KPRB_PONAB
ID KPRB_PONAB Reviewed; 369 AA.
AC Q5RBA8;
DT 24-MAR-2009, integrated into UniProtKB/Swiss-Prot.
DT 21-DEC-2004, sequence version 1.
DT 25-MAY-2022, entry version 74.
DE RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 2;
DE Short=PRPP synthase-associated protein 2;
GN Name=PRPSAP2;
OS Pongo abelii (Sumatran orangutan) (Pongo pygmaeus abelii).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Pongo.
OX NCBI_TaxID=9601;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
RC TISSUE=Kidney;
RG The German cDNA consortium;
RL Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases.
CC -!- FUNCTION: Seems to play a negative regulatory role in 5-phosphoribose
CC 1-diphosphate synthesis. {ECO:0000250}.
CC -!- SUBUNIT: Binds to PRPS1 and PRPS2. {ECO:0000250}.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase family.
CC {ECO:0000305}.
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DR EMBL; CR858743; CAH90952.1; -; mRNA.
DR RefSeq; NP_001127355.1; NM_001133883.1.
DR AlphaFoldDB; Q5RBA8; -.
DR SMR; Q5RBA8; -.
DR STRING; 9601.ENSPPYP00000009060; -.
DR GeneID; 100174419; -.
DR KEGG; pon:100174419; -.
DR CTD; 5636; -.
DR eggNOG; KOG1503; Eukaryota.
DR InParanoid; Q5RBA8; -.
DR OrthoDB; 1043963at2759; -.
DR Proteomes; UP000001595; Unplaced.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR CDD; cd06223; PRTases_typeI; 1.
DR Gene3D; 3.40.50.2020; -; 2.
DR InterPro; IPR029099; Pribosyltran_N.
DR InterPro; IPR000836; PRibTrfase_dom.
DR InterPro; IPR029057; PRTase-like.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR PANTHER; PTHR10210; PTHR10210; 1.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR Pfam; PF13793; Pribosyltran_N; 1.
DR SUPFAM; SSF53271; SSF53271; 2.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE 2: Evidence at transcript level;
KW Acetylation; Nucleotide biosynthesis; Phosphoprotein; Reference proteome.
FT CHAIN 1..369
FT /note="Phosphoribosyl pyrophosphate synthase-associated
FT protein 2"
FT /id="PRO_0000366926"
FT MOD_RES 1
FT /note="N-acetylmethionine"
FT /evidence="ECO:0000250|UniProtKB:O60256"
FT MOD_RES 5
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:O60256"
FT MOD_RES 219
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60256"
FT MOD_RES 227
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60256"
FT MOD_RES 233
FT /note="Phosphoserine"
FT /evidence="ECO:0000250|UniProtKB:O60256"
SQ SEQUENCE 369 AA; 40897 MW; C24FD6BF79E4647B CRC64;
MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR
VQIQESVRGK DVFIIQTISK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR
KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY
RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS
LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG
LLSSDAPRLI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY
LFRNIGLDD