PIHD1_RAT
ID PIHD1_RAT Reviewed; 290 AA.
AC Q4V7F5;
DT 23-OCT-2007, integrated into UniProtKB/Swiss-Prot.
DT 05-JUL-2005, sequence version 1.
DT 03-AUG-2022, entry version 95.
DE RecName: Full=PIH1 domain-containing protein 1;
GN Name=Pih1d1;
OS Rattus norvegicus (Rat).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Rattus.
OX NCBI_TaxID=10116;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Spleen;
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 [2]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12 AND SER-16, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=22673903; DOI=10.1038/ncomms1871;
RA Lundby A., Secher A., Lage K., Nordsborg N.B., Dmytriyev A., Lundby C.,
RA Olsen J.V.;
RT "Quantitative maps of protein phosphorylation sites across 14 different rat
RT organs and tissues.";
RL Nat. Commun. 3:876-876(2012).
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 and mediates interaction of TELO2 with the
CC R2TP complex (By similarity). Interacts with phosphorylated ECD,
CC EFTUD2/SNRP116, RPB1 and UBR5 and with RPB1 in a phosphorylation-
CC independent manner (By similarity). Interacts with the core C/D box
CC snoRNP particle components NOP58 and FBL and with RUVBL1/TIP49 (By
CC similarity). Interacts with RPAP3 and DNAAF10 (By similarity).
CC Interacts with histone H4 and with SWI/SNF complex member SMARCB1/SNF5
CC (By similarity). Interacts with the mTORC1 complex member RPTOR (By
CC similarity). Interacts with MSL1 (By similarity).
CC {ECO:0000250|UniProtKB:Q9CQJ2, ECO:0000250|UniProtKB:Q9NWS0}.
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250|UniProtKB:Q9CQJ2}.
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; BC097946; AAH97946.1; -; mRNA.
DR RefSeq; NP_001020039.1; NM_001024868.1.
DR RefSeq; XP_006229089.1; XM_006229027.2.
DR RefSeq; XP_006229090.1; XM_006229028.3.
DR AlphaFoldDB; Q4V7F5; -.
DR SMR; Q4V7F5; -.
DR IntAct; Q4V7F5; 1.
DR MINT; Q4V7F5; -.
DR STRING; 10116.ENSRNOP00000028022; -.
DR iPTMnet; Q4V7F5; -.
DR PhosphoSitePlus; Q4V7F5; -.
DR PaxDb; Q4V7F5; -.
DR Ensembl; ENSRNOT00000119250; ENSRNOP00000089848; ENSRNOG00000020634.
DR GeneID; 292898; -.
DR KEGG; rno:292898; -.
DR UCSC; RGD:1309809; rat.
DR CTD; 55011; -.
DR RGD; 1309809; Pih1d1.
DR eggNOG; KOG4356; Eukaryota.
DR GeneTree; ENSGT00510000048192; -.
DR HOGENOM; CLU_062696_0_0_1; -.
DR InParanoid; Q4V7F5; -.
DR OMA; KLKNRKC; -.
DR OrthoDB; 1130314at2759; -.
DR PhylomeDB; Q4V7F5; -.
DR TreeFam; TF324376; -.
DR PRO; PR:Q4V7F5; -.
DR Proteomes; UP000002494; Chromosome 1.
DR Bgee; ENSRNOG00000020634; Expressed in testis and 20 other tissues.
DR Genevisible; Q4V7F5; RN.
DR GO; GO:0005737; C:cytoplasm; ISO:RGD.
DR GO; GO:0005730; C:nucleolus; ISO:RGD.
DR GO; GO:0005634; C:nucleus; ISS:UniProtKB.
DR GO; GO:0070761; C:pre-snoRNP complex; ISO:RGD.
DR GO; GO:0097255; C:R2TP complex; ISO:RGD.
DR GO; GO:1990904; C:ribonucleoprotein complex; IBA:GO_Central.
DR GO; GO:1990062; C:RPAP3/R2TP/prefoldin-like complex; ISO:RGD.
DR GO; GO:0051117; F:ATPase binding; ISO:RGD.
DR GO; GO:0042393; F:histone binding; ISO:RGD.
DR GO; GO:0051219; F:phosphoprotein binding; ISO:RGD.
DR GO; GO:0019901; F:protein kinase binding; ISO:RGD.
DR GO; GO:0001164; F:RNA polymerase I core promoter sequence-specific DNA binding; ISO:RGD.
DR GO; GO:0000492; P:box C/D snoRNP assembly; ISO:RGD.
DR GO; GO:0006338; P:chromatin remodeling; ISO:RGD.
DR GO; GO:0030855; P:epithelial cell differentiation; ISO:RGD.
DR GO; GO:0071169; P:establishment of protein localization to chromatin; ISO:RGD.
DR GO; GO:2001268; P:negative regulation of cysteine-type endopeptidase activity involved in apoptotic signaling pathway; ISO:RGD.
DR GO; GO:1900110; P:negative regulation of histone H3-K9 dimethylation; ISO:RGD.
DR GO; GO:1900113; P:negative regulation of histone H3-K9 trimethylation; ISO:RGD.
DR GO; GO:2000619; P:negative regulation of histone H4-K16 acetylation; ISO:RGD.
DR GO; GO:1902661; P:positive regulation of glucose mediated signaling pathway; ISO:RGD.
DR GO; GO:2000617; P:positive regulation of histone H3-K9 acetylation; ISO:RGD.
DR GO; GO:0090240; P:positive regulation of histone H4 acetylation; ISO:RGD.
DR GO; GO:0071902; P:positive regulation of protein serine/threonine kinase activity; ISO:RGD.
DR GO; GO:0031334; P:positive regulation of protein-containing complex assembly; ISO:RGD.
DR GO; GO:1904263; P:positive regulation of TORC1 signaling; ISO:RGD.
DR GO; GO:1901838; P:positive regulation of transcription of nucleolar large rRNA by RNA polymerase I; ISO:RGD.
DR GO; GO:0051569; P:regulation of histone H3-K4 methylation; ISO:RGD.
DR GO; GO:0006364; P:rRNA processing; IBA:GO_Central.
DR GO; GO:0048254; P:snoRNA localization; ISO:RGD.
DR GO; GO:1905669; P:TORC1 complex assembly; ISO:RGD.
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 Nucleus; Phosphoprotein; Reference proteome; Transcription;
KW Transcription regulation.
FT CHAIN 1..290
FT /note="PIH1 domain-containing protein 1"
FT /id="PRO_0000307330"
FT SITE 57
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000250|UniProtKB:Q9NWS0"
FT SITE 64
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000250|UniProtKB:Q9NWS0"
FT SITE 113
FT /note="Interacts with TELO2"
FT /evidence="ECO:0000250|UniProtKB:Q9CQJ2"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 16
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 173
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q9NWS0"
SQ SEQUENCE 290 AA; 32361 MW; 8BC897FEC041D4C4 CRC64;
MADSKLLAPE LSDAESMGEE TVRFQELLLK ASKELQQAQT ARPESTQIQP KPGFCIKTNS
SEGKVFINIC HSPSIPPPVD VTEDELLQML EEDQAGFRIP MSLGEPHAEL DAKGQGCTAY
DVAVNSNFYL RMQNSDFLRE LVVTIAREGL EDKYGLQLNP EWRMLKYRSF LGSISQQSIR
SQQRPRIQEL GTLDTHDSLG TRHGPERPHL NLWLEAPDLL LAEVDLPKLD GAQGLALEIG
ENRLVVGGPQ QLYHLDACIP LRINSEASRA AFHHRRKQLM VSMPLLSASS
