Skip Header

Contribute Send feedback
Read comments (0) or add your own

Reviewed, UniProtKB/Swiss-Prot P49815 (TSC2_HUMAN)

Last modified February 9, 2010. Version 115. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Alternative products · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Tuberin
Alternative name(s):
    Tuberous sclerosis 2 protein
Gene names
Name: TSC2
Synonyms: TSC4
OrganismHomo sapiens (Human) [Complete proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length1807 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

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. Ref.15 Ref.16 Ref.18

Subunit structure

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. Ref.11 Ref.12 Ref.13 Ref.17 Ref.20

Subcellular location

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

Tissue specificity

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

Post-translational modification

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.

Involvement in disease

Defects in TSC2 are the cause of tuberous sclerosis complex (TSC) [MIM:191100]. The molecular basis of TSC is a functional impairment of the tuberin-hamartin complex. TSC is an autosomal dominant multi-system disorder that affects especially the brain, kidneys, heart, and skin. TSC 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 symptoms can range from benign hypopigmented macules of the skin to profound mental retardation with intractable seizures to premature death from a variety of disease-associated causes. Ref.15 Ref.16 Ref.12 Ref.13 Ref.17 Ref.20 Ref.26 Ref.27 Ref.28 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.38 Ref.39

Defects in TSC2 are a cause of lymphangioleiomyomatosis (LAM) [MIM:606690]. LAM is a 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. Ref.37

Sequence similarities

Contains 1 Rap-GAP domain.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseDisease mutation
Tumor suppressor
   Molecular functionGTPase activation
   PTMPhosphoprotein
   Technical termComplete proteome
Gene Ontology (GO)
   Biological processendocytosis Ref.11

Traceable author statement. Source: ProtInc

heart development

Inferred from sequence or structural similarity. Source: UniProtKB

insulin-like growth factor receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of phosphoinositide 3-kinase cascade

Inferred from sequence or structural similarity. Source: UniProtKB

negative regulation of protein kinase B signaling cascade

Inferred from sequence or structural similarity. Source: UniProtKB

neural tube closure

Inferred from sequence or structural similarity. Source: UniProtKB

positive chemotaxis

Inferred from sequence or structural similarity. Source: UniProtKB

positive regulation of GTPase activity

Inferred from electronic annotation. Source: InterPro

protein import into nucleus

Inferred from sequence or structural similarity. Source: UniProtKB

protein kinase B signaling cascade

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of endocytosis

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of insulin receptor signaling pathway

Inferred from sequence or structural similarity. Source: UniProtKB

regulation of small GTPase mediated signal transduction

Inferred from electronic annotation. Source: InterPro

   Cellular componentGolgi apparatus Ref.13

Inferred from direct assay. Source: UniProtKB

TSC1-TSC2 complex Ref.12

Inferred from direct assay. Source: UniProtKB

extrinsic to membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

nucleus

Inferred from direct assay. Source: UniProtKB

perinuclear region of cytoplasm

Inferred from direct assay. Source: UniProtKB

   Molecular functionGTPase activator activity Ref.11

Inferred from direct assay. Source: UniProtKB

protein homodimerization activity Ref.13

Inferred from physical interaction. Source: UniProtKB

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 6 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P49815-1)

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.
Isoform 2 (identifier: P49815-2)

The sequence of this isoform differs from the canonical sequence as follows:
     946-988: Missing.
Note: No experimental confirmation available.
Isoform 3 (identifier: P49815-3)

The sequence of this isoform differs from the canonical sequence as follows:
     946-989: Missing.
Note: No experimental confirmation available.
Isoform 4 (identifier: P49815-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1272-1294: Missing.
Isoform 5 (identifier: P49815-5)

The sequence of this isoform differs from the canonical sequence as follows:
     946-989: Missing.
     1272-1294: Missing.
Isoform 6 (identifier: P49815-6)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 18071807Tuberin
PRO_0000065654

Regions

Domain1531 – 1758228Rap-GAP
Region1 – 400400Required for interaction with TSC1

Amino acid modifications

Modified residue9271Phosphothreonine Ref.23
Modified residue9391Phosphoserine; by PKB/AKT1 Ref.14
Modified residue9811Phosphoserine Ref.23
Modified residue10971Phosphoserine Ref.21
Modified residue11321Phosphoserine Ref.23
Modified residue11551Phosphoserine Ref.23 Ref.21 Ref.22 Ref.25
Modified residue13341Phosphoserine Ref.23
Modified residue13371Phosphoserine Ref.23
Modified residue13381Phosphoserine Ref.23
Modified residue13411Phosphoserine Ref.23
Modified residue13641Phosphoserine By similarity
Modified residue13871Phosphoserine Ref.17
Modified residue13881Phosphoserine Ref.24
Modified residue14111Phosphoserine Ref.23 Ref.22 Ref.19
Modified residue14181Phosphoserine Ref.17
Modified residue14201Phosphoserine Ref.17 Ref.23 Ref.24
Modified residue14491Phosphoserine Ref.23 Ref.25
Modified residue14521Phosphoserine Ref.23
Modified residue14621Phosphothreonine; by PKB/AKT1 Ref.14 Ref.25
Modified residue17981Phosphoserine Ref.25 Ref.19

Natural variations

Alternative sequence76 – 11237Missing in isoform 6.
VSP_038355
Alternative sequence946 – 98944Missing in isoform 3 and isoform 5.
VSP_004471
Alternative sequence946 – 98843Missing in isoform 2 and isoform 6.
VSP_004470
Alternative sequence1272 – 129423Missing in isoform 4, isoform 5 and isoform 6.
VSP_004472
Natural variant941P → T: dbSNP rs1051616. Ref.4
VAR_008019
Natural variant1371H → R in TSC; could be a polymorphism. dbSNP rs45517107. Ref.35
VAR_009415
Natural variant1601L → V: dbSNP rs45517109.
VAR_009416
Natural variant2271C → Y in TSC. dbSNP rs45517122.
VAR_008020
Natural variant2581K → N in TSC.
VAR_009417
Natural variant2611R → P in TSC. dbSNP rs45502703.
VAR_009418
Natural variant2611R → W: dbSNP rs45517130.
VAR_009419
Natural variant2861M → T: dbSNP rs45517136.
VAR_009420
Natural variant2861M → V: dbSNP rs1800748.
VAR_009421
Natural variant2921L → P in TSC. dbSNP rs45517138.
VAR_005646
Natural variant2941G → E in TSC. dbSNP rs45487497.
VAR_009422
Natural variant3041W → WGMALW in TSC.
VAR_009423
Natural variant3091L → Q
VAR_009424
Natural variant3201L → F Could be associated with TSC. dbSNP rs1131825. Ref.35 Ref.36 Ref.4
VAR_009425
Natural variant3311N → K in TSC. dbSNP rs45517153.
VAR_008021
Natural variant3611L → P in TSC. dbSNP rs45517147.
VAR_009426
Natural variant3651Missing in TSC.
VAR_009427
Natural variant3671R → Q: dbSNP rs1800725. Ref.39
VAR_009428
Natural variant3781P → L: dbSNP rs45517154.
VAR_009429
Natural variant4071Y → D in TSC.
VAR_005647
Natural variant4401G → S
VAR_009430
Natural variant4491M → I in TSC. Ref.26
VAR_005648
Natural variant4631I → V
VAR_009431
Natural variant4861N → I in TSC.
VAR_008022
Natural variant4901I → V
VAR_008023
Natural variant5251N → S in TSC.
VAR_009432
Natural variant5361A → V
VAR_008024
Natural variant5831A → T: dbSNP rs1800729.
VAR_009433
Natural variant5931H → R
VAR_009434
Natural variant5991K → M in TSC; impairs repression of EIF4EBP1 phosphorylation. Ref.15
VAR_009435
Natural variant6071A → T
VAR_005649
Natural variant6111R → Q in TSC and LAM; impairs phosphorylation at S-1387, S-1418 and S-1420. Ref.17 Ref.35 Ref.39 Ref.37
VAR_005650
Natural variant6111R → W in TSC; impairs phosphorylation at S-1387, S-1418 and S-1420. Ref.17 Ref.26 Ref.36 Ref.39
VAR_005651
Natural variant6141A → D in TSC.
VAR_009436
Natural variant6151F → S
VAR_008025
Natural variant6191L → F: dbSNP rs1131826. Ref.4
VAR_060584
Natural variant6471D → N in TSC; could be a polymorphism. Ref.35
VAR_009437
Natural variant6941Missing in TSC.
VAR_009438
Natural variant6961C → Y in TSC.
VAR_009439
Natural variant7171L → R in TSC. Ref.32 Ref.35
VAR_009440
Natural variant7691V → E in TSC; could be a polymorphism. Ref.35
VAR_009441
Natural variant8021S → R: dbSNP rs1051621. Ref.4 Ref.1
VAR_060585
Natural variant8161P → L in TSC.
VAR_008026
Natural variant8261L → M in TSC.
VAR_005652
Natural variant8621A → V
VAR_018600
Natural variant8951M → V in TSC.
VAR_009442
Natural variant9051R → Q in TSC.
VAR_005653
Natural variant9051R → W in TSC. Ref.36
VAR_005654
Natural variant9631V → M in TSC; could be a polymorphism. Ref.35
VAR_009443
Natural variant10271L → P in TSC. Ref.39
VAR_022919
Natural variant10841D → E in TSC.
VAR_005655
Natural variant11411A → V: dbSNP rs34870424.
VAR_057014
Natural variant11441V → M in TSC.
VAR_008027
Natural variant12001R → W in TSC.
VAR_005656
Natural variant12271P → L in TSC. Ref.26
VAR_005657
Natural variant12401R → W in TSC. Ref.26
VAR_005658
Natural variant12821S → G
VAR_009444
Natural variant12951D → V in TSC.
VAR_005659
Natural variant13151P → S in TSC.
VAR_008028
Natural variant13291R → H in TSC.
VAR_008029
Natural variant13411S → R
VAR_022920
Natural variant14291A → S
VAR_018601
Natural variant14501P → R
VAR_018602
Natural variant14971P → R in TSC.
VAR_009445
Natural variant14981S → N in TSC.
VAR_009446
Natural variant15091Missing in TSC; could be a rare polymorphism.
VAR_005660
Natural variant15491Y → C in TSC.
VAR_005661
Natural variant15941L → M in TSC; could be a polymorphism. Ref.27
VAR_009447
Natural variant16141Missing in TSC.
VAR_005662
Natural variant16201H → Y in TSC.
VAR_009448
Natural variant16361D → N
VAR_022921
Natural variant16431N → I in TSC.
VAR_005663
Natural variant16431N → K in TSC; Abolishes GAP activity. Ref.16 Ref.27
VAR_009449
Natural variant16501Y → C in TSC.
VAR_005664
Natural variant16511N → S in TSC; greatly reduces the ability to enhance the RHEB GTPase activity. Ref.15 Ref.16 Ref.27 Ref.38
VAR_009450
Natural variant16531S → F in TSC. Ref.38
VAR_018603
Natural variant16731V → L
VAR_022922
Natural variant16751P → L in TSC. Ref.27 Ref.35 Ref.38
VAR_009451
Natural variant16811N → K in TSC; Abolishes GAP activity. Ref.16 Ref.27
VAR_009452
Natural variant16901D → Y in TSC.
VAR_005665
Natural variant17041S → T in TSC.
VAR_009453
Natural variant17091P → L in TSC.
VAR_008030
Natural variant17121A → E in TSC. Ref.26
VAR_005666
Natural variant17431R → P in TSC; Abolishes GAP activity. Ref.16
VAR_009454
Natural variant17431R → Q in TSC.
VAR_008031
Natural variant17441L → P in TSC. Ref.36
VAR_009455
Natural variant1746 – 17516Missing in TSC.
VAR_009456
Natural variant17501L → F in TSC.
VAR_005667
Natural variant17731H → P in TSC.
VAR_008032
Natural variant17741S → T: dbSNP rs9209.
VAR_057015
Natural variant17831E → Q in TSC.
VAR_008033
Natural variant17871G → S
VAR_009457
Natural variant17911G → S
VAR_009458

Experimental info

Mutagenesis9391S → A: Inhibits insulin-stimulated phosphorylation and activation of S6K1; when associated with A-1462.
Mutagenesis14621T → A: Inhibits insulin-stimulated phosphorylation and activation of S6K1; when associated with A-939.
Mutagenesis1637 – 16393KKR → QQQ: Abolishes GAP activity.
Mutagenesis17451R → Q: Abolishes GAP activity. Ref.16
Mutagenesis1749 – 17513RLR → QLQ: No effect. Ref.16
Sequence conflict1871N → S in BAG61344. Ref.6
Sequence conflict2101A → V in AAI50301. Ref.9
Sequence conflict3351S → P in BAG61344. Ref.6
Sequence conflict3921E → V in BAG58569. Ref.6
Sequence conflict4221S → P in BAG58569. Ref.6
Sequence conflict6601S → N in BAG61344. Ref.6
Sequence conflict7041K → E in AAI50301. Ref.9
Sequence conflict7061L → P in BAG58569. Ref.6
Sequence conflict10151L → M in AAI50301. Ref.9
Sequence conflict12391E → V in BAG61344. Ref.6
Sequence conflict13981L → V in BAG61344. Ref.6
Sequence conflict16721I → M in AAI50301. Ref.9
Sequence conflict18071V → A in BAG61344. Ref.6

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified November 24, 2009. Version 2.
Checksum: 7B915C46970D7D31

FASTA1,807200,608
        10         20         30         40         50         60 
MAKPTSKDSG LKEKFKILLG LGTPRPNPRS AEGKQTEFII TAEILRELSM ECGLNNRIRM 

        70         80         90        100        110        120 
IGQICEVAKT KKFEEHAVEA LWKAVADLLQ PERPLEARHA VLALLKAIVQ GQGERLGVLR 

       130        140        150        160        170        180 
ALFFKVIKDY PSNEDLHERL EVFKALTDNG RHITYLEEEL ADFVLQWMDV GLSSEFLLVL 

       190        200        210        220        230        240 
VNLVKFNSCY LDEYIARMVQ MICLLCVRTA SSVDIEVSLQ VLDAVVCYNC LPAESLPLFI 

       250        260        270        280        290        300 
VTLCRTINVK ELCEPCWKLM RNLLGTHLGH SAIYNMCHLM EDRAYMEDAP LLRGAVFFVG 

       310        320        330        340        350        360 
MALWGAHRLY SLRNSPTSVL PSFYQAMACP NEVVSYEIVL SITRLIKKYR KELQVVAWDI 

       370        380        390        400        410        420 
LLNIIERLLQ QLQTLDSPEL RTIVHDLLTT VEELCDQNEF HGSQERYFEL VERCADQRPE 

       430        440        450        460        470        480 
SSLLNLISYR AQSIHPAKDG WIQNLQALME RFFRSESRGA VRIKVLDVLS FVLLINRQFY 

       490        500        510        520        530        540 
EEELINSVVI SQLSHIPEDK DHQVRKLATQ LLVDLAEGCH THHFNSLLDI IEKVMARSLS 

       550        560        570        580        590        600 
PPPELEERDV AAYSASLEDV KTAVLGLLVI LQTKLYTLPA SHATRVYEML VSHIQLHYKH 

       610        620        630        640        650        660 
SYTLPIASSI RLQAFDFLLL LRADSLHRLG LPNKDGVVRF SPYCVCDYME PERGSEKKTS 

       670        680        690        700        710        720 
GPLSPPTGPP GPAPAGPAVR LGSVPYSLLF RVLLQCLKQE SDWKVLKLVL GRLPESLRYK 

       730        740        750        760        770        780 
VLIFTSPCSV DQLCSALCSM LSGPKTLERL RGAPEGFSRT DLHLAVVPVL TALISYHNYL 

       790        800        810        820        830        840 
DKTKQREMVY CLEQGLIHRC ASQCVVALSI CSVEMPDIII KALPVLVVKL THISATASMA 

       850        860        870        880        890        900 
VPLLEFLSTL ARLPHLYRNF AAEQYASVFA ISLPYTNPSK FNQYIVCLAH HVIAMWFIRC 

       910        920        930        940        950        960 
RLPFRKDFVP FITKGLRSNV LLSFDDTPEK DSFRARSTSL NERPKSLRIA RPPKQGLNNS 

       970        980        990       1000       1010       1020 
PPVKEFKESS AAEAFRCRSI SVSEHVVRSR IQTSLTSASL GSADENSVAQ ADDSLKNLHL 

      1030       1040       1050       1060       1070       1080 
ELTETCLDMM ARYVFSNFTA VPKRSPVGEF LLAGGRTKTW LVGNKLVTVT TSVGTGTRSL 

      1090       1100       1110       1120       1130       1140 
LGLDSGELQS GPESSSSPGV HVRQTKEAPA KLESQAGQQV SRGARDRVRS MSGGHGLRVG 

      1150       1160       1170       1180       1190       1200 
ALDVPASQFL GSATSPGPRT APAAKPEKAS AGTRVPVQEK TNLAAYVPLL TQGWAEILVR 

      1210       1220       1230       1240       1250       1260 
RPTGNTSWLM SLENPLSPFS SDINNMPLQE LSNALMAAER FKEHRDTALY KSLSVPAAST 

      1270       1280       1290       1300       1310       1320 
AKPPPLPRSN TVASFSSLYQ SSCQGQLHRS VSWADSAVVM EEGSPGEVPV LVEPPGLEDV 

      1330       1340       1350       1360       1370       1380 
EAALGMDRRT DAYSRSSSVS SQEEKSLHAE ELVGRGIPIE RVVSSEGGRP SVDLSFQPSQ 

      1390       1400       1410       1420       1430       1440 
PLSKSSSSPE LQTLQDILGD PGDKADVGRL SPEVKARSQS GTLDGESAAW SASGEDSRGQ 

      1450       1460       1470       1480       1490       1500 
PEGPLPSSSP RSPSGLRPRG YTISDSAPSR RGKRVERDAL KSRATASNAE KVPGINPSFV 

      1510       1520       1530       1540       1550       1560 
FLQLYHSPFF GDESNKPILL PNESQSFERS VQLLDQIPSY DTHKIAVLYV GEGQSNSELA 

      1570       1580       1590       1600       1610       1620 
ILSNEHGSYR YTEFLTGLGR LIELKDCQPD KVYLGGLDVC GEDGQFTYCW HDDIMQAVFH 

      1630       1640       1650       1660       1670       1680 
IATLMPTKDV DKHRCDKKRH LGNDFVSIVY NDSGEDFKLG TIKGQFNFVH VIVTPLDYEC 

      1690       1700       1710       1720       1730       1740 
NLVSLQCRKD MEGLVDTSVA KIVSDRNLPF VARQMALHAN MASQVHHSRS NPTDIYPSKW 

      1750       1760       1770       1780       1790       1800 
IARLRHIKRL RQRICEEAAY SNPSLPLVHP PSHSKAPAQT PAEPTPGYEV GQRKRLISSV 


EDFTEFV 

« Hide

Isoform 2.

Checksum: EECB8D3132AFFBA2
Show »

FASTA1,764195,847
Isoform 3.

Checksum: 9EBB34789D67D71C
Show »

FASTA1,763195,760
Isoform 4.

Checksum: 36A09DD2BBCD369A
Show »

FASTA1,784198,097
Isoform 5.

Checksum: A0886EF0FBE7652E
Show »

FASTA1,740193,249
Isoform 6.

Checksum: AD89389C5CDB4B2C
Show »

FASTA1,704189,298

References

« Hide 'large scale' references
[1]"Identification and characterization of the tuberous sclerosis gene on chromosome 16."
The European chromosome 16 tuberous sclerosis consortium
Nellist M., Janssen B., Brook-Carter P.T., Hesseling-Janssen A.L.W., Maheshwar M.M., Verhoef S., van den Ouweland A.M.W., Lindhout D., Eussen B., Cordeiro I., Santos H., Halley D.J.J., Sampson J.R., Ward C.J., Peral B., Thomas S., Hughes J., Harris P.C. expand/collapse author list , Roelfsema J.H., Saris J.J., Spruit L., Peters D.J.M., Dauwerse J.G., Breuning M.H.
Cell 75:1305-1315(1993) [PubMed: 8269512] [Abstract]
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: 7558029] [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: 8789450] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS THR-94; PHE-320; PHE-619 AND ARG-802.
[5]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.
[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. expand/collapse author list , 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: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 5 AND 6).
Tissue: Hippocampus.
[7]"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. expand/collapse author list , 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: 15616553] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[8]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. expand/collapse author list , 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 (SEP-2005) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[9]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
Tissue: Lymph.
[10]"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: 9831664] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 1-199.
Tissue: Placenta.
[11]"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: 9045618] [Abstract]
Cited for: INTERACTION WITH RABEP1.
[12]"Interaction between hamartin and tuberin, the TSC1 and TSC2 gene products."
van Slegtenhorst M.A., Nellist M., Nagelkerken B., Cheadle J.P., Snell R.G., van den Ouweland A.M.W., Reuser A., Sampson J.R., Halley D.J.J., van der Sluijs P.
Hum. Mol. Genet. 7:1053-1057(1998) [PubMed: 9580671] [Abstract]
Cited for: INTERACTION WITH TSC1.
[13]"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: 10585443] [Abstract]
Cited for: INTERACTION WITH TSC1.
[14]"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: 12150915] [Abstract]
Cited for: PHOSPHORYLATION AT SER-939 AND THR-1462.
[15]"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: 12271141] [Abstract]
Cited for: FUNCTION, CHARACTERIZATION OF VARIANTS TSC MET-599 AND TSC SER-1651.
[16]"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: 15340059] [Abstract]
Cited for: FUNCTION, MUTAGENESIS OF 1637-LYS--ARG-1639; ARG-1745 AND 1749-ARG--ARG-1751, CHARACTERIZATION OF VARIANTS TSC LYS-1643; TSC SER-1651; TSC LYS-1681 AND TSC PRO-1743.
[17]"Phosphorylation and binding partner analysis of the TSC1-TSC2 complex."
Nellist M., Burgers P.C., van den Ouweland A.M.W., Halley D.J.J., Luider T.M.
Biochem. Biophys. Res. Commun. 333:818-826(2005) [PubMed: 15963462] [Abstract]
Cited for: PHOSPHORYLATION AT SER-1387; SER-1418 AND SER-1420, MASS SPECTROMETRY, INTERACTION WITH HSPA1; HSPA8 AND TSC1, CHARACTERIZATION OF VARIANTS TSC TRP-611 AND GLN-611.
[18]"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: 16707451] [Abstract]
Cited for: FUNCTION IN PROTEIN TRANSPORT.
[19]"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: 17081983] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1411 AND SER-1798, MASS SPECTROMETRY.
Tissue: Epithelium.
[20]"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: 16464865] [Abstract]
Cited for: INTERACTION WITH HERC1 AND TSC1.
[21]"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: 18220336] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1097 AND SER-1155, MASS SPECTROMETRY.
[22]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155 AND SER-1411, MASS SPECTROMETRY.
[23]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-927; SER-981; SER-1132; SER-1155; SER-1334; SER-1337; SER-1338; SER-1341; SER-1411; SER-1420; SER-1449 AND SER-1452, MASS SPECTROMETRY.
[24]"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: 19413330] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1388 AND SER-1420, MASS SPECTROMETRY.
[25]"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: 19690332] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1155; SER-1449; THR-1462 AND SER-1798, MASS SPECTROMETRY.
Tissue: T-cell.
[26]"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: 8824881] [Abstract]
Cited for: VARIANTS TSC ILE-449; TRP-611; LEU-1227; TRP-1240; PHE-1509 DEL AND GLU-1712.
[27]"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: 9302281] [Abstract]
Cited for: VARIANTS TSC PHE-1509 DEL; MET-1594; LYS-1643; SER-1651; LEU-1675 AND LYS-1681.
[28]"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: 9463313] [Abstract]
Cited for: VARIANTS TSC.
[29]"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: 9829910] [Abstract]
Cited for: VARIANTS TSC.
[30]"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: 10732801] [Abstract]
Cited for: VARIANTS TSC.
[31]"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: 10205261] [Abstract]
Cited for: VARIANTS TSC, VARIANTS.
[32]"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: 10069705] [Abstract]
Cited for: VARIANT TSC ARG-717.
[33]"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: 10735580] [Abstract]
Cited for: VARIANTS TSC, VARIANTS.
[34]"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: 10533067] [Abstract]
Cited for: VARIANTS TSC, VARIANTS.
Tissue: Blood and Lymphoblast.
[35]"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: 10570911] [Abstract]
Cited for: VARIANTS TSC ARG-137; GLN-611; ASN-647; ARG-717; GLU-769; MET-963 AND LEU-1675, VARIANT PHE-320, POSSIBLE ASSOCIATION WITH TSC.
[36]"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: 10607950] [Abstract]
Cited for: VARIANTS TSC TRP-611; TRP-905; PRO-1744 AND 1746-HIS--ARG-1751 DEL, VARIANT PHE-320.
Tissue: Peripheral blood leukocyte.
[37]"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: 10823953] [Abstract]
Cited for: VARIANT LAM GLN-611.
[38]"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: 15024740] [Abstract]
Cited for: VARIANTS TSC SER-1651; PHE-1653; LEU-1675 AND 1746-HIS--ARG-1751 DEL, VARIANTS THR-607; VAL-862; SER-1429 AND ARG-1450.
[39]"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: 15595939] [Abstract]
Cited for: VARIANTS TSC GLN-611; TRP-611 AND PRO-1027, VARIANTS GLN-367; ARG-1341; ASN-1636 AND LEU-1673.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
X75621 mRNA. Translation: CAA53287.1.
L48546 expand/collapse EMBL AC list , 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.
AB210000 mRNA. Translation: BAE06082.1. Different initiation.
AK295728 mRNA. Translation: BAG58569.1.
AK299343 mRNA. Translation: BAG61344.1.
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.
IPIIPI00028493.
IPI00218881.
IPI00218883.
IPI00879496.
IPI00952929.
IPI00954095.
PIRA49420.
RefSeqNP_000539.2.
NP_001070651.1.
NP_001107854.1.
UniGeneHs.90303

3D structure databases

SMRP49815. Positions 1503-1723.
ModBaseSearch...

Protein-protein interaction databases

IntActP49815. 6 interactions.
STRINGP49815.

PTM databases

PhosphoSiteP49815.

Proteomic databases

PRIDEP49815.

Genome annotation databases

EnsemblENST00000219476; ENSP00000219476; ENSG00000103197; Homo sapiens. [Genome view]
GeneID7249.
KEGGhsa:7249.
UCSCuc002con.1. human.
uc010bsd.1. human.

Organism-specific databases

CTD7249.
GeneCardsGC16P002038.
H-InvDBHIX0012712.
HGNCHGNC:12363. TSC2.
HPACAB002225.
MIM191092. gene.
191100. phenotype.
606690. phenotype.
Orphanet538. Lymphangioleiomyomatosis.
88924. Polycystic kidney disease, autosomal dominant, type 1, with tuberous sclerosis.
805. Tuberous sclerosis.
PharmGKBPA32846.
GenAtlasSearch...

Phylogenomic databases

eggNOGprNOG18472.
HOGENOMHBG714363.
HOVERGENP49815.
InParanoidP49815.

Enzyme and pathway databases

Pathway_Interaction_DBpi3kciaktpathway. Class I PI3K signaling events mediated by Akt.
mtor_4pathway. mTOR signaling pathway.
p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
ReactomeREACT_11061. Signalling by NGF.
REACT_498. Signaling by Insulin receptor.

Gene expression databases

ArrayExpressP49815.
BgeeP49815.
CleanExHS_TSC2.
GenevestigatorP49815.
GermOnlineENSG00000103197. Homo sapiens.

Family and domain databases

InterProIPR016024. ARM-type_fold.
IPR000331. Rap_GAP.
IPR003913. Tuberin.
[Graphical view]
PfamPF02145. Rap_GAP. 1 hit.
[Graphical view]
PRINTSPR01431. TUBERIN.
PROSITEPS50085. RAPGAP. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

SOURCESearch...

Entry information

Entry nameTSC2_HUMAN
AccessionPrimary (citable) accession number: P49815
Secondary accession number(s): A7E2E2 expand/collapse secondary AC list , B4DIQ7, B4DRN2, C9J378, O75275, Q4LE71, Q8TAZ1
Entry history
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: November 24, 2009
Last modified: February 9, 2010
This is version 115 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)
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.

Relevant documents

Human chromosome 16

Human chromosome 16: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

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