Mass (Da):43,256
Checksum:iD67B01D4E68E859E
GO
Isoform 3 (identifier: Q8N122-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     504-661: Missing.

Show »
Length:1,177
Mass (Da):131,515
Checksum:i1CE0DA04E72105B2
GO

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Sequence conflicti217 – 218LE → RQ in BAA92541 (PubMed:10718198).Curated2

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_010174380 – 1335Missing in isoform 2. 1 PublicationAdd BLAST956
Alternative sequenceiVSP_054042504 – 661Missing in isoform 3. 1 PublicationAdd BLAST158

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
GQ183898 mRNA. Translation: ACS44766.1.
CCDSiCCDS11773.1. [Q8N122-1]
CCDS54175.1. [Q8N122-3]
RefSeqiNP_001156506.1. NM_001163034.1. [Q8N122-3]
NP_065812.1. NM_020761.2. [Q8N122-1]
UniGeneiHs.133044.

Genome annotation databases

EnsembliENST00000306801; ENSP00000307272; ENSG00000141564. [Q8N122-1]
ENST00000544334; ENSP00000442479; ENSG00000141564. [Q8N122-3]
ENST00000570891; ENSP00000460136; ENSG00000141564. [Q8N122-2]
GeneIDi57521.
KEGGihsa:57521.
UCSCiuc002jys.5. human. [Q8N122-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
GQ183898 mRNA. Translation: ACS44766.1.
CCDSiCCDS11773.1. [Q8N122-1]
CCDS54175.1. [Q8N122-3]
RefSeqiNP_001156506.1. NM_001163034.1. [Q8N122-3]
NP_065812.1. NM_020761.2. [Q8N122-1]
UniGeneiHs.133044.

3D structure databases

ProteinModelPortaliQ8N122.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi121582. 97 interactors.
DIPiDIP-39482N.
IntActiQ8N122. 35 interactors.
MINTiMINT-3038940.
STRINGi9606.ENSP00000307272.

Chemistry databases

ChEMBLiCHEMBL3120040.

PTM databases

iPTMnetiQ8N122.
PhosphoSitePlusiQ8N122.

Polymorphism and mutation databases

BioMutaiRPTOR.
DMDMi46577501.

Proteomic databases

EPDiQ8N122.
MaxQBiQ8N122.
PaxDbiQ8N122.
PeptideAtlasiQ8N122.
PRIDEiQ8N122.

Protocols and materials databases

DNASUi57521.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000306801; ENSP00000307272; ENSG00000141564. [Q8N122-1]
ENST00000544334; ENSP00000442479; ENSG00000141564. [Q8N122-3]
ENST00000570891; ENSP00000460136; ENSG00000141564. [Q8N122-2]
GeneIDi57521.
KEGGihsa:57521.
UCSCiuc002jys.5. human. [Q8N122-1]

Organism-specific databases

CTDi57521.
DisGeNETi57521.
GeneCardsiRPTOR.
HGNCiHGNC:30287. RPTOR.
HPAiCAB013514.
HPA029821.
HPA064306.
MIMi607130. gene.
neXtProtiNX_Q8N122.
OpenTargetsiENSG00000141564.
PharmGKBiPA165432629.
HUGEiSearch...
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG1517. Eukaryota.
ENOG410XQKJ. LUCA.
GeneTreeiENSGT00640000091541.
HOGENOMiHOG000184479.
HOVERGENiHBG059496.
InParanoidiQ8N122.
KOiK07204.
OMAiEPGGHRN.
OrthoDBiEOG091G00H9.
PhylomeDBiQ8N122.
TreeFamiTF105729.

Enzyme and pathway databases

ReactomeiR-HSA-1632852. Macroautophagy.
R-HSA-165159. mTOR signalling.
R-HSA-166208. mTORC1-mediated signalling.
R-HSA-3371571. HSF1-dependent transactivation.
R-HSA-380972. Energy dependent regulation of mTOR by LKB1-AMPK.
R-HSA-5628897. TP53 Regulates Metabolic Genes.
SignaLinkiQ8N122.
SIGNORiQ8N122.

Miscellaneous databases

ChiTaRSiRPTOR. human.
GeneWikiiRPTOR.
GenomeRNAii57521.
PROiQ8N122.
SOURCEiSearch...

Gene expression databases

BgeeiENSG00000141564.
ExpressionAtlasiQ8N122. baseline and differential.
GenevisibleiQ8N122. HS.

Family and domain databases

Gene3Di1.25.10.10. 2 hits.
2.130.10.10. 1 hit.
InterProiIPR011989. ARM-like.
IPR016024. ARM-type_fold.
IPR000357. HEAT.
IPR004083. Raptor.
IPR029347. Raptor_N.
IPR015943. WD40/YVTN_repeat-like_dom.
IPR001680. WD40_repeat.
IPR017986. WD40_repeat_dom.
[Graphical view]
PANTHERiPTHR12848. PTHR12848. 1 hit.
PfamiPF02985. HEAT. 1 hit.
PF14538. Raptor_N. 1 hit.
PF00400. WD40. 1 hit.
[Graphical view]
SMARTiSM01302. Raptor_N. 1 hit.
SM00320. WD40. 7 hits.
[Graphical view]
SUPFAMiSSF48371. SSF48371. 2 hits.
SSF50978. SSF50978. 1 hit.
PROSITEiPS50294. WD_REPEATS_REGION. 1 hit.
[Graphical view]
ProtoNetiSearch...

Entry informationi

Entry nameiRPTOR_HUMAN
AccessioniPrimary (citable) accession number: Q8N122
Secondary accession number(s): B2RN36
, C6KEF2, F5H7J5, Q8N4V9, Q8TB32, Q9P2P3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 26, 2004
Last sequence update: October 1, 2002
Last modified: November 30, 2016
This is version 148 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. Human chromosome 17
    Human chromosome 17: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.