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Reviewed, UniProtKB/Swiss-Prot P42345 (FRAP_HUMAN)

Last modified June 16, 2009. Version 92. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    FKBP12-rapamycin complex-associated protein
Alternative name(s):
    FK506-binding protein 12-rapamycin complex-associated protein 1
    Rapamycin target protein
    RAPT1
    Mammalian target of rapamycin
      Short name=mTOR
Gene names
Name: FRAP1
Synonyms: FRAP, FRAP2
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2549 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Acts as the target for the cell-cycle arrest and immunosuppressive effects of the FKBP12-rapamycin complex. Part of the TORC2 complex which plays a critical role in AKT1 Ser-473 phosphorylation, and may modulate the phosphorylation of PKCA and regulate actin cytoskeleton organization. Ref.8 Ref.9

Subunit structure

Interacts with the FKBP12-rapamycin complex. Binds UBQLN1. Forms part of the mammalian target of rapamycin 2 complex (TORC2) comprised of FRAP1, GBL, PRR5, RICTOR and SIN. TORC2 does not bind to and is not sensitive to FKBP12-rapamycin. Binds directly to PRR5 and RICTOR within the TORC2 complex. Ref.8 Ref.7 Ref.10

Tissue specificity

Expressed in numerous tissues, with highest levels in testis. Ref.6

Sequence similarities

Belongs to the PI3/PI4-kinase family.

Contains 1 FAT domain.

Contains 1 FATC domain.

Contains 7 HEAT repeats.

Contains 1 PI3K/PI4K domain.

Sequence caution

The sequence AAC39933.1 differs from that shown. Reason: Frameshift at positions 956 and 999.

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 25492549FKBP12-rapamycin complex-associated protein
PRO_0000088808

Regions

Repeat16 – 5338HEAT 1
Repeat650 – 68839HEAT 2
Repeat859 – 89739HEAT 3
Repeat988 – 102538HEAT 4
Repeat1069 – 110638HEAT 5
Repeat1109 – 114840HEAT 6
Repeat1150 – 118637HEAT 7
Domain1382 – 1982601FAT
Domain2182 – 2516335PI3K/PI4K
Domain2517 – 254933FATC

Amino acid modifications

Modified residue5671Phosphoserine Ref.12
Modified residue11621Phosphothreonine Ref.11
Modified residue12611Phosphoserine Ref.12
Modified residue24781Phosphoserine Ref.13
Modified residue24811Phosphoserine Ref.13

Natural variations

Natural variant81A → S in a lung large cell carcinoma sample; somatic mutation. Ref.17
VAR_041537
Natural variant1351M → T in a metastatic melanoma sample; somatic mutation. Ref.17
VAR_041538
Natural variant10831M → V Ref.17
VAR_041539
Natural variant11341A → V Ref.17
VAR_041540
Natural variant11781S → F Ref.17
VAR_041541
Natural variant20111M → V in an ovarian mucinous carcinoma sample; somatic mutation. Ref.17
VAR_041542
Natural variant22151S → Y in a colorectal adenocarcinoma sample; somatic mutation. Ref.17
VAR_041543
Natural variant24761P → L in a glioblastoma multiforme sample; somatic mutation. Ref.17
VAR_041544

Experimental info

Sequence conflict3531K → N in AAC39933. Ref.2
Sequence conflict3591S → N in AAC39933. Ref.2
Sequence conflict3641D → N in AAC39933. Ref.2
Sequence conflict3901M → L in AAC39933. Ref.2
Sequence conflict4301R → L in AAC39933. Ref.2
Sequence conflict455 – 4573VLD → GVE in AAC39933. Ref.2
Sequence conflict4611A → G in AAC39933. Ref.2
Sequence conflict482 – 4843VFT → FFN in AAC39933. Ref.2
Sequence conflict4891L → V in AAC39933. Ref.2
Sequence conflict5131L → I in AAC39933. Ref.2
Sequence conflict5391L → V in AAC39933. Ref.2
Sequence conflict5531R → C in AAC39933. Ref.2
Sequence conflict10751I → S in AAC39933. Ref.2

Secondary structure

......... 2549
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P42345-1 [UniParc].

Last modified November 1, 1995. Version 1.
Checksum: 7D9AD6E784882AB4

FASTA2,549288,892
        10         20         30         40         50         60 
MLGTGPAAAT TAATTSSNVS VLQQFASGLK SRNEETRAKA AKELQHYVTM ELREMSQEES 

        70         80         90        100        110        120 
TRFYDQLNHH IFELVSSSDA NERKGGILAI ASLIGVEGGN ATRIGRFANY LRNLLPSNDP 

       130        140        150        160        170        180 
VVMEMASKAI GRLAMAGDTF TAEYVEFEVK RALEWLGADR NEGRRHAAVL VLRELAISVP 

       190        200        210        220        230        240 
TFFFQQVQPF FDNIFVAVWD PKQAIREGAV AALRACLILT TQREPKEMQK PQWYRHTFEE 

       250        260        270        280        290        300 
AEKGFDETLA KEKGMNRDDR IHGALLILNE LVRISSMEGE RLREEMEEIT QQQLVHDKYC 

       310        320        330        340        350        360 
KDLMGFGTKP RHITPFTSFQ AVQPQQSNAL VGLLGYSSHQ GLMGFGTSPS PAKSTLVESR 

       370        380        390        400        410        420 
CCRDLMEEKF DQVCQWVLKC RNSKNSLIQM TILNLLPRLA AFRPSAFTDT QYLQDTMNHV 

       430        440        450        460        470        480 
LSCVKKEKER TAAFQALGLL SVAVRSEFKV YLPRVLDIIR AALPPKDFAH KRQKAMQVDA 

       490        500        510        520        530        540 
TVFTCISMLA RAMGPGIQQD IKELLEPMLA VGLSPALTAV LYDLSRQIPQ LKKDIQDGLL 

       550        560        570        580        590        600 
KMLSLVLMHK PLRHPGMPKG LAHQLASPGL TTLPEASDVG SITLALRTLG SFEFEGHSLT 

       610        620        630        640        650        660 
QFVRHCADHF LNSEHKEIRM EAARTCSRLL TPSIHLISGH AHVVSQTAVQ VVADVLSKLL 

       670        680        690        700        710        720 
VVGITDPDPD IRYCVLASLD ERFDAHLAQA ENLQALFVAL NDQVFEIREL AICTVGRLSS 

       730        740        750        760        770        780 
MNPAFVMPFL RKMLIQILTE LEHSGIGRIK EQSARMLGHL VSNAPRLIRP YMEPILKALI 

       790        800        810        820        830        840 
LKLKDPDPDP NPGVINNVLA TIGELAQVSG LEMRKWVDEL FIIIMDMLQD SSLLAKRQVA 

       850        860        870        880        890        900 
LWTLGQLVAS TGYVVEPYRK YPTLLEVLLN FLKTEQNQGT RREAIRVLGL LGALDPYKHK 

       910        920        930        940        950        960 
VNIGMIDQSR DASAVSLSES KSSQDSSDYS TSEMLVNMGN LPLDEFYPAV SMVALMRIFR 

       970        980        990       1000       1010       1020 
DQSLSHHHTM VVQAITFIFK SLGLKCVQFL PQVMPTFLNV IRVCDGAIRE FLFQQLGMLV 

      1030       1040       1050       1060       1070       1080 
SFVKSHIRPY MDEIVTLMRE FWVMNTSIQS TIILLIEQIV VALGGEFKLY LPQLIPHMLR 

      1090       1100       1110       1120       1130       1140 
VFMHDNSPGR IVSIKLLAAI QLFGANLDDY LHLLLPPIVK LFDAPEAPLP SRKAALETVD 

      1150       1160       1170       1180       1190       1200 
RLTESLDFTD YASRIIHPIV RTLDQSPELR STAMDTLSSL VFQLGKKYQI FIPMVNKVLV 

      1210       1220       1230       1240       1250       1260 
RHRINHQRYD VLICRIVKGY TLADEEEDPL IYQHRMLRSG QGDALASGPV ETGPMKKLHV 

      1270       1280       1290       1300       1310       1320 
STINLQKAWG AARRVSKDDW LEWLRRLSLE LLKDSSSPSL RSCWALAQAY NPMARDLFNA 

      1330       1340       1350       1360       1370       1380 
AFVSCWSELN EDQQDELIRS IELALTSQDI AEVTQTLLNL AEFMEHSDKG PLPLRDDNGI 

      1390       1400       1410       1420       1430       1440 
VLLGERAAKC RAYAKALHYK ELEFQKGPTP AILESLISIN NKLQQPEAAA GVLEYAMKHF 

      1450       1460       1470       1480       1490       1500 
GELEIQATWY EKLHEWEDAL VAYDKKMDTN KDDPELMLGR MRCLEALGEW GQLHQQCCEK 

      1510       1520       1530       1540       1550       1560 
WTLVNDETQA KMARMAAAAA WGLGQWDSME EYTCMIPRDT HDGAFYRAVL ALHQDLFSLA 

      1570       1580       1590       1600       1610       1620 
QQCIDKARDL LDAELTAMAG ESYSRAYGAM VSCHMLSELE EVIQYKLVPE RREIIRQIWW 

      1630       1640       1650       1660       1670       1680 
ERLQGCQRIV EDWQKILMVR SLVVSPHEDM RTWLKYASLC GKSGRLALAH KTLVLLLGVD 

      1690       1700       1710       1720       1730       1740 
PSRQLDHPLP TVHPQVTYAY MKNMWKSARK IDAFQHMQHF VQTMQQQAQH AIATEDQQHK 

      1750       1760       1770       1780       1790       1800 
QELHKLMARC FLKLGEWQLN LQGINESTIP KVLQYYSAAT EHDRSWYKAW HAWAVMNFEA 

      1810       1820       1830       1840       1850       1860 
VLHYKHQNQA RDEKKKLRHA SGANITNATT AATTAATATT TASTEGSNSE SEAESTENSP 

      1870       1880       1890       1900       1910       1920 
TPSPLQKKVT EDLSKTLLMY TVPAVQGFFR SISLSRGNNL QDTLRVLTLW FDYGHWPDVN 

      1930       1940       1950       1960       1970       1980 
EALVEGVKAI QIDTWLQVIP QLIARIDTPR PLVGRLIHQL LTDIGRYHPQ ALIYPLTVAS 

      1990       2000       2010       2020       2030       2040 
KSTTTARHNA ANKILKNMCE HSNTLVQQAM MVSEELIRVA ILWHEMWHEG LEEASRLYFG 

      2050       2060       2070       2080       2090       2100 
ERNVKGMFEV LEPLHAMMER GPQTLKETSF NQAYGRDLME AQEWCRKYMK SGNVKDLTQA 

      2110       2120       2130       2140       2150       2160 
WDLYYHVFRR ISKQLPQLTS LELQYVSPKL LMCRDLELAV PGTYDPNQPI IRIQSIAPSL 

      2170       2180       2190       2200       2210       2220 
QVITSKQRPR KLTLMGSNGH EFVFLLKGHE DLRQDERVMQ LFGLVNTLLA NDPTSLRKNL 

      2230       2240       2250       2260       2270       2280 
SIQRYAVIPL STNSGLIGWV PHCDTLHALI RDYREKKKIL LNIEHRIMLR MAPDYDHLTL 

      2290       2300       2310       2320       2330       2340 
MQKVEVFEHA VNNTAGDDLA KLLWLKSPSS EVWFDRRTNY TRSLAVMSMV GYILGLGDRH 

      2350       2360       2370       2380       2390       2400 
PSNLMLDRLS GKILHIDFGD CFEVAMTREK FPEKIPFRLT RMLTNAMEVT GLDGNYRITC 

      2410       2420       2430       2440       2450       2460 
HTVMEVLREH KDSVMAVLEA FVYDPLLNWR LMDTNTKGNK RSRTRTDSYS AGQSVEILDG 

      2470       2480       2490       2500       2510       2520 
VELGEPAHKK TGTTVPESIH SFIGDGLVKP EALNKKAIQI INRVRDKLTG RDFSHDDTLD 

      2530       2540 
VPTQVELLIK QATSHENLCQ CYIGWCPFW 

« Hide

References

« Hide 'large scale' references
[1]"A mammalian protein targeted by G1-arresting rapamycin-receptor complex."
Brown E.J., Albers M.W., Shin T.B., Ichikawa K., Keith C.T., Lane W.S., Schreiber S.L.
Nature 369:756-758(1994) [PubMed: 8008069] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
Tissue: Brain.
[2]"Molecular cloning and expression analysis of five novel genes in chromosome 1p36."
Onyango P., Lubyova B., Gardellin P., Kurzbauer R., Weith A.
Genomics 50:187-198(1998) [PubMed: 9653645] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"The DNA sequence and biological annotation of human chromosome 1."
Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K. expand/collapse author list , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
Nature 441:315-321(2006) [PubMed: 16710414] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"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].
Tissue: Cerebellum.
[5]"The human gene for mannan-binding lectin-associated serine protease-2 (MASP-2), the effector component of the lectin route of complement activation, is part of a tightly linked gene cluster on chromosome 1p36.2-3."
Stover C., Endo Y., Takahashi M., Lynch N., Constantinescu C., Vorup-Jensen T., Thiel S., Friedl H., Hankeln T., Hall R., Gregory S., Fujita T., Schwaeble W.
Genes Immun. 2:119-127(2001) [PubMed: 11426320] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1362-2549.
[6]"RAPT1, a mammalian homolog of yeast Tor, interacts with the FKBP12/rapamycin complex."
Chiu M.I., Katz H., Berlin V.
Proc. Natl. Acad. Sci. U.S.A. 91:12574-12578(1994) [PubMed: 7809080] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1987-2146, TISSUE SPECIFICITY.
Tissue: B-cell.
[7]"Characterization of ubiquilin 1, an mTOR-interacting protein."
Wu S., Mikhailov A., Kallo-Hosein H., Hara K., Yonezawa K., Avruch J.
Biochim. Biophys. Acta 1542:41-56(2002) [PubMed: 11853878] [Abstract]
Cited for: INTERACTION WITH UBQLN1.
[8]"Rictor, a novel binding partner of mTOR, defines a rapamycin-insensitive and raptor-independent pathway that regulates the cytoskeleton."
Sarbassov D.D., Ali S.M., Kim D.-H., Guertin D.A., Latek R.R., Erdjument-Bromage H., Tempst P., Sabatini D.M.
Curr. Biol. 14:1296-1302(2004) [PubMed: 15268862] [Abstract]
Cited for: FUNCTION, IDENTIFICATION IN TORC2 COMPLEX, INTERACTION WITH RICTOR.
[9]"Phosphorylation and regulation of Akt/PKB by the rictor-mTOR complex."
Sarbassov D.D., Guertin D.A., Ali S.M., Sabatini D.M.
Science 307:1098-1101(2005) [PubMed: 15718470] [Abstract]
Cited for: FUNCTION.
[10]"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: 17599906] [Abstract]
Cited for: IDENTIFICATION IN TORC2 COMPLEX, INTERACTION WITH PRR5.
[11]"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 THR-1162, MASS SPECTROMETRY.
[12]"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-567 AND SER-1261, MASS SPECTROMETRY.
[13]"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-2478 AND SER-2481, MASS SPECTROMETRY.
[14]Colinge J., Superti-Furga G., Bennett K.L.
Submitted (OCT-2008) to UniProtKB
Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]"Structure of the FKBP12-rapamycin complex interacting with the binding domain of human FRAP."
Choi J., Chen J., Schreiber S.L., Clardy J.
Science 273:239-242(1996) [PubMed: 8662507] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.7 ANGSTROMS) OF 2018-2112.
[16]"Refined structure of the FKBP12-rapamycin-FRB ternary complex at 2.2 A resolution."
Liang J., Choi J., Clardy J.
Acta Crystallogr. D 55:736-744(1999) [PubMed: 10089303] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS) OF 2018-2112.
[17]"Patterns of somatic mutation in human cancer genomes."
Greenman C., Stephens P., Smith R., Dalgliesh G.L., Hunter C., Bignell G., Davies H., Teague J., Butler A., Stevens C., Edkins S., O'Meara S., Vastrik I., Schmidt E.E., Avis T., Barthorpe S., Bhamra G., Buck G. expand/collapse author list , Choudhury B., Clements J., Cole J., Dicks E., Forbes S., Gray K., Halliday K., Harrison R., Hills K., Hinton J., Jenkinson A., Jones D., Menzies A., Mironenko T., Perry J., Raine K., Richardson D., Shepherd R., Small A., Tofts C., Varian J., Webb T., West S., Widaa S., Yates A., Cahill D.P., Louis D.N., Goldstraw P., Nicholson A.G., Brasseur F., Looijenga L., Weber B.L., Chiew Y.-E., DeFazio A., Greaves M.F., Green A.R., Campbell P., Birney E., Easton D.F., Chenevix-Trench G., Tan M.-H., Khoo S.K., Teh B.T., Yuen S.T., Leung S.Y., Wooster R., Futreal P.A., Stratton M.R.
Nature 446:153-158(2007) [PubMed: 17344846] [Abstract]
Cited for: VARIANTS [LARGE SCALE ANALYSIS] SER-8; THR-135; VAL-1083; VAL-1134; PHE-1178; VAL-2011; TYR-2215 AND LEU-2476.
+Additional computationally mapped references.

Cross-references

Sequence databases

L34075 mRNA. Translation: AAA58486.1.
U88966 mRNA. Translation: AAC39933.1. Frameshift.
AL109811, AL049653, AL391561 Genomic DNA. Translation: CAI22105.1.
AL391561, AL049653, AL109811 Genomic DNA. Translation: CAI17228.1.
AL049653, AL109811, AL391561 Genomic DNA. Translation: CAI22145.1.
BC117166 mRNA. Translation: AAI17167.1.
AJ300188 Genomic DNA. Translation: CAC15570.1.
L35478 mRNA. Translation: AAC41713.1.
IPIIPI00031410.
PIRS45340.
RefSeqNP_004949.1.
UniGeneHs.338207

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1AUEX-ray2.33A/B2015-2114[»]
1FAPX-ray2.70B2018-2112[»]
1NSGX-ray2.20B2019-2112[»]
2FAPX-ray2.20B2019-2112[»]
2GAQNMR-A2015-2114[»]
2NPUNMR-A2015-2114[»]
3FAPX-ray1.85B2019-2112[»]
4FAPX-ray2.80B2019-2112[»]
ModBaseSearch...

Protein-protein interaction databases

DIPDIP:790N.
IntActP42345. 24 interactions.

PTM databases

PhosphoSiteP42345.

Proteomic databases

PRIDEP42345.

Genome annotation databases

EnsemblENSG00000198793. Homo sapiens. [Contig view]
GeneID2475.
KEGGhsa:2475.

Organism-specific databases

GeneCardsGC01M011100.
H-InvDBHIX0021581.
HGNCHGNC:3942. FRAP1.
HPACAB005057.
MIM601231. gene.
PharmGKBPA28360.
GenAtlasSearch...

Phylogenomic databases

HOVERGENP42345.
OMAP42345. VFMHDNS.

Enzyme and pathway databases

Pathway_Interaction_DBpi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
endothelinpathway. Endothelins.
ifngpathway. IFN-gamma pathway.
il12_2pathway. IL12-mediated signaling events.
il2_pi3kpathway. IL2 signaling events mediated by PI3K.
il4_2pathway. IL4-mediated signaling events.
mtor_4pathway. mTOR signaling pathway.
telomerasepathway. Regulation of Telomerase.
ReactomeREACT_11061. Signalling by NGF.
REACT_498. Signaling by Insulin receptor.

Gene expression databases

ArrayExpressP42345.
BgeeP42345.
CleanExHS_FRAP1.
GermOnlineENSG00000198793. Homo sapiens.

Family and domain databases

InterProIPR011989. ARM-like.
IPR003152. FATC.
IPR009076. FKBP_rapamycin-assoc_FKBP12-bd.
IPR000403. PI3/4_kinase_cat.
IPR018936. PI3/4_kinase_CS.
IPR003151. PIK-rel_kinase_FAT.
IPR014009. PIK_FAT.
[Graphical view]
Gene3DG3DSA:1.25.10.10. ARM-like. 2 hits.
G3DSA:1.20.120.150. FRAP_FKBP12_bd. 1 hit.
G3DSA:1.10.1070.11. PI3/4_kinase_cat. 1 hit.
PfamPF02259. FAT. 1 hit.
PF02260. FATC. 1 hit.
PF00454. PI3_PI4_kinase. 1 hit.
PF08771. Rapamycin_bind. 1 hit.
[Graphical view]
SMARTSM00146. PI3Kc. 1 hit.
[Graphical view]
PROSITEPS51189. FAT. 1 hit.
PS51190. FATC. 1 hit.
PS50077. HEAT_REPEAT. False negative.
PS00915. PI3_4_KINASE_1. 1 hit.
PS00916. PI3_4_KINASE_2. 1 hit.
PS50290. PI3_4_KINASE_3. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio9805.
SOURCESearch...

Entry information

Entry nameFRAP_HUMAN
AccessionPrimary (citable) accession number: P42345
Secondary accession number(s): Q5TER1 expand/collapse secondary AC list , Q6LE87, Q96QG3, Q9Y4I3
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1995
Last sequence update: November 1, 1995
Last modified: June 16, 2009
This is version 92 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 1

Human chromosome 1: 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

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

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