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Database: UniProt
Entry: E9PCX8_HUMAN
LinkDB: E9PCX8_HUMAN
Original site: E9PCX8_HUMAN 
ID   E9PCX8_HUMAN            Unreviewed;      1548 AA.
AC   E9PCX8;
DT   05-APR-2011, integrated into UniProtKB/TrEMBL.
DT   03-MAY-2023, sequence version 9.
DT   24-JAN-2024, entry version 86.
DE   SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSP00000414358.2};
GN   Name=TNS3 {ECO:0000313|Ensembl:ENSP00000414358.2};
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606 {ECO:0000313|Ensembl:ENSP00000414358.2, ECO:0000313|Proteomes:UP000005640};
RN   [1] {ECO:0000313|Ensembl:ENSP00000414358.2, ECO:0000313|Proteomes:UP000005640}
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX   PubMed=12853948; DOI=10.1038/nature01782;
RA   Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H.,
RA   Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K.,
RA   Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A.,
RA   Delehaunty K.D., Miner T.L., Nash W.E., Cordes M., Du H., Sun H.,
RA   Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A.,
RA   Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P.,
RA   Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M.,
RA   Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S.,
RA   Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R.,
RA   Strowmatt C., Latreille P., Miller N., Johnson D., Murray J.,
RA   Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W.,
RA   Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E.,
RA   Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A.,
RA   Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E.,
RA   Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E.,
RA   Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A.,
RA   Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A.,
RA   Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R.,
RA   McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H.,
RA   Wilson R.K.;
RT   "The DNA sequence of human chromosome 7.";
RL   Nature 424:157-164(2003).
RN   [2] {ECO:0007829|PubMed:18220336}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18220336; DOI=10.1021/pr0705441;
RA   Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.D., Yates J.R.;
RT   "Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient
RT   phosphoproteomic analysis.";
RL   J. Proteome Res. 7:1346-1351(2008).
RN   [3] {ECO:0007829|PubMed:18669648}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA   Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA   Elledge S.J., Gygi S.P.;
RT   "A quantitative atlas of mitotic phosphorylation.";
RL   Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN   [4] {ECO:0007829|PubMed:19413330}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=19413330; DOI=10.1021/ac9004309;
RA   Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.;
RT   "Lys-N and trypsin cover complementary parts of the phosphoproteome in a
RT   refined SCX-based approach.";
RL   Anal. Chem. 81:4493-4501(2009).
RN   [5] {ECO:0007829|PubMed:20068231}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA   Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA   Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT   "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT   site occupancy during mitosis.";
RL   Sci. Signal. 3:RA3-RA3(2010).
RN   [6] {ECO:0007829|PubMed:21269460}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA   Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Burckstummer T.,
RA   Bennett K.L., Superti-Furga G., Colinge J.;
RT   "Initial characterization of the human central proteome.";
RL   BMC Syst. Biol. 5:17-17(2011).
RN   [7] {ECO:0007829|PubMed:21406692}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA   Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA   Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT   "System-wide temporal characterization of the proteome and phosphoproteome
RT   of human embryonic stem cell differentiation.";
RL   Sci. Signal. 4:RS3-RS3(2011).
RN   [8] {ECO:0007829|PubMed:22814378}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA   Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA   Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA   Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT   "N-terminal acetylome analyses and functional insights of the N-terminal
RT   acetyltransferase NatB.";
RL   Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN   [9] {ECO:0007829|PubMed:23186163}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=23186163;
RA   Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA   Mohammed S.;
RT   "Toward a comprehensive characterization of a human cancer cell
RT   phosphoproteome.";
RL   J. Proteome Res. 12:260-271(2013).
RN   [10] {ECO:0007829|PubMed:24275569}
RP   IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA   Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA   Ye M., Zou H.;
RT   "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT   phosphoproteome.";
RL   J. Proteomics 96:253-262(2014).
RN   [11] {ECO:0000313|Ensembl:ENSP00000414358.2}
RP   IDENTIFICATION.
RG   Ensembl;
RL   Submitted (SEP-2023) to UniProtKB.
CC   -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC       {ECO:0000256|ARBA:ARBA00004246}.
CC   -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC       {ECO:0000256|ARBA:ARBA00007881}.
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DR   EMBL; AC073341; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; AC092000; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF510290; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; KF511035; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   RefSeq; XP_011513779.1; XM_011515477.2.
DR   AlphaFoldDB; E9PCX8; -.
DR   SMR; E9PCX8; -.
DR   MassIVE; E9PCX8; -.
DR   PeptideAtlas; E9PCX8; -.
DR   ProteomicsDB; 19540; -.
DR   Antibodypedia; 1019; 155 antibodies from 26 providers.
DR   Ensembl; ENST00000457718.6; ENSP00000414358.2; ENSG00000136205.18.
DR   UCSC; uc064dnf.1; human.
DR   HGNC; HGNC:21616; TNS3.
DR   VEuPathDB; HostDB:ENSG00000136205; -.
DR   GeneTree; ENSGT00940000156328; -.
DR   ChiTaRS; TNS3; human.
DR   Proteomes; UP000005640; Chromosome 7.
DR   Bgee; ENSG00000136205; Expressed in renal glomerulus and 204 other cell types or tissues.
DR   ExpressionAtlas; E9PCX8; baseline and differential.
DR   GO; GO:0042995; C:cell projection; IEA:UniProtKB-KW.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0005925; C:focal adhesion; IDA:HPA.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0004721; F:phosphoprotein phosphatase activity; IEA:UniProtKB-KW.
DR   GO; GO:0016311; P:dephosphorylation; IEA:InterPro.
DR   CDD; cd20889; C1_TNS3_v; 1.
DR   CDD; cd01213; PTB_tensin; 1.
DR   CDD; cd14561; PTP_tensin-3; 1.
DR   CDD; cd09927; SH2_Tensin_like; 1.
DR   Gene3D; 2.60.40.1110; -; 1.
DR   Gene3D; 3.30.60.20; -; 1.
DR   Gene3D; 2.30.29.30; Pleckstrin-homology domain (PH domain)/Phosphotyrosine-binding domain (PTB); 1.
DR   Gene3D; 3.90.190.10; Protein tyrosine phosphatase superfamily; 1.
DR   Gene3D; 3.30.505.10; SH2 domain; 1.
DR   InterPro; IPR046349; C1-like_sf.
DR   InterPro; IPR035892; C2_domain_sf.
DR   InterPro; IPR002219; PE/DAG-bd.
DR   InterPro; IPR011993; PH-like_dom_sf.
DR   InterPro; IPR029021; Prot-tyrosine_phosphatase-like.
DR   InterPro; IPR013625; PTB.
DR   InterPro; IPR006020; PTB/PI_dom.
DR   InterPro; IPR000980; SH2.
DR   InterPro; IPR036860; SH2_dom_sf.
DR   InterPro; IPR035012; Tensin-like_SH2.
DR   InterPro; IPR014020; Tensin_C2-dom.
DR   InterPro; IPR029023; Tensin_phosphatase.
DR   InterPro; IPR033929; Tensin_PTB.
DR   InterPro; IPR003595; Tyr_Pase_cat.
DR   InterPro; IPR000387; Tyr_Pase_dom.
DR   PANTHER; PTHR45734; TENSIN; 1.
DR   PANTHER; PTHR45734:SF5; TENSIN-3; 1.
DR   Pfam; PF00130; C1_1; 1.
DR   Pfam; PF08416; PTB; 1.
DR   Pfam; PF10409; PTEN_C2; 1.
DR   Pfam; PF00017; SH2; 1.
DR   SMART; SM00109; C1; 1.
DR   SMART; SM00462; PTB; 1.
DR   SMART; SM01326; PTEN_C2; 1.
DR   SMART; SM00404; PTPc_motif; 1.
DR   SMART; SM00252; SH2; 1.
DR   SUPFAM; SSF52799; (Phosphotyrosine protein) phosphatases II; 1.
DR   SUPFAM; SSF49562; C2 domain (Calcium/lipid-binding domain, CaLB); 1.
DR   SUPFAM; SSF57889; Cysteine-rich domain; 1.
DR   SUPFAM; SSF50729; PH domain-like; 1.
DR   SUPFAM; SSF55550; SH2 domain; 1.
DR   PROSITE; PS51182; C2_TENSIN; 1.
DR   PROSITE; PS51181; PPASE_TENSIN; 1.
DR   PROSITE; PS50001; SH2; 1.
DR   PROSITE; PS50056; TYR_PHOSPHATASE_2; 1.
DR   PROSITE; PS00479; ZF_DAG_PE_1; 1.
DR   PROSITE; PS50081; ZF_DAG_PE_2; 1.
PE   1: Evidence at protein level;
KW   Cell junction {ECO:0000256|ARBA:ARBA00022949};
KW   Cell projection {ECO:0000256|ARBA:ARBA00023273};
KW   Hydrolase {ECO:0000256|ARBA:ARBA00022912};
KW   Metal-binding {ECO:0000256|ARBA:ARBA00022723};
KW   Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW   Proteomics identification {ECO:0007829|EPD:E9PCX8,
KW   ECO:0007829|MaxQB:E9PCX8};
KW   Reference proteome {ECO:0000313|Proteomes:UP000005640};
KW   SH2 domain {ECO:0000256|ARBA:ARBA00022999, ECO:0000256|PROSITE-
KW   ProRule:PRU00191}; Zinc {ECO:0000256|ARBA:ARBA00022833}.
FT   DOMAIN          23..70
FT                   /note="Phorbol-ester/DAG-type"
FT                   /evidence="ECO:0000259|PROSITE:PS50081"
FT   DOMAIN          101..273
FT                   /note="Phosphatase tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51181"
FT   DOMAIN          206..262
FT                   /note="Tyrosine specific protein phosphatases"
FT                   /evidence="ECO:0000259|PROSITE:PS50056"
FT   DOMAIN          278..404
FT                   /note="C2 tensin-type"
FT                   /evidence="ECO:0000259|PROSITE:PS51182"
FT   DOMAIN          1275..1385
FT                   /note="SH2"
FT                   /evidence="ECO:0000259|PROSITE:PS50001"
FT   REGION          461..524
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          641..671
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          721..798
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          820..872
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          962..1084
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          1179..1230
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        479..501
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..747
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        822..836
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1013..1053
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        1213..1230
FT                   /note="Polar residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ   SEQUENCE   1548 AA;  166559 MW;  F0C01DF20CC9381F CRC64;
     MNWLCRNQDP NPPPQPEELT SSLHAFKNKA FKKSKVCGVC KQIIDGQGIS CRACKYSCHK
     KCEAKVVIPC GVQVRLEQAP GSSTLSSSLC RDKPLRPVIL SPTMEEGHGL DLTYITERII
     AVSFPAGCSE ESYLHNLQEV TRMLKSKHGD NYLVLNLSEK RYDLTKLNPK IMDVGWPELH
     APPLDKMCTI CKAQESWLNS NLQHVVVIHC RGGKGRIGVV ISSYMHFTNV SASADQALDR
     FAMKKFYDDK VSALMQPSQK RYVQFLSGLL SGSVKMNASP LFLHFVILHG TPNFDTGGVC
     RPFLKLYQAM QPVYTSGIYN VGPENPSRIC IVIEPAQLLK GDVMVKCYHK KYRSATRDVI
     FRLQFHTGAV QGYGLVFGKE DLDNASKDDR FPDYGKVELV FSATPEKIQG SEHLYNDHGV
     IVDYNTTDPL IRWDSYENLS ADGEVLHTQG PVDGSLYAKV RKKSSSDPGI PGGPQAIPAT
     NSPDHSDHTL SVSSDSGHST ASARTDKTEE RLAPGTRRGL SAQEKAELDQ LLSGFGLEDP
     GSSLKEMTDA RSKYSGTRHV VPAQVHVNGD AALKDRETDI LDDEMPHHDL HSVDSLGTLS
     SSEGPQSAHL GPFTCHKSSQ NSLLSDGFGS NVGEDPQGTL VPDLGLGMDG PYERERTFGS
     REPKQPQPLL RKPSVSAQMQ AYGQSSYSTQ TWVRQQQMVV AHQYSFAPDG EARLVSRCPA
     DNPGLVQAQP RVPLTPTRGT SSRVAVQRGV GSGPHPPDTQ QPSPSKAFKP RFPGDQVVNG
     AGPELSTGPS PGSPTLDIDQ SIEQLNRLIL ELDPTFEPIP THMNALGSQA NGSVSPDSVG
     GGLRASSRLP DTGEGPSRAT GRQGSSAEQP LGGRLRKLSL GQYDNDAGGQ LPFSKCAWGK
     AGVDYAPNLP PFPSPADVKE TMTPGYPQDL DIIDGRILSS KESMCSTPAF PVSPETPYVK
     TALRHPPFSP PEPPLSSPAS QHKGGREPRS CPETLTHAVG MSESPIGPKS TMLRADASST
     PSFQQAFASS CTISSNGPGQ RRESSSSAER QWVESSPKPM VSLLGSGRPT GSPLSAEFSG
     TRKDSPVLSC FPPSELQAPF HSHELSLAEP PDSLAPPSSQ AFLGFGTAPV GSGLPPEEDL
     GALLANSHGA SPTPSIPLTA TGAADNGFLS HNFLTVAPGH SSHHSPGLQG QGVTLPGQPP
     LPEKKRASEG DRSLGSVSPS SSGFSSPHSG STISIPFPNV LPDFSKASEA ASPLPDSPGD
     KLVIVKFVQD TSKFWYKADI SREQAIAMLK DKEPGSFIVR DSHSFRGAYG LAMKVATPPP
     SVLQLNKKAG DLANELVRHF LIECTPKGVR LKGCSNEPYF GSLTALVCQH SITPLALPCK
     LLIPERDPLE EIAESSPQTA ANSAAELLKQ GAACNVWYLN SVEMESLTGH QAIQKALSIT
     LVQEPPPVST VVHFKVSAQG ITLTDNQRKL FFRRHYPVNS VIFCALDPQD RKWIKDGPSS
     KVFGFVARKQ GSATDNVCHL FAEHDPEQPA SAIVNFVSKV MIGSPKKV
//
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