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Reactome (instancebrowser)
Reactome: A Curated Pathway Database
Details
IdentifierUniProt:P60484
DatabaseUniProt
SpeciesHomo sapiens
DescriptionrecommendedName: Phosphatidylinositol 3,4,5-trisphosphate 3-phosphatase and dual-specificity protein phosphatase PTEN ecNumber3.1.3.16/ecNumber ecNumber3.1.3.48/ecNumber ecNumber3.1.3.67/ecNumber alternativeName: Mutated in multiple advanced cancers 1 alternativeName: Phosphatase and tensin homolog
Links to corresponding entries in other databasesBioGPS Gene:5728
BioGPS Gene:731292
Brenda:3.1.3.16
Brenda:3.1.3.48
Brenda:3.1.3.67
CTD Gene:5728
CTD Gene:731292
DOCK Blaster:1D5R
EC:3.1.3.16
EC:3.1.3.48
EC:3.1.3.67
ENSEMBL:ENSG00000171862
GeneCards:P60484
HapMap:NM_000314
IntEnz:3.1.3.16
IntEnz:3.1.3.48
IntEnz:3.1.3.67
KEGG Gene:5728
NCBI Gene:5728
NCBI Gene:731292
OMIM:137800
OMIM:153480
OMIM:158350
OMIM:176807
OMIM:176920
OMIM:275355
OMIM:276950
OMIM:601728
OMIM:605309
OMIM:608089
Protein Data Bank:1D5R
RefSeq:NM_000314
RefSeq:NP_000305
UCSC human:P60484
UniProt:P60484
dbSNP Gene:5728
dbSNP Gene:731292
Other identifiers related to this sequencePTEN_HUMAN, B2R904, O00633, O02679, Q6ICT7, ENSG00000171862, ENST00000371953, ENSP00000361021, 1434_at, 204054_at, 217492_s_at, 225363_at, 204053_x_at, 211711_s_at, 217494_s_at, 227469_at, 39552_at, 39553_at, 31675_s_at, 64073_at, 58901_at, 91768_at, U92436_at, g4506248_3p_at, Hs.10712.1.A1_3p_at, Hs.278506.0.A1_3p_at, g13543309_3p_s_at, Hs.27865.0.S1_3p_at, Hs.278506.0.S1_3p_s_at, Hs.10712.1.A1_3p_s_at, A_32_P109637, A_24_P252785, A_32_P205139, A_24_P913115, A_23_P98085, A_32_P109632, A_32_P205144, A_32_P71234, CCDS31238, GE59570, AF017999, AF019083, U96180, U92436, U93051, AF143315, AF143312, AF143313, AF143314, AF000734, AF000726, AF000727, AF000728, AF000729, AF000730, AF000731, AF000732, AF000733, AF067844, CR450306, DQ073384, BC005821, EntrezGene:5728, EntrezGene:731292, GI_38505204-S, ILMN_90355, ILMN_25851, IPI00012587, IPI00305944, IPI00786886, MIM:601728, MIM:137800, MIM:153480, MIM:158350, MIM:176807, MIM:176920, MIM:275355, MIM:276950, MIM:605309, MIM:608089, OTTHUMT00000049241, 1D5R, AAB70558, AAC52017, AAB66902, AAC51182, AAC51183, AAD38372, AAC08699, AAD13528, CAG29302, AAY57327, AAH05821, NM_000314, XM_001130021, NP_000305, XP_001130021, Hs.500466, Hs.599624, Hs.606086, Hs.607341, O14781, O43460, P60484, O14781_HUMAN, O43460_HUMAN, PTEN_HUMAN, IPR000387, IPR000340, IPR014019, IPR014020
Molecules with this sequencePTEN [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R130G [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN C124S [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R130Q [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R130L [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R130P [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN C124R [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN C124F [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN C124Y [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R173H [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R173C [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R173P [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN S170N [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN S170R [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN S170I [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN S170G [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN H123Y [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN G129R [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN G129V [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN G129E [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN H93Y [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN H93R [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN H93A [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN H93D [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN H93Q [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R335* [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R130* [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
PTEN R233* [cytosol] UKENNBBCCddOOOOOOOOOORHGURPD
Component ofPTEN:Mg2+ [cytosol]
Represented by generalisation(s)PTEN Phosphatase Domain Missense Mutants [cytosol]
PTEN Truncation Mutants [cytosol]
PTEN Mutants [cytosol]
Processes where molecules and complexes with this sequence are involved

Immune System

Signal Transduction

Metabolism

Disease

Modifications in molecules with this sequenceL-arginine 130 replaced with glycine
L-cysteine 124 replaced with L-serine
L-arginine 130 replaced with L-glutamine
L-arginine 130 replaced with L-leucine
L-arginine 130 replaced with L-proline
L-cysteine 124 replaced with L-arginine
L-cysteine 124 replaced with L-phenylalanine
L-cysteine 124 replaced with L-tyrosine
L-arginine 173 replaced with L-histidine
L-arginine 173 replaced with L-proline
L-arginine 173 replaced with L-cysteine
L-serine 170 replaced with L-asparagine
L-serine 170 replaced with L-arginine
L-serine 170 replaced with L-isoleucine
L-serine 170 replaced with glycine
L-histidine 123 replaced with L-tyrosine
glycine 129 replaced with L-glutamic acid
glycine 129 replaced with L-arginine
glycine 129 replaced with L-valine
L-histidine 93 replaced with L-tyrosine
L-histidine 93 replaced with L-arginine
L-histidine 93 replaced with L-alanine
L-histidine 93 replaced with L-glutamine
L-histidine 93 replaced with L-aspartic acid
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