PIHD1_MOUSE
ID PIHD1_MOUSE Reviewed; 290 AA.
AC Q9CQJ2; Q6NV90;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 01-JUN-2001, sequence version 1.
DT 03-AUG-2022, entry version 130.
DE RecName: Full=PIH1 domain-containing protein 1;
DE AltName: Full=Nucleolar protein 17 homolog;
GN Name=Pih1d1; Synonyms=Nop17;
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, and NOD;
RC TISSUE=Bone marrow, Embryo, Placenta, Testis, and Thymus;
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=C57BL/6J; TISSUE=Embryo;
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 INTERACTION WITH MSL1, AND SUBCELLULAR LOCATION.
RX PubMed=17335777; DOI=10.1016/j.bbrc.2007.02.073;
RA Dmitriev R.I., Korneenko T.V., Bessonov A.A., Shakhparonov M.I.,
RA Modyanov N.N., Pestov N.B.;
RT "Characterization of hampin/MSL1 as a node in the nuclear interactome.";
RL Biochem. Biophys. Res. Commun. 355:1051-1057(2007).
RN [4]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Pancreas, Spleen, and 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 [5]
RP X-RAY CRYSTALLOGRAPHY (1.9 ANGSTROMS) OF 47-179 IN COMPLEX WITH TELO2
RP PHOSPHOPEPTIDE, INTERACTION WITH TELO2, AND MUTAGENESIS OF LYS-57; LYS-64
RP AND LYS-153.
RX PubMed=24794838; DOI=10.1016/j.str.2014.04.001;
RA Pal M., Morgan M., Phelps S.E., Roe S.M., Parry-Morris S., Downs J.A.,
RA Polier S., Pearl L.H., Prodromou C.;
RT "Structural basis for phosphorylation-dependent recruitment of Tel2 to
RT Hsp90 by Pih1.";
RL Structure 22:805-818(2014).
CC -!- FUNCTION: Involved in the assembly of C/D box small nucleolar
CC ribonucleoprotein (snoRNP) particles (By similarity). Recruits the
CC SWI/SNF complex to the core promoter of rRNA genes and enhances pre-
CC rRNA transcription (By similarity). Mediates interaction of TELO2 with
CC the R2TP complex which is necessary for the stability of MTOR and SMG1
CC (By similarity). Positively regulates the assembly and activity of the
CC mTORC1 complex (By similarity). {ECO:0000250|UniProtKB:Q9NWS0}.
CC -!- SUBUNIT: Component of the R2TP complex composed at least of RUVBL1,
CC RUVBL2, RPAP3 and PIHD1 (By similarity). Component of the PAQosome
CC complex which is responsible for the biogenesis of several protein
CC complexes and which consists of R2TP complex members RUVBL1, RUVBL2,
CC RPAP3 and PIH1D1, URI complex members PFDN2, PFDN6, PDRG1, UXT and URI1
CC as well as ASDURF, POLR2E and DNAAF10/WDR92 (By similarity). Interacts
CC with phosphorylated TELO2 (PubMed:24794838). Mediates interaction of
CC TELO2 with the R2TP complex (By similarity). Interacts with
CC phosphorylated ECD, EFTUD2/SNRP116, RPB1 and UBR5 and with RPB1 in a
CC phosphorylation-independent manner (By similarity). Interacts with the
CC core C/D box snoRNP particle components NOP58 and FBL and with
CC RUVBL1/TIP49 (By similarity). Interacts with RPAP3 and DNAAF10 (By
CC similarity). Interacts with histone H4 and with SWI/SNF complex member
CC SMARCB1/SNF5 (By similarity). Interacts with the mTORC1 complex member
CC RPTOR (By similarity). Interacts with isoform 1 of MSL1
CC (PubMed:17335777). {ECO:0000250|UniProtKB:Q9NWS0,
CC ECO:0000269|PubMed:17335777, ECO:0000269|PubMed:24794838}.
CC -!- INTERACTION:
CC Q9CQJ2; Q9DC40: Telo2; NbExp=3; IntAct=EBI-11658528, EBI-1571482;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17335777}.
CC -!- DOMAIN: The N-terminal region is required for binding to phosphorylated
CC substrates while the C-terminal region binds to the other R2TP complex
CC components. {ECO:0000250|UniProtKB:Q9NWS0}.
CC -!- SIMILARITY: Belongs to the PIH1 family. {ECO:0000305}.
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DR EMBL; AK004341; BAB23269.1; -; mRNA.
DR EMBL; AK016797; BAB30435.1; -; mRNA.
DR EMBL; AK089003; BAC40694.1; -; mRNA.
DR EMBL; AK146039; BAE26851.1; -; mRNA.
DR EMBL; AK152695; BAE31425.1; -; mRNA.
DR EMBL; BC068254; AAH68254.1; -; mRNA.
DR CCDS; CCDS21232.1; -.
DR RefSeq; NP_001265136.1; NM_001278207.1.
DR RefSeq; NP_001272833.1; NM_001285904.1.
DR RefSeq; NP_083682.1; NM_029406.4.
DR RefSeq; XP_006541219.1; XM_006541156.1.
DR RefSeq; XP_017167766.1; XM_017312277.1.
DR PDB; 4CKT; X-ray; 3.00 A; A/B=1-200.
DR PDB; 4CSE; X-ray; 3.30 A; A/B=47-179.
DR PDB; 4CV4; X-ray; 1.90 A; A=47-179.
DR PDBsum; 4CKT; -.
DR PDBsum; 4CSE; -.
DR PDBsum; 4CV4; -.
DR AlphaFoldDB; Q9CQJ2; -.
DR SMR; Q9CQJ2; -.
DR BioGRID; 213080; 4.
DR DIP; DIP-60996N; -.
DR IntAct; Q9CQJ2; 5.
DR MINT; Q9CQJ2; -.
DR STRING; 10090.ENSMUSP00000082490; -.
DR iPTMnet; Q9CQJ2; -.
DR PhosphoSitePlus; Q9CQJ2; -.
DR EPD; Q9CQJ2; -.
DR MaxQB; Q9CQJ2; -.
DR PaxDb; Q9CQJ2; -.
DR PeptideAtlas; Q9CQJ2; -.
DR PRIDE; Q9CQJ2; -.
DR ProteomicsDB; 289423; -.
DR Antibodypedia; 32006; 238 antibodies from 25 providers.
DR DNASU; 68845; -.
DR Ensembl; ENSMUST00000085375; ENSMUSP00000082490; ENSMUSG00000003423.
DR Ensembl; ENSMUST00000107811; ENSMUSP00000103441; ENSMUSG00000003423.
DR Ensembl; ENSMUST00000210139; ENSMUSP00000148186; ENSMUSG00000003423.
DR GeneID; 68845; -.
DR KEGG; mmu:68845; -.
DR UCSC; uc009gtv.1; mouse.
DR CTD; 55011; -.
DR MGI; MGI:1916095; Pih1d1.
DR VEuPathDB; HostDB:ENSMUSG00000003423; -.
DR eggNOG; KOG4356; Eukaryota.
DR GeneTree; ENSGT00510000048192; -.
DR HOGENOM; CLU_062696_0_0_1; -.
DR InParanoid; Q9CQJ2; -.
DR OMA; KLKNRKC; -.
DR OrthoDB; 1130314at2759; -.
DR PhylomeDB; Q9CQJ2; -.
DR TreeFam; TF324376; -.
DR BioGRID-ORCS; 68845; 4 hits in 72 CRISPR screens.
DR ChiTaRS; Pih1d1; mouse.
DR PRO; PR:Q9CQJ2; -.
DR Proteomes; UP000000589; Chromosome 7.
DR RNAct; Q9CQJ2; protein.
DR Bgee; ENSMUSG00000003423; Expressed in spermatid and 257 other tissues.
DR ExpressionAtlas; Q9CQJ2; baseline and differential.
DR Genevisible; Q9CQJ2; MM.
DR GO; GO:0005737; C:cytoplasm; ISO:MGI.
DR GO; GO:0005730; C:nucleolus; ISO:MGI.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0070761; C:pre-snoRNP complex; ISO:MGI.
DR GO; GO:0097255; C:R2TP complex; ISO:MGI.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:MGI.
DR GO; GO:0051117; F:ATPase binding; ISO:MGI.
DR GO; GO:0042393; F:histone binding; ISO:MGI.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:MGI.
DR GO; GO:0019901; F:protein kinase binding; ISO:MGI.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:MGI.
DR GO; GO:0000492; P:box C/D snoRNP assembly; ISO:MGI.
DR GO; GO:0006338; P:chromatin remodeling; ISO:MGI.
DR GO; GO:0030855; P:epithelial cell differentiation; IEA:Ensembl.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; ISO:MGI.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:MGI.
DR GO; GO:1900110; P:negative regulation of histone H3-K9 dimethylation; ISO:MGI.
DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; ISO:MGI.
DR GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; ISO:MGI.
DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; ISO:MGI.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; ISO:MGI.
DR GO; GO:0090240; P:positive regulation of histone H4 acetylation; ISO:MGI.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:MGI.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:MGI.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISO:MGI.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:MGI.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; ISO:MGI.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0048254; P:snoRNA localization; ISO:MGI.
DR GO; GO:1905669; P:TORC1 complex assembly; ISO:MGI.
DR InterPro; IPR012981; PIH1_N.
DR InterPro; IPR041442; PIH1D1/2/3_CS-like.
DR Pfam; PF08190; PIH1; 1.
DR Pfam; PF18201; PIH1_CS; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..290
FT /note="PIH1 domain-containing protein 1"
FT /id="PRO_0000307329"
FT SITE 57
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000269|PubMed:24794838"
FT SITE 64
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000269|PubMed:24794838"
FT SITE 113
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000269|PubMed:24794838"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V7F5"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q4V7F5"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWS0"
FT MUTAGEN 57
FT /note="K->E: Abolishes binding to TELO2-phosphopeptide."
FT /evidence="ECO:0000269|PubMed:24794838"
FT MUTAGEN 64
FT /note="K->E: Abolishes binding to TELO2-phosphopeptide."
FT /evidence="ECO:0000269|PubMed:24794838"
FT MUTAGEN 153
FT /note="K->E: No effect on binding to TELO2-phosphopeptide."
FT /evidence="ECO:0000269|PubMed:24794838"
FT CONFLICT 289
FT /note="S -> P (in Ref. 2; AAH68254)"
FT /evidence="ECO:0000305"
FT STRAND 51..58
FT /evidence="ECO:0007829|PDB:4CV4"
FT STRAND 65..72
FT /evidence="ECO:0007829|PDB:4CV4"
FT HELIX 83..91
FT /evidence="ECO:0007829|PDB:4CV4"
FT HELIX 95..98
FT /evidence="ECO:0007829|PDB:4CV4"
FT STRAND 107..110
FT /evidence="ECO:0007829|PDB:4CV4"
FT STRAND 112..114
FT /evidence="ECO:0007829|PDB:4CKT"
FT STRAND 116..125
FT /evidence="ECO:0007829|PDB:4CV4"
FT HELIX 126..133
FT /evidence="ECO:0007829|PDB:4CV4"
FT HELIX 136..154
FT /evidence="ECO:0007829|PDB:4CV4"
FT HELIX 174..176
FT /evidence="ECO:0007829|PDB:4CV4"
SQ SEQUENCE 290 AA; 32209 MW; 8624B7EF592E3F59 CRC64;
MADSTFLAPE LSDTESMGEE TVRFQELLLK ASKELQQAQT ARPDSTQIQP KPGFCVKTNS
SEGKVFINIC HSPSIPPPAD VTEDELLQML EEDQAGFRIP MSLGEPHAEL DAKGQGCTAY
DVAVNSNFYL RMQNSDFLRE LVVTIAREGL EDKYGLQLNP EWRMLKYRSF LGSISQQNIR
SQQRPRIQEL GTLDASGSLG TCHGPERPHL NLWLEAPDLL LAEVDLPKLD GAQGLALEIG
ENRLVIGGPQ QLYHLDATVP LRINSEASRA AFHRRRKQLM VSMPLLTASS
