TENS4_HUMAN
ID TENS4_HUMAN Reviewed; 715 AA.
AC Q8IZW8; A6NMJ7; Q71RB7; Q8WV64; Q96JV4;
DT 05-SEP-2006, integrated into UniProtKB/Swiss-Prot.
DT 05-MAY-2009, sequence version 3.
DT 03-AUG-2022, entry version 150.
DE RecName: Full=Tensin-4;
DE AltName: Full=C-terminal tensin-like protein;
DE Flags: Precursor;
GN Name=TNS4; Synonyms=CTEN; ORFNames=PP14434;
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;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION, TISSUE SPECIFICITY, AND
RP VARIANTS PRO-179 AND ASN-498.
RX PubMed=12154022;
RA Lo S.H., Lo T.B.;
RT "Cten, a COOH-terminal tensin-like protein with prostate restricted
RT expression, is down-regulated in prostate cancer.";
RL Cancer Res. 62:4217-4221(2002).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RX PubMed=15498874; DOI=10.1073/pnas.0404089101;
RA Wan D., Gong Y., Qin W., Zhang P., Li J., Wei L., Zhou X., Li H., Qiu X.,
RA Zhong F., He L., Yu J., Yao G., Jiang H., Qian L., Yu Y., Shu H., Chen X.,
RA Xu H., Guo M., Pan Z., Chen Y., Ge C., Yang S., Gu J.;
RT "Large-scale cDNA transfection screening for genes related to cancer
RT development and progression.";
RL Proc. Natl. Acad. Sci. U.S.A. 101:15724-15729(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT ASN-498.
RC TISSUE=Placenta;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R., Gnerre S.,
RA Goldstein S., Grafham D.V., Grocock R., Hafez N., Hagopian D.S., Hart E.,
RA Norman C.H., Humphray S., Jaffe D.B., Jones M., Kamal M., Khodiyar V.K.,
RA LaButti K., Laird G., Lehoczky J., Liu X., Lokyitsang T., Loveland J.,
RA Lui A., Macdonald P., Major J.E., Matthews L., Mauceli E., McCarroll S.A.,
RA Mihalev A.H., Mudge J., Nguyen C., Nicol R., O'Leary S.B., Osoegawa K.,
RA Schwartz D.C., Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in the
RT human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Brain;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP CLEAVAGE BY CASPASE-3, AND MUTAGENESIS OF ASP-506 AND ASP-570.
RX PubMed=15806167; DOI=10.1038/sj.onc.1208571;
RA Lo S.-S., Lo S.H., Lo S.H.;
RT "Cleavage of cten by caspase-3 during apoptosis.";
RL Oncogene 24:4311-4314(2005).
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-82 AND SER-248, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18691976; DOI=10.1016/j.molcel.2008.07.007;
RA Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R.,
RA Greff Z., Keri G., Stemmann O., Mann M.;
RT "Kinase-selective enrichment enables quantitative phosphoproteomics of the
RT kinome across the cell cycle.";
RL Mol. Cell 31:438-448(2008).
RN [8]
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., Buerckstuemmer 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 [9]
RP VARIANT [LARGE SCALE ANALYSIS] CYS-642.
RX PubMed=16959974; DOI=10.1126/science.1133427;
RA Sjoeblom T., Jones S., Wood L.D., Parsons D.W., Lin J., Barber T.D.,
RA Mandelker D., Leary R.J., Ptak J., Silliman N., Szabo S., Buckhaults P.,
RA Farrell C., Meeh P., Markowitz S.D., Willis J., Dawson D., Willson J.K.V.,
RA Gazdar A.F., Hartigan J., Wu L., Liu C., Parmigiani G., Park B.H.,
RA Bachman K.E., Papadopoulos N., Vogelstein B., Kinzler K.W.,
RA Velculescu V.E.;
RT "The consensus coding sequences of human breast and colorectal cancers.";
RL Science 314:268-274(2006).
CC -!- FUNCTION: May be involved in cell migration, cartilage development and
CC in linking signal transduction pathways to the cytoskeleton (By
CC similarity). May promote apoptosis, via its cleavage by caspase-3.
CC {ECO:0000250}.
CC -!- SUBUNIT: Binds to actin filaments and interacts with phosphotyrosine-
CC containing proteins. {ECO:0000250}.
CC -!- INTERACTION:
CC Q8IZW8; Q9H257-2: CARD9; NbExp=3; IntAct=EBI-7543499, EBI-11530605;
CC Q8IZW8; A8MQ03: CYSRT1; NbExp=3; IntAct=EBI-7543499, EBI-3867333;
CC Q8IZW8; O75031: HSF2BP; NbExp=3; IntAct=EBI-7543499, EBI-7116203;
CC Q8IZW8; Q674X7-2: KAZN; NbExp=3; IntAct=EBI-7543499, EBI-12024294;
CC Q8IZW8; Q9NWS0: PIH1D1; NbExp=3; IntAct=EBI-7543499, EBI-357318;
CC Q8IZW8; Q08209-2: PPP3CA; NbExp=5; IntAct=EBI-7543499, EBI-11959013;
CC Q8IZW8; Q15276: RABEP1; NbExp=3; IntAct=EBI-7543499, EBI-447043;
CC Q8IZW8; P19474: TRIM21; NbExp=3; IntAct=EBI-7543499, EBI-81290;
CC Q8IZW8; P14373: TRIM27; NbExp=3; IntAct=EBI-7543499, EBI-719493;
CC Q8IZW8; P42681: TXK; NbExp=3; IntAct=EBI-7543499, EBI-7877438;
CC Q8IZW8; Q9UGI0: ZRANB1; NbExp=3; IntAct=EBI-7543499, EBI-527853;
CC -!- SUBCELLULAR LOCATION: Cell junction, focal adhesion
CC {ECO:0000269|PubMed:12154022}. Cytoplasm, cytoskeleton
CC {ECO:0000269|PubMed:12154022}.
CC -!- TISSUE SPECIFICITY: Prostate and placenta. Down regulated in prostate
CC cancer. {ECO:0000269|PubMed:12154022}.
CC -!- PTM: Proteolytically cleaved by caspase-3 during apoptosis.
CC {ECO:0000269|PubMed:15806167}.
CC -!- SIMILARITY: Belongs to the PTEN phosphatase protein family.
CC {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAQ15257.1; Type=Frameshift; Evidence={ECO:0000305};
CC -!- WEB RESOURCE: Name=Atlas of Genetics and Cytogenetics in Oncology and
CC Haematology;
CC URL="http://atlasgeneticsoncology.org/Genes/TNS4ID40190ch17q21.html";
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DR EMBL; AF417488; AAN32666.1; -; mRNA.
DR EMBL; AF370421; AAQ15257.1; ALT_FRAME; mRNA.
DR EMBL; AK027856; BAB55413.1; -; mRNA.
DR EMBL; AC018629; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC018706; AAH18706.1; -; mRNA.
DR CCDS; CCDS11368.1; -.
DR RefSeq; NP_116254.4; NM_032865.5.
DR AlphaFoldDB; Q8IZW8; -.
DR SMR; Q8IZW8; -.
DR BioGRID; 124383; 42.
DR IntAct; Q8IZW8; 23.
DR MINT; Q8IZW8; -.
DR STRING; 9606.ENSP00000254051; -.
DR iPTMnet; Q8IZW8; -.
DR PhosphoSitePlus; Q8IZW8; -.
DR BioMuta; TNS4; -.
DR DMDM; 229463025; -.
DR EPD; Q8IZW8; -.
DR jPOST; Q8IZW8; -.
DR MassIVE; Q8IZW8; -.
DR MaxQB; Q8IZW8; -.
DR PaxDb; Q8IZW8; -.
DR PeptideAtlas; Q8IZW8; -.
DR PRIDE; Q8IZW8; -.
DR ProteomicsDB; 71438; -.
DR Antibodypedia; 16494; 218 antibodies from 27 providers.
DR DNASU; 84951; -.
DR Ensembl; ENST00000254051.11; ENSP00000254051.6; ENSG00000131746.13.
DR GeneID; 84951; -.
DR KEGG; hsa:84951; -.
DR MANE-Select; ENST00000254051.11; ENSP00000254051.6; NM_032865.6; NP_116254.4.
DR UCSC; uc010cxb.4; human.
DR CTD; 84951; -.
DR DisGeNET; 84951; -.
DR GeneCards; TNS4; -.
DR HGNC; HGNC:24352; TNS4.
DR HPA; ENSG00000131746; Tissue enhanced (salivary gland, skin, vagina).
DR MIM; 608385; gene.
DR neXtProt; NX_Q8IZW8; -.
DR OpenTargets; ENSG00000131746; -.
DR PharmGKB; PA142670717; -.
DR VEuPathDB; HostDB:ENSG00000131746; -.
DR eggNOG; KOG1930; Eukaryota.
DR GeneTree; ENSGT00940000160142; -.
DR HOGENOM; CLU_398985_0_0_1; -.
DR InParanoid; Q8IZW8; -.
DR OMA; SQPSMKF; -.
DR OrthoDB; 172407at2759; -.
DR PhylomeDB; Q8IZW8; -.
DR TreeFam; TF315996; -.
DR PathwayCommons; Q8IZW8; -.
DR Reactome; R-HSA-8875513; MET interacts with TNS proteins.
DR SignaLink; Q8IZW8; -.
DR BioGRID-ORCS; 84951; 10 hits in 1071 CRISPR screens.
DR ChiTaRS; TNS4; human.
DR GeneWiki; TNS4; -.
DR GenomeRNAi; 84951; -.
DR Pharos; Q8IZW8; Tbio.
DR PRO; PR:Q8IZW8; -.
DR Proteomes; UP000005640; Chromosome 17.
DR RNAct; Q8IZW8; protein.
DR Bgee; ENSG00000131746; Expressed in skin of abdomen and 145 other tissues.
DR ExpressionAtlas; Q8IZW8; baseline and differential.
DR Genevisible; Q8IZW8; HS.
DR GO; GO:0005856; C:cytoskeleton; IEA:UniProtKB-SubCell.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
DR GO; GO:0003779; F:actin binding; IEA:UniProtKB-KW.
DR GO; GO:0006915; P:apoptotic process; IEA:UniProtKB-KW.
DR GO; GO:0008104; P:protein localization; IDA:UniProtKB.
DR CDD; cd01213; PTB_tensin; 1.
DR Gene3D; 2.30.29.30; -; 1.
DR Gene3D; 3.30.505.10; -; 1.
DR InterPro; IPR011993; PH-like_dom_sf.
DR InterPro; IPR013625; PTB.
DR InterPro; IPR006020; PTB/PI_dom.
DR InterPro; IPR000980; SH2.
DR InterPro; IPR036860; SH2_dom_sf.
DR InterPro; IPR033929; Tensin_PTB.
DR Pfam; PF08416; PTB; 1.
DR Pfam; PF00017; SH2; 1.
DR SMART; SM00462; PTB; 1.
DR SMART; SM00252; SH2; 1.
DR SUPFAM; SSF55550; SSF55550; 1.
DR PROSITE; PS50001; SH2; 1.
PE 1: Evidence at protein level;
KW Actin-binding; Apoptosis; Cell junction; Cytoplasm; Cytoskeleton;
KW Phosphoprotein; Reference proteome; SH2 domain; Signal.
FT SIGNAL 1..18
FT /evidence="ECO:0000255"
FT CHAIN 19..715
FT /note="Tensin-4"
FT /id="PRO_0000248213"
FT DOMAIN 449..556
FT /note="SH2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00191"
FT DOMAIN 548..714
FT /note="Phosphatase tensin-type"
FT REGION 159..183
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 195..251
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 291..364
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 376..435
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 161..176
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 291..346
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 389..424
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT SITE 570..571
FT /note="Cleavage; by caspase-3"
FT MOD_RES 82
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT MOD_RES 248
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18691976"
FT VARIANT 179
FT /note="L -> P (in dbSNP:rs3764424)"
FT /evidence="ECO:0000269|PubMed:12154022"
FT /id="VAR_027264"
FT VARIANT 327
FT /note="T -> K (in dbSNP:rs33923045)"
FT /id="VAR_055292"
FT VARIANT 498
FT /note="S -> N (in dbSNP:rs2290207)"
FT /evidence="ECO:0000269|PubMed:12154022,
FT ECO:0000269|PubMed:14702039"
FT /id="VAR_027265"
FT VARIANT 642
FT /note="R -> C (in a colorectal cancer sample; somatic
FT mutation; dbSNP:rs148022611)"
FT /evidence="ECO:0000269|PubMed:16959974"
FT /id="VAR_036515"
FT MUTAGEN 506
FT /note="D->A: No effect on cleavage by caspase-3."
FT /evidence="ECO:0000269|PubMed:15806167"
FT MUTAGEN 570
FT /note="D->A: Abolishes cleavage by caspase-3."
FT /evidence="ECO:0000269|PubMed:15806167"
FT CONFLICT 163
FT /note="G -> W (in Ref. 1; AAN32666)"
FT /evidence="ECO:0000305"
FT CONFLICT 360
FT /note="S -> I (in Ref. 1; AAN32666 and 3; BAB55413)"
FT /evidence="ECO:0000305"
FT CONFLICT 623
FT /note="K -> E (in Ref. 1; AAN32666 and 3; BAB55413)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 715 AA; 76764 MW; E6AD7CB6B6DDA5D2 CRC64;
MSQVMSSPLL AGGHAVSLAP CDEPRRTLHP APSPSLPPQC SYYTTEGWGA QALMAPVPCM
GPPGRLQQAP QVEAKATCFL PSPGEKALGT PEDLDSYIDF SLESLNQMIL ELDPTFQLLP
PGTGGSQAEL AQSTMSMRKK EESEALDIKY IEVTSARSRC HDGPQHCSSP SVTPPFGSLR
SGGLLLSRDV PRETRSSSES LIFSGNQGRG HQRPLPPSEG LSPRPPNSPS ISIPCMGSKA
SSPHGLGSPL VASPRLEKRL GGLAPQRGSR ISVLSASPVS DVSYMFGSSQ SLLHSSNSSH
QSSSRSLESP ANSSSSLHSL GSVSLCTRPS DFQAPRNPTL TMGQPRTPHS PPLAKEHASS
CPPSITNSMV DIPIVLINGC PEPGSSPPQR TPGHQNSVQP GAASPSNPCP ATRSNSQTLS
DAPFTTCPEG PARDMQPTMK FVMDTSKYWF KPNITREQAI ELLRKEEPGA FVIRDSSSYR
GSFGLALKVQ EVPASAQSRP GEDSNDLIRH FLIESSAKGV HLKGADEEPY FGSLSAFVCQ
HSIMALALPC KLTIPQRELG GADGASDSTD SPASCQKKSA GCHTLYLSSV SVETLTGALA
VQKAISTTFE RDILPTPTVV HFKVTEQGIT LTDVQRKVFF RRHYPLTTLR FCGMDPEQRK
WQKYCKPSWI FGFVAKSQTE PQENVCHLFA EYDMVQPASQ VIGLVTALLQ DAERM
