ID TIPRL_MOUSE Reviewed; 271 AA.
AC Q8BH58;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-MAR-2003, sequence version 1.
DT 24-JAN-2024, entry version 137.
DE RecName: Full=TIP41-like protein;
GN Name=Tiprl;
OS Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=C57BL/6J;
RC TISSUE=Embryonic stem cell, Fetal spinal cord, and Pancreas;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC STRAIN=Czech II; TISSUE=Mammary tumor, and Olfactory epithelium;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Spleen, and
RC Testis;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
RN [4]
RP INTERACTION WITH PPP4C AND PPP4R2.
RX PubMed=26717153; DOI=10.1371/journal.pone.0145938;
RA Rosales K.R., Reid M.A., Yang Y., Tran T.Q., Wang W.I., Lowman X., Pan M.,
RA Kong M.;
RT "TIPRL inhibits protein phosphatase 4 activity and promotes H2AX
RT phosphorylation in the DNA damage response.";
RL PLoS ONE 10:E0145938-E0145938(2015).
CC -!- FUNCTION: May be a allosteric regulator of serine/threonine-protein
CC phosphatase 2A (PP2A). Inhibits catalytic activity of the PP2A(D) core
CC complex in vitro. The PP2A(C):TIPRL complex does not show phosphatase
CC activity. Acts as a negative regulator of serine/threonine-protein
CC phosphatase 4 probably by inhibiting the formation of the active
CC PPP4C:PPP4R2 complex; the function is proposed to implicate it in DNA
CC damage response by promoting H2AX phosphorylated on Ser-140 (gamma-
CC H2AX). May play a role in the regulation of ATM/ATR signaling pathway
CC controlling DNA replication and repair (By similarity).
CC {ECO:0000250|UniProtKB:O75663}.
CC -!- SUBUNIT: Interacts 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):IGBP1 complex (By
CC similarity). Interacts with PPP4C and PPP4R2 (PubMed:26717153).
CC {ECO:0000250|UniProtKB:O75663, ECO:0000269|PubMed:26717153}.
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000250|UniProtKB:O75663}.
CC -!- SIMILARITY: Belongs to the TIP41 family. {ECO:0000305}.
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; AK049119; BAC33553.1; -; mRNA.
DR EMBL; AK049784; BAC33919.1; -; mRNA.
DR EMBL; AK075774; BAC35948.1; -; mRNA.
DR EMBL; BC002098; AAH02098.1; -; mRNA.
DR EMBL; BC058250; AAH58250.1; -; mRNA.
DR CCDS; CCDS15441.1; -.
DR RefSeq; NP_663488.1; NM_145513.4.
DR PDB; 5W0W; X-ray; 3.80 A; B/E/H/K=12-259.
DR PDB; 5W0X; X-ray; 2.72 A; A=12-259.
DR PDBsum; 5W0W; -.
DR PDBsum; 5W0X; -.
DR AlphaFoldDB; Q8BH58; -.
DR SMR; Q8BH58; -.
DR BioGRID; 230535; 13.
DR IntAct; Q8BH58; 1.
DR MINT; Q8BH58; -.
DR STRING; 10090.ENSMUSP00000037514; -.
DR GlyGen; Q8BH58; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; Q8BH58; -.
DR PhosphoSitePlus; Q8BH58; -.
DR SwissPalm; Q8BH58; -.
DR EPD; Q8BH58; -.
DR jPOST; Q8BH58; -.
DR MaxQB; Q8BH58; -.
DR PaxDb; 10090-ENSMUSP00000037514; -.
DR PeptideAtlas; Q8BH58; -.
DR ProteomicsDB; 259510; -.
DR Pumba; Q8BH58; -.
DR Antibodypedia; 34349; 281 antibodies from 32 providers.
DR DNASU; 226591; -.
DR Ensembl; ENSMUST00000043235.8; ENSMUSP00000037514.6; ENSMUSG00000040843.11.
DR GeneID; 226591; -.
DR KEGG; mmu:226591; -.
DR UCSC; uc007diz.2; mouse.
DR AGR; MGI:1915087; -.
DR CTD; 261726; -.
DR MGI; MGI:1915087; Tiprl.
DR VEuPathDB; HostDB:ENSMUSG00000040843; -.
DR eggNOG; KOG3224; Eukaryota.
DR GeneTree; ENSGT00390000006659; -.
DR HOGENOM; CLU_039187_2_0_1; -.
DR InParanoid; Q8BH58; -.
DR OMA; DMILFED; -.
DR OrthoDB; 443048at2759; -.
DR PhylomeDB; Q8BH58; -.
DR TreeFam; TF105943; -.
DR BioGRID-ORCS; 226591; 24 hits in 80 CRISPR screens.
DR ChiTaRS; Tiprl; mouse.
DR PRO; PR:Q8BH58; -.
DR Proteomes; UP000000589; Chromosome 1.
DR RNAct; Q8BH58; Protein.
DR Bgee; ENSMUSG00000040843; Expressed in embryonic post-anal tail and 269 other cell types or tissues.
DR ExpressionAtlas; Q8BH58; baseline and differential.
DR Genevisible; Q8BH58; MM.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR GO; GO:0000077; P:DNA damage checkpoint signaling; ISO:MGI.
DR GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR InterPro; IPR007303; TIP41-like.
DR PANTHER; PTHR21021; GAF/PUTATIVE CYTOSKELETAL PROTEIN; 1.
DR PANTHER; PTHR21021:SF16; TIP41-LIKE PROTEIN; 1.
DR Pfam; PF04176; TIP41; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Cytoplasm; Phosphoprotein; Reference proteome.
FT CHAIN 1..271
FT /note="TIP41-like protein"
FT /id="PRO_0000301854"
FT REGION 173..271
FT /note="Interaction with PPP2CA"
FT /evidence="ECO:0000250"
FT MOD_RES 106
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:O75663"
FT MOD_RES 265
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O75663"
FT MOD_RES 270
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:A2VCX1"
FT STRAND 13..15
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 18..23
FT /evidence="ECO:0007829|PDB:5W0X"
FT HELIX 30..39
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 47..49
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 54..59
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 64..68
FT /evidence="ECO:0007829|PDB:5W0X"
FT HELIX 69..73
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 119..121
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 128..131
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 148..158
FT /evidence="ECO:0007829|PDB:5W0X"
FT HELIX 160..162
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 163..174
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 176..189
FT /evidence="ECO:0007829|PDB:5W0X"
FT TURN 190..192
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 193..204
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 208..220
FT /evidence="ECO:0007829|PDB:5W0X"
FT HELIX 221..223
FT /evidence="ECO:0007829|PDB:5W0X"
FT HELIX 229..233
FT /evidence="ECO:0007829|PDB:5W0X"
FT HELIX 235..238
FT /evidence="ECO:0007829|PDB:5W0X"
FT HELIX 239..241
FT /evidence="ECO:0007829|PDB:5W0X"
FT STRAND 244..253
FT /evidence="ECO:0007829|PDB:5W0X"
SQ SEQUENCE 271 AA; 31254 MW; 49558C6DDE0E2A7F CRC64;
MMIHGFQSSH QDFSFGPWKL TASKTHIMKS ADVEKLADEL HMPSLPEMMF GDNVLRIQHG
SGFGIEFNAT DALRCVNNYQ GMLKVACAEE WQESRTEGEH SKEVIKPYDW TYTTDYKGTL
LGESLKLKVV PTTDHIDTEK LKAREQIKFF EEVLLFEDEL HDHGVSSLSV KIRVMPSSFF
LLLRFFLRID GVLIRMNDTR LYHEADKTYM LREYTSRESK IANLMHVPPS LFTEPNEISQ
YLPIKEAVCE KLVFPERIDP NPVDSQSTPS E
//
