RICTR_MOUSE
ID RICTR_MOUSE Reviewed; 1708 AA.
AC Q6QI06; E9QPE0; Q0VAV4; Q69Z40; Q6PDL2; Q6RI74; Q8BPH9; Q8CBF2;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 27-JUL-2011, sequence version 2.
DT 03-AUG-2022, entry version 134.
DE RecName: Full=Rapamycin-insensitive companion of mTOR;
DE AltName: Full=AVO3 homolog;
DE Short=mAVO3;
DE AltName: Full=Protein pianissimo;
GN Name=Rictor {ECO:0000250|UniProtKB:Q6R327};
GN Synonyms=Kiaa1999 {ECO:0000312|EMBL:BAD32604.1};
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1] {ECO:0000305, ECO:0000312|EMBL:AAR89074.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND IDENTIFICATION IN TORC2
RP COMPLEX.
RC STRAIN=C3H/HeJ {ECO:0000312|EMBL:AAR89074.1};
RX PubMed=15467718; DOI=10.1038/ncb1183;
RA Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.;
RT "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin
RT insensitive.";
RL Nat. Cell Biol. 6:1122-1128(2004).
RN [2] {ECO:0000305, ECO:0000312|EMBL:AAS46920.1}
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN TORC2
RP COMPLEX, AND DISRUPTION PHENOTYPE.
RC STRAIN=LAF1 {ECO:0000312|EMBL:AAS46920.1};
RX PubMed=16962829; DOI=10.1016/j.devcel.2006.08.013;
RA Shiota C., Woo J.-T., Lindner J., Shelton K.D., Magnuson M.A.;
RT "Multiallelic disruption of the rictor gene in mice reveals that mTOR
RT complex 2 is essential for fetal growth and viability.";
RL Dev. Cell 11:583-589(2006).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=C57BL/6J;
RX PubMed=19468303; DOI=10.1371/journal.pbio.1000112;
RA Church D.M., Goodstadt L., Hillier L.W., Zody M.C., Goldstein S., She X.,
RA Bult C.J., Agarwala R., Cherry J.L., DiCuccio M., Hlavina W., Kapustin Y.,
RA Meric P., Maglott D., Birtle Z., Marques A.C., Graves T., Zhou S.,
RA Teague B., Potamousis K., Churas C., Place M., Herschleb J., Runnheim R.,
RA Forrest D., Amos-Landgraf J., Schwartz D.C., Cheng Z., Lindblad-Toh K.,
RA Eichler E.E., Ponting C.P.;
RT "Lineage-specific biology revealed by a finished genome assembly of the
RT mouse.";
RL PLoS Biol. 7:E1000112-E1000112(2009).
RN [4] {ECO:0000305, ECO:0000312|EMBL:AAI20904.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:AAH58643.1};
RC TISSUE=Brain {ECO:0000312|EMBL:AAH58643.1};
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [5] {ECO:0000305, ECO:0000312|EMBL:BAC29321.2}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-825 (ISOFORM 1), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1347-1708 (ISOFORM 1/2).
RC STRAIN=C57BL/6J {ECO:0000312|EMBL:BAC29321.2};
RC TISSUE=Cerebellum {ECO:0000312|EMBL:BAC29321.2}, and
RC Embryo {ECO:0000312|EMBL:BAC35882.1};
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [6] {ECO:0000305, ECO:0000312|EMBL:BAD32604.1}
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 826-1708 (ISOFORM 1/2).
RC TISSUE=Thymus {ECO:0000312|EMBL:BAD32604.1};
RX PubMed=15368895; DOI=10.1093/dnares/11.3.205;
RA Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S.,
RA Saga Y., Seino S., Nishimura M., Kaisho T., Hoshino K., Kitamura H.,
RA Nagase T., Ohara O., Koga H.;
RT "Prediction of the coding sequences of mouse homologues of KIAA gene: IV.
RT The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs
RT identified by screening of terminal sequences of cDNA clones randomly
RT sampled from size-fractionated libraries.";
RL DNA Res. 11:205-218(2004).
RN [7] {ECO:0000305}
RP FUNCTION.
RX PubMed=16221682; DOI=10.1074/jbc.m508361200;
RA Hresko R.C., Mueckler M.;
RT "mTOR.RICTOR is the Ser473 kinase for Akt/protein kinase B in 3T3-L1
RT adipocytes.";
RL J. Biol. Chem. 280:40406-40416(2005).
RN [8] {ECO:0000305}
RP FUNCTION, AND IDENTIFICATION IN TORC2 COMPLEX.
RX PubMed=16962653; DOI=10.1016/j.cell.2006.08.033;
RA Jacinto E., Facchinetti V., Liu D., Soto N., Wei S., Jung S.Y., Huang Q.,
RA Qin J., Su B.;
RT "SIN1/MIP1 maintains rictor-mTOR complex integrity and regulates Akt
RT phosphorylation and substrate specificity.";
RL Cell 127:125-137(2006).
RN [9]
RP FUNCTION, AND DISRUPTION PHENOTYPE.
RX PubMed=17141160; DOI=10.1016/j.devcel.2006.10.007;
RA Guertin D.A., Stevens D.M., Thoreen C.C., Burds A.A., Kalaany N.Y.,
RA Moffat J., Brown M., Fitzgerald K.J., Sabatini D.M.;
RT "Ablation in mice of the mTORC components raptor, rictor, or mLST8 reveals
RT that mTORC2 is required for signaling to Akt-FOXO and PKCalpha, but not
RT S6K1.";
RL Dev. Cell 11:859-871(2006).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1234; SER-1312;
RP SER-1384 AND SER-1387, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
RP ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Kidney, Lung, Pancreas, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [11]
RP TISSUE SPECIFICITY.
RX PubMed=33378666; DOI=10.1016/j.celrep.2020.108564;
RA Wrobel L., Siddiqi F.H., Hill S.M., Son S.M., Karabiyik C., Kim H.,
RA Rubinsztein D.C.;
RT "mTORC2 Assembly Is Regulated by USP9X-Mediated Deubiquitination of
RT RICTOR.";
RL Cell Rep. 33:108564-108564(2020).
CC -!- FUNCTION: Subunit of mTORC2, which regulates cell growth and survival
CC in response to hormonal signals. mTORC2 is activated by growth factors,
CC but, in contrast to mTORC1, seems to be nutrient-insensitive. mTORC2
CC seems to function upstream of Rho GTPases to regulate the actin
CC cytoskeleton, probably by activating one or more Rho-type guanine
CC nucleotide exchange factors. mTORC2 promotes the serum-induced
CC formation of stress-fibers or F-actin. mTORC2 plays a critical role in
CC AKT1 'Ser-473' phosphorylation, which may facilitate the
CC phosphorylation of the activation loop of AKT1 on 'Thr-308' by PDK1
CC which is a prerequisite for full activation. mTORC2 regulates the
CC phosphorylation of SGK1 at 'Ser-422'. mTORC2 also modulates the
CC phosphorylation of PRKCA on 'Ser-657'. Plays an essential role in
CC embryonic growth and development. {ECO:0000269|PubMed:16221682,
CC ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:16962829,
CC ECO:0000269|PubMed:17141160}.
CC -!- SUBUNIT: Part of the mammalian target of rapamycin complex 2 (mTORC2)
CC which contains MTOR, MLST8, PRR5, RICTOR, MAPKAP1 and DEPTOR
CC (PubMed:15467718, PubMed:16962829, PubMed:16962653). Contrary to
CC mTORC1, mTORC2 does not bind to and is not sensitive to FKBP12-
CC rapamycin. Binds directly to MTOR and PRR5 within the TORC2 complex;
CC interaction with MTOR is enhanced by deubiquitination of RICTOR by
CC USP9X. Interaction with MAPKAP1 is not enhanced by RICTOR
CC deubiquitination by USP9X (By similarity). Interacts with CCDC28B.
CC Interacts with NBN. Interacts with PRR5L (By similarity). Interacts
CC with SIK3 (By similarity). Interacts with NCKAP1L (By similarity).
CC Interacts with FBXW7; the interaction results in RICTOR ubiquitination
CC and degradation (By similarity). Interacts with USP9X; the interaction
CC results in deubiquitination of RICTOR and protection from proteasomal
CC degradation, thus promoting mTORC2 complex assembly (By similarity).
CC {ECO:0000250|UniProtKB:Q6R327, ECO:0000269|PubMed:15467718,
CC ECO:0000269|PubMed:16962653, ECO:0000269|PubMed:16962829}.
CC -!- INTERACTION:
CC Q6QI06; Q9JLN9: Mtor; NbExp=12; IntAct=EBI-4286572, EBI-1571628;
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1 {ECO:0000269|PubMed:15467718, ECO:0000269|PubMed:16962829};
CC IsoId=Q6QI06-1; Sequence=Displayed;
CC Name=2 {ECO:0000269|PubMed:15489334};
CC IsoId=Q6QI06-2; Sequence=VSP_052583;
CC -!- TISSUE SPECIFICITY: Highest levels in liver and brain with expression
CC also detected in heart, muscle, spleen and kidney (at protein level).
CC {ECO:0000269|PubMed:33378666}.
CC -!- PTM: Phosphorylated by MTOR; when part of mTORC2 (By similarity).
CC Phosphorylated at Thr-1135 by RPS6KB1; phosphorylation of RICTOR
CC inhibits mTORC2 and AKT1 signaling (By similarity).
CC {ECO:0000250|UniProtKB:Q6R327}.
CC -!- PTM: Ubiquitinated by the SCF(FBXW7) complex, leading to its
CC degradation by the proteasome (By similarity). Deubiquitinated by
CC USP9X; deubiquitination stabilizes RICTOR and enhances its binding to
CC MTOR, thus promoting mTORC2 complex assembly (By similarity).
CC {ECO:0000250|UniProtKB:Q6R327}.
CC -!- DISRUPTION PHENOTYPE: Mice develop normally until E9.5, and then
CC display growth arrest and embryonic lethality by 11.5 dpc.
CC {ECO:0000269|PubMed:16962829, ECO:0000269|PubMed:17141160}.
CC -!- SIMILARITY: Belongs to the RICTOR family. {ECO:0000305}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
DR EMBL; AY497009; AAR89074.1; -; mRNA.
DR EMBL; AY540053; AAS46920.1; -; mRNA.
DR EMBL; AC102825; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC158901; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC058643; AAH58643.1; -; mRNA.
DR EMBL; BC120903; AAI20904.1; -; mRNA.
DR EMBL; AK036149; BAC29321.2; -; mRNA.
DR EMBL; AK075662; BAC35882.1; -; mRNA.
DR EMBL; AK173326; BAD32604.1; -; mRNA.
DR CCDS; CCDS37032.1; -. [Q6QI06-1]
DR RefSeq; NP_084444.3; NM_030168.3. [Q6QI06-1]
DR AlphaFoldDB; Q6QI06; -.
DR SMR; Q6QI06; -.
DR BioGRID; 219616; 7.
DR ComplexPortal; CPX-4472; mTORC2 complex.
DR DIP; DIP-46323N; -.
DR IntAct; Q6QI06; 8.
DR MINT; Q6QI06; -.
DR STRING; 10090.ENSMUSP00000051809; -.
DR iPTMnet; Q6QI06; -.
DR PhosphoSitePlus; Q6QI06; -.
DR EPD; Q6QI06; -.
DR jPOST; Q6QI06; -.
DR MaxQB; Q6QI06; -.
DR PaxDb; Q6QI06; -.
DR PeptideAtlas; Q6QI06; -.
DR PRIDE; Q6QI06; -.
DR ProteomicsDB; 253239; -. [Q6QI06-1]
DR ProteomicsDB; 253240; -. [Q6QI06-2]
DR Antibodypedia; 23075; 685 antibodies from 41 providers.
DR DNASU; 78757; -.
DR Ensembl; ENSMUST00000061656; ENSMUSP00000051809; ENSMUSG00000050310. [Q6QI06-1]
DR GeneID; 78757; -.
DR KEGG; mmu:78757; -.
DR UCSC; uc007vdr.2; mouse. [Q6QI06-1]
DR CTD; 253260; -.
DR MGI; MGI:1926007; Rictor.
DR VEuPathDB; HostDB:ENSMUSG00000050310; -.
DR eggNOG; KOG3694; Eukaryota.
DR GeneTree; ENSGT00390000002096; -.
DR HOGENOM; CLU_001013_2_0_1; -.
DR InParanoid; Q6QI06; -.
DR OMA; VFEYLIT; -.
DR OrthoDB; 128601at2759; -.
DR PhylomeDB; Q6QI06; -.
DR TreeFam; TF343656; -.
DR Reactome; R-MMU-1257604; PIP3 activates AKT signaling.
DR Reactome; R-MMU-389357; CD28 dependent PI3K/Akt signaling.
DR Reactome; R-MMU-5218920; VEGFR2 mediated vascular permeability.
DR Reactome; R-MMU-6804757; Regulation of TP53 Degradation.
DR BioGRID-ORCS; 78757; 7 hits in 74 CRISPR screens.
DR ChiTaRS; Rictor; mouse.
DR PRO; PR:Q6QI06; -.
DR Proteomes; UP000000589; Chromosome 15.
DR RNAct; Q6QI06; protein.
DR Bgee; ENSMUSG00000050310; Expressed in cerebellum lobe and 220 other tissues.
DR Genevisible; Q6QI06; MM.
DR GO; GO:0031932; C:TORC2 complex; IDA:UniProtKB.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0043539; F:protein serine/threonine kinase activator activity; IBA:GO_Central.
DR GO; GO:0043022; F:ribosome binding; IDA:UniProtKB.
DR GO; GO:0031532; P:actin cytoskeleton reorganization; ISS:UniProtKB.
DR GO; GO:0031669; P:cellular response to nutrient levels; IC:ComplexPortal.
DR GO; GO:0007010; P:cytoskeleton organization; IC:ComplexPortal.
DR GO; GO:0009792; P:embryo development ending in birth or egg hatching; IMP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; IC:ComplexPortal.
DR GO; GO:0018105; P:peptidyl-serine phosphorylation; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; ISO:MGI.
DR GO; GO:0030838; P:positive regulation of actin filament polymerization; IMP:MGI.
DR GO; GO:0030307; P:positive regulation of cell growth; IC:ComplexPortal.
DR GO; GO:0001938; P:positive regulation of endothelial cell proliferation; ISO:MGI.
DR GO; GO:0050731; P:positive regulation of peptidyl-tyrosine phosphorylation; IMP:MGI.
DR GO; GO:0051897; P:positive regulation of protein kinase B signaling; ISO:MGI.
DR GO; GO:0032008; P:positive regulation of TOR signaling; ISO:MGI.
DR GO; GO:0032956; P:regulation of actin cytoskeleton organization; ISO:MGI.
DR GO; GO:2000114; P:regulation of establishment of cell polarity; IMP:MGI.
DR GO; GO:0010468; P:regulation of gene expression; IMP:MGI.
DR GO; GO:0043087; P:regulation of GTPase activity; IMP:MGI.
DR GO; GO:0050727; P:regulation of inflammatory response; IMP:MGI.
DR GO; GO:0033135; P:regulation of peptidyl-serine phosphorylation; IMP:MGI.
DR GO; GO:0042325; P:regulation of phosphorylation; ISO:MGI.
DR GO; GO:0051896; P:regulation of protein kinase B signaling; IDA:UniProtKB.
DR GO; GO:0001932; P:regulation of protein phosphorylation; IMP:CACAO.
DR GO; GO:0038203; P:TORC2 signaling; IBA:GO_Central.
DR InterPro; IPR016024; ARM-type_fold.
DR InterPro; IPR028268; Pianissimo_fam.
DR InterPro; IPR028267; Pianissimo_N.
DR InterPro; IPR029453; Rictor_IV.
DR InterPro; IPR029451; RICTOR_M.
DR InterPro; IPR029259; RICTOR_phospho.
DR InterPro; IPR029452; RICTOR_V.
DR PANTHER; PTHR13298; PTHR13298; 1.
DR Pfam; PF14663; RasGEF_N_2; 1.
DR Pfam; PF14666; RICTOR_M; 1.
DR Pfam; PF14664; RICTOR_N; 1.
DR Pfam; PF14665; RICTOR_phospho; 1.
DR Pfam; PF14668; RICTOR_V; 1.
DR SMART; SM01307; RICTOR_M; 1.
DR SMART; SM01308; RICTOR_N; 1.
DR SMART; SM01309; RICTOR_phospho; 1.
DR SMART; SM01310; RICTOR_V; 1.
DR SUPFAM; SSF48371; SSF48371; 2.
PE 1: Evidence at protein level;
KW Alternative splicing; Developmental protein; Isopeptide bond;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..1708
FT /note="Rapamycin-insensitive companion of mTOR"
FT /id="PRO_0000308180"
FT REGION 1..789
FT /note="Interaction with NBN"
FT /evidence="ECO:0000250"
FT REGION 1021..1045
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1101..1198
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1218..1247
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1021..1042
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1131..1160
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1218..1240
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 21
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1103
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1135
FT /note="Phosphothreonine; by RPS6KB1"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1161
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1234
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1277
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1281
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1283
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1294
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1301
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1312
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1331
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1345
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1352
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1384
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1387
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:21183079"
FT MOD_RES 1395
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1410
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT MOD_RES 1591
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT CROSSLNK 274
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in ubiquitin)"
FT /evidence="ECO:0000250|UniProtKB:Q6R327"
FT VAR_SEQ 1..152
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_052583"
FT CONFLICT 15
FT /note="I -> V (in Ref. 1; AAR89074)"
FT /evidence="ECO:0000305"
FT CONFLICT 185
FT /note="R -> Q (in Ref. 1; AAR89074)"
FT /evidence="ECO:0000305"
FT CONFLICT 405
FT /note="L -> I (in Ref. 1; AAR89074)"
FT /evidence="ECO:0000305"
FT CONFLICT 698
FT /note="I -> L (in Ref. 2; AAS46920)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1708 AA; 191570 MW; 309CEE9B1404316D CRC64;
MAAIGRGRSL KNLRIRGRND SGEENVPLDL TREPSDNLRE ILQNVAKLQG VSNMRKLGHL
NNFTKLLCDI GHSEEKLGFN YEDIIICLRL ALLNEAKEVR AAGLRALRYL IQDSSILQKV
LKLKVDYLIA RCIDIQQSNE VERTQALRLV RKMITVNASL FPSSVANSLI AVGNDGLQER
DRMVRACIAI ICELALQNPE VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT
RQYVRADVEL ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN
LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTDEFIEAL LSVDPGRFQD
SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI RNGLLEGLVE VITNSDDHIS
VRATILLGEL LHMANTILPH SHSHHLHCLP TLMNMAASFD IPKEKRLRAS AALNCLNRFH
EMKKRGPKPY SLHLDHIIQK AIATHHKRDQ YLRVQKDIFV LKDTEEALLI NLRDSQVLQH
KENLDWDWNL IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAS LDLDLAKSKQ
LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGV KPERSLQNNG LLTTLSQHYF
LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLIKL TVSSLDYSRD GLARVILSKI
LTAATDACRL YATKHLRVLL RANVEFFNNW GIELLVTQLH DKNKTISSEA LDILDEACED
KANLHALIQM KPALSHLGDK GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHKEYNSKYV
DLIEEQLNEA LTTYRKPIDG DNYVRRSNQR LQRPHVYLPV HLYGQLVHHK TGCHLLEVQS
IITELCHNVR TPDLDKWEDI KKLKASLWAL GNIGSSNWGL NLLQEENVIP DILKLAKQCE
VLSIRGTCVY VLGLIAKTKQ GCDILKCHSW DSVRHSRKHL WPVVPDDVEQ LCNELSSVPS
TLSLNSESTS SRHNSESESA PSSMFMLEDD RFGSTSTSTF FLDINEDAEP AFYDRPGPIK
DKNSFPFFGS SKLVKNRILN SLTLPTKKHR SSSDPKGGKL SSENKTSNRR IRTLTEPSVD
LNHSEDFTSS SAQKSLQLEP SFVGNKHLED AGSTPSIGEN DLKFPKSFGT ETHRENTSRE
RLVVEGSASS HIKIRSQSFN TDTTTSGISS MSSSPSRETV AVDPTAMDTD CGSLSTVVST
KTVKTSHYLT PQSNHLSLSK SNSVSLVPPG SSHTLPRRAQ SLKAPSIATI KSLADCNFSY
TSSRDAFGYA TLKRLQQQRM HPSLSHSEAL ASPAKDVLFT DTITMKANSF ESRLTPSRFM
KALSYASLDK EDLLSPINHN TLQRSSSVRS MVSSATYGGS DDYIGLALPV DINDIFQIKD
VPYFQSKHVP PPDDRGARMF SHDGAGLSSG AGGLVKNSFH LLRQQMSLTE IMNSVHSDAS
LFLESTEDTG LQEHTDDNCL YCVCIELLGF QPSNQLSSIC SHSDLQDIPY SDWCEQTIHN
PLEVVPSKFS GISGCSDGAS QEEGSASSTK STELLLGVKT IPDDTPMCRI LLRKEVLRLV
VNLSSSVSTK CHETGLLTIK EKYPQTFDDI CLYSEVSHLL SHCTFRLQCR RFIQELFQDV
QFLQMHEEAE AVLAIPPIQP IVDESAES
