<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functionⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functionⁱ

1. protein kinase binding Source: ParkinsonsUK-UCL

   <p>Inferred from Physical Interaction</p> <p>Covers physical interactions between the gene product of interest and another molecule (or ion, or complex).</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ipi">GO evidence code guide</a></p> Inferred from physical interactionⁱ

   • 21177249

2. ribosome binding Source: Ensembl

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processⁱ

1. actin cytoskeleton reorganization Source: UniProtKB

   <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

   • 15268862

2. embryo development Source: UniProtKB
3. epidermal growth factor receptor signaling pathway Source: Reactome
4. Fc-epsilon receptor signaling pathway Source: Reactome
5. fibroblast growth factor receptor signaling pathway Source: Reactome
6. innate immune response Source: Reactome
7. neurotrophin TRK receptor signaling pathway Source: Reactome
8. peptidyl-serine phosphorylation Source: ParkinsonsUK-UCL

   <p>Inferred from Genetic Interaction</p> <p>Used to describe “traditional” genetic interactions such as suppressors and synthetic lethals as well as other techniques such as functional complementation, rescue experiments, or inferences about a gene drawn from the phenotype of a mutation in a different gene.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#igi">GO evidence code guide</a></p> Inferred from genetic interactionⁱ

   • 21177249

9. phosphatidylinositol-mediated signaling Source: Reactome
10. positive regulation of actin filament polymerization Source: Ensembl
11. positive regulation of endothelial cell proliferation Source: Ensembl
12. positive regulation of peptidyl-tyrosine phosphorylation Source: Ensembl
13. positive regulation of protein kinase B signaling Source: Ensembl
14. positive regulation of TOR signaling Source: UniProtKB

    <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

    • 15467718

15. regulation of actin cytoskeleton organization Source: UniProtKB

    <p>Inferred from Mutant Phenotype</p> <p>Describes annotations that are concluded from looking at variations or changes in a gene product such as mutations or abnormal levels and includes techniques such as knockouts, overexpression, anti-sense experiments and use of specific protein inhibitors.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#imp">GO evidence code guide</a></p> Inferred from mutant phenotypeⁱ

    • 15467718

16. regulation of protein kinase B signaling Source: UniProtKB

    <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

    • 15718470

17. regulation of Rac GTPase activity Source: Ensembl
18. T cell costimulation Source: Reactome
19. TOR signaling Source: InterPro

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Molecular functionⁱ

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyⁱ

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationⁱ

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componentⁱ

1. cytosol Source: Reactome
2. TORC2 complex Source: UniProtKB

   <p>Inferred from Direct Assay</p> <p>Used to indicate a direct assay for the function, process or component indicated by the GO term.</p> <p>More information in the <a href="http://geneontology.org/page/guide-go-evidence-codes#ida">GO evidence code guide</a></p> Inferred from direct assayⁱ

   • 15268862
   • 15467718

<p>Provides information on the disease(s) and phenotype(s) associated with the deficiency of a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechⁱ

Organism-specific databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the extent of a polypeptide chain in the mature protein following processing.</p><p><a href='../manual/chain' target='_top'>More...</a></p>Chaini	1 – 1708	1708	Rapamycin-insensitive companion of mTOR		PRO_0000308179	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	21 – 21	1	Phosphoserine7 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.9 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.12 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.13 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.14 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1282; SER-1388 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.16 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1284; SER-1388 AND SER-1411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.18 "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis." Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M. Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.20 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1135 – 1135	1	Phosphothreonine; by RPS6KB11 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.17 "mTORC1-activated S6K1 phosphorylates Rictor on threonine 1135 and regulates mTORC2 signaling." Julien L.A., Carriere A., Moreau J., Roux P.P. Mol. Cell. Biol. 30:908-921(2010) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION AT THR-1135.
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1282 – 1282	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.14 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1282; SER-1388 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1284 – 1284	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.16 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1284; SER-1388 AND SER-1411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1388 – 1388	1	Phosphoserine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.14 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1282; SER-1388 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.16 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1284; SER-1388 AND SER-1411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1396 – 1396	1	Phosphoserine2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.13 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.14 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1282; SER-1388 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1411 – 1411	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.16 "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] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1284; SER-1388 AND SER-1411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
<p>Specifies the position and type of each modified residue excluding <a href="/manual/lipid">lipids</a>, <a href="/manual/carbohyd">glycans</a> and <a href="/manual/crosslnk">protein cross-links</a>.</p><p><a href='../manual/mod_res' target='_top'>More...</a></p>Modified residuei	1591 – 1591	1	Phosphoserine1 Publication <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.20 "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation." Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B. Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

<p>Describes post-translational modifications (PTMs). This subsection complements the information provided at the sequence level or describes modifications for which position-specific data is not yet available.</p><p><a href='../manual/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - PTMⁱ

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressionⁱ

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactionⁱ

<p>Provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the ‘Function’ section).</p><p><a href='../manual/subunit_structure' target='_top'>More...</a></p>Subunit structureⁱ

<p>Provides information about binary protein-protein interactions. The data presented in this section are a quality-filtered subset of binary interactions automatically derived from the <a href="http://www.ebi.ac.uk/intact/">IntAct database</a>. It is updated on a monthly basis. Each binary interaction is displayed on a separate line.</p><p><a href='../manual/binary_interactions' target='_top'>More...</a></p>Binary interactionsⁱ

Protein-protein interaction databases

<p>Provides information on the tertiary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structureⁱ

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsⁱ

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes a region of interest that cannot be described in other subsections.</p><p><a href='../manual/region' target='_top'>More...</a></p>Regioni	1 – 789	789	Interaction with NBN			Add BLAST

Compositional bias

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.</p><p><a href='../manual/compbias' target='_top'>More...</a></p>Compositional biasi	1016 – 1058	43	Ser-richSequence Analysis			Add BLAST

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesⁱ

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (3)ⁱ

<p>Indicates if the canonical sequence displayed by default in the entry is complete or not.</p><p><a href='../manual/sequence_status' target='_top'>More...</a></p>Sequence statusⁱ: Complete.

This entry describes 3<p>Lists the alternative protein sequences (isoforms) that can be generated from the same gene by a single or by the combination of up to four biological events (alternative promoter usage, alternative splicing, alternative initiation and ribosomal frameshifting). Additionally, this section gives relevant information on each alternative protein isoform.</p><p><a href='../manual/alternative_products' target='_top'>More...</a></p> isoformsⁱ produced by alternative splicing. Align

        10         20         30         40         50
MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG 
        60         70         80         90        100
VSNMRKLGHL NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR 
       110        120        130        140        150
AAGLRALRYL IQDSSILQKV LKLKVDYLIA RCIDIQQSNE VERTQALRLV 
       160        170        180        190        200
RKMITVNASL FPSSVTNSLI AVGNDGLQER DRMVRACIAI ICELALQNPE 
       210        220        230        240        250
VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT RQYVRADVEL 
       260        270        280        290        300
ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN 
       310        320        330        340        350
LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTEEFIEAL 
       360        370        380        390        400
LSVDPGRFQD SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI 
       410        420        430        440        450
RNGLLEGLVE VITNSDDHIS VRATILLGEL LHMANTILPH SHSHHLHCLP 
       460        470        480        490        500
TLMNMAASFD IPKEKRLRAS AALNCLKRFH EMKKRGPKPY SLHLDHIIQK 
       510        520        530        540        550
AIATHQKRDQ YLRVQKDIFI LKDTEEALLI NLRDSQVLQH KENLEWNWNL 
       560        570        580        590        600
IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAN LDLDFAKAKQ 
       610        620        630        640        650
LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGM KPERSLQNNG 
       660        670        680        690        700
LLTTLSQHYF LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL 
       710        720        730        740        750
TVSSLDYSRD GLARVILSKI LTAATDACRL YATKHLRVLL RANVEFFNNW 
       760        770        780        790        800
GIELLVTQLH DKNKTISSEA LDILDEACED KANLHALIQM KPALSHLGDK 
       810        820        830        840        850
GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHREYNSKYV DLIEEQLNEA 
       860        870        880        890        900
LTTYRKPVDG DNYVRRSNQR LQRPHVYLPI HLYGQLVHHK TGCHLLEVQN 
       910        920        930        940        950
IITELCRNVR TPDLDKWEEI KKLKASLWAL GNIGSSNWGL NLLQEENVIP 
       960        970        980        990       1000
DILKLAKQCE VLSIRGTCVY VLGLIAKTKQ GCDILKCHNW DAVRHSRKHL 
      1010       1020       1030       1040       1050
WPVVPDDVEQ LCNELSSIPS TLSLNSESTS SRHNSESESV PSSMFILEDD 
      1060       1070       1080       1090       1100
RFGSSSTSTF FLDINEDTEP TFYDRSGPIK DKNSFPFFAS SKLVKNRILN 
      1110       1120       1130       1140       1150
SLTLPNKKHR SSSDPKGGKL SSESKTSNRR IRTLTEPSVD FNHSDDFTPI 
      1160       1170       1180       1190       1200
STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR 
      1210       1220       1230       1240       1250
ERLVVESSTS SHMKIRSQSF NTDTTTSGIS SMSSSPSRET VGVDATTMDT 
      1260       1270       1280       1290       1300
DCGSMSTVVS TKTIKTSHYL TPQSNHLSLS KSNSVSLVPP GSSHTLPRRA 
      1310       1320       1330       1340       1350
QSLKAPSIAT IKSLADCNFS YTSSRDAFGY ATLKRLQQQR MHPSLSHSEA 
      1360       1370       1380       1390       1400
LASPAKDVLF TDTITMKANS FESRLTPSRF MKALSYASLD KEDLLSPINQ 
      1410       1420       1430       1440       1450
NTLQRSSSVR SMVSSATYGG SDDYIGLALP VDINDIFQVK DIPYFQTKNI 
      1460       1470       1480       1490       1500
PPHDDRGARA FAHDAGGLPS GTGGLVKNSF HLLRQQMSLT EIMNSIHSDA 
      1510       1520       1530       1540       1550
SLFLESTEDT GLQEHTDDNC LYCVCIEILG FQPSNQLSAI CSHSDFQDIP 
      1560       1570       1580       1590       1600
YSDWCEQTIH NPLEVVPSKF SGISGCSDGV SQEGSASSTK STELLLGVKT 
      1610       1620       1630       1640       1650
IPDDTPMCRI LLRKEVLRLV INLSSSVSTK CHETGLLTIK EKYPQTFDDI 
      1660       1670       1680       1690       1700
CLYSEVSHLL SHCTFRLPCR RFIQELFQDV QFLQMHEEAE AVLATPPKQP 

IVDTSAES                                             

        10         20         30         40         50
MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG 
        60         70         80         90        100
VSNMRKLGHL NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR 
       110        120        130        140        150
AAGLRALRYL IQDSSILQKV LKLKVDYLIA RCIDIQQSNE VERTQALRLV 
       160        170        180        190        200
RKMITVNASL FPSSVTNSLI AVGNDGLQER DRMVRACIAI ICELALQNPE 
       210        220        230        240        250
VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT RQYVRADVEL 

ENFSTLY                                             

        10         20         30         40         50
MAAIGRGRSL KNLRVRGRND SGEENVPLDL TREPSDNLRE ILQNVARLQG 
        60         70         80         90        100
VSNMRKLGHL NNFTKLLCDI GHSEEKLGFH YEDIIICLRL ALLNEAKEVR 
       110        120        130        140        150
AAGLRALRYL IQDSSILQKV LKLKVDYLIA RCIDIQQSNE VERTQALRLV 
       160        170        180        190        200
RKMITVNASL FPSSVTNSLI AVGNDGLQER DRMVRACIAI ICELALQNPE 
       210        220        230        240        250
VVALRGGLNT ILKNVIDCQL SRINEALITT ILHLLNHPKT RQYVRADVEL 
       260        270        280        290        300
ERILAPYTDF HYRHSPDTAE GQLKEDREAR FLASKMGIIA TFRSWAGIIN 
       310        320        330        340        350
LCKPGNSGIQ SLIGVLCIPN MEIRRGLLEV LYDIFRLPLP VVTEEFIEAL 
       360        370        380        390        400
LSVDPGRFQD SWRLSDGFVA AEAKTILPHR ARSRPDLMDN YLALILSAFI 
       410        420        430        440        450
RNGLLEGLVE VITNSDDHIS VRATILLGEL LHMANTILPH SHSHHLHCLP 
       460        470        480        490        500
TLMNMAASFD IPKEKRLRAS AALNCLKRFH EMKKRGPKPY SLHLDHIIQK 
       510        520        530        540        550
AIATHQKRDQ YLRVQKDIFI LKDTEEALLI NLRDSQVLQH KENLEWNWNL 
       560        570        580        590        600
IGTILKWPNV NLRNYKDEQL HRFVRRLLYF YKPSSKLYAN LDLDFAKAKQ 
       610        620        630        640        650
LTVVGCQFTE FLLESEEDGQ GYLEDLVKDI VQWLNASSGM KPERSLQNNG 
       660        670        680        690        700
LLTTLSQHYF LFIGTLSCHP HGVKMLEKCS VFQCLLNLCS LKNQDHLLKL 
       710        720        730        740        750
TVSSLDYSRD GLARVILSKI LTAATDACRL YATKHLRVLL RANVEFFNNW 
       760        770        780        790        800
GIELLVTQLH DKNKTISSEA LDILDEACED KANLHALIQM KPALSHLGDK 
       810        820        830        840        850
GLLLLLRFLS IPKGFSYLNE RGYVAKQLEK WHREYNSKYV DLIEEQLNEA 
       860        870        880        890        900
LTTYRKPVDG DNYVRRSNQR LQRPHVYLPI HLYGQLVHHK TGCHLLEVQN 
       910        920        930        940        950
IITELCRNVR TPDLDKWEEI KKLKASLWAL GNIGSSNWGL NLLQEENVIP 
       960        970        980        990       1000
DILKLAKQCE VLSIRGTCVY VLGLIAKTKQ GCDILKCHNW DAVRHSRKHL 
      1010       1020       1030       1040       1050
WPVVPDDVEQ LCNELSSIPS TLSLNSESTS SRHNSESESV PSSMFILEDD 
      1060       1070       1080       1090       1100
RFGSSSTSTF FLDINEDTEP TFYDRSGPIK DKNSFPFFAS SKLVKNRILN 
      1110       1120       1130       1140       1150
SLTLPNKKHR SSSDPKGGKL SSESKTSNRR IRTLTEPSVD FNHSDDFTPI 
      1160       1170       1180       1190       1200
STVQKTLQLE TSFMGNKHIE DTGSTPSIGE NDLKFTKNFG TENHRENTSR 
      1210       1220       1230       1240       1250
ERLVVESSTS SHMKIRSQSF NTDTTTSGIS SMSSSPSRET VGVDATTMDT 
      1260       1270       1280       1290       1300
DCGSMSTVVS TKTIKTSHYL TPQSNHLSLS KSNSVSLVPP GSSHTLPRRA 
      1310       1320       1330       1340       1350
QSLKAPSIAT IKSLADCNFS YTSSRDAFGY ATLKRLQQQR MHPSLSHSEA 
      1360       1370       1380       1390       1400
LASPAKDVLF TDTITMKANS FESRLTPSRI DFKKKHVGGI RSLRPTITNN 
      1410       1420       1430       1440       1450
LFRFMKALSY ASLDKEDLLS PINQNTLQRS SSVRSMVSSA TYGGSDDYIG 
      1460       1470       1480       1490       1500
LALPVDINDI FQVKDIPYFQ TKNIPPHDDR GARAFAHDAG GLPSGTGGLV 
      1510       1520       1530       1540       1550
KNSFHLLRQQ MSLTEIMNSI HSDASLFLES TEDTGLQEHT DDNCLYCVCI 
      1560       1570       1580       1590       1600
EILGFQPSNQ LSAICSHSDF QDIPYSDWCE QTIHNPLEVV PSKFSGISGC 
      1610       1620       1630       1640       1650
SDGVSQEGSA SSTKSTELLL GVKTIPDDTP MCRILLRKEV LRLVINLSSS 
      1660       1670       1680       1690       1700
VSTKCHETGL LTIKEKYPQT FDDICLYSEV SHLLSHCTFR LPCRRFIQEL 
      1710       1720       1730 
FQDVQFLQMH EEAEAVLATP PKQPIVDTSA ES            

<p>Reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.</p><p><a href='../manual/sequence_caution' target='_top'>More...</a></p>Sequence cautionⁱ

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	545 – 545	1	E → G in CAH18135. (PubMed:17974005)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	815 – 815	1	F → L in CAH18135. (PubMed:17974005)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	1283 – 1283	1	N → S in CAH18135. (PubMed:17974005)Curated
<p>Reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.</p><p><a href='../manual/conflict' target='_top'>More...</a></p>Sequence conflicti	1699 – 1699	1	Q → R in AAH51729. (PubMed:15489334)Curated

Natural variant

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes natural variant(s) of the protein sequence.</p><p><a href='../manual/variant' target='_top'>More...</a></p>Natural varianti	837 – 837	1	S → F.2 Publications <p>Manually curated information for which there is published experimental evidence.</p> <p><a href="/manual/evidences#ECO:0000269">More…</a></p> Manual assertion based on experiment ini Ref.2 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 932-1708 (ISOFORM 3), VARIANT PHE-837. Ref.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] (ISOFORMS 1 AND 3), VARIANT PHE-837. Corresponds to variant rs2043112 [ dbSNP | Ensembl ].		VAR_051320

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	252 – 257	6	RILAPY → NFSTLY in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.2 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 932-1708 (ISOFORM 3), VARIANT PHE-837.		VSP_038362
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	258 – 1708	1451	Missing in isoform 2. 1 Publication <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.2 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 932-1708 (ISOFORM 3), VARIANT PHE-837.		VSP_038363	Add BLAST
<p>Describes the sequence of naturally occurring alternative protein isoform(s). The changes in the amino acid sequence may be due to alternative splicing, alternative promoter usage, alternative initiation, or ribosomal frameshifting. The information stored in this subsection is used to automatically construct alternative protein sequence(s) for display.</p><p><a href='../manual/var_seq' target='_top'>More...</a></p>Alternative sequencei	1379 – 1379	1	R → RIDFKKKHVGGIRSLRPTIT NNLFR in isoform 3. 2 Publications <p>Manually curated information that is based on statements in scientific articles for which there is no experimental support.</p> <p><a href="/manual/evidences#ECO:0000303">More…</a></p> Manual assertion based on opinion ini Ref.2 "The full-ORF clone resource of the German cDNA consortium." Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I. BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 932-1708 (ISOFORM 3), VARIANT PHE-837. Ref.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] (ISOFORMS 1 AND 3), VARIANT PHE-837.		VSP_052581

Sequence databases

Genome annotation databases

Polymorphism databases

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Coding sequence diversityⁱ

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesⁱ

Sequence databases

3D structure databases

Protein-protein interaction databases

Chemistry

PTM databases

Polymorphism databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Contains the literature citations that are the sources of data used to annotate the entry. Each reference is numbered and contains several subsections allowing a precise description of a given citation.</p><p><a href='../manual/publications_section' target='_top'>More...</a></p>Publicationsⁱ

1. "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] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH MTOR.
2. "The full-ORF clone resource of the German cDNA consortium."
   Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U., Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A., Wiemann S., Schupp I.
   BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 932-1708 (ISOFORM 3), VARIANT PHE-837.
   Tissue: Amygdala.
   
3. "The DNA sequence and comparative analysis of human chromosome 5."
   Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.

   , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
   Nature 431:268-274(2004) [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.

   , 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] (ISOFORMS 1 AND 3), VARIANT PHE-837.
   Tissue: Brain and LymphImported

   <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More…</a></p> Manual assertion inferred from database entriesⁱ

   • EMBL:AAH51729.1
   .
   
6. "Characterization of size-fractionated cDNA libraries generated by the in vitro recombination-assisted method."
   Ohara O., Nagase T., Mitsui G., Kohga H., Kikuno R., Hiraoka S., Takahashi Y., Kitajima S., Saga Y., Koseki H.
   DNA Res. 9:47-57(2002) [PubMed] [Europe PMC] [Abstract]
   Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 434-1708 (ISOFORM 1).
   Tissue: BrainImported

   <p>Manually validated information which has been imported from another database.</p> <p><a href="/manual/evidences#ECO:0000312">More…</a></p> Manual assertion inferred from database entriesⁱ

   • EMBL:BAC02708.1
   .
   
7. "Mammalian TOR complex 2 controls the actin cytoskeleton and is rapamycin insensitive."
   Jacinto E., Loewith R., Schmidt A., Lin S., Ruegg M.A., Hall A., Hall M.N.
   Nat. Cell Biol. 6:1122-1128(2004) [PubMed] [Europe PMC] [Abstract]
   Cited for: FUNCTION, IDENTIFICATION IN THE TORC2 COMPLEX, PHOSPHORYLATION.
8. "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] [Europe PMC] [Abstract]
   Cited for: FUNCTION.
9. "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] [Europe PMC] [Abstract]
   Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
   Tissue: Cervix carcinoma.
   
10. "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 PRR5 AND PRR5L.
11. "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: IDENTIFICATION IN THE TORC2 COMPLEX, INTERACTION WITH PRR5.
12. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
    
13. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
    
14. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1282; SER-1388 AND SER-1396, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
    
15. "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] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
16. "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] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-1284; SER-1388 AND SER-1411, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
    
17. "mTORC1-activated S6K1 phosphorylates Rictor on threonine 1135 and regulates mTORC2 signaling."
    Julien L.A., Carriere A., Moreau J., Roux P.P.
    Mol. Cell. Biol. 30:908-921(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT THR-1135.
18. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
    
19. "Initial characterization of the human central proteome."
    Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
    BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
20. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21 AND SER-1591, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
21. "The Bardet-Biedl syndrome-related protein CCDC28B modulates mTORC2 function and interacts with SIN1 to control cilia length independently of the mTOR complex."
    Cardenas-Rodriguez M., Irigoin F., Osborn D.P., Gascue C., Katsanis N., Beales P.L., Badano J.L.
    Hum. Mol. Genet. 22:4031-4042(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH CCDC28B.
22. "Interaction between NBS1 and the mTOR/Rictor/SIN1 complex through specific domains."
    Wang J.Q., Chen J.H., Chen Y.C., Chen M.Y., Hsieh C.Y., Teng S.C., Wu K.J.
    PLoS ONE 8:E65586-E65586(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH NBN.

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationⁱ

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousⁱ

<p>UniProtKB Keywords constitute a <a target="_top" href="/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='../help/keywords' target='_top'>More...</a></p>Keywords - Technical termⁱ

Documents

1. Human chromosome 5
   Human chromosome 5: entries, gene names and cross-references to MIM
2. Human entries with polymorphisms or disease mutations
   List of human entries with polymorphisms or disease mutations
3. Human polymorphisms and disease mutations
   Index of human polymorphisms and disease mutations
4. MIM cross-references
   Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
5. SIMILARITY comments
   Index of protein domains and families

External Data

<p>Provides links to the UniProt Reference Clusters (<a href="/help/uniref">UniRef</a>). UniRef consists of clusters for UniProtKB sequences (including isoforms) and selected UniParc sequences, in order to obtain complete coverage of the sequence space at resolutions of 100%, 90% and 50% identity.</p><p><a href='../manual/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsⁱ