P49815 (TSC2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Tuberin

Alternative name(s):
Tuberous sclerosis 2 protein

Gene names

Name:	TSC2
Synonyms:	TSC4

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	1807 AA.
Sequence status	Complete.
Protein existence	Evidence 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.17 Ref.20
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. Interacts with DAPK1. Ref.11 Ref.12 Ref.13 Ref.19 Ref.22 Ref.27
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. 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. Ref.14 Ref.16 Ref.18 Ref.19 Ref.21 Ref.23 Ref.24 Ref.25 Ref.26 Ref.27 Ref.28
Involvement in disease	Defects in TSC2 are the cause of tuberous sclerosis type 2 (TSC2) [MIM:613254]. TSC2 is 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 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.17 Ref.19 Ref.29 Ref.30 Ref.31 Ref.32 Ref.33 Ref.34 Ref.35 Ref.36 Ref.37 Ref.38 Ref.39 Ref.41 Ref.42 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.40
Sequence similarities	Contains 1 Rap-GAP domain.
Sequence caution	The sequence BAE06082.1 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
Cellular component	Cytoplasm Membrane
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Disease mutation Tumor suppressor
Molecular function	GTPase activation
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	cell cycle arrest Traceable author statement. Source: Reactome endocytosis Traceable author statement. Source: ProtInc fibroblast growth factor receptor signaling pathway Traceable author statement. Source: Reactome heart development Inferred from sequence or structural similarity. Source: UniProtKB insulin receptor signaling pathway Traceable author statement. Source: Reactome insulin-like growth factor receptor signaling pathway Inferred from sequence or structural similarity. Source: UniProtKB negative regulation of TOR signaling cascade Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of Wnt receptor signaling pathway Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of cell size Inferred from Biological aspect of Ancestor. Source: RefGenome negative regulation of phosphatidylinositol 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 nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome neural tube closure Inferred from sequence or structural similarity. Source: UniProtKB positive chemotaxis Inferred from sequence or structural similarity. Source: UniProtKB 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 component	Golgi apparatus Inferred from direct assay Ref.13. Source: UniProtKB TSC1-TSC2 complex Inferred from direct assay Ref.12. Source: UniProtKB nucleus Inferred from direct assay. Source: UniProtKB perinuclear region of cytoplasm Inferred from direct assay. Source: UniProtKB
Molecular function	GTPase activator activity Inferred from direct assay Ref.11. Source: UniProtKB phosphatase binding Inferred from direct assay. Source: UniProtKB protein homodimerization activity Inferred from physical interaction Ref.13. Source: UniProtKB
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
TSC1	Q92574	7	EBI-396587,EBI-1047085

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 key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 1807	1807	Tuberin		PRO_0000065654
Regions
	Domain	1531 – 1758	228	Rap-GAP
	Region	1 – 400	400	Required for interaction with TSC1
Amino acid modifications
	Modified residue	927	1	Phosphothreonine Ref.25
	Modified residue	939	1	Phosphoserine; by PKB/AKT1 Ref.14
	Modified residue	981	1	Phosphoserine Ref.25
	Modified residue	1097	1	Phosphoserine Ref.23
	Modified residue	1132	1	Phosphoserine Ref.25
	Modified residue	1155	1	Phosphoserine Ref.23 Ref.24 Ref.25 Ref.28
	Modified residue	1330	1	Phosphothreonine; by AMPK Ref.16
	Modified residue	1334	1	Phosphoserine Ref.25
	Modified residue	1337	1	Phosphoserine Ref.25
	Modified residue	1338	1	Phosphoserine Ref.25
	Modified residue	1341	1	Phosphoserine Ref.25
	Modified residue	1364	1	Phosphoserine By similarity
	Modified residue	1387	1	Phosphoserine Ref.19
	Modified residue	1388	1	Phosphoserine Ref.26
	Modified residue	1411	1	Phosphoserine Ref.21 Ref.24 Ref.25
	Modified residue	1418	1	Phosphoserine Ref.19
	Modified residue	1420	1	Phosphoserine Ref.19 Ref.25 Ref.26
	Modified residue	1448	1	Phosphoserine; by AMPK Ref.16
	Modified residue	1449	1	Phosphoserine Ref.25 Ref.28
	Modified residue	1452	1	Phosphoserine Ref.25
	Modified residue	1462	1	Phosphothreonine; by PKB/AKT1 Ref.14 Ref.28
	Modified residue	1798	1	Phosphoserine; by RPS6KA1 Ref.18 Ref.21 Ref.28
Natural variations
	Alternative sequence	76 – 112	37	Missing in isoform 6.		VSP_038355
	Alternative sequence	946 – 989	44	Missing in isoform 3 and isoform 5.		VSP_004471
	Alternative sequence	946 – 988	43	Missing in isoform 2 and isoform 6.		VSP_004470
	Alternative sequence	1272 – 1294	23	Missing in isoform 4, isoform 5 and isoform 6.		VSP_004472
	Natural variant	94	1	P → T. Ref.4 Corresponds to variant rs1051616 [ dbSNP | Ensembl ].		VAR_008019
	Natural variant	137	1	H → R in TSC2; could be a polymorphism. Ref.38 Corresponds to variant rs45517107 [ dbSNP | Ensembl ].		VAR_009415
	Natural variant	160	1	L → V. Corresponds to variant rs45517109 [ dbSNP | Ensembl ].		VAR_009416
	Natural variant	227	1	C → Y in TSC2. Corresponds to variant rs45517122 [ dbSNP | Ensembl ].		VAR_008020
	Natural variant	258	1	K → N in TSC2.		VAR_009417
	Natural variant	261	1	R → P in TSC2. Corresponds to variant rs45502703 [ dbSNP | Ensembl ].		VAR_009418
	Natural variant	261	1	R → W. Corresponds to variant rs45517130 [ dbSNP | Ensembl ].		VAR_009419
	Natural variant	286	1	M → T. Corresponds to variant rs45517136 [ dbSNP | Ensembl ].		VAR_009420
	Natural variant	286	1	M → V. Corresponds to variant rs1800748 [ dbSNP | Ensembl ].		VAR_009421
	Natural variant	292	1	L → P in TSC2. Corresponds to variant rs45517138 [ dbSNP | Ensembl ].		VAR_005646
	Natural variant	294	1	G → E in TSC2. Corresponds to variant rs45487497 [ dbSNP | Ensembl ].		VAR_009422
	Natural variant	304	1	W → WGMALW in TSC2.		VAR_009423
	Natural variant	309	1	L → Q.		VAR_009424
	Natural variant	320	1	L → F Could be associated with TSC2. Ref.4 Ref.38 Ref.39 Corresponds to variant rs1131825 [ dbSNP | Ensembl ].		VAR_009425
	Natural variant	331	1	N → K in TSC2. Corresponds to variant rs45517153 [ dbSNP | Ensembl ].		VAR_008021
	Natural variant	361	1	L → P in TSC2. Corresponds to variant rs45517147 [ dbSNP | Ensembl ].		VAR_009426
	Natural variant	365	1	Missing in TSC2.		VAR_009427
	Natural variant	367	1	R → Q. Ref.42 Corresponds to variant rs1800725 [ dbSNP | Ensembl ].		VAR_009428
	Natural variant	378	1	P → L. Corresponds to variant rs45517154 [ dbSNP | Ensembl ].		VAR_009429
	Natural variant	407	1	Y → D in TSC2.		VAR_005647
	Natural variant	440	1	G → S.		VAR_009430
	Natural variant	449	1	M → I in TSC2. Ref.29		VAR_005648
	Natural variant	463	1	I → V.		VAR_009431
	Natural variant	486	1	N → I in TSC2.		VAR_008022
	Natural variant	490	1	I → V.		VAR_008023
	Natural variant	525	1	N → S in TSC2.		VAR_009432
	Natural variant	536	1	A → V.		VAR_008024
	Natural variant	583	1	A → T. Corresponds to variant rs1800729 [ dbSNP | Ensembl ].		VAR_009433
	Natural variant	593	1	H → R.		VAR_009434
	Natural variant	599	1	K → M in TSC2; impairs repression of EIF4EBP1 phosphorylation. Ref.15		VAR_009435
	Natural variant	607	1	A → T. Ref.41		VAR_005649
	Natural variant	611	1	R → Q in TSC2 and LAM; impairs phosphorylation at S-1387, S-1418 and S-1420. Ref.19 Ref.38 Ref.40 Ref.42		VAR_005650
	Natural variant	611	1	R → W in TSC2; impairs phosphorylation at S-1387, S-1418 and S-1420. Ref.19 Ref.29 Ref.39 Ref.42		VAR_005651
	Natural variant	614	1	A → D in TSC2.		VAR_009436
	Natural variant	615	1	F → S.		VAR_008025
	Natural variant	619	1	L → F. Ref.4 Corresponds to variant rs1131826 [ dbSNP | Ensembl ].		VAR_060584
	Natural variant	647	1	D → N in TSC2; could be a polymorphism. Ref.38		VAR_009437
	Natural variant	694	1	Missing in TSC2.		VAR_009438
	Natural variant	696	1	C → Y in TSC2.		VAR_009439
	Natural variant	717	1	L → R in TSC2. Ref.35 Ref.38		VAR_009440
	Natural variant	769	1	V → E in TSC2; could be a polymorphism. Ref.38		VAR_009441
	Natural variant	802	1	S → R. Ref.1 Ref.4 Corresponds to variant rs1051621 [ dbSNP | Ensembl ].		VAR_060585
	Natural variant	816	1	P → L in TSC2.		VAR_008026
	Natural variant	826	1	L → M in TSC2.		VAR_005652
	Natural variant	862	1	A → V. Ref.41		VAR_018600
	Natural variant	895	1	M → V in TSC2.		VAR_009442
	Natural variant	905	1	R → Q in TSC2.		VAR_005653
	Natural variant	905	1	R → W in TSC2. Ref.39		VAR_005654
	Natural variant	963	1	V → M in TSC2; could be a polymorphism. Ref.38		VAR_009443
	Natural variant	1027	1	L → P in TSC2. Ref.42		VAR_022919
	Natural variant	1084	1	D → E in TSC2.		VAR_005655
	Natural variant	1141	1	A → V. Corresponds to variant rs34870424 [ dbSNP | Ensembl ].		VAR_057014
	Natural variant	1144	1	V → M in TSC2.		VAR_008027
	Natural variant	1200	1	R → W in TSC2.		VAR_005656
	Natural variant	1227	1	P → L in TSC2. Ref.29		VAR_005657
	Natural variant	1240	1	R → W in TSC2. Ref.29		VAR_005658
	Natural variant	1282	1	S → G.		VAR_009444
	Natural variant	1295	1	D → V in TSC2.		VAR_005659
	Natural variant	1315	1	P → S in TSC2.		VAR_008028
	Natural variant	1329	1	R → H in TSC2.		VAR_008029
	Natural variant	1341	1	S → R. Ref.42		VAR_022920
	Natural variant	1429	1	A → S. Ref.41		VAR_018601
	Natural variant	1450	1	P → R. Ref.41		VAR_018602
	Natural variant	1497	1	P → R in TSC2.		VAR_009445
	Natural variant	1498	1	S → N in TSC2.		VAR_009446
	Natural variant	1509	1	Missing in TSC2; could be a rare polymorphism.		VAR_005660
	Natural variant	1549	1	Y → C in TSC2.		VAR_005661
	Natural variant	1594	1	L → M in TSC2; could be a polymorphism. Ref.30		VAR_009447
	Natural variant	1614	1	Missing in TSC2.		VAR_005662
	Natural variant	1620	1	H → Y in TSC2.		VAR_009448
	Natural variant	1636	1	D → N. Ref.42		VAR_022921
	Natural variant	1643	1	N → I in TSC2.		VAR_005663
	Natural variant	1643	1	N → K in TSC2; Abolishes GAP activity. Ref.17 Ref.30		VAR_009449
	Natural variant	1650	1	Y → C in TSC2.		VAR_005664
	Natural variant	1651	1	N → S in TSC2; greatly reduces the ability to enhance the RHEB GTPase activity. Ref.15 Ref.17 Ref.30 Ref.41		VAR_009450
	Natural variant	1653	1	S → F in TSC2. Ref.41		VAR_018603
	Natural variant	1673	1	V → L. Ref.42		VAR_022922
	Natural variant	1675	1	P → L in TSC2. Ref.30 Ref.38 Ref.41		VAR_009451
	Natural variant	1681	1	N → K in TSC2; Abolishes GAP activity. Ref.17 Ref.30		VAR_009452
	Natural variant	1690	1	D → Y in TSC2.		VAR_005665
	Natural variant	1704	1	S → T in TSC2.		VAR_009453
	Natural variant	1709	1	P → L in TSC2.		VAR_008030
	Natural variant	1712	1	A → E in TSC2. Ref.29		VAR_005666
	Natural variant	1743	1	R → P in TSC2; Abolishes GAP activity. Ref.17		VAR_009454
	Natural variant	1743	1	R → Q in TSC2.		VAR_008031
	Natural variant	1744	1	L → P in TSC2. Ref.39		VAR_009455
	Natural variant	1746 – 1751	6	Missing in TSC2.		VAR_009456
	Natural variant	1750	1	L → F in TSC2.		VAR_005667
	Natural variant	1773	1	H → P in TSC2.		VAR_008032
	Natural variant	1774	1	S → T. Corresponds to variant rs9209 [ dbSNP | Ensembl ].		VAR_057015
	Natural variant	1783	1	E → Q in TSC2.		VAR_008033
	Natural variant	1787	1	G → S.		VAR_009457
	Natural variant	1791	1	G → S.		VAR_009458
Experimental info
	Mutagenesis	939	1	S → A: Inhibits insulin-stimulated phosphorylation and activation of S6K1; when associated with A-1462.
	Mutagenesis	1330	1	T → A: Abolishes AMPK-mediated phosphorylation; when associated with A-1448. Ref.16
	Mutagenesis	1448	1	S → A: Abolishes AMPK-mediated phosphorylation; when associated with A-1330. Ref.16
	Mutagenesis	1462	1	T → A: Inhibits insulin-stimulated phosphorylation and activation of S6K1; when associated with A-939.
	Mutagenesis	1637 – 1639	3	KKR → QQQ: Abolishes GAP activity. Ref.17
	Mutagenesis	1745	1	R → Q: Abolishes GAP activity. Ref.17
	Mutagenesis	1749 – 1751	3	RLR → QLQ: No effect. Ref.17
	Sequence conflict	187	1	N → S in BAG61344. Ref.6
	Sequence conflict	210	1	A → V in AAI50301. Ref.9
	Sequence conflict	335	1	S → P in BAG61344. Ref.6
	Sequence conflict	392	1	E → V in BAG58569. Ref.6
	Sequence conflict	422	1	S → P in BAG58569. Ref.6
	Sequence conflict	660	1	S → N in BAG61344. Ref.6
	Sequence conflict	704	1	K → E in AAI50301. Ref.9
	Sequence conflict	706	1	L → P in BAG58569. Ref.6
	Sequence conflict	1015	1	L → M in AAI50301. Ref.9
	Sequence conflict	1239	1	E → V in BAG61344. Ref.6
	Sequence conflict	1398	1	L → V in BAG61344. Ref.6
	Sequence conflict	1672	1	I → M in AAI50301. Ref.9
	Sequence conflict	1807	1	V → A in BAG61344. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified November 24, 2009. Version 2. Checksum: 7B915C46970D7D31	FASTA	1,807	200,608
	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
	Isoform 2 [UniParc]. Checksum: EECB8D3132AFFBA2	FASTA	1,764	195,847
	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 NERPKSRIQT SLTSASLGSA 970 980 990 1000 1010 1020 DENSVAQADD SLKNLHLELT ETCLDMMARY VFSNFTAVPK RSPVGEFLLA GGRTKTWLVG 1030 1040 1050 1060 1070 1080 NKLVTVTTSV GTGTRSLLGL DSGELQSGPE SSSSPGVHVR QTKEAPAKLE SQAGQQVSRG 1090 1100 1110 1120 1130 1140 ARDRVRSMSG GHGLRVGALD VPASQFLGSA TSPGPRTAPA AKPEKASAGT RVPVQEKTNL 1150 1160 1170 1180 1190 1200 AAYVPLLTQG WAEILVRRPT GNTSWLMSLE NPLSPFSSDI NNMPLQELSN ALMAAERFKE 1210 1220 1230 1240 1250 1260 HRDTALYKSL SVPAASTAKP PPLPRSNTVA SFSSLYQSSC QGQLHRSVSW ADSAVVMEEG 1270 1280 1290 1300 1310 1320 SPGEVPVLVE PPGLEDVEAA LGMDRRTDAY SRSSSVSSQE EKSLHAEELV GRGIPIERVV 1330 1340 1350 1360 1370 1380 SSEGGRPSVD LSFQPSQPLS KSSSSPELQT LQDILGDPGD KADVGRLSPE VKARSQSGTL 1390 1400 1410 1420 1430 1440 DGESAAWSAS GEDSRGQPEG PLPSSSPRSP SGLRPRGYTI SDSAPSRRGK RVERDALKSR 1450 1460 1470 1480 1490 1500 ATASNAEKVP GINPSFVFLQ LYHSPFFGDE SNKPILLPNE SQSFERSVQL LDQIPSYDTH 1510 1520 1530 1540 1550 1560 KIAVLYVGEG QSNSELAILS NEHGSYRYTE FLTGLGRLIE LKDCQPDKVY LGGLDVCGED 1570 1580 1590 1600 1610 1620 GQFTYCWHDD IMQAVFHIAT LMPTKDVDKH RCDKKRHLGN DFVSIVYNDS GEDFKLGTIK 1630 1640 1650 1660 1670 1680 GQFNFVHVIV TPLDYECNLV SLQCRKDMEG LVDTSVAKIV SDRNLPFVAR QMALHANMAS 1690 1700 1710 1720 1730 1740 QVHHSRSNPT DIYPSKWIAR LRHIKRLRQR ICEEAAYSNP SLPLVHPPSH SKAPAQTPAE 1750 1760 PTPGYEVGQR KRLISSVEDF TEFV
	Isoform 3 [UniParc]. Checksum: 9EBB34789D67D71C	FASTA	1,763	195,760
	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 NERPKRIQTS LTSASLGSAD 970 980 990 1000 1010 1020 ENSVAQADDS LKNLHLELTE TCLDMMARYV FSNFTAVPKR SPVGEFLLAG GRTKTWLVGN 1030 1040 1050 1060 1070 1080 KLVTVTTSVG TGTRSLLGLD SGELQSGPES SSSPGVHVRQ TKEAPAKLES QAGQQVSRGA 1090 1100 1110 1120 1130 1140 RDRVRSMSGG HGLRVGALDV PASQFLGSAT SPGPRTAPAA KPEKASAGTR VPVQEKTNLA 1150 1160 1170 1180 1190 1200 AYVPLLTQGW AEILVRRPTG NTSWLMSLEN PLSPFSSDIN NMPLQELSNA LMAAERFKEH 1210 1220 1230 1240 1250 1260 RDTALYKSLS VPAASTAKPP PLPRSNTVAS FSSLYQSSCQ GQLHRSVSWA DSAVVMEEGS 1270 1280 1290 1300 1310 1320 PGEVPVLVEP PGLEDVEAAL GMDRRTDAYS RSSSVSSQEE KSLHAEELVG RGIPIERVVS 1330 1340 1350 1360 1370 1380 SEGGRPSVDL SFQPSQPLSK SSSSPELQTL QDILGDPGDK ADVGRLSPEV KARSQSGTLD 1390 1400 1410 1420 1430 1440 GESAAWSASG EDSRGQPEGP LPSSSPRSPS GLRPRGYTIS DSAPSRRGKR VERDALKSRA 1450 1460 1470 1480 1490 1500 TASNAEKVPG INPSFVFLQL YHSPFFGDES NKPILLPNES QSFERSVQLL DQIPSYDTHK 1510 1520 1530 1540 1550 1560 IAVLYVGEGQ SNSELAILSN EHGSYRYTEF LTGLGRLIEL KDCQPDKVYL GGLDVCGEDG 1570 1580 1590 1600 1610 1620 QFTYCWHDDI MQAVFHIATL MPTKDVDKHR CDKKRHLGND FVSIVYNDSG EDFKLGTIKG 1630 1640 1650 1660 1670 1680 QFNFVHVIVT PLDYECNLVS LQCRKDMEGL VDTSVAKIVS DRNLPFVARQ MALHANMASQ 1690 1700 1710 1720 1730 1740 VHHSRSNPTD IYPSKWIARL RHIKRLRQRI CEEAAYSNPS LPLVHPPSHS KAPAQTPAEP 1750 1760 TPGYEVGQRK RLISSVEDFT EFV
	Isoform 4 [UniParc]. Checksum: 36A09DD2BBCD369A	FASTA	1,784	198,097
	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 TDSAVVMEEG SPGEVPVLVE PPGLEDVEAA LGMDRRTDAY SRSSSVSSQE 1330 1340 1350 1360 1370 1380 EKSLHAEELV GRGIPIERVV SSEGGRPSVD LSFQPSQPLS KSSSSPELQT LQDILGDPGD 1390 1400 1410 1420 1430 1440 KADVGRLSPE VKARSQSGTL DGESAAWSAS GEDSRGQPEG PLPSSSPRSP SGLRPRGYTI 1450 1460 1470 1480 1490 1500 SDSAPSRRGK RVERDALKSR ATASNAEKVP GINPSFVFLQ LYHSPFFGDE SNKPILLPNE 1510 1520 1530 1540 1550 1560 SQSFERSVQL LDQIPSYDTH KIAVLYVGEG QSNSELAILS NEHGSYRYTE FLTGLGRLIE 1570 1580 1590 1600 1610 1620 LKDCQPDKVY LGGLDVCGED GQFTYCWHDD IMQAVFHIAT LMPTKDVDKH RCDKKRHLGN 1630 1640 1650 1660 1670 1680 DFVSIVYNDS GEDFKLGTIK GQFNFVHVIV TPLDYECNLV SLQCRKDMEG LVDTSVAKIV 1690 1700 1710 1720 1730 1740 SDRNLPFVAR QMALHANMAS QVHHSRSNPT DIYPSKWIAR LRHIKRLRQR ICEEAAYSNP 1750 1760 1770 1780 SLPLVHPPSH SKAPAQTPAE PTPGYEVGQR KRLISSVEDF TEFV
	Isoform 5 [UniParc]. Checksum: A0886EF0FBE7652E	FASTA	1,740	193,249
	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 NERPKRIQTS LTSASLGSAD 970 980 990 1000 1010 1020 ENSVAQADDS LKNLHLELTE TCLDMMARYV FSNFTAVPKR SPVGEFLLAG GRTKTWLVGN 1030 1040 1050 1060 1070 1080 KLVTVTTSVG TGTRSLLGLD SGELQSGPES SSSPGVHVRQ TKEAPAKLES QAGQQVSRGA 1090 1100 1110 1120 1130 1140 RDRVRSMSGG HGLRVGALDV PASQFLGSAT SPGPRTAPAA KPEKASAGTR VPVQEKTNLA 1150 1160 1170 1180 1190 1200 AYVPLLTQGW AEILVRRPTG NTSWLMSLEN PLSPFSSDIN NMPLQELSNA LMAAERFKEH 1210 1220 1230 1240 1250 1260 RDTALYKSLS VPAASTAKPP PLPRSNTDSA VVMEEGSPGE VPVLVEPPGL EDVEAALGMD 1270 1280 1290 1300 1310 1320 RRTDAYSRSS SVSSQEEKSL HAEELVGRGI PIERVVSSEG GRPSVDLSFQ PSQPLSKSSS 1330 1340 1350 1360 1370 1380 SPELQTLQDI LGDPGDKADV GRLSPEVKAR SQSGTLDGES AAWSASGEDS RGQPEGPLPS 1390 1400 1410 1420 1430 1440 SSPRSPSGLR PRGYTISDSA PSRRGKRVER DALKSRATAS NAEKVPGINP SFVFLQLYHS 1450 1460 1470 1480 1490 1500 PFFGDESNKP ILLPNESQSF ERSVQLLDQI PSYDTHKIAV LYVGEGQSNS ELAILSNEHG 1510 1520 1530 1540 1550 1560 SYRYTEFLTG LGRLIELKDC QPDKVYLGGL DVCGEDGQFT YCWHDDIMQA VFHIATLMPT 1570 1580 1590 1600 1610 1620 KDVDKHRCDK KRHLGNDFVS IVYNDSGEDF KLGTIKGQFN FVHVIVTPLD YECNLVSLQC 1630 1640 1650 1660 1670 1680 RKDMEGLVDT SVAKIVSDRN LPFVARQMAL HANMASQVHH SRSNPTDIYP SKWIARLRHI 1690 1700 1710 1720 1730 1740 KRLRQRICEE AAYSNPSLPL VHPPSHSKAP AQTPAEPTPG YEVGQRKRLI SSVEDFTEFV
	Isoform 6 [UniParc]. Checksum: AD89389C5CDB4B2C	FASTA	1,704	189,298
	10 20 30 40 50 60 MAKPTSKDSG LKEKFKILLG LGTPRPNPRS AEGKQTEFII TAEILRELSM ECGLNNRIRM 70 80 90 100 110 120 IGQICEVAKT KKFEEGERLG VLRALFFKVI KDYPSNEDLH ERLEVFKALT DNGRHITYLE 130 140 150 160 170 180 EELADFVLQW MDVGLSSEFL LVLVNLVKFN SCYLDEYIAR MVQMICLLCV RTASSVDIEV 190 200 210 220 230 240 SLQVLDAVVC YNCLPAESLP LFIVTLCRTI NVKELCEPCW KLMRNLLGTH LGHSAIYNMC 250 260 270 280 290 300 HLMEDRAYME DAPLLRGAVF FVGMALWGAH RLYSLRNSPT SVLPSFYQAM ACPNEVVSYE 310 320 330 340 350 360 IVLSITRLIK KYRKELQVVA WDILLNIIER LLQQLQTLDS PELRTIVHDL LTTVEELCDQ 370 380 390 400 410 420 NEFHGSQERY FELVERCADQ RPESSLLNLI SYRAQSIHPA KDGWIQNLQA LMERFFRSES 430 440 450 460 470 480 RGAVRIKVLD VLSFVLLINR QFYEEELINS VVISQLSHIP EDKDHQVRKL ATQLLVDLAE 490 500 510 520 530 540 GCHTHHFNSL LDIIEKVMAR SLSPPPELEE RDVAAYSASL EDVKTAVLGL LVILQTKLYT 550 560 570 580 590 600 LPASHATRVY EMLVSHIQLH YKHSYTLPIA SSIRLQAFDF LLLLRADSLH RLGLPNKDGV 610 620 630 640 650 660 VRFSPYCVCD YMEPERGSEK KTSGPLSPPT GPPGPAPAGP AVRLGSVPYS LLFRVLLQCL 670 680 690 700 710 720 KQESDWKVLK LVLGRLPESL RYKVLIFTSP CSVDQLCSAL CSMLSGPKTL ERLRGAPEGF 730 740 750 760 770 780 SRTDLHLAVV PVLTALISYH NYLDKTKQRE MVYCLEQGLI HRCASQCVVA LSICSVEMPD 790 800 810 820 830 840 IIIKALPVLV VKLTHISATA SMAVPLLEFL STLARLPHLY RNFAAEQYAS VFAISLPYTN 850 860 870 880 890 900 PSKFNQYIVC LAHHVIAMWF IRCRLPFRKD FVPFITKGLR SNVLLSFDDT PEKDSFRARS 910 920 930 940 950 960 TSLNERPKSR IQTSLTSASL GSADENSVAQ ADDSLKNLHL ELTETCLDMM ARYVFSNFTA 970 980 990 1000 1010 1020 VPKRSPVGEF LLAGGRTKTW LVGNKLVTVT TSVGTGTRSL LGLDSGELQS GPESSSSPGV 1030 1040 1050 1060 1070 1080 HVRQTKEAPA KLESQAGQQV SRGARDRVRS MSGGHGLRVG ALDVPASQFL GSATSPGPRT 1090 1100 1110 1120 1130 1140 APAAKPEKAS AGTRVPVQEK TNLAAYVPLL TQGWAEILVR RPTGNTSWLM SLENPLSPFS 1150 1160 1170 1180 1190 1200 SDINNMPLQE LSNALMAAER FKEHRDTALY KSLSVPAAST AKPPPLPRSN TDSAVVMEEG 1210 1220 1230 1240 1250 1260 SPGEVPVLVE PPGLEDVEAA LGMDRRTDAY SRSSSVSSQE EKSLHAEELV GRGIPIERVV 1270 1280 1290 1300 1310 1320 SSEGGRPSVD LSFQPSQPLS KSSSSPELQT LQDILGDPGD KADVGRLSPE VKARSQSGTL 1330 1340 1350 1360 1370 1380 DGESAAWSAS GEDSRGQPEG PLPSSSPRSP SGLRPRGYTI SDSAPSRRGK RVERDALKSR 1390 1400 1410 1420 1430 1440 ATASNAEKVP GINPSFVFLQ LYHSPFFGDE SNKPILLPNE SQSFERSVQL LDQIPSYDTH 1450 1460 1470 1480 1490 1500 KIAVLYVGEG QSNSELAILS NEHGSYRYTE FLTGLGRLIE LKDCQPDKVY LGGLDVCGED 1510 1520 1530 1540 1550 1560 GQFTYCWHDD IMQAVFHIAT LMPTKDVDKH RCDKKRHLGN DFVSIVYNDS GEDFKLGTIK 1570 1580 1590 1600 1610 1620 GQFNFVHVIV TPLDYECNLV SLQCRKDMEG LVDTSVAKIV SDRNLPFVAR QMALHANMAS 1630 1640 1650 1660 1670 1680 QVHHSRSNPT DIYPSKWIAR LRHIKRLRQR ICEEAAYSNP SLPLVHPPSH SKAPAQTPAE 1690 1700 PTPGYEVGQR KRLISSVEDF TEFV

References

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[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. , 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. , 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. , 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. , 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 TSC2 MET-599 AND SER-1651.
[16]	"TSC2 mediates cellular energy response to control cell growth and survival." Inoki K., Zhu T., Guan K.L. Cell 115:577-590(2003) [PubMed: 14651849] [Abstract] Cited for: PHOSPHORYLATION AT THR-1330 AND SER-1448, MUTAGENESIS OF THR-1330 AND SER-1448.
[17]	"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 TSC2 LYS-1643; SER-1651; LYS-1681 AND PRO-1743.
[18]	"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: 15342917] [Abstract] Cited for: PHOSPHORYLATION AT SER-1798.
[19]	"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 TSC2 TRP-611 AND GLN-611.
[20]	"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.
[21]	"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: Cervix carcinoma.
[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: 16464865] [Abstract] Cited for: INTERACTION WITH HERC1 AND TSC1.
[23]	"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. Tissue: Cervix carcinoma.
[24]	"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. Tissue: Cervix carcinoma.
[25]	"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. Tissue: Cervix carcinoma.
[26]	"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. Tissue: Embryonic kidney.
[27]	"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: 18974095] [Abstract] Cited for: PHOSPHORYLATION BY DAPK1, INTERACTION WITH DAPK1.
[28]	"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: Leukemic T-cell.
[29]	"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 TSC2 ILE-449; TRP-611; LEU-1227; TRP-1240; PHE-1509 DEL AND GLU-1712.
[30]	"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 TSC2 PHE-1509 DEL; MET-1594; LYS-1643; SER-1651; LEU-1675 AND LYS-1681.
[31]	"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 TSC2.
[32]	"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 TSC2.
[33]	"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 TSC2.
[34]	"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 TSC2, VARIANTS.
[35]	"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 TSC2 ARG-717.
[36]	"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 TSC2, VARIANTS.
[37]	"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 TSC2, VARIANTS. Tissue: Blood and Lymphoblast.
[38]	"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 TSC2 ARG-137; GLN-611; ASN-647; ARG-717; GLU-769; MET-963 AND LEU-1675, VARIANT PHE-320, POSSIBLE ASSOCIATION WITH TSC.
[39]	"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 TSC2 TRP-611; TRP-905; PRO-1744 AND 1746-HIS--ARG-1751 DEL, VARIANT PHE-320. Tissue: Peripheral blood leukocyte.
[40]	"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.
[41]	"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 TSC2 SER-1651; PHE-1653; LEU-1675 AND 1746-HIS--ARG-1751 DEL, VARIANTS THR-607; VAL-862; SER-1429 AND ARG-1450.
[42]	"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 TSC2 GLN-611; TRP-611 AND PRO-1027, VARIANTS GLN-367; ARG-1341; ASN-1636 AND LEU-1673.
+	Additional computationally mapped references.

Web resources

Atlas of Genetics and Cytogenetics in Oncology and Haematology

GeneReviews

Cross-references

Sequence databases
EMBL GenBank DDBJ	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. 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.
IPI	IPI00028493. IPI00218881. IPI00218883. IPI00879496. IPI00952929. IPI00954095.
PIR	A49420.
RefSeq	NP_000539.2. NM_000548.3. NP_001070651.1. NM_001077183.1. NP_001107854.1. NM_001114382.1.
UniGene	Hs.90303.
3D structure databases
ProteinModelPortal	P49815.
SMR	P49815. Positions 1516-1725.
ModBase	Search...
Protein-protein interaction databases
IntAct	P49815. 6 interactions.
MINT	MINT-250244.
STRING	P49815.
PTM databases
PhosphoSite	P49815.
Polymorphism databases
DMDM	269849475.
Proteomic databases
PRIDE	P49815.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000219476; ENSP00000219476; ENSG00000103197.
GeneID	7249.
KEGG	hsa:7249.
UCSC	uc002con.1. human. uc010bsd.1. human.
Organism-specific databases
CTD	7249.
GeneCards	GC16P002097.
HGNC	HGNC:12363. TSC2.
HPA	CAB002225. HPA030409.
MIM	191092. gene. 606690. phenotype. 613254. phenotype.
neXtProt	NX_P49815.
Orphanet	88924. Autosomal dominant polycystic kidney disease type 1 with tuberous sclerosis. 538. Lymphangioleiomyomatosis. 805. Tuberous sclerosis.
PharmGKB	PA37035.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG18472.
GeneTree	ENSGT00390000017866.
HOGENOM	HBG714363.
HOVERGEN	HBG018005.
InParanoid	P49815.
OMA	GNTSWLM.
OrthoDB	EOG4N8R3W.
PhylomeDB	P49815.
Enzyme and pathway databases
Pathway_Interaction_DB	pi3kciaktpathway. Class I PI3K signaling events mediated by Akt. mtor_4pathway. mTOR signaling pathway. p38_mk2pathway. p38 signaling mediated by MAPKAP kinases.
Reactome	REACT_111102. Signal Transduction.
Gene expression databases
ArrayExpress	P49815.
Bgee	P49815.
CleanEx	HS_TSC2.
Genevestigator	P49815.
GermOnline	ENSG00000103197. Homo sapiens.
Family and domain databases
InterPro	IPR011989. ARM-like. IPR016024. ARM-type_fold. IPR000331. Rap_GAP. IPR003913. Tuberin. IPR018515. Tuberin-type_domain. IPR024584. Tuberin_N. [Graphical view]
Gene3D	G3DSA:1.25.10.10. ARM-like. 3 hits.
KO	K07207.
Pfam	PF11864. DUF3384. 2 hits. PF02145. Rap_GAP. 1 hit. PF03542. Tuberin. 1 hit. [Graphical view]
PRINTS	PR01431. TUBERIN.
SUPFAM	SSF48371. ARM-type_fold. 1 hit.
PROSITE	PS50085. RAPGAP. 1 hit. [Graphical view]
ProtoNet	Search...
Other
SOURCE	Search...

Entry information

Entry name

TSC2_HUMAN

Accession

Primary (citable) accession number: P49815
Secondary accession number(s): A7E2E2 , B4DIQ7, B4DRN2, C9J378, O75275, Q4LE71, Q8TAZ1

Entry history

Integrated into UniProtKB/Swiss-Prot:	October 1, 1996
Last sequence update:	November 24, 2009
Last modified:	January 25, 2012
This is version 134 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.