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P49815

- TSC2_HUMAN

UniProt

P49815 - TSC2_HUMAN

Protein

Tuberin

Gene

TSC2

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 164 (01 Oct 2014)
      Sequence version 2 (24 Nov 2009)
      Previous versions | rss
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    Functioni

    In complex with TSC1, inhibits the nutrient-mediated or growth factor-stimulated phosphorylation of S6K1 and EIF4EBP1 by negatively regulating mTORC1 signaling. Acts as a GTPase-activating protein (GAP) for the small GTPase RHEB, a direct activator of the protein kinase activity of mTORC1. Implicated as a tumor suppressor. Involved in microtubule-mediated protein transport, but this seems to be due to unregulated mTOR signaling. Stimulates weakly the intrinsic GTPase activity of the Ras-related proteins RAP1A and RAB5 in vitro. Mutations in TSC2 lead to constitutive activation of RAP1A in tumors.3 Publications

    GO - Molecular functioni

    1. GTPase activator activity Source: UniProtKB
    2. phosphatase binding Source: UniProtKB
    3. protein binding Source: UniProtKB
    4. protein homodimerization activity Source: UniProtKB

    GO - Biological processi

    1. acute-phase response Source: Ensembl
    2. cell cycle arrest Source: Reactome
    3. cell projection organization Source: Ensembl
    4. endocytosis Source: ProtInc
    5. epidermal growth factor receptor signaling pathway Source: Reactome
    6. Fc-epsilon receptor signaling pathway Source: Reactome
    7. fibroblast growth factor receptor signaling pathway Source: Reactome
    8. heart development Source: UniProtKB
    9. innate immune response Source: Reactome
    10. insulin-like growth factor receptor signaling pathway Source: UniProtKB
    11. insulin receptor signaling pathway Source: Reactome
    12. negative regulation of cell proliferation Source: UniProtKB
    13. negative regulation of cell size Source: Ensembl
    14. negative regulation of epithelial cell proliferation Source: Ensembl
    15. negative regulation of insulin receptor signaling pathway Source: RefGenome
    16. negative regulation of MAP kinase activity Source: Ensembl
    17. negative regulation of phosphatidylinositol 3-kinase signaling Source: UniProtKB
    18. negative regulation of protein kinase activity Source: UniProtKB
    19. negative regulation of protein kinase B signaling Source: UniProtKB
    20. negative regulation of TOR signaling Source: RefGenome
    21. negative regulation of Wnt signaling pathway Source: RefGenome
    22. neural tube closure Source: UniProtKB
    23. neurotrophin TRK receptor signaling pathway Source: Reactome
    24. phosphatidylinositol 3-kinase signaling Source: Ensembl
    25. phosphatidylinositol-mediated signaling Source: Reactome
    26. positive chemotaxis Source: UniProtKB
    27. positive regulation of Ras GTPase activity Source: RefGenome
    28. protein heterooligomerization Source: Ensembl
    29. protein homooligomerization Source: Ensembl
    30. protein import into nucleus Source: UniProtKB
    31. protein kinase B signaling Source: UniProtKB
    32. protein localization Source: UniProtKB
    33. regulation of cell cycle Source: RefGenome
    34. regulation of endocytosis Source: UniProtKB
    35. regulation of insulin receptor signaling pathway Source: UniProtKB
    36. response to hypoxia Source: Ensembl
    37. vesicle-mediated transport Source: ProtInc

    Keywords - Molecular functioni

    GTPase activation

    Enzyme and pathway databases

    ReactomeiREACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21393. Regulation of Rheb GTPase activity by AMPK.
    REACT_6743. Inhibition of TSC complex formation by PKB.
    SignaLinkiP49815.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    Tuberin
    Alternative name(s):
    Tuberous sclerosis 2 protein
    Gene namesi
    Name:TSC2
    Synonyms:TSC4
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 16

    Organism-specific databases

    HGNCiHGNC:12363. TSC2.

    Subcellular locationi

    Cytoplasm. Membrane; Peripheral membrane protein
    Note: At steady state found in association with membranes.

    GO - Cellular componenti

    1. caveola Source: Ensembl
    2. cytoplasm Source: UniProtKB
    3. cytosol Source: UniProtKB
    4. dendrite Source: Ensembl
    5. Golgi apparatus Source: UniProtKB
    6. growth cone Source: Ensembl
    7. membrane Source: UniProtKB
    8. neuronal cell body Source: Ensembl
    9. nucleus Source: UniProtKB
    10. perinuclear region of cytoplasm Source: UniProtKB
    11. TSC1-TSC2 complex Source: UniProtKB

    Keywords - Cellular componenti

    Cytoplasm, Membrane

    Pathology & Biotechi

    Involvement in diseasei

    Tuberous sclerosis 2 (TSC2) [MIM:613254]: An autosomal dominant multi-system disorder that affects especially the brain, kidneys, heart, and skin. It is characterized by hamartomas (benign overgrowths predominantly of a cell or tissue type that occurs normally in the organ) and hamartias (developmental abnormalities of tissue combination). Clinical manifestations include epilepsy, learning difficulties, behavioral problems, and skin lesions. Seizures can be intractable and premature death can occur from a variety of disease-associated causes.13 Publications
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti137 – 1371H → R in TSC2; unknown pathological significance. 1 Publication
    Corresponds to variant rs45517107 [ dbSNP | Ensembl ].
    VAR_009415
    Natural varianti227 – 2271C → Y in TSC2.
    Corresponds to variant rs45517122 [ dbSNP | Ensembl ].
    VAR_008020
    Natural varianti258 – 2581K → N in TSC2.
    VAR_009417
    Natural varianti261 – 2611R → P in TSC2.
    Corresponds to variant rs45502703 [ dbSNP | Ensembl ].
    VAR_009418
    Natural varianti292 – 2921L → P in TSC2.
    Corresponds to variant rs45517138 [ dbSNP | Ensembl ].
    VAR_005646
    Natural varianti294 – 2941G → E in TSC2.
    Corresponds to variant rs45487497 [ dbSNP | Ensembl ].
    VAR_009422
    Natural varianti304 – 3041W → WGMALW in TSC2.
    VAR_009423
    Natural varianti320 – 3201L → F Could be associated with TSC2. 3 Publications
    Corresponds to variant rs1131825 [ dbSNP | Ensembl ].
    VAR_009425
    Natural varianti331 – 3311N → K in TSC2.
    Corresponds to variant rs45517153 [ dbSNP | Ensembl ].
    VAR_008021
    Natural varianti361 – 3611L → P in TSC2.
    Corresponds to variant rs45517147 [ dbSNP | Ensembl ].
    VAR_009426
    Natural varianti365 – 3651Missing in TSC2.
    VAR_009427
    Natural varianti407 – 4071Y → D in TSC2.
    VAR_005647
    Natural varianti449 – 4491M → I in TSC2. 1 Publication
    VAR_005648
    Natural varianti486 – 4861N → I in TSC2.
    VAR_008022
    Natural varianti525 – 5251N → S in TSC2.
    VAR_009432
    Natural varianti599 – 5991K → M in TSC2; impairs repression of EIF4EBP1 phosphorylation.
    VAR_009435
    Natural varianti611 – 6111R → Q in TSC2 and LAM; impairs phosphorylation at S-1387, S-1418 and S-1420; enhances ubiquitination by MYCBP2. 3 Publications
    VAR_005650
    Natural varianti611 – 6111R → W in TSC2; impairs phosphorylation at S-1387, S-1418 and S-1420. 3 Publications
    VAR_005651
    Natural varianti614 – 6141A → D in TSC2.
    VAR_009436
    Natural varianti647 – 6471D → N in TSC2; unknown pathological significance. 1 Publication
    VAR_009437
    Natural varianti694 – 6941Missing in TSC2.
    VAR_009438
    Natural varianti696 – 6961C → Y in TSC2.
    VAR_009439
    Natural varianti717 – 7171L → R in TSC2. 2 Publications
    VAR_009440
    Natural varianti769 – 7691V → E in TSC2; unknown pathological significance. 1 Publication
    VAR_009441
    Natural varianti816 – 8161P → L in TSC2.
    VAR_008026
    Natural varianti826 – 8261L → M in TSC2.
    VAR_005652
    Natural varianti895 – 8951M → V in TSC2.
    VAR_009442
    Natural varianti905 – 9051R → Q in TSC2.
    VAR_005653
    Natural varianti905 – 9051R → W in TSC2. 1 Publication
    VAR_005654
    Natural varianti963 – 9631V → M in TSC2; unknown pathological significance. 1 Publication
    VAR_009443
    Natural varianti1027 – 10271L → P in TSC2. 1 Publication
    VAR_022919
    Natural varianti1084 – 10841D → E in TSC2.
    VAR_005655
    Natural varianti1144 – 11441V → M in TSC2.
    VAR_008027
    Natural varianti1200 – 12001R → W in TSC2.
    VAR_005656
    Natural varianti1227 – 12271P → L in TSC2. 1 Publication
    VAR_005657
    Natural varianti1240 – 12401R → W in TSC2. 1 Publication
    VAR_005658
    Natural varianti1295 – 12951D → V in TSC2.
    VAR_005659
    Natural varianti1315 – 13151P → S in TSC2.
    VAR_008028
    Natural varianti1329 – 13291R → H in TSC2.
    Corresponds to variant rs45517323 [ dbSNP | Ensembl ].
    VAR_008029
    Natural varianti1497 – 14971P → R in TSC2.
    VAR_009445
    Natural varianti1498 – 14981S → N in TSC2.
    VAR_009446
    Natural varianti1509 – 15091Missing in TSC2; unknown pathological significance. 2 Publications
    VAR_005660
    Natural varianti1549 – 15491Y → C in TSC2.
    VAR_005661
    Natural varianti1594 – 15941L → M in TSC2; unknown pathological significance. 1 Publication
    VAR_009447
    Natural varianti1614 – 16141Missing in TSC2.
    VAR_005662
    Natural varianti1620 – 16201H → Y in TSC2.
    VAR_009448
    Natural varianti1643 – 16431N → I in TSC2.
    VAR_005663
    Natural varianti1643 – 16431N → K in TSC2; Abolishes GAP activity. 1 Publication
    VAR_009449
    Natural varianti1650 – 16501Y → C in TSC2.
    VAR_005664
    Natural varianti1651 – 16511N → S in TSC2; greatly reduces the ability to enhance the RHEB GTPase activity. 2 Publications
    VAR_009450
    Natural varianti1653 – 16531S → F in TSC2. 1 Publication
    VAR_018603
    Natural varianti1675 – 16751P → L in TSC2. 3 Publications
    VAR_009451
    Natural varianti1681 – 16811N → K in TSC2; Abolishes GAP activity. 1 Publication
    VAR_009452
    Natural varianti1690 – 16901D → Y in TSC2.
    VAR_005665
    Natural varianti1704 – 17041S → T in TSC2.
    VAR_009453
    Natural varianti1709 – 17091P → L in TSC2.
    VAR_008030
    Natural varianti1712 – 17121A → E in TSC2. 1 Publication
    VAR_005666
    Natural varianti1743 – 17431R → P in TSC2; Abolishes GAP activity.
    VAR_009454
    Natural varianti1743 – 17431R → Q in TSC2.
    VAR_008031
    Natural varianti1744 – 17441L → P in TSC2. 1 Publication
    VAR_009455
    Natural varianti1746 – 17516Missing in TSC2.
    VAR_009456
    Natural varianti1750 – 17501L → F in TSC2.
    VAR_005667
    Natural varianti1773 – 17731H → P in TSC2.
    VAR_008032
    Natural varianti1783 – 17831E → Q in TSC2.
    VAR_008033
    Lymphangioleiomyomatosis (LAM) [MIM:606690]: Progressive and often fatal lung disease characterized by a diffuse proliferation of abnormal smooth muscle cells in the lungs. It affects almost exclusively young women and can occur as an isolated disorder or in association with tuberous sclerosis complex.1 Publication
    Note: The disease is caused by mutations affecting the gene represented in this entry.
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti611 – 6111R → Q in TSC2 and LAM; impairs phosphorylation at S-1387, S-1418 and S-1420; enhances ubiquitination by MYCBP2. 3 Publications
    VAR_005650

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi939 – 9391S → A: Inhibits insulin-stimulated phosphorylation and activation of S6K1; when associated with A-1462.
    Mutagenesisi1330 – 13301T → A: Abolishes AMPK-mediated phosphorylation; when associated with A-1448. 1 Publication
    Mutagenesisi1448 – 14481S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-1330. 1 Publication
    Mutagenesisi1462 – 14621T → A: Inhibits insulin-stimulated phosphorylation and activation of S6K1; when associated with A-939.
    Mutagenesisi1637 – 16393KKR → QQQ: Abolishes GAP activity.
    Mutagenesisi1745 – 17451R → Q: Abolishes GAP activity. 1 Publication
    Mutagenesisi1749 – 17513RLR → QLQ: No effect.

    Keywords - Diseasei

    Disease mutation, Tumor suppressor

    Organism-specific databases

    MIMi606690. phenotype.
    613254. phenotype.
    Orphaneti88924. Autosomal dominant polycystic kidney disease type 1 with tuberous sclerosis.
    538. Lymphangioleiomyomatosis.
    805. Tuberous sclerosis.
    PharmGKBiPA37035.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 18071807TuberinPRO_0000065654Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei540 – 5401Phosphoserine2 Publications
    Modified residuei664 – 6641Phosphoserine2 Publications
    Modified residuei927 – 9271Phosphothreonine2 Publications
    Modified residuei939 – 9391Phosphoserine; by PKB/AKT13 Publications
    Modified residuei981 – 9811Phosphoserine2 Publications
    Modified residuei1132 – 11321Phosphoserine3 Publications
    Modified residuei1155 – 11551Phosphoserine3 Publications
    Modified residuei1330 – 13301Phosphothreonine; by AMPK2 Publications
    Modified residuei1337 – 13371Phosphoserine2 Publications
    Modified residuei1338 – 13381Phosphoserine2 Publications
    Modified residuei1346 – 13461Phosphoserine2 Publications
    Modified residuei1387 – 13871Phosphoserine3 Publications
    Modified residuei1411 – 14111Phosphoserine2 Publications
    Modified residuei1418 – 14181Phosphoserine2 Publications
    Modified residuei1420 – 14201Phosphoserine3 Publications
    Modified residuei1448 – 14481Phosphoserine; by AMPK2 Publications
    Modified residuei1452 – 14521Phosphoserine2 Publications
    Modified residuei1462 – 14621Phosphothreonine; by PKB/AKT14 Publications
    Modified residuei1798 – 17981Phosphoserine; by RPS6KA15 Publications

    Post-translational modificationi

    Phosphorylation at Ser-1387, Ser-1418 or Ser-1420 does not affect interaction with TSC1. Phosphorylation at Ser-939 and Thr-1462 by PKB/AKT1 is induced by growth factor stimulation. Phosphorylation by AMPK activates it and leads to negatively regulates the mTORC1 complex. Phosphorylated at Ser-1798 by RPS6KA1; phosphorylation inhibits TSC2 ability to suppress mTORC1 signaling. Phosphorylated by DAPK1.7 Publications
    Ubiquitinated by the DCX(FBXW5) E3 ubiquitin-protein ligase complex, leading to its subsequent degradation. Ubiquitinated by MYCBP2 inependently of its phosphorylation status leading to subsequent degradation; association with TSC1 protects from ubiquitination.2 Publications

    Keywords - PTMi

    Phosphoprotein, Ubl conjugation

    Proteomic databases

    MaxQBiP49815.
    PaxDbiP49815.
    PRIDEiP49815.

    PTM databases

    PhosphoSiteiP49815.

    Expressioni

    Tissue specificityi

    Liver, brain, heart, lymphocytes, fibroblasts, biliary epithelium, pancreas, skeletal muscle, kidney, lung and placenta.

    Gene expression databases

    ArrayExpressiP49815.
    BgeeiP49815.
    CleanExiHS_TSC2.
    GenevestigatoriP49815.

    Organism-specific databases

    HPAiCAB002225.
    HPA030409.
    HPA049679.

    Interactioni

    Subunit structurei

    Interacts with TSC1 and HERC1; the interaction with TSC1 stabilizes TSC2 and prevents the interaction with HERC1. May also interact with the adapter molecule RABEP1. The final complex contains TSC2 and RABEP1 linked to RAB5 Probable. Interacts with HSPA1 and HSPA8. Interacts with DAPK1 and FBXW5. Interacts with NAA10 (via C-terminal domain).8 PublicationsCurated

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    PPP1CAP621362EBI-396587,EBI-357253
    SIRT1Q96EB62EBI-396587,EBI-1802965
    TSC1Q9257410EBI-396587,EBI-1047085
    YWHABP319464EBI-396587,EBI-359815
    YWHAZP631047EBI-396587,EBI-347088

    Protein-protein interaction databases

    BioGridi113100. 42 interactions.
    IntActiP49815. 13 interactions.
    MINTiMINT-250244.
    STRINGi9606.ENSP00000219476.

    Structurei

    3D structure databases

    ProteinModelPortaliP49815.
    SMRiP49815. Positions 1517-1691.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1531 – 1758228Rap-GAPPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni1 – 400400Required for interaction with TSC1Add
    BLAST

    Sequence similaritiesi

    Contains 1 Rap-GAP domain.PROSITE-ProRule annotation

    Phylogenomic databases

    eggNOGiNOG290929.
    HOVERGENiHBG018005.
    InParanoidiP49815.
    KOiK07207.
    OMAiHRSISWA.
    OrthoDBiEOG7KM5S3.
    PhylomeDBiP49815.
    TreeFamiTF324484.

    Family and domain databases

    Gene3Di1.25.10.10. 3 hits.
    InterProiIPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000331. Rap_GAP_dom.
    IPR003913. Tuberin.
    IPR018515. Tuberin-type_domain.
    IPR024584. Tuberin_N.
    [Graphical view]
    PANTHERiPTHR10063:SF1. PTHR10063:SF1. 1 hit.
    PfamiPF11864. DUF3384. 1 hit.
    PF02145. Rap_GAP. 1 hit.
    PF03542. Tuberin. 1 hit.
    [Graphical view]
    PRINTSiPR01431. TUBERIN.
    SUPFAMiSSF48371. SSF48371. 1 hit.
    PROSITEiPS50085. RAPGAP. 1 hit.
    [Graphical view]

    Sequences (8)i

    Sequence statusi: Complete.

    This entry describes 8 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: P49815-1) [UniParc]FASTAAdd to Basket

    This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

    « Hide

    MAKPTSKDSG LKEKFKILLG LGTPRPNPRS AEGKQTEFII TAEILRELSM     50
    ECGLNNRIRM IGQICEVAKT KKFEEHAVEA LWKAVADLLQ PERPLEARHA 100
    VLALLKAIVQ GQGERLGVLR ALFFKVIKDY PSNEDLHERL EVFKALTDNG 150
    RHITYLEEEL ADFVLQWMDV GLSSEFLLVL VNLVKFNSCY LDEYIARMVQ 200
    MICLLCVRTA SSVDIEVSLQ VLDAVVCYNC LPAESLPLFI VTLCRTINVK 250
    ELCEPCWKLM RNLLGTHLGH SAIYNMCHLM EDRAYMEDAP LLRGAVFFVG 300
    MALWGAHRLY SLRNSPTSVL PSFYQAMACP NEVVSYEIVL SITRLIKKYR 350
    KELQVVAWDI LLNIIERLLQ QLQTLDSPEL RTIVHDLLTT VEELCDQNEF 400
    HGSQERYFEL VERCADQRPE SSLLNLISYR AQSIHPAKDG WIQNLQALME 450
    RFFRSESRGA VRIKVLDVLS FVLLINRQFY EEELINSVVI SQLSHIPEDK 500
    DHQVRKLATQ LLVDLAEGCH THHFNSLLDI IEKVMARSLS PPPELEERDV 550
    AAYSASLEDV KTAVLGLLVI LQTKLYTLPA SHATRVYEML VSHIQLHYKH 600
    SYTLPIASSI RLQAFDFLLL LRADSLHRLG LPNKDGVVRF SPYCVCDYME 650
    PERGSEKKTS GPLSPPTGPP GPAPAGPAVR LGSVPYSLLF RVLLQCLKQE 700
    SDWKVLKLVL GRLPESLRYK VLIFTSPCSV DQLCSALCSM LSGPKTLERL 750
    RGAPEGFSRT DLHLAVVPVL TALISYHNYL DKTKQREMVY CLEQGLIHRC 800
    ASQCVVALSI CSVEMPDIII KALPVLVVKL THISATASMA VPLLEFLSTL 850
    ARLPHLYRNF AAEQYASVFA ISLPYTNPSK FNQYIVCLAH HVIAMWFIRC 900
    RLPFRKDFVP FITKGLRSNV LLSFDDTPEK DSFRARSTSL NERPKSLRIA 950
    RPPKQGLNNS PPVKEFKESS AAEAFRCRSI SVSEHVVRSR IQTSLTSASL 1000
    GSADENSVAQ ADDSLKNLHL ELTETCLDMM ARYVFSNFTA VPKRSPVGEF 1050
    LLAGGRTKTW LVGNKLVTVT TSVGTGTRSL LGLDSGELQS GPESSSSPGV 1100
    HVRQTKEAPA KLESQAGQQV SRGARDRVRS MSGGHGLRVG ALDVPASQFL 1150
    GSATSPGPRT APAAKPEKAS AGTRVPVQEK TNLAAYVPLL TQGWAEILVR 1200
    RPTGNTSWLM SLENPLSPFS SDINNMPLQE LSNALMAAER FKEHRDTALY 1250
    KSLSVPAAST AKPPPLPRSN TVASFSSLYQ SSCQGQLHRS VSWADSAVVM 1300
    EEGSPGEVPV LVEPPGLEDV EAALGMDRRT DAYSRSSSVS SQEEKSLHAE 1350
    ELVGRGIPIE RVVSSEGGRP SVDLSFQPSQ PLSKSSSSPE LQTLQDILGD 1400
    PGDKADVGRL SPEVKARSQS GTLDGESAAW SASGEDSRGQ PEGPLPSSSP 1450
    RSPSGLRPRG YTISDSAPSR RGKRVERDAL KSRATASNAE KVPGINPSFV 1500
    FLQLYHSPFF GDESNKPILL PNESQSFERS VQLLDQIPSY DTHKIAVLYV 1550
    GEGQSNSELA ILSNEHGSYR YTEFLTGLGR LIELKDCQPD KVYLGGLDVC 1600
    GEDGQFTYCW HDDIMQAVFH IATLMPTKDV DKHRCDKKRH LGNDFVSIVY 1650
    NDSGEDFKLG TIKGQFNFVH VIVTPLDYEC NLVSLQCRKD MEGLVDTSVA 1700
    KIVSDRNLPF VARQMALHAN MASQVHHSRS NPTDIYPSKW IARLRHIKRL 1750
    RQRICEEAAY SNPSLPLVHP PSHSKAPAQT PAEPTPGYEV GQRKRLISSV 1800
    EDFTEFV 1807
    Length:1,807
    Mass (Da):200,608
    Last modified:November 24, 2009 - v2
    Checksum:i7B915C46970D7D31
    GO
    Isoform 2 (identifier: P49815-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         946-988: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,764
    Mass (Da):195,847
    Checksum:iEECB8D3132AFFBA2
    GO
    Isoform 3 (identifier: P49815-3) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         946-989: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,763
    Mass (Da):195,760
    Checksum:i9EBB34789D67D71C
    GO
    Isoform 4 (identifier: P49815-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1272-1294: Missing.

    Show »
    Length:1,784
    Mass (Da):198,097
    Checksum:i36A09DD2BBCD369A
    GO
    Isoform 5 (identifier: P49815-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         946-989: Missing.
         1272-1294: Missing.

    Show »
    Length:1,740
    Mass (Da):193,249
    Checksum:iA0886EF0FBE7652E
    GO
    Isoform 6 (identifier: P49815-6) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         76-112: Missing.
         946-988: Missing.
         1272-1294: Missing.

    Show »
    Length:1,704
    Mass (Da):189,298
    Checksum:iAD89389C5CDB4B2C
    GO
    Isoform 7 (identifier: P49815-7) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1-49: Missing.
         946-988: Missing.
         1272-1294: Missing.

    Note: No experimental confirmation available.

    Show »
    Length:1,692
    Mass (Da):187,956
    Checksum:i2EBACFD19189839B
    GO
    Isoform 8 (identifier: P49815-8) [UniParc]FASTAAdd to Basket

    Also known as: H, I

    The sequence of this isoform differs from the canonical sequence as follows:
         113-239: GERLGVLRAL...CLPAESLPLF → VRPRATLGWV...SLHSICAGLG
         240-1807: Missing.

    Show »
    Length:239
    Mass (Da):25,773
    Checksum:i66E9726DB8FC2B57
    GO

    Sequence cautioni

    The sequence BAE06082.1 differs from that shown. Reason: Erroneous initiation.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti187 – 1871N → S in BAG61344. 1 PublicationCurated
    Sequence conflicti210 – 2101A → V in AAI50301. (PubMed:15489334)Curated
    Sequence conflicti335 – 3351S → P in BAG61344. 1 PublicationCurated
    Sequence conflicti392 – 3921E → V in BAG58569. 1 PublicationCurated
    Sequence conflicti422 – 4221S → P in BAG58569. 1 PublicationCurated
    Sequence conflicti660 – 6601S → N in BAG61344. 1 PublicationCurated
    Sequence conflicti704 – 7041K → E in AAI50301. (PubMed:15489334)Curated
    Sequence conflicti706 – 7061L → P in BAG58569. 1 PublicationCurated
    Sequence conflicti1015 – 10151L → M in AAI50301. (PubMed:15489334)Curated
    Sequence conflicti1239 – 12391E → V in BAG61344. 1 PublicationCurated
    Sequence conflicti1398 – 13981L → V in BAG61344. 1 PublicationCurated
    Sequence conflicti1672 – 16721I → M in AAI50301. (PubMed:15489334)Curated
    Sequence conflicti1807 – 18071V → A in BAG61344. 1 PublicationCurated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti94 – 941P → T.1 Publication
    Corresponds to variant rs1051616 [ dbSNP | Ensembl ].
    VAR_008019
    Natural varianti137 – 1371H → R in TSC2; unknown pathological significance. 1 Publication
    Corresponds to variant rs45517107 [ dbSNP | Ensembl ].
    VAR_009415
    Natural varianti160 – 1601L → V.
    Corresponds to variant rs45517109 [ dbSNP | Ensembl ].
    VAR_009416
    Natural varianti227 – 2271C → Y in TSC2.
    Corresponds to variant rs45517122 [ dbSNP | Ensembl ].
    VAR_008020
    Natural varianti258 – 2581K → N in TSC2.
    VAR_009417
    Natural varianti261 – 2611R → P in TSC2.
    Corresponds to variant rs45502703 [ dbSNP | Ensembl ].
    VAR_009418
    Natural varianti261 – 2611R → W.
    Corresponds to variant rs45517130 [ dbSNP | Ensembl ].
    VAR_009419
    Natural varianti286 – 2861M → T.
    Corresponds to variant rs45517136 [ dbSNP | Ensembl ].
    VAR_009420
    Natural varianti286 – 2861M → V.
    Corresponds to variant rs1800748 [ dbSNP | Ensembl ].
    VAR_009421
    Natural varianti292 – 2921L → P in TSC2.
    Corresponds to variant rs45517138 [ dbSNP | Ensembl ].
    VAR_005646
    Natural varianti294 – 2941G → E in TSC2.
    Corresponds to variant rs45487497 [ dbSNP | Ensembl ].
    VAR_009422
    Natural varianti304 – 3041W → WGMALW in TSC2.
    VAR_009423
    Natural varianti309 – 3091L → Q.
    VAR_009424
    Natural varianti320 – 3201L → F Could be associated with TSC2. 3 Publications
    Corresponds to variant rs1131825 [ dbSNP | Ensembl ].
    VAR_009425
    Natural varianti331 – 3311N → K in TSC2.
    Corresponds to variant rs45517153 [ dbSNP | Ensembl ].
    VAR_008021
    Natural varianti361 – 3611L → P in TSC2.
    Corresponds to variant rs45517147 [ dbSNP | Ensembl ].
    VAR_009426
    Natural varianti365 – 3651Missing in TSC2.
    VAR_009427
    Natural varianti367 – 3671R → Q.1 Publication
    Corresponds to variant rs1800725 [ dbSNP | Ensembl ].
    VAR_009428
    Natural varianti378 – 3781P → L.
    Corresponds to variant rs45517154 [ dbSNP | Ensembl ].
    VAR_009429
    Natural varianti407 – 4071Y → D in TSC2.
    VAR_005647
    Natural varianti440 – 4401G → S.
    Corresponds to variant rs45484298 [ dbSNP | Ensembl ].
    VAR_009430
    Natural varianti449 – 4491M → I in TSC2. 1 Publication
    VAR_005648
    Natural varianti463 – 4631I → V.
    VAR_009431
    Natural varianti486 – 4861N → I in TSC2.
    VAR_008022
    Natural varianti490 – 4901I → V.
    VAR_008023
    Natural varianti525 – 5251N → S in TSC2.
    VAR_009432
    Natural varianti536 – 5361A → V.
    VAR_008024
    Natural varianti583 – 5831A → T.
    Corresponds to variant rs1800729 [ dbSNP | Ensembl ].
    VAR_009433
    Natural varianti593 – 5931H → R.
    VAR_009434
    Natural varianti599 – 5991K → M in TSC2; impairs repression of EIF4EBP1 phosphorylation.
    VAR_009435
    Natural varianti607 – 6071A → T.1 Publication
    VAR_005649
    Natural varianti611 – 6111R → Q in TSC2 and LAM; impairs phosphorylation at S-1387, S-1418 and S-1420; enhances ubiquitination by MYCBP2. 3 Publications
    VAR_005650
    Natural varianti611 – 6111R → W in TSC2; impairs phosphorylation at S-1387, S-1418 and S-1420. 3 Publications
    VAR_005651
    Natural varianti614 – 6141A → D in TSC2.
    VAR_009436
    Natural varianti615 – 6151F → S.
    VAR_008025
    Natural varianti619 – 6191L → F.1 Publication
    Corresponds to variant rs1131826 [ dbSNP | Ensembl ].
    VAR_060584
    Natural varianti647 – 6471D → N in TSC2; unknown pathological significance. 1 Publication
    VAR_009437
    Natural varianti694 – 6941Missing in TSC2.
    VAR_009438
    Natural varianti696 – 6961C → Y in TSC2.
    VAR_009439
    Natural varianti717 – 7171L → R in TSC2. 2 Publications
    VAR_009440
    Natural varianti769 – 7691V → E in TSC2; unknown pathological significance. 1 Publication
    VAR_009441
    Natural varianti802 – 8021S → R.2 Publications
    Corresponds to variant rs1051621 [ dbSNP | Ensembl ].
    VAR_060585
    Natural varianti816 – 8161P → L in TSC2.
    VAR_008026
    Natural varianti826 – 8261L → M in TSC2.
    VAR_005652
    Natural varianti862 – 8621A → V.1 Publication
    VAR_018600
    Natural varianti895 – 8951M → V in TSC2.
    VAR_009442
    Natural varianti905 – 9051R → Q in TSC2.
    VAR_005653
    Natural varianti905 – 9051R → W in TSC2. 1 Publication
    VAR_005654
    Natural varianti963 – 9631V → M in TSC2; unknown pathological significance. 1 Publication
    VAR_009443
    Natural varianti1027 – 10271L → P in TSC2. 1 Publication
    VAR_022919
    Natural varianti1084 – 10841D → E in TSC2.
    VAR_005655
    Natural varianti1141 – 11411A → V.
    Corresponds to variant rs34870424 [ dbSNP | Ensembl ].
    VAR_057014
    Natural varianti1144 – 11441V → M in TSC2.
    VAR_008027
    Natural varianti1200 – 12001R → W in TSC2.
    VAR_005656
    Natural varianti1227 – 12271P → L in TSC2. 1 Publication
    VAR_005657
    Natural varianti1240 – 12401R → W in TSC2. 1 Publication
    VAR_005658
    Natural varianti1282 – 12821S → G.
    VAR_009444
    Natural varianti1295 – 12951D → V in TSC2.
    VAR_005659
    Natural varianti1315 – 13151P → S in TSC2.
    VAR_008028
    Natural varianti1329 – 13291R → H in TSC2.
    Corresponds to variant rs45517323 [ dbSNP | Ensembl ].
    VAR_008029
    Natural varianti1341 – 13411S → R.1 Publication
    VAR_022920
    Natural varianti1429 – 14291A → S.1 Publication
    Corresponds to variant rs45474795 [ dbSNP | Ensembl ].
    VAR_018601
    Natural varianti1450 – 14501P → R.1 Publication
    VAR_018602
    Natural varianti1497 – 14971P → R in TSC2.
    VAR_009445
    Natural varianti1498 – 14981S → N in TSC2.
    VAR_009446
    Natural varianti1509 – 15091Missing in TSC2; unknown pathological significance. 2 Publications
    VAR_005660
    Natural varianti1549 – 15491Y → C in TSC2.
    VAR_005661
    Natural varianti1594 – 15941L → M in TSC2; unknown pathological significance. 1 Publication
    VAR_009447
    Natural varianti1614 – 16141Missing in TSC2.
    VAR_005662
    Natural varianti1620 – 16201H → Y in TSC2.
    VAR_009448
    Natural varianti1636 – 16361D → N.1 Publication
    VAR_022921
    Natural varianti1643 – 16431N → I in TSC2.
    VAR_005663
    Natural varianti1643 – 16431N → K in TSC2; Abolishes GAP activity. 1 Publication
    VAR_009449
    Natural varianti1650 – 16501Y → C in TSC2.
    VAR_005664
    Natural varianti1651 – 16511N → S in TSC2; greatly reduces the ability to enhance the RHEB GTPase activity. 2 Publications
    VAR_009450
    Natural varianti1653 – 16531S → F in TSC2. 1 Publication
    VAR_018603
    Natural varianti1673 – 16731V → L.1 Publication
    VAR_022922
    Natural varianti1675 – 16751P → L in TSC2. 3 Publications
    VAR_009451
    Natural varianti1681 – 16811N → K in TSC2; Abolishes GAP activity. 1 Publication
    VAR_009452
    Natural varianti1690 – 16901D → Y in TSC2.
    VAR_005665
    Natural varianti1704 – 17041S → T in TSC2.
    VAR_009453
    Natural varianti1709 – 17091P → L in TSC2.
    VAR_008030
    Natural varianti1712 – 17121A → E in TSC2. 1 Publication
    VAR_005666
    Natural varianti1743 – 17431R → P in TSC2; Abolishes GAP activity.
    VAR_009454
    Natural varianti1743 – 17431R → Q in TSC2.
    VAR_008031
    Natural varianti1744 – 17441L → P in TSC2. 1 Publication
    VAR_009455
    Natural varianti1746 – 17516Missing in TSC2.
    VAR_009456
    Natural varianti1750 – 17501L → F in TSC2.
    VAR_005667
    Natural varianti1773 – 17731H → P in TSC2.
    VAR_008032
    Natural varianti1774 – 17741S → T.
    Corresponds to variant rs9209 [ dbSNP | Ensembl ].
    VAR_057015
    Natural varianti1783 – 17831E → Q in TSC2.
    VAR_008033
    Natural varianti1787 – 17871G → S.
    Corresponds to variant rs45517419 [ dbSNP | Ensembl ].
    VAR_009457
    Natural varianti1791 – 17911G → S.
    VAR_009458

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei1 – 4949Missing in isoform 7. 1 PublicationVSP_054163Add
    BLAST
    Alternative sequencei76 – 11237Missing in isoform 6. 1 PublicationVSP_038355Add
    BLAST
    Alternative sequencei113 – 239127GERLG…SLPLF → VRPRATLGWVTSGCPLTVLS LLGRVWTPASVSCWAQGLGA DGLWSWMACGVSWCHEVCVT VGTASSPVNRWSLHLPLMGC SGDHMRQFSQSAEIVPGSWC GATVLFCPCTLSGPLPCSLH SICAGLG in isoform 8. 2 PublicationsVSP_055896Add
    BLAST
    Alternative sequencei240 – 18071568Missing in isoform 8. 2 PublicationsVSP_055897Add
    BLAST
    Alternative sequencei946 – 98944Missing in isoform 3 and isoform 5. 2 PublicationsVSP_004471Add
    BLAST
    Alternative sequencei946 – 98843Missing in isoform 2, isoform 6 and isoform 7. 1 PublicationVSP_004470Add
    BLAST
    Alternative sequencei1272 – 129423Missing in isoform 4, isoform 5, isoform 6 and isoform 7. 3 PublicationsVSP_004472Add
    BLAST

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75621 mRNA. Translation: CAA53287.1.
    L48546
    , L48517, L48518, L48519, L48521, L48522, L48523, L48524, L48525, L48526, L48527, L48528, L48529, L48530, L48531, L48532, L48533, L48534, L48535, L48536, L48537, L48538, L48539, L48540, L48541, L48542, L48543, L48544, L48545 Genomic DNA. Translation: AAB41564.1.
    KJ535038 mRNA. Translation: AHW56677.1.
    KJ535051 mRNA. Translation: AHW56690.1.
    AK294548 mRNA. Translation: BAH11804.1.
    AK295672 mRNA. Translation: BAG58530.1.
    AK295728 mRNA. Translation: BAG58569.1.
    AK299343 mRNA. Translation: BAG61344.1.
    AB210000 mRNA. Translation: BAE06082.1. Different initiation.
    AC005600 Genomic DNA. Translation: AAC34210.1.
    AC093513 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85556.1.
    BC150300 mRNA. Translation: AAI50301.1.
    BC025364 mRNA. Translation: AAH25364.1.
    BC046929 mRNA. Translation: AAH46929.1.
    AB014460 Genomic DNA. Translation: BAA32694.1.
    CCDSiCCDS10458.1. [P49815-1]
    CCDS45384.1. [P49815-4]
    CCDS58408.1. [P49815-5]
    PIRiA49420.
    RefSeqiNP_000539.2. NM_000548.3. [P49815-1]
    NP_001070651.1. NM_001077183.1. [P49815-5]
    NP_001107854.1. NM_001114382.1. [P49815-4]
    UniGeneiHs.90303.

    Genome annotation databases

    EnsembliENST00000219476; ENSP00000219476; ENSG00000103197. [P49815-1]
    ENST00000350773; ENSP00000344383; ENSG00000103197. [P49815-4]
    ENST00000382538; ENSP00000371978; ENSG00000103197. [P49815-7]
    ENST00000401874; ENSP00000384468; ENSG00000103197. [P49815-5]
    ENST00000439673; ENSP00000399232; ENSG00000103197. [P49815-6]
    GeneIDi7249.
    KEGGihsa:7249.
    UCSCiuc002con.3. human. [P49815-1]
    uc002coo.3. human. [P49815-5]
    uc002cop.3. human. [P49815-3]
    uc010bsd.3. human. [P49815-4]
    uc010uvv.2. human. [P49815-6]

    Polymorphism databases

    DMDMi269849475.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Web resourcesi

    Atlas of Genetics and Cytogenetics in Oncology and Haematology
    Tuberous sclerosis database Tuberous sclerosis 2 (TSC2)

    Leiden Open Variation Database (LOVD)

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    X75621 mRNA. Translation: CAA53287.1 .
    L48546
    , L48517 , L48518 , L48519 , L48521 , L48522 , L48523 , L48524 , L48525 , L48526 , L48527 , L48528 , L48529 , L48530 , L48531 , L48532 , L48533 , L48534 , L48535 , L48536 , L48537 , L48538 , L48539 , L48540 , L48541 , L48542 , L48543 , L48544 , L48545 Genomic DNA. Translation: AAB41564.1 .
    KJ535038 mRNA. Translation: AHW56677.1 .
    KJ535051 mRNA. Translation: AHW56690.1 .
    AK294548 mRNA. Translation: BAH11804.1 .
    AK295672 mRNA. Translation: BAG58530.1 .
    AK295728 mRNA. Translation: BAG58569.1 .
    AK299343 mRNA. Translation: BAG61344.1 .
    AB210000 mRNA. Translation: BAE06082.1 . Different initiation.
    AC005600 Genomic DNA. Translation: AAC34210.1 .
    AC093513 Genomic DNA. No translation available.
    CH471112 Genomic DNA. Translation: EAW85556.1 .
    BC150300 mRNA. Translation: AAI50301.1 .
    BC025364 mRNA. Translation: AAH25364.1 .
    BC046929 mRNA. Translation: AAH46929.1 .
    AB014460 Genomic DNA. Translation: BAA32694.1 .
    CCDSi CCDS10458.1. [P49815-1 ]
    CCDS45384.1. [P49815-4 ]
    CCDS58408.1. [P49815-5 ]
    PIRi A49420.
    RefSeqi NP_000539.2. NM_000548.3. [P49815-1 ]
    NP_001070651.1. NM_001077183.1. [P49815-5 ]
    NP_001107854.1. NM_001114382.1. [P49815-4 ]
    UniGenei Hs.90303.

    3D structure databases

    ProteinModelPortali P49815.
    SMRi P49815. Positions 1517-1691.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 113100. 42 interactions.
    IntActi P49815. 13 interactions.
    MINTi MINT-250244.
    STRINGi 9606.ENSP00000219476.

    PTM databases

    PhosphoSitei P49815.

    Polymorphism databases

    DMDMi 269849475.

    Proteomic databases

    MaxQBi P49815.
    PaxDbi P49815.
    PRIDEi P49815.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000219476 ; ENSP00000219476 ; ENSG00000103197 . [P49815-1 ]
    ENST00000350773 ; ENSP00000344383 ; ENSG00000103197 . [P49815-4 ]
    ENST00000382538 ; ENSP00000371978 ; ENSG00000103197 . [P49815-7 ]
    ENST00000401874 ; ENSP00000384468 ; ENSG00000103197 . [P49815-5 ]
    ENST00000439673 ; ENSP00000399232 ; ENSG00000103197 . [P49815-6 ]
    GeneIDi 7249.
    KEGGi hsa:7249.
    UCSCi uc002con.3. human. [P49815-1 ]
    uc002coo.3. human. [P49815-5 ]
    uc002cop.3. human. [P49815-3 ]
    uc010bsd.3. human. [P49815-4 ]
    uc010uvv.2. human. [P49815-6 ]

    Organism-specific databases

    CTDi 7249.
    GeneCardsi GC16P002097.
    GeneReviewsi TSC2.
    HGNCi HGNC:12363. TSC2.
    HPAi CAB002225.
    HPA030409.
    HPA049679.
    MIMi 191092. gene.
    606690. phenotype.
    613254. phenotype.
    neXtProti NX_P49815.
    Orphaneti 88924. Autosomal dominant polycystic kidney disease type 1 with tuberous sclerosis.
    538. Lymphangioleiomyomatosis.
    805. Tuberous sclerosis.
    PharmGKBi PA37035.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi NOG290929.
    HOVERGENi HBG018005.
    InParanoidi P49815.
    KOi K07207.
    OMAi HRSISWA.
    OrthoDBi EOG7KM5S3.
    PhylomeDBi P49815.
    TreeFami TF324484.

    Enzyme and pathway databases

    Reactomei REACT_12564. AKT phosphorylates targets in the cytosol.
    REACT_147727. Constitutive PI3K/AKT Signaling in Cancer.
    REACT_21393. Regulation of Rheb GTPase activity by AMPK.
    REACT_6743. Inhibition of TSC complex formation by PKB.
    SignaLinki P49815.

    Miscellaneous databases

    GeneWikii TSC2.
    GenomeRNAii 7249.
    NextBioi 28347.
    PROi P49815.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P49815.
    Bgeei P49815.
    CleanExi HS_TSC2.
    Genevestigatori P49815.

    Family and domain databases

    Gene3Di 1.25.10.10. 3 hits.
    InterProi IPR011989. ARM-like.
    IPR016024. ARM-type_fold.
    IPR000331. Rap_GAP_dom.
    IPR003913. Tuberin.
    IPR018515. Tuberin-type_domain.
    IPR024584. Tuberin_N.
    [Graphical view ]
    PANTHERi PTHR10063:SF1. PTHR10063:SF1. 1 hit.
    Pfami PF11864. DUF3384. 1 hit.
    PF02145. Rap_GAP. 1 hit.
    PF03542. Tuberin. 1 hit.
    [Graphical view ]
    PRINTSi PR01431. TUBERIN.
    SUPFAMi SSF48371. SSF48371. 1 hit.
    PROSITEi PS50085. RAPGAP. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT ARG-802.
      Tissue: Brain.
    2. Sampson J.R.
      Submitted (DEC-1998) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Alternative splicing of the tuberous sclerosis 2 (TSC2) gene in human and mouse tissues."
      Xu L., Sterner C., Maheshwar M.M., Wilson P.J., Nellist M., Short M.P., Haines J.L., Sampson J.R., Ramesh V.
      Genomics 27:475-480(1995) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], ALTERNATIVE SPLICING (ISOFORMS 1; 2 AND 3).
    4. "Comparative analysis and genomic structure of the tuberous sclerosis 2 (TSC2) gene in human and pufferfish."
      Maheshwar M.M., Sandford R., Nellist M., Cheadle J.P., Sgotto B., Vaudin M., Sampson J.R.
      Hum. Mol. Genet. 5:131-137(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-94; PHE-320; PHE-619 AND ARG-802.
    5. "Protein interaction network of alternatively spliced isoforms from brain links genetic risk factors for autism."
      Corominas R., Yang X., Lin G.N., Kang S., Shen Y., Ghamsari L., Broly M., Rodriguez M., Tam S., Wanamaker S.A., Fan C., Yi S., Tasan M., Lemmens I., Kuang X., Zhao N., Malhotra D., Michaelson J.J.
      , Vacic V., Calderwood M.A., Roth F.P., Tavernier J., Horvath S., Salehi-Ashtiani K., Korkin D., Sebat J., Hill D.E., Hao T., Vidal M., Iakoucheva L.M.
      Nat. Commun. 5:3650-3650(2014) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 8).
      Tissue: Brain.
    6. "Complete sequencing and characterization of 21,243 full-length human cDNAs."
      Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.
      , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
      Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5; 6; 7 AND 8).
      Tissue: Amygdala and Hippocampus.
    7. Nakajima D., Saito K., Yamakawa H., Kikuno R.F., Nakayama M., Ohara R., Okazaki N., Koga H., Nagase T., Ohara O.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
      Tissue: Aortic endothelium.
    8. "The sequence and analysis of duplication-rich human chromosome 16."
      Martin J., Han C., Gordon L.A., Terry A., Prabhakar S., She X., Xie G., Hellsten U., Chan Y.M., Altherr M., Couronne O., Aerts A., Bajorek E., Black S., Blumer H., Branscomb E., Brown N.C., Bruno W.J.
      , Buckingham J.M., Callen D.F., Campbell C.S., Campbell M.L., Campbell E.W., Caoile C., Challacombe J.F., Chasteen L.A., Chertkov O., Chi H.C., Christensen M., Clark L.M., Cohn J.D., Denys M., Detter J.C., Dickson M., Dimitrijevic-Bussod M., Escobar J., Fawcett J.J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Goodwin L.A., Grady D.L., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Hildebrand C.E., Huang W., Israni S., Jett J., Jewett P.B., Kadner K., Kimball H., Kobayashi A., Krawczyk M.-C., Leyba T., Longmire J.L., Lopez F., Lou Y., Lowry S., Ludeman T., Manohar C.F., Mark G.A., McMurray K.L., Meincke L.J., Morgan J., Moyzis R.K., Mundt M.O., Munk A.C., Nandkeshwar R.D., Pitluck S., Pollard M., Predki P., Parson-Quintana B., Ramirez L., Rash S., Retterer J., Ricke D.O., Robinson D.L., Rodriguez A., Salamov A., Saunders E.H., Scott D., Shough T., Stallings R.L., Stalvey M., Sutherland R.D., Tapia R., Tesmer J.G., Thayer N., Thompson L.S., Tice H., Torney D.C., Tran-Gyamfi M., Tsai M., Ulanovsky L.E., Ustaszewska A., Vo N., White P.S., Williams A.L., Wills P.L., Wu J.-R., Wu K., Yang J., DeJong P., Bruce D., Doggett N.A., Deaven L., Schmutz J., Grimwood J., Richardson P., Rokhsar D.S., Eichler E.E., Gilna P., Lucas S.M., Myers R.M., Rubin E.M., Pennacchio L.A.
      Nature 432:988-994(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    9. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    10. "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] (ISOFORM 4).
      Tissue: Lymph.
    11. "Genomic structure and sequence of a human homologue (NTHL1/NTH1) of Escherichia coli endonuclease III with those of the adjacent parts of TSC2 and SLC9A3R2 genes."
      Imai K., Sarker A.H., Akiyama K., Ikeda S., Yao M., Tsutsui K., Shohmori T., Seki S.
      Gene 222:287-295(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-199.
      Tissue: Placenta.
    12. "The tuberous sclerosis 2 gene product, tuberin, functions as a Rab5 GTPase activating protein (GAP) in modulating endocytosis."
      Xiao G.-H., Shoarinejad F., Jin F., Golemis E.A., Yeung R.S.
      J. Biol. Chem. 272:6097-6100(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH RABEP1.
    13. Cited for: INTERACTION WITH TSC1.
    14. "Characterization of the cytosolic tuberin-hamartin complex. Tuberin is a cytosolic chaperone for hamartin."
      Nellist M., van Slegtenhorst M.A., Goedbloed M., van den Ouweland A.M.W., Halley D.J.J., van der Sluijs P.
      J. Biol. Chem. 274:35647-35652(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH TSC1.
    15. "Identification of the tuberous sclerosis complex-2 tumor suppressor gene product tuberin as a target of the phosphoinositide 3-kinase/akt pathway."
      Manning B.D., Tee A.R., Logsdon M.N., Blenis J., Cantley L.C.
      Mol. Cell 10:151-162(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-939 AND THR-1462.
    16. "Tuberous sclerosis complex-1 and -2 gene products function together to inhibit mammalian target of rapamycin (mTOR)-mediated downstream signaling."
      Tee A.R., Fingar D.C., Manning B.D., Kwiatkowski D.J., Cantley L.C., Blenis J.
      Proc. Natl. Acad. Sci. U.S.A. 99:13571-13576(2002) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS TSC2 MET-599 AND SER-1651.
    17. "TSC2 mediates cellular energy response to control cell growth and survival."
      Inoki K., Zhu T., Guan K.L.
      Cell 115:577-590(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT THR-1330 AND SER-1448, MUTAGENESIS OF THR-1330 AND SER-1448.
    18. "Biochemical and functional characterizations of small GTPase Rheb and TSC2 GAP activity."
      Li Y., Inoki K., Guan K.-L.
      Mol. Cell. Biol. 24:7965-7975(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, MUTAGENESIS OF 1637-LYS--ARG-1639; ARG-1745 AND 1749-ARG--ARG-1751, CHARACTERIZATION OF VARIANTS TSC2 LYS-1643; SER-1651; LYS-1681 AND PRO-1743.
    19. "Tumor-promoting phorbol esters and activated Ras inactivate the tuberous sclerosis tumor suppressor complex via p90 ribosomal S6 kinase."
      Roux P.P., Ballif B.A., Anjum R., Gygi S.P., Blenis J.
      Proc. Natl. Acad. Sci. U.S.A. 101:13489-13494(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION AT SER-1798.
    20. Cited for: PHOSPHORYLATION AT SER-1387; SER-1418 AND SER-1420, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH HSPA1; HSPA8 AND TSC1, CHARACTERIZATION OF VARIANTS TSC2 TRP-611 AND GLN-611.
    21. "Regulation of microtubule-dependent protein transport by the TSC2/mammalian target of rapamycin pathway."
      Jiang X., Yeung R.S.
      Cancer Res. 66:5258-5269(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION IN PROTEIN TRANSPORT.
    22. "TSC1 stabilizes TSC2 by inhibiting the interaction between TSC2 and the HERC1 ubiquitin ligase."
      Chong-Kopera H., Inoki K., Li Y., Zhu T., Garcia-Gonzalo F.R., Rosa J.L., Guan K.-L.
      J. Biol. Chem. 281:8313-8316(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH HERC1 AND TSC1.
    23. "Pam (Protein associated with Myc) functions as an E3 ubiquitin ligase and regulates TSC/mTOR signaling."
      Han S., Witt R.M., Santos T.M., Polizzano C., Sabatini B.L., Ramesh V.
      Cell. Signal. 20:1084-1091(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION BY MYCBP2, PHOSPHORYLATION AT SER-540; SER-664; SER-939; THR-1462 AND SER-1798, CHARACTERIZATION OF VARIANT GLN-611.
    24. "WD40 protein FBW5 promotes ubiquitination of tumor suppressor TSC2 by DDB1-CUL4-ROC1 ligase."
      Hu J., Zacharek S., He Y.J., Lee H., Shumway S., Duronio R.J., Xiong Y.
      Genes Dev. 22:866-871(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: UBIQUITINATION, INTERACTION WITH FBXW5.
    25. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    26. "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: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    27. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-927; SER-981; SER-1132; SER-1155; SER-1337; SER-1338; SER-1387; SER-1411; SER-1420 AND SER-1452, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    28. "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].
    29. "Peptide combinatorial libraries identify TSC2 as a death-associated protein kinase (DAPK) death domain-binding protein and reveal a stimulatory role for DAPK in mTORC1 signaling."
      Stevens C., Lin Y., Harrison B., Burch L., Ridgway R.A., Sansom O., Hupp T.
      J. Biol. Chem. 284:334-344(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION BY DAPK1, INTERACTION WITH DAPK1.
    30. "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-1155; THR-1462 AND SER-1798, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    31. Cited for: INTERACTION WITH NAA10.
    32. "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-1346 AND SER-1798, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    33. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    34. "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-1132, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    35. "Novel mutations detected in the TSC2 gene from both sporadic and familial TSC patients."
      Wilson P.J., Ramesh V., Kristiansen A., Bove C., Jozwiak S., Kwiatkowski D.J., Short M.P., Haines J.L.
      Hum. Mol. Genet. 5:249-256(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2 ILE-449; TRP-611; LEU-1227; TRP-1240; PHE-1509 DEL AND GLU-1712.
    36. "The GAP-related domain of tuberin, the product of the TSC2 gene, is a target for missense mutations in tuberous sclerosis."
      Maheshwar M.M., Cheadle J.P., Jones A.C., Myring J., Fryer A.E., Harris P.C., Sampson J.R.
      Hum. Mol. Genet. 6:1991-1996(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2 PHE-1509 DEL; MET-1594; LYS-1643; SER-1651; LEU-1675 AND LYS-1681.
    37. "Germ-line mutational analysis of the TSC2 gene in 90 tuberous-sclerosis patients."
      Au K.-S., Rodriguez J.A., Finch J.L., Volcik K.A., Roach E.S., Delgado M.R., Rodriguez E. Jr., Northrup H.
      Am. J. Hum. Genet. 62:286-294(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2.
    38. "Exon scanning of the entire TSC2 gene for germline mutations in 40 unrelated patients with tuberous sclerosis."
      Beauchamp R.L., Banwell A., McNamara P., Jacobsen M., Higgins E., Northrup H., Short M.P., Sims K., Ozelius L., Ramesh V.
      Hum. Mutat. 12:408-416(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2.
    39. "Mutation and polymorphism analysis in the tuberous sclerosis 2 (TSC2) gene."
      Gilbert J.R., Guy V., Kumar A., Wolpert C., Kandt R., Aylesworth A., Roses A.D., Pericak-Vance M.A.
      Neurogenetics 1:267-272(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2.
    40. "Comprehensive mutation analysis of TSC1 and TSC2- and phenotypic correlations in 150 families with tuberous sclerosis."
      Jones A.C., Shyamsundar M.M., Thomas M.W., Maynard J., Idziaszczyk S.A., Tomkins S., Sampson J.R., Cheadle J.P.
      Am. J. Hum. Genet. 64:1305-1315(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2, VARIANTS.
    41. "Novel TSC2 mutation in a patient with pulmonary tuberous sclerosis: lack of loss of heterozygosity in a lung cyst."
      Zhang H., Yamamoto T., Nanba E., Kitamura Y., Terada T., Akaboshi S., Yuasa I., Ohtani K., Nakamoto S., Takeshita K., Ohno K.
      Am. J. Med. Genet. 82:368-370(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT TSC2 ARG-717.
    42. "Superiority of denaturing high performance liquid chromatography over single-stranded conformation and conformation-sensitive gel electrophoresis for mutation detection in TSC2."
      Choy Y.S., Dabora S.L., Hall F., Ramesh V., Niida Y., Franz D., Kasprzyk-Obara J., Reeve M.P., Kwiatkowski D.J.
      Ann. Hum. Genet. 63:383-391(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2, VARIANTS.
    43. "Analysis of both TSC1 and TSC2 for germline mutations in 126 unrelated patients with tuberous sclerosis."
      Niida Y., Lawrence-Smith N., Banwell A., Hammer E., Lewis J., Beauchamp R.L., Sims K., Ramesh V., Ozelius L.
      Hum. Mutat. 14:412-422(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2, VARIANTS.
      Tissue: Blood and Lymphoblast.
    44. "Mutational analysis of TSC1 and TSC2 genes in Japanese patients with tuberous sclerosis complex."
      Zhang H., Nanba E., Yamamoto T., Ninomiya H., Ohno K., Mizuguchi M., Takeshita K.
      J. Hum. Genet. 44:391-396(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2 ARG-137; GLN-611; ASN-647; ARG-717; GLU-769; MET-963 AND LEU-1675, VARIANT PHE-320, POSSIBLE ASSOCIATION WITH TSC.
    45. "Analysis of all exons of TSC1 and TSC2 genes for germline mutations in Japanese patients with tuberous sclerosis: report of 10 mutations."
      Yamashita Y., Ono J., Okada S., Wataya-Kaneda M., Yoshikawa K., Nishizawa M., Hirayama Y., Kobayashi E., Seyama K., Hino O.
      Am. J. Med. Genet. 90:123-126(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2 TRP-611; TRP-905; PRO-1744 AND 1746-HIS--ARG-1751 DEL, VARIANT PHE-320.
      Tissue: Peripheral blood leukocyte.
    46. "Mutations in the tuberous sclerosis complex gene TSC2 are a cause of sporadic pulmonary lymphangioleiomyomatosis."
      Carsillo T., Astrinidis A., Henske E.P.
      Proc. Natl. Acad. Sci. U.S.A. 97:6085-6090(2000) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANT LAM GLN-611.
    47. "Novel TSC2 mutations and decreased expression of tuberin in cultured tumor cells with an insertion mutation."
      Feng J.-H., Yamamoto T., Nanba E., Ninomiya H., Oka A., Ohno K.
      Hum. Mutat. 23:397-397(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2 SER-1651; PHE-1653; LEU-1675 AND 1746-HIS--ARG-1751 DEL, VARIANTS THR-607; VAL-862; SER-1429 AND ARG-1450.
    48. "Mutation and polymorphism analysis of TSC1 and TSC2 genes in Indian patients with tuberous sclerosis complex."
      Ali M., Girimaji S.C., Markandaya M., Shukla A.K., Sacchidanand S., Kumar A.
      Acta Neurol. Scand. 111:54-63(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: VARIANTS TSC2 GLN-611; TRP-611 AND PRO-1027, VARIANTS GLN-367; ARG-1341; ASN-1636 AND LEU-1673.

    Entry informationi

    Entry nameiTSC2_HUMAN
    AccessioniPrimary (citable) accession number: P49815
    Secondary accession number(s): A7E2E2
    , B4DIL8, B4DIQ7, B4DRN2, B7Z2B8, C9J378, O75275, Q4LE71, Q8TAZ1
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: October 1, 1996
    Last sequence update: November 24, 2009
    Last modified: October 1, 2014
    This is version 164 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Reference proteome

    Documents

    1. Human chromosome 16
      Human chromosome 16: 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

    Dasty 3