ID   RP9_MOUSE               Reviewed;         213 AA.
AC   P97762;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   01-MAY-1997, sequence version 1.
DT   03-AUG-2022, entry version 146.
DE   RecName: Full=Retinitis pigmentosa 9 protein homolog;
DE   AltName: Full=Pim-1-associated protein;
DE            Short=PAP-1;
GN   Name=rp9; Synonyms=Rp9h;
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 [MRNA], INTERACTION WITH PIM1, AND PHOSPHORYLATION AT
RP   SER-204 AND SER-206 BY PIM1.
RC   TISSUE=T-cell lymphoma;
RX   PubMed=10931201; DOI=10.1046/j.1432-1327.2000.01585.x;
RA   Maita H., Harada Y., Nagakubo D., Kitaura H., Ikeda M., Tamai K.,
RA   Takahashi K., Ariga H., Iguchi-Ariga S.M.M.;
RT   "PAP-1, a novel target protein of phosphorylation by Pim-1 kinase.";
RL   Eur. J. Biochem. 267:5168-5178(2000).
RN   [2]
RP   PROTEIN SEQUENCE OF 1-8, AND IDENTIFICATION BY MASS SPECTROMETRY.
RC   STRAIN=OF1; TISSUE=Hippocampus;
RA   Lubec G., Sunyer B., Chen W.-Q.;
RL   Submitted (JAN-2009) to UniProtKB.
RN   [3]
RP   INTERACTION WITH ZNHIT4.
RX   PubMed=15556297; DOI=10.1016/j.gene.2004.05.025;
RA   Kuroda T.S., Maita H., Tabata T., Taira T., Kitaura H., Ariga H.,
RA   Iguchi-Ariga S.M.M.;
RT   "A novel nucleolar protein, PAPA-1, induces growth arrest as a result of
RT   cell cycle arrest at the G1 phase.";
RL   Gene 340:83-98(2004).
CC   -!- FUNCTION: Is thought to be a target protein for the PIM1 kinase. May
CC       play some roles in B-cell proliferation in association with PIM1.
CC   -!- SUBUNIT: Binds to PIM1. Binds to ZNHIT4.
CC   -!- INTERACTION:
CC       P97762; Q9DA19: Cir1; NbExp=6; IntAct=EBI-626715, EBI-309693;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000305}.
CC   -!- TISSUE SPECIFICITY: Highly expressed in the testis, moderately in the
CC       kidney, liver and spleen, and weakly in the skeletal muscle and heart.
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DR   EMBL; D78255; BAA11319.1; -; mRNA.
DR   CCDS; CCDS40564.1; -.
DR   RefSeq; NP_061209.1; NM_018739.2.
DR   AlphaFoldDB; P97762; -.
DR   BioGRID; 207733; 2.
DR   DIP; DIP-33838N; -.
DR   IntAct; P97762; 2.
DR   STRING; 10090.ENSMUSP00000034763; -.
DR   iPTMnet; P97762; -.
DR   PhosphoSitePlus; P97762; -.
DR   EPD; P97762; -.
DR   PaxDb; P97762; -.
DR   PeptideAtlas; P97762; -.
DR   PRIDE; P97762; -.
DR   Antibodypedia; 26407; 48 antibodies from 17 providers.
DR   DNASU; 55934; -.
DR   Ensembl; ENSMUST00000034763; ENSMUSP00000034763; ENSMUSG00000032239.
DR   GeneID; 55934; -.
DR   KEGG; mmu:55934; -.
DR   UCSC; uc009ooq.2; mouse.
DR   CTD; 6100; -.
DR   MGI; MGI:2157166; Rp9.
DR   VEuPathDB; HostDB:ENSMUSG00000032239; -.
DR   eggNOG; KOG3794; Eukaryota.
DR   GeneTree; ENSGT00940000162896; -.
DR   HOGENOM; CLU_108306_0_0_1; -.
DR   InParanoid; P97762; -.
DR   OMA; PGYIKEH; -.
DR   OrthoDB; 1479659at2759; -.
DR   PhylomeDB; P97762; -.
DR   TreeFam; TF329160; -.
DR   BioGRID-ORCS; 55934; 5 hits in 73 CRISPR screens.
DR   ChiTaRS; Rp9; mouse.
DR   PRO; PR:P97762; -.
DR   Proteomes; UP000000589; Chromosome 9.
DR   RNAct; P97762; protein.
DR   Bgee; ENSMUSG00000032239; Expressed in embryonic brain and 256 other tissues.
DR   ExpressionAtlas; P97762; baseline and differential.
DR   Genevisible; P97762; MM.
DR   GO; GO:0016607; C:nuclear speck; ISO:MGI.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0050890; P:cognition; ISO:MGI.
DR   GO; GO:0008380; P:RNA splicing; IEA:InterPro.
DR   InterPro; IPR034585; PAP-1.
DR   PANTHER; PTHR35252; PTHR35252; 1.
PE   1: Evidence at protein level;
KW   Direct protein sequencing; Isopeptide bond; Metal-binding; Nucleus;
KW   Phosphoprotein; Reference proteome; Ubl conjugation; Zinc; Zinc-finger.
FT   CHAIN           1..213
FT                   /note="Retinitis pigmentosa 9 protein homolog"
FT                   /id="PRO_0000097429"
FT   ZN_FING         96..114
FT                   /note="CCHC-type"
FT   REGION          1..147
FT                   /note="PIM1-binding"
FT   REGION          1..61
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          154..213
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        175..203
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         204
FT                   /note="Phosphoserine; by PIM1; in vitro"
FT                   /evidence="ECO:0000305|PubMed:10931201"
FT   MOD_RES         206
FT                   /note="Phosphoserine; by PIM1; in vitro"
FT                   /evidence="ECO:0000305|PubMed:10931201"
FT   CROSSLNK        121
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0000250|UniProtKB:Q8TA86"
SQ   SEQUENCE   213 AA;  25262 MW;  EDFA8EEE2130E882 CRC64;
     MSSGAGSRRP REPPEHELQR RREQKRRRHD AQQLQQLKHL ESFYEKPPPG FIKEDETKPE
     DCIPDVPGNE HAREFLAHAP TKGLWMPLGR EVKVMQCWRC KRYGHRTGDK ECPFFIKGNQ
     KLEQFRVAHE DPMYDIIREN KRHEKDVRIQ QLKQLLEDST SDDDGSSSSS SGDREKRKKR
     KKKEKHKKRK KEKKKKKKRK HKASKSSESS DSE