HAP28_RAT
ID HAP28_RAT Reviewed; 181 AA.
AC Q62785; Q62890;
DT 01-NOV-1997, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1996, sequence version 1.
DT 03-AUG-2022, entry version 122.
DE RecName: Full=28 kDa heat- and acid-stable phosphoprotein;
DE AltName: Full=PDGF-associated protein;
DE Short=PAP;
DE AltName: Full=PDGFA-associated protein 1;
DE Short=PAP1;
GN Name=Pdap1; Synonyms=Haspp28;
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 [MRNA], AND PARTIAL PROTEIN SEQUENCE.
RC STRAIN=Sprague-Dawley; TISSUE=Brain;
RX PubMed=8615683; DOI=10.1006/abbi.1996.0101;
RA Shen L., Huang K.P., Chen H.C., Huang F.L.;
RT "Molecular cloning and characterization of a novel casein kinase II
RT substrate, HASPP28, from rat brain.";
RL Arch. Biochem. Biophys. 327:131-141(1996).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA].
RC TISSUE=Retina;
RX PubMed=8780057; DOI=10.1046/j.1471-4159.1996.66052213.x;
RA Fischer W.H., Schubert D.;
RT "Characterization of a novel platelet-derived growth factor-associated
RT protein.";
RL J. Neurochem. 66:2213-2216(1996).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Thymus;
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 [4]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-60 AND SER-63, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=16396499; DOI=10.1021/pr0503073;
RA Moser K., White F.M.;
RT "Phosphoproteomic analysis of rat liver by high capacity IMAC and LC-
RT MS/MS.";
RL J. Proteome Res. 5:98-104(2006).
RN [5]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-18; SER-57; SER-60 AND
RP SER-63, AND 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 -!- TISSUE SPECIFICITY: Present in all tissues tested, including brain,
CC lung, spleen, kidney, liver, heart, and muscle, in decreasing order of
CC abundance.
CC -!- PTM: Phosphorylated by several kinases in vitro. In vivo, can be
CC phosphorylated by CK2.
CC -!- SIMILARITY: Belongs to the PDAP1 family. {ECO:0000305}.
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DR EMBL; U26541; AAC52455.1; -; mRNA.
DR EMBL; U41744; AAC52531.1; -; mRNA.
DR EMBL; BC088140; AAH88140.1; -; mRNA.
DR PIR; S62782; S62782.
DR RefSeq; NP_072117.1; NM_022595.1.
DR AlphaFoldDB; Q62785; -.
DR SMR; Q62785; -.
DR BioGRID; 249111; 2.
DR STRING; 10116.ENSRNOP00000001310; -.
DR iPTMnet; Q62785; -.
DR PhosphoSitePlus; Q62785; -.
DR jPOST; Q62785; -.
DR PaxDb; Q62785; -.
DR PRIDE; Q62785; -.
DR Ensembl; ENSRNOT00000001310; ENSRNOP00000001310; ENSRNOG00000000990.
DR GeneID; 64527; -.
DR KEGG; rno:64527; -.
DR CTD; 11333; -.
DR RGD; 620442; Pdap1.
DR eggNOG; KOG3375; Eukaryota.
DR GeneTree; ENSGT00390000018509; -.
DR HOGENOM; CLU_084870_1_0_1; -.
DR InParanoid; Q62785; -.
DR OMA; FLRQRMK; -.
DR OrthoDB; 1572985at2759; -.
DR PhylomeDB; Q62785; -.
DR TreeFam; TF324338; -.
DR Reactome; R-RNO-6798695; Neutrophil degranulation.
DR PRO; PR:Q62785; -.
DR Proteomes; UP000002494; Chromosome 12.
DR Bgee; ENSRNOG00000000990; Expressed in ovary and 20 other tissues.
DR Genevisible; Q62785; RN.
DR GO; GO:0005829; C:cytosol; IBA:GO_Central.
DR InterPro; IPR019380; Casein_kinase_sb_PP28.
DR InterPro; IPR039876; HAP28.
DR PANTHER; PTHR22055; PTHR22055; 1.
DR Pfam; PF10252; PP28; 1.
PE 1: Evidence at protein level;
KW Acetylation; Direct protein sequencing; Isopeptide bond; Methylation;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..181
FT /note="28 kDa heat- and acid-stable phosphoprotein"
FT /id="PRO_0000083899"
FT REGION 1..118
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 151..181
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 45..60
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 99..118
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 151..169
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 18
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 19
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13442"
FT MOD_RES 57
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:22673903"
FT MOD_RES 60
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 63
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:16396499,
FT ECO:0007744|PubMed:22673903"
FT MOD_RES 70
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHX2"
FT MOD_RES 126
FT /note="N6-methyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13442"
FT MOD_RES 132
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q13442"
FT MOD_RES 164
FT /note="N6-acetyllysine"
FT /evidence="ECO:0000250|UniProtKB:Q3UHX2"
FT MOD_RES 176
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13442"
FT MOD_RES 178
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:Q13442"
FT CROSSLNK 52
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0000250|UniProtKB:Q13442"
FT CONFLICT 13
FT /note="R -> S (in Ref. 2; AAC52531)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 181 AA; 20605 MW; C9A74B7C41174F87 CRC64;
MPKGGRKGGH KGRVRQYTSP EEIDAQLQAE KQKANEEDEQ EEGGDGASGD PKKEKKSLDS
DESEDEDDDY QQKRKGVEGL IDIENPNRVA QTTKKVTQLD LDGPKELSRR EREEIEKQKA
KERYMKMHLA GKTEQAKADL ARLAIIRKQR EEAARKKEEE RKAKDDATLS GKRMQSLSLN
K
