ID C9JHU5_HUMAN Unreviewed; 1534 AA.
AC C9JHU5;
DT 03-NOV-2009, integrated into UniProtKB/TrEMBL.
DT 03-MAY-2023, sequence version 2.
DT 27-MAR-2024, entry version 97.
DE SubName: Full=Tensin 3 {ECO:0000313|Ensembl:ENSP00000396914.2};
GN Name=TNS3 {ECO:0000313|Ensembl:ENSP00000396914.2};
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:ENSP00000396914.2, ECO:0000313|Proteomes:UP000005640};
RN [1] {ECO:0000313|Ensembl:ENSP00000396914.2, 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: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 [3] {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 [4] {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 [5] {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 [6] {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 [7] {ECO:0000313|Ensembl:ENSP00000396914.2}
RP IDENTIFICATION.
RG Ensembl;
RL Submitted (NOV-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}.
CC ---------------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution (CC BY 4.0) License
CC ---------------------------------------------------------------------------
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_011513780.1; XM_011515478.2.
DR AlphaFoldDB; C9JHU5; -.
DR SMR; C9JHU5; -.
DR MassIVE; C9JHU5; -.
DR MaxQB; C9JHU5; -.
DR PeptideAtlas; C9JHU5; -.
DR ProteomicsDB; 10255; -.
DR Antibodypedia; 1019; 155 antibodies from 26 providers.
DR Ensembl; ENST00000450444.6; ENSP00000396914.2; ENSG00000136205.18.
DR GeneID; 64759; -.
DR UCSC; uc064dng.1; human.
DR CTD; 64759; -.
DR HGNC; HGNC:21616; TNS3.
DR VEuPathDB; HostDB:ENSG00000136205; -.
DR GeneTree; ENSGT00940000156328; -.
DR HOGENOM; CLU_020105_2_1_1; -.
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; C9JHU5; 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 Phosphoprotein {ECO:0000256|ARBA:ARBA00022553};
KW Protein phosphatase {ECO:0000256|ARBA:ARBA00022912};
KW Proteomics identification {ECO:0007829|EPD:C9JHU5,
KW ECO:0007829|MaxQB:C9JHU5};
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 9..56
FT /note="Phorbol-ester/DAG-type"
FT /evidence="ECO:0000259|PROSITE:PS50081"
FT DOMAIN 87..259
FT /note="Phosphatase tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51181"
FT DOMAIN 192..248
FT /note="Tyrosine specific protein phosphatases"
FT /evidence="ECO:0000259|PROSITE:PS50056"
FT DOMAIN 264..390
FT /note="C2 tensin-type"
FT /evidence="ECO:0000259|PROSITE:PS51182"
FT DOMAIN 1261..1371
FT /note="SH2"
FT /evidence="ECO:0000259|PROSITE:PS50001"
FT REGION 447..510
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 627..657
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 707..784
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 806..858
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 948..1070
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 1165..1216
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 465..487
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 719..733
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 808..822
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 999..1039
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1199..1216
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
SQ SEQUENCE 1534 AA; 164898 MW; 0A2249D41A070CB7 CRC64;
MPEELTSSLH AFKNKAFKKS KVCGVCKQII DGQGISCRAC KYSCHKKCEA KVVIPCGVQV
RLEQAPGSST LSSSLCRDKP LRPVILSPTM EEGHGLDLTY ITERIIAVSF PAGCSEESYL
HNLQEVTRML KSKHGDNYLV LNLSEKRYDL TKLNPKIMDV GWPELHAPPL DKMCTICKAQ
ESWLNSNLQH VVVIHCRGGK GRIGVVISSY MHFTNVSASA DQALDRFAMK KFYDDKVSAL
MQPSQKRYVQ FLSGLLSGSV KMNASPLFLH FVILHGTPNF DTGGVCRPFL KLYQAMQPVY
TSGIYNVGPE NPSRICIVIE PAQLLKGDVM VKCYHKKYRS ATRDVIFRLQ FHTGAVQGYG
LVFGKEDLDN ASKDDRFPDY GKVELVFSAT PEKIQGSEHL YNDHGVIVDY NTTDPLIRWD
SYENLSADGE VLHTQGPVDG SLYAKVRKKS SSDPGIPGGP QAIPATNSPD HSDHTLSVSS
DSGHSTASAR TDKTEERLAP GTRRGLSAQE KAELDQLLSG FGLEDPGSSL KEMTDARSKY
SGTRHVVPAQ VHVNGDAALK DRETDILDDE MPHHDLHSVD SLGTLSSSEG PQSAHLGPFT
CHKSSQNSLL SDGFGSNVGE DPQGTLVPDL GLGMDGPYER ERTFGSREPK QPQPLLRKPS
VSAQMQAYGQ SSYSTQTWVR QQQMVVAHQY SFAPDGEARL VSRCPADNPG LVQAQPRVPL
TPTRGTSSRV AVQRGVGSGP HPPDTQQPSP SKAFKPRFPG DQVVNGAGPE LSTGPSPGSP
TLDIDQSIEQ LNRLILELDP TFEPIPTHMN ALGSQANGSV SPDSVGGGLR ASSRLPDTGE
GPSRATGRQG SSAEQPLGGR LRKLSLGQYD NDAGGQLPFS KCAWGKAGVD YAPNLPPFPS
PADVKETMTP GYPQDLDIID GRILSSKESM CSTPAFPVSP ETPYVKTALR HPPFSPPEPP
LSSPASQHKG GREPRSCPET LTHAVGMSES PIGPKSTMLR ADASSTPSFQ QAFASSCTIS
SNGPGQRRES SSSAERQWVE SSPKPMVSLL GSGRPTGSPL SAEFSGTRKD SPVLSCFPPS
ELQAPFHSHE LSLAEPPDSL APPSSQAFLG FGTAPVGSGL PPEEDLGALL ANSHGASPTP
SIPLTATGAA DNGFLSHNFL TVAPGHSSHH SPGLQGQGVT LPGQPPLPEK KRASEGDRSL
GSVSPSSSGF SSPHSGSTIS IPFPNVLPDF SKASEAASPL PDSPGDKLVI VKFVQDTSKF
WYKADISREQ AIAMLKDKEP GSFIVRDSHS FRGAYGLAMK VATPPPSVLQ LNKKAGDLAN
ELVRHFLIEC TPKGVRLKGC SNEPYFGSLT ALVCQHSITP LALPCKLLIP ERDPLEEIAE
SSPQTAANSA AELLKQGAAC NVWYLNSVEM ESLTGHQAIQ KALSITLVQE PPPVSTVVHF
KVSAQGITLT DNQRKLFFRR HYPVNSVIFC ALDPQDRKWI KDGPSSKVFG FVARKQGSAT
DNVCHLFAEH DPEQPASAIV NFVSKVMIGS PKKV
//
