ID   RP9_HUMAN               Reviewed;         221 AA.
AC   Q8TA86;
DT   14-NOV-2003, integrated into UniProtKB/Swiss-Prot.
DT   14-NOV-2003, sequence version 2.
DT   27-MAR-2024, entry version 168.
DE   RecName: Full=Retinitis pigmentosa 9 protein;
DE   AltName: Full=Pim-1-associated protein;
DE            Short=PAP-1;
GN   Name=RP9;
OS   Homo sapiens (Human).
OC   Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC   Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC   Homo.
OX   NCBI_TaxID=9606;
RN   [1]
RP   NUCLEOTIDE SEQUENCE [MRNA].
RA   Bruck C.E., Coche T., Cassart J.-P., Vinals-Bassols C.;
RT   "Compounds related to PAP-1.";
RL   Patent number WO9949030, 30-SEP-1999.
RN   [2]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC   TISSUE=Muscle;
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 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).
RN   [4]
RP   SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-129, AND IDENTIFICATION BY MASS
RP   SPECTROMETRY [LARGE SCALE ANALYSIS].
RX   PubMed=28112733; DOI=10.1038/nsmb.3366;
RA   Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA   Nielsen M.L.;
RT   "Site-specific mapping of the human SUMO proteome reveals co-modification
RT   with phosphorylation.";
RL   Nat. Struct. Mol. Biol. 24:325-336(2017).
RN   [5]
RP   VARIANTS RP9 LEU-137 AND GLY-170, AND VARIANT ARG-210.
RX   PubMed=12032732; DOI=10.1038/sj.ejhg.5200797;
RA   Keen T.J., Hims M.M., McKie A.B., Moore A.T., Doran R.M., Mackey D.A.,
RA   Mansfield D.C., Mueller R.F., Bhattacharya S.S., Bird A.C., Markham A.F.,
RA   Inglehearn C.F.;
RT   "Mutations in a protein target of the Pim-1 kinase associated with the RP9
RT   form of autosomal dominant retinitis pigmentosa.";
RL   Eur. J. Hum. Genet. 10:245-249(2002).
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 (By
CC       similarity). {ECO:0000250}.
CC   -!- SUBUNIT: Binds to PIM1 (By similarity). Binds to ZNHIT4. {ECO:0000250}.
CC   -!- INTERACTION:
CC       Q8TA86; Q9BXS5: AP1M1; NbExp=3; IntAct=EBI-630339, EBI-541426;
CC       Q8TA86; Q13895: BYSL; NbExp=3; IntAct=EBI-630339, EBI-358049;
CC       Q8TA86; P61328-2: FGF12; NbExp=3; IntAct=EBI-630339, EBI-10699759;
CC       Q8TA86; Q9BU76: MMTAG2; NbExp=3; IntAct=EBI-630339, EBI-742459;
CC       Q8TA86; Q6ZUT1: NKAPD1; NbExp=3; IntAct=EBI-630339, EBI-3920396;
CC       Q8TA86; O00560: SDCBP; NbExp=5; IntAct=EBI-630339, EBI-727004;
CC       Q8TA86; Q8N9Q2: SREK1IP1; NbExp=3; IntAct=EBI-630339, EBI-10268630;
CC   -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC   -!- TISSUE SPECIFICITY: Appears to be expressed in a wide range of tissues.
CC   -!- DISEASE: Retinitis pigmentosa 9 (RP9) [MIM:180104]: A retinal dystrophy
CC       belonging to the group of pigmentary retinopathies. Retinitis
CC       pigmentosa is characterized by retinal pigment deposits visible on
CC       fundus examination and primary loss of rod photoreceptor cells followed
CC       by secondary loss of cone photoreceptors. Patients typically have night
CC       vision blindness and loss of midperipheral visual field. As their
CC       condition progresses, they lose their far peripheral visual field and
CC       eventually central vision as well. {ECO:0000269|PubMed:12032732}.
CC       Note=The disease is caused by variants affecting the gene represented
CC       in this entry.
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DR   EMBL; AX016710; -; NOT_ANNOTATED_CDS; mRNA.
DR   EMBL; BC025928; AAH25928.2; -; mRNA.
DR   CCDS; CCDS5440.1; -.
DR   RefSeq; NP_976033.1; NM_203288.1.
DR   AlphaFoldDB; Q8TA86; -.
DR   BioGRID; 112027; 96.
DR   IntAct; Q8TA86; 20.
DR   MINT; Q8TA86; -.
DR   STRING; 9606.ENSP00000297157; -.
DR   iPTMnet; Q8TA86; -.
DR   PhosphoSitePlus; Q8TA86; -.
DR   BioMuta; RP9; -.
DR   DMDM; 38372427; -.
DR   EPD; Q8TA86; -.
DR   jPOST; Q8TA86; -.
DR   MassIVE; Q8TA86; -.
DR   MaxQB; Q8TA86; -.
DR   PaxDb; 9606-ENSP00000297157; -.
DR   PeptideAtlas; Q8TA86; -.
DR   ProteomicsDB; 73839; -.
DR   Pumba; Q8TA86; -.
DR   Antibodypedia; 26407; 53 antibodies from 18 providers.
DR   DNASU; 6100; -.
DR   Ensembl; ENST00000297157.8; ENSP00000297157.3; ENSG00000164610.10.
DR   GeneID; 6100; -.
DR   KEGG; hsa:6100; -.
DR   MANE-Select; ENST00000297157.8; ENSP00000297157.3; NM_203288.2; NP_976033.1.
DR   UCSC; uc003tdm.4; human.
DR   AGR; HGNC:10288; -.
DR   CTD; 6100; -.
DR   DisGeNET; 6100; -.
DR   GeneCards; RP9; -.
DR   GeneReviews; RP9; -.
DR   HGNC; HGNC:10288; RP9.
DR   HPA; ENSG00000164610; Low tissue specificity.
DR   MalaCards; RP9; -.
DR   MIM; 180104; phenotype.
DR   MIM; 607331; gene.
DR   neXtProt; NX_Q8TA86; -.
DR   OpenTargets; ENSG00000164610; -.
DR   Orphanet; 791; Retinitis pigmentosa.
DR   PharmGKB; PA34650; -.
DR   VEuPathDB; HostDB:ENSG00000164610; -.
DR   eggNOG; KOG3794; Eukaryota.
DR   GeneTree; ENSGT00940000162896; -.
DR   InParanoid; Q8TA86; -.
DR   OMA; PPGYIKE; -.
DR   OrthoDB; 12033at2759; -.
DR   PhylomeDB; Q8TA86; -.
DR   TreeFam; TF329160; -.
DR   PathwayCommons; Q8TA86; -.
DR   SignaLink; Q8TA86; -.
DR   SIGNOR; Q8TA86; -.
DR   BioGRID-ORCS; 6100; 15 hits in 1161 CRISPR screens.
DR   ChiTaRS; RP9; human.
DR   GeneWiki; RP9; -.
DR   GenomeRNAi; 6100; -.
DR   Pharos; Q8TA86; Tbio.
DR   PRO; PR:Q8TA86; -.
DR   Proteomes; UP000005640; Chromosome 7.
DR   RNAct; Q8TA86; Protein.
DR   Bgee; ENSG00000164610; Expressed in oocyte and 185 other cell types or tissues.
DR   ExpressionAtlas; Q8TA86; baseline and differential.
DR   GO; GO:0005634; C:nucleus; IEA:UniProtKB-SubCell.
DR   GO; GO:0005785; C:signal recognition particle receptor complex; IEA:Ensembl.
DR   GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR   GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR   GO; GO:0050890; P:cognition; IMP:UniProtKB.
DR   GO; GO:0008380; P:RNA splicing; TAS:UniProtKB.
DR   InterPro; IPR034585; PAP-1.
DR   PANTHER; PTHR35252; RETINITIS PIGMENTOSA 9 PROTEIN; 1.
DR   PANTHER; PTHR35252:SF1; RETINITIS PIGMENTOSA 9 PROTEIN; 1.
DR   Genevisible; Q8TA86; HS.
PE   1: Evidence at protein level;
KW   Disease variant; Isopeptide bond; Metal-binding; Nucleus; Phosphoprotein;
KW   Reference proteome; Retinitis pigmentosa; Ubl conjugation; Zinc;
KW   Zinc-finger.
FT   CHAIN           1..221
FT                   /note="Retinitis pigmentosa 9 protein"
FT                   /id="PRO_0000097428"
FT   ZN_FING         104..122
FT                   /note="CCHC-type"
FT   REGION          1..155
FT                   /note="PIM1-binding"
FT                   /evidence="ECO:0000250"
FT   REGION          1..76
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   REGION          147..221
FT                   /note="Disordered"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        10..43
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        56..76
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        147..182
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        183..211
FT                   /note="Basic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   MOD_RES         212
FT                   /note="Phosphoserine; by PIM1"
FT                   /evidence="ECO:0000250|UniProtKB:P97762"
FT   MOD_RES         214
FT                   /note="Phosphoserine; by PIM1"
FT                   /evidence="ECO:0000250|UniProtKB:P97762"
FT   CROSSLNK        129
FT                   /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT                   G-Cter in SUMO2)"
FT                   /evidence="ECO:0007744|PubMed:28112733"
FT   VARIANT         137
FT                   /note="H -> L (in RP9; dbSNP:rs104894037)"
FT                   /evidence="ECO:0000269|PubMed:12032732"
FT                   /id="VAR_017252"
FT   VARIANT         170
FT                   /note="D -> G (in RP9; dbSNP:rs104894039)"
FT                   /evidence="ECO:0000269|PubMed:12032732"
FT                   /id="VAR_017253"
FT   VARIANT         210
FT                   /note="K -> R (in dbSNP:rs150987618)"
FT                   /evidence="ECO:0000269|PubMed:12032732"
FT                   /id="VAR_017254"
SQ   SEQUENCE   221 AA;  26107 MW;  63774BDB40A63E4F CRC64;
     MSSRPGREDV GAAGARRPRE PPEQELQRRR EQKRRRHDAQ QLQQLKHLES FYEKPPPGLI
     KEDETKPEDC IPDVPGNEHA REFLAHAPTK GLWMPLGKEV KVMQCWRCKR YGHRTGDKEC
     PFFIKGNQKL EQFRVAHEDP MYDIIRDNKR HEKDVRIQQL KQLLEDSTSD EDRSSSSSSE
     GKEKHKKKKK KEKHKKRKKE KKKKKKRKHK SSKSNEGSDS E
//