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
//