Full text data of TIPRL
TIPRL
[Confidence: low (only semi-automatic identification from reviews)]
TIP41-like protein (Putative MAPK-activating protein PM10; Type 2A-interacting protein; TIP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
TIP41-like protein (Putative MAPK-activating protein PM10; Type 2A-interacting protein; TIP)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
O75663
ID TIPRL_HUMAN Reviewed; 272 AA.
AC O75663; B2R8V3; Q5HYB2; Q8IZ86;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1999, sequence version 2.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=TIP41-like protein;
DE AltName: Full=Putative MAPK-activating protein PM10;
DE AltName: Full=Type 2A-interacting protein;
DE Short=TIP;
GN Name=TIPRL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Rhodes S.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-272 (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP INTERACTION WITH PPP2CB; PPP4C AND PPP6C.
RX PubMed=16085932; DOI=10.1074/mcp.M500231-MCP200;
RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R.,
RA Fields S., Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT "A novel, evolutionarily conserved protein phosphatase complex
RT involved in cisplatin sensitivity.";
RL Mol. Cell. Proteomics 4:1725-1740(2005).
RN [9]
RP INTERACTION WITH PPP2CA; PPP2CB; PPP4C; PPP6C AND IGBP1, SUBUNIT,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-71; TYR-79; ILE-136;
RP MET-196 AND ASP-198.
RX PubMed=17944932; DOI=10.1111/j.1742-4658.2007.06112.x;
RA Smetana J.H., Zanchin N.I.;
RT "Interaction analysis of the heterotrimer formed by the phosphatase 2A
RT catalytic subunit, alpha4 and the mammalian ortholog of yeast Tip41
RT (TIPRL).";
RL FEBS J. 274:5891-5904(2007).
RN [10]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), AND INTERACTION WITH
RP PPP2CA; PPP4C AND PPP6C.
RX PubMed=17384681; DOI=10.1038/sj.onc.1210406;
RA McConnell J.L., Gomez R.J., McCorvey L.R., Law B.K., Wadzinski B.E.;
RT "Identification of a PP2A-interacting protein that functions as a
RT negative regulator of phosphatase activity in the ATM/ATR signaling
RT pathway.";
RL Oncogene 26:6021-6030(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be a allosteric regulator of serine/threonine-
CC protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic
CC activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL
CC complex does not show phosphatase activity. May play a role in the
CC regulation of ATM/ATR signaling pathway controlling DNA
CC replication and repair.
CC -!- SUBUNIT: Isoform 1 interacts with PPP2CA. Isoform 2 does not
CC interact with PPP2CA. Interacts with PPP2CB, PPP4C and PPP6C.
CC Interacts with IGBP1; the interaction is dependent on PPP2CA.
CC Associates with a protein phosphatase 2A PP2A(C):alpha-4 complex.
CC -!- INTERACTION:
CC P78318:IGBP1; NbExp=2; IntAct=EBI-1054735, EBI-1055954;
CC P67775:PPP2CA; NbExp=3; IntAct=EBI-1054735, EBI-712311;
CC P63331:Ppp2ca (xeno); NbExp=3; IntAct=EBI-1054735, EBI-7050205;
CC P60510:PPP4C; NbExp=3; IntAct=EBI-1054735, EBI-1046072;
CC O00743:PPP6C; NbExp=4; IntAct=EBI-1054735, EBI-359751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75663-1; Sequence=Displayed;
CC Name=2; Synonyms=TIP_i2;
CC IsoId=O75663-2; Sequence=VSP_027883, VSP_027884;
CC -!- SIMILARITY: Belongs to the TIP41 family.
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DR EMBL; AL049670; CAB41244.1; -; mRNA.
DR EMBL; AB097034; BAC77387.1; -; mRNA.
DR EMBL; AK313520; BAG36300.1; -; mRNA.
DR EMBL; AL021397; CAA16171.1; -; Genomic_DNA.
DR EMBL; AL021397; CAI22473.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90821.1; -; Genomic_DNA.
DR EMBL; BC009506; AAH09506.1; -; mRNA.
DR EMBL; BX648646; CAI46265.1; -; Transcribed_RNA.
DR RefSeq; NP_001026970.1; NM_001031800.1.
DR RefSeq; NP_690866.1; NM_152902.3.
DR UniGene; Hs.209431; -.
DR ProteinModelPortal; O75663; -.
DR IntAct; O75663; 10.
DR MINT; MINT-7002837; -.
DR STRING; 9606.ENSP00000356807; -.
DR PhosphoSite; O75663; -.
DR PaxDb; O75663; -.
DR PeptideAtlas; O75663; -.
DR PRIDE; O75663; -.
DR Ensembl; ENST00000367830; ENSP00000356804; ENSG00000143155.
DR Ensembl; ENST00000367833; ENSP00000356807; ENSG00000143155.
DR GeneID; 261726; -.
DR KEGG; hsa:261726; -.
DR UCSC; uc001gfg.3; human.
DR CTD; 261726; -.
DR GeneCards; GC01P168148; -.
DR HGNC; HGNC:30231; TIPRL.
DR HPA; HPA027995; -.
DR MIM; 611807; gene.
DR neXtProt; NX_O75663; -.
DR PharmGKB; PA142670811; -.
DR eggNOG; NOG263659; -.
DR HOGENOM; HOG000213547; -.
DR HOVERGEN; HBG053157; -.
DR InParanoid; O75663; -.
DR KO; K17607; -.
DR OMA; EMLFGDN; -.
DR OrthoDB; EOG72RN01; -.
DR PhylomeDB; O75663; -.
DR ChiTaRS; TIPRL; human.
DR GenomeRNAi; 261726; -.
DR NextBio; 93221; -.
DR PRO; PR:O75663; -.
DR Bgee; O75663; -.
DR CleanEx; HS_TIPRL; -.
DR Genevestigator; O75663; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:0034048; P:negative regulation of protein phosphatase type 2A activity; IDA:UniProtKB.
DR InterPro; IPR007303; TIP41-like.
DR Pfam; PF04176; TIP41; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Reference proteome.
FT CHAIN 1 272 TIP41-like protein.
FT /FTId=PRO_0000301853.
FT REGION 173 272 Interaction with PPP2CA.
FT MOD_RES 106 106 N6-acetyllysine.
FT VAR_SEQ 173 178 RVMPSS -> PGGGHL (in isoform 2).
FT /FTId=VSP_027883.
FT VAR_SEQ 179 272 Missing (in isoform 2).
FT /FTId=VSP_027884.
FT MUTAGEN 71 71 D->L: Abolishes interaction with PPP2CA,
FT PPP2CB and PPP4C.
FT MUTAGEN 79 79 Y->H: Diminishes interaction with PPP2CA.
FT MUTAGEN 136 136 I->T: Abolishes interaction with PPP2CA,
FT PPP2CB and PPP4C.
FT MUTAGEN 196 196 M->V: Abolishes interaction with PPP2CA,
FT PPP2CB and PPP4C.
FT MUTAGEN 198 198 D->N: Abolishes interaction with PPP2CA,
FT PPP2CB and PPP4C.
SQ SEQUENCE 272 AA; 31444 MW; 23B730E0BC27DCEA CRC64;
MMIHGFQSSH RDFCFGPWKL TASKTHIMKS ADVEKLADEL HMPSLPEMMF GDNVLRIQHG
SGFGIEFNAT DALRCVNNYQ GMLKVACAEE WQESRTEGEH SKEVIKPYDW TYTTDYKGTL
LGESLKLKVV PTTDHIDTEK LKAREQIKFF EEVLLFEDEL HDHGVSSLSV KIRVMPSSFF
LLLRFFLRID GVLIRMNDTR LYHEADKTYM LREYTSRESK ISSLMHVPPS LFTEPNEISQ
YLPIKEAVCE KLIFPERIDP NPADSQKSTQ VE
//
ID TIPRL_HUMAN Reviewed; 272 AA.
AC O75663; B2R8V3; Q5HYB2; Q8IZ86;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JAN-1999, sequence version 2.
DT 22-JAN-2014, entry version 94.
DE RecName: Full=TIP41-like protein;
DE AltName: Full=Putative MAPK-activating protein PM10;
DE AltName: Full=Type 2A-interacting protein;
DE Short=TIP;
GN Name=TIPRL;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Rhodes S.;
RL Submitted (APR-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lung fibroblast;
RX PubMed=12761501; DOI=10.1038/sj.onc.1206406;
RA Matsuda A., Suzuki Y., Honda G., Muramatsu S., Matsuzaki O.,
RA Nagano Y., Doi T., Shimotohno K., Harada T., Nishida E., Hayashi H.,
RA Sugano S.;
RT "Large-scale identification and characterization of human genes that
RT activate NF-kappaB and MAPK signaling pathways.";
RL Oncogene 22:3307-3318(2003).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D.,
RA Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A.,
RA Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F.,
RA McDonald L., Evans R., Phillips K., Atkinson A., Cooper R., Jones C.,
RA Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P.,
RA Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K.,
RA Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G.,
RA Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D.,
RA Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G.,
RA Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J.,
RA Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R.,
RA Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D.,
RA Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G.,
RA Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M.,
RA Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J.,
RA Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M.,
RA Loveland J., Lovell J., Lush M.J., Lyne R., Martin S.,
RA Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S.,
RA Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C.,
RA Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z.,
RA Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E.,
RA Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A.,
RA Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R.,
RA Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V.,
RA Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Muscle;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 205-272 (ISOFORM 1).
RC TISSUE=Fetal kidney;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
RA Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
RA Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [8]
RP INTERACTION WITH PPP2CB; PPP4C AND PPP6C.
RX PubMed=16085932; DOI=10.1074/mcp.M500231-MCP200;
RA Gingras A.-C., Caballero M., Zarske M., Sanchez A., Hazbun T.R.,
RA Fields S., Sonenberg N., Hafen E., Raught B., Aebersold R.;
RT "A novel, evolutionarily conserved protein phosphatase complex
RT involved in cisplatin sensitivity.";
RL Mol. Cell. Proteomics 4:1725-1740(2005).
RN [9]
RP INTERACTION WITH PPP2CA; PPP2CB; PPP4C; PPP6C AND IGBP1, SUBUNIT,
RP SUBCELLULAR LOCATION, AND MUTAGENESIS OF ASP-71; TYR-79; ILE-136;
RP MET-196 AND ASP-198.
RX PubMed=17944932; DOI=10.1111/j.1742-4658.2007.06112.x;
RA Smetana J.H., Zanchin N.I.;
RT "Interaction analysis of the heterotrimer formed by the phosphatase 2A
RT catalytic subunit, alpha4 and the mammalian ortholog of yeast Tip41
RT (TIPRL).";
RL FEBS J. 274:5891-5904(2007).
RN [10]
RP FUNCTION, ALTERNATIVE SPLICING (ISOFORM 2), AND INTERACTION WITH
RP PPP2CA; PPP4C AND PPP6C.
RX PubMed=17384681; DOI=10.1038/sj.onc.1210406;
RA McConnell J.L., Gomez R.J., McCorvey L.R., Law B.K., Wadzinski B.E.;
RT "Identification of a PP2A-interacting protein that functions as a
RT negative regulator of phosphatase activity in the ATM/ATR signaling
RT pathway.";
RL Oncogene 26:6021-6030(2007).
RN [11]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-106, AND MASS SPECTROMETRY.
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
RA Walther T.C., Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [12]
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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: May be a allosteric regulator of serine/threonine-
CC protein phosphatase 2A (PP2A). Isoform 1 inhibits catalytic
CC activity of the PP2A(D) core complex in vitro. The PP2A(C):TIPRL
CC complex does not show phosphatase activity. May play a role in the
CC regulation of ATM/ATR signaling pathway controlling DNA
CC replication and repair.
CC -!- SUBUNIT: Isoform 1 interacts with PPP2CA. Isoform 2 does not
CC interact with PPP2CA. Interacts with PPP2CB, PPP4C and PPP6C.
CC Interacts with IGBP1; the interaction is dependent on PPP2CA.
CC Associates with a protein phosphatase 2A PP2A(C):alpha-4 complex.
CC -!- INTERACTION:
CC P78318:IGBP1; NbExp=2; IntAct=EBI-1054735, EBI-1055954;
CC P67775:PPP2CA; NbExp=3; IntAct=EBI-1054735, EBI-712311;
CC P63331:Ppp2ca (xeno); NbExp=3; IntAct=EBI-1054735, EBI-7050205;
CC P60510:PPP4C; NbExp=3; IntAct=EBI-1054735, EBI-1046072;
CC O00743:PPP6C; NbExp=4; IntAct=EBI-1054735, EBI-359751;
CC -!- SUBCELLULAR LOCATION: Cytoplasm.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=O75663-1; Sequence=Displayed;
CC Name=2; Synonyms=TIP_i2;
CC IsoId=O75663-2; Sequence=VSP_027883, VSP_027884;
CC -!- SIMILARITY: Belongs to the TIP41 family.
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DR EMBL; AL049670; CAB41244.1; -; mRNA.
DR EMBL; AB097034; BAC77387.1; -; mRNA.
DR EMBL; AK313520; BAG36300.1; -; mRNA.
DR EMBL; AL021397; CAA16171.1; -; Genomic_DNA.
DR EMBL; AL021397; CAI22473.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90821.1; -; Genomic_DNA.
DR EMBL; BC009506; AAH09506.1; -; mRNA.
DR EMBL; BX648646; CAI46265.1; -; Transcribed_RNA.
DR RefSeq; NP_001026970.1; NM_001031800.1.
DR RefSeq; NP_690866.1; NM_152902.3.
DR UniGene; Hs.209431; -.
DR ProteinModelPortal; O75663; -.
DR IntAct; O75663; 10.
DR MINT; MINT-7002837; -.
DR STRING; 9606.ENSP00000356807; -.
DR PhosphoSite; O75663; -.
DR PaxDb; O75663; -.
DR PeptideAtlas; O75663; -.
DR PRIDE; O75663; -.
DR Ensembl; ENST00000367830; ENSP00000356804; ENSG00000143155.
DR Ensembl; ENST00000367833; ENSP00000356807; ENSG00000143155.
DR GeneID; 261726; -.
DR KEGG; hsa:261726; -.
DR UCSC; uc001gfg.3; human.
DR CTD; 261726; -.
DR GeneCards; GC01P168148; -.
DR HGNC; HGNC:30231; TIPRL.
DR HPA; HPA027995; -.
DR MIM; 611807; gene.
DR neXtProt; NX_O75663; -.
DR PharmGKB; PA142670811; -.
DR eggNOG; NOG263659; -.
DR HOGENOM; HOG000213547; -.
DR HOVERGEN; HBG053157; -.
DR InParanoid; O75663; -.
DR KO; K17607; -.
DR OMA; EMLFGDN; -.
DR OrthoDB; EOG72RN01; -.
DR PhylomeDB; O75663; -.
DR ChiTaRS; TIPRL; human.
DR GenomeRNAi; 261726; -.
DR NextBio; 93221; -.
DR PRO; PR:O75663; -.
DR Bgee; O75663; -.
DR CleanEx; HS_TIPRL; -.
DR Genevestigator; O75663; -.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0000077; P:DNA damage checkpoint; IMP:UniProtKB.
DR GO; GO:0034048; P:negative regulation of protein phosphatase type 2A activity; IDA:UniProtKB.
DR InterPro; IPR007303; TIP41-like.
DR Pfam; PF04176; TIP41; 1.
PE 1: Evidence at protein level;
KW Acetylation; Alternative splicing; Complete proteome; Cytoplasm;
KW Reference proteome.
FT CHAIN 1 272 TIP41-like protein.
FT /FTId=PRO_0000301853.
FT REGION 173 272 Interaction with PPP2CA.
FT MOD_RES 106 106 N6-acetyllysine.
FT VAR_SEQ 173 178 RVMPSS -> PGGGHL (in isoform 2).
FT /FTId=VSP_027883.
FT VAR_SEQ 179 272 Missing (in isoform 2).
FT /FTId=VSP_027884.
FT MUTAGEN 71 71 D->L: Abolishes interaction with PPP2CA,
FT PPP2CB and PPP4C.
FT MUTAGEN 79 79 Y->H: Diminishes interaction with PPP2CA.
FT MUTAGEN 136 136 I->T: Abolishes interaction with PPP2CA,
FT PPP2CB and PPP4C.
FT MUTAGEN 196 196 M->V: Abolishes interaction with PPP2CA,
FT PPP2CB and PPP4C.
FT MUTAGEN 198 198 D->N: Abolishes interaction with PPP2CA,
FT PPP2CB and PPP4C.
SQ SEQUENCE 272 AA; 31444 MW; 23B730E0BC27DCEA CRC64;
MMIHGFQSSH RDFCFGPWKL TASKTHIMKS ADVEKLADEL HMPSLPEMMF GDNVLRIQHG
SGFGIEFNAT DALRCVNNYQ GMLKVACAEE WQESRTEGEH SKEVIKPYDW TYTTDYKGTL
LGESLKLKVV PTTDHIDTEK LKAREQIKFF EEVLLFEDEL HDHGVSSLSV KIRVMPSSFF
LLLRFFLRID GVLIRMNDTR LYHEADKTYM LREYTSRESK ISSLMHVPPS LFTEPNEISQ
YLPIKEAVCE KLIFPERIDP NPADSQKSTQ VE
//
MIM
611807
*RECORD*
*FIELD* NO
611807
*FIELD* TI
*611807 TIP41-LIKE PROTEIN; TIPRL
;;TIP41, S. CEREVISIAE, HOMOLOG OF; TIP41;;
PROTEIN PHOSPHATASE 2A-INTERACTING PROTEIN; TIP
read more*FIELD* TX
DESCRIPTION
TIPRL is an inhibitory regulator of protein phosphatase-2A (PP2A) (see
PPP2CA; 176915), PP4 (see PPP4C; 602035), and PP6 (see PPP6C; 612725)
(McConnell et al., 2007).
CLONING
By database analysis, Jacinto et al. (2001) identified human TIPRL as a
homolog of yeast Tip41. TIPRL shares 35% amino acid identity with the
yeast protein.
McConnell et al. (2007) cloned human TIPRL, which they called TIP, from
a T-cell lymphoma cDNA library. The predicted protein contains 272 amino
acids. They also cloned a TIP splice variant that encodes a C-terminally
truncated protein (TIP isoform-2) that shares the first 172 amino acids
with TIP, but ends with 6 unique amino acids. Immunoblot analysis showed
ubiquitous expression of a 33-kD TIP protein.
GENE FUNCTION
Using immunoprecipitation analysis, McConnell et al. (2007) found that,
unlike yeast Tip41, human TIP did not interact with alpha-4 (IGBP1;
300139), the human homolog of yeast Tap42, in the presence of rapamycin.
Instead, TIP interacted with the catalytic subunits of PP2A, PP4, and
PP6 in a rapamycin-independent manner. TIP isoform-2 did not interact
with PP2A, suggesting that the C terminus of TIP is important for PP2A
binding. Incubation of PP2A with TIP, but not TIP isoform-2, resulted in
dose-dependent inhibition of PP2A phosphatase activity. Cells in which
TIP was depleted by small interfering RNA exhibited decreased
phosphorylation of a 32-kD substrate of ATM (607585)/ATR (601215)
kinases. McConnell et al. (2007) concluded that TIP is an inhibitory
regulator of PP2A and that the TIP/PP2A complex has a role within the
ATM/ATR signaling pathway controlling DNA replication and repair.
GENE STRUCTURE
McConnell et al. (2007) determined that the TIPRL gene contains 7 exons.
Exons 1 through 4, 6, and 7 encode TIP, and exons 1 through 5 encode TIP
isoform-2.
MAPPING
By genomic sequence analysis, McConnell et al. (2007) mapped the TIPRL
gene to chromosome 1q23.2.
*FIELD* RF
1. Jacinto, E.; Guo, B.; Arndt, K. T.; Schmelzle, T.; Hall, M. N.
: TIP41 interacts with TAP42 and negatively regulates the TOR signaling
pathway. Molec. Cell 8: 1017-1026, 2001.
2. McConnell, J. L.; Gomez, R. J.; McCorvey, L. R. A.; Law, B. K.;
Wadzinski, B. E.: Identification of a PP2A-interacting protein that
functions as a negative regulator of phosphatase activity in the ATM/ATR
signaling pathway. Oncogene 26: 6021-6030, 2007.
*FIELD* CD
Paul J. Converse: 2/21/2008
*FIELD* ED
carol: 06/23/2011
terry: 9/7/2010
mgross: 2/21/2008
*RECORD*
*FIELD* NO
611807
*FIELD* TI
*611807 TIP41-LIKE PROTEIN; TIPRL
;;TIP41, S. CEREVISIAE, HOMOLOG OF; TIP41;;
PROTEIN PHOSPHATASE 2A-INTERACTING PROTEIN; TIP
read more*FIELD* TX
DESCRIPTION
TIPRL is an inhibitory regulator of protein phosphatase-2A (PP2A) (see
PPP2CA; 176915), PP4 (see PPP4C; 602035), and PP6 (see PPP6C; 612725)
(McConnell et al., 2007).
CLONING
By database analysis, Jacinto et al. (2001) identified human TIPRL as a
homolog of yeast Tip41. TIPRL shares 35% amino acid identity with the
yeast protein.
McConnell et al. (2007) cloned human TIPRL, which they called TIP, from
a T-cell lymphoma cDNA library. The predicted protein contains 272 amino
acids. They also cloned a TIP splice variant that encodes a C-terminally
truncated protein (TIP isoform-2) that shares the first 172 amino acids
with TIP, but ends with 6 unique amino acids. Immunoblot analysis showed
ubiquitous expression of a 33-kD TIP protein.
GENE FUNCTION
Using immunoprecipitation analysis, McConnell et al. (2007) found that,
unlike yeast Tip41, human TIP did not interact with alpha-4 (IGBP1;
300139), the human homolog of yeast Tap42, in the presence of rapamycin.
Instead, TIP interacted with the catalytic subunits of PP2A, PP4, and
PP6 in a rapamycin-independent manner. TIP isoform-2 did not interact
with PP2A, suggesting that the C terminus of TIP is important for PP2A
binding. Incubation of PP2A with TIP, but not TIP isoform-2, resulted in
dose-dependent inhibition of PP2A phosphatase activity. Cells in which
TIP was depleted by small interfering RNA exhibited decreased
phosphorylation of a 32-kD substrate of ATM (607585)/ATR (601215)
kinases. McConnell et al. (2007) concluded that TIP is an inhibitory
regulator of PP2A and that the TIP/PP2A complex has a role within the
ATM/ATR signaling pathway controlling DNA replication and repair.
GENE STRUCTURE
McConnell et al. (2007) determined that the TIPRL gene contains 7 exons.
Exons 1 through 4, 6, and 7 encode TIP, and exons 1 through 5 encode TIP
isoform-2.
MAPPING
By genomic sequence analysis, McConnell et al. (2007) mapped the TIPRL
gene to chromosome 1q23.2.
*FIELD* RF
1. Jacinto, E.; Guo, B.; Arndt, K. T.; Schmelzle, T.; Hall, M. N.
: TIP41 interacts with TAP42 and negatively regulates the TOR signaling
pathway. Molec. Cell 8: 1017-1026, 2001.
2. McConnell, J. L.; Gomez, R. J.; McCorvey, L. R. A.; Law, B. K.;
Wadzinski, B. E.: Identification of a PP2A-interacting protein that
functions as a negative regulator of phosphatase activity in the ATM/ATR
signaling pathway. Oncogene 26: 6021-6030, 2007.
*FIELD* CD
Paul J. Converse: 2/21/2008
*FIELD* ED
carol: 06/23/2011
terry: 9/7/2010
mgross: 2/21/2008