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TIPRL_MOUSE
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   03-AUG-2022, entry version 129.
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 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}.
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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   iPTMnet; Q8BH58; -.
DR   PhosphoSitePlus; Q8BH58; -.
DR   EPD; Q8BH58; -.
DR   jPOST; Q8BH58; -.
DR   MaxQB; Q8BH58; -.
DR   PaxDb; Q8BH58; -.
DR   PeptideAtlas; Q8BH58; -.
DR   PRIDE; Q8BH58; -.
DR   ProteomicsDB; 259510; -.
DR   Antibodypedia; 34349; 253 antibodies from 32 providers.
DR   DNASU; 226591; -.
DR   Ensembl; ENSMUST00000043235; ENSMUSP00000037514; ENSMUSG00000040843.
DR   GeneID; 226591; -.
DR   KEGG; mmu:226591; -.
DR   UCSC; uc007diz.2; mouse.
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; GIPIPEM; -.
DR   OrthoDB; 1377237at2759; -.
DR   PhylomeDB; Q8BH58; -.
DR   TreeFam; TF105943; -.
DR   BioGRID-ORCS; 226591; 24 hits in 76 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 265 other 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:0032515; P:negative regulation of phosphoprotein phosphatase activity; ISO:MGI.
DR   GO; GO:0043666; P:regulation of phosphoprotein phosphatase activity; IBA:GO_Central.
DR   GO; GO:0031929; P:TOR signaling; IBA:GO_Central.
DR   InterPro; IPR007303; TIP41-like.
DR   PANTHER; PTHR21021:SF16; PTHR21021:SF16; 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
 
 
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