Full text data of PRPSAP2
PRPSAP2
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
Phosphoribosyl pyrophosphate synthase-associated protein 2; PRPP synthase-associated protein 2 (41 kDa phosphoribosypyrophosphate synthetase-associated protein; PAP41)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Phosphoribosyl pyrophosphate synthase-associated protein 2; PRPP synthase-associated protein 2 (41 kDa phosphoribosypyrophosphate synthetase-associated protein; PAP41)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
hRBCD
IPI00003168
IPI00003168 Phosphoribosyl pyrophosphate synthetase-associated protein 2 enzyme inhibitor activity, Seems to play a negative regulatory role in PRPP synthesis, Ubiquitous soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
IPI00003168 Phosphoribosyl pyrophosphate synthetase-associated protein 2 enzyme inhibitor activity, Seems to play a negative regulatory role in PRPP synthesis, Ubiquitous soluble n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a n/a cytoplasmic n/a found at its expected molecular weight found at molecular weight
UniProt
O60256
ID KPRB_HUMAN Reviewed; 369 AA.
AC O60256; B4E1M8; B7ZKZ1; E7EMY2; Q6IAS2;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1998, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 2;
DE Short=PRPP synthase-associated protein 2;
DE AltName: Full=41 kDa phosphoribosypyrophosphate synthetase-associated protein;
DE Short=PAP41;
GN Name=PRPSAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9545573; DOI=10.1016/S0167-4781(97)00217-0;
RA Katashima R., Iwahana H., Fujimura M., Yamaoka T., Ishizuka T.,
RA Tatibana M., Itakura M.;
RT "Molecular cloning of a human cDNA for the 41-kDa
RT phosphoribosylpyrophosphate synthetase-associated protein.";
RL Biochim. Biophys. Acta 1396:245-250(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 18-36; 49-57; 61-97; 103-115; 137-181; 205-232;
RP 250-288; 293-330; 338-350 AND 352-363, PHOSPHORYLATION AT SER-227, AND
RP MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 13-369.
RG Structural genomics consortium (SGC);
RT "Human phosphoribosylpyrophosphate synthetase-associated protein 41
RT (Pap41).";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Seems to play a negative regulatory role in 5-
CC phosphoribose 1-diphosphate synthesis.
CC -!- SUBUNIT: Binds to PRPS1 and PRPS2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O60256-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60256-2; Sequence=VSP_044731;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O60256-3; Sequence=VSP_046462;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
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DR EMBL; AB007851; BAA25435.1; -; mRNA.
DR EMBL; AK303911; BAG64840.1; -; mRNA.
DR EMBL; CR457082; CAG33363.1; -; mRNA.
DR EMBL; AC090286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106050; AAI06051.1; -; mRNA.
DR EMBL; BC101670; AAI01671.1; -; mRNA.
DR EMBL; BC101672; AAI01673.1; -; mRNA.
DR EMBL; BC143475; AAI43476.1; -; mRNA.
DR RefSeq; NP_001230865.1; NM_001243936.1.
DR RefSeq; NP_001230869.1; NM_001243940.1.
DR RefSeq; NP_001230870.1; NM_001243941.1.
DR RefSeq; NP_001230871.1; NM_001243942.1.
DR RefSeq; NP_002758.1; NM_002767.3.
DR RefSeq; XP_005256781.1; XM_005256724.1.
DR RefSeq; XP_005256782.1; XM_005256725.1.
DR RefSeq; XP_005256783.1; XM_005256726.1.
DR UniGene; Hs.632236; -.
DR PDB; 2JI4; X-ray; 2.55 A; A=13-369.
DR PDBsum; 2JI4; -.
DR ProteinModelPortal; O60256; -.
DR SMR; O60256; 19-368.
DR IntAct; O60256; 1.
DR MINT; MINT-5003869; -.
DR STRING; 9606.ENSP00000268835; -.
DR BindingDB; O60256; -.
DR ChEMBL; CHEMBL2646; -.
DR PhosphoSite; O60256; -.
DR PaxDb; O60256; -.
DR PeptideAtlas; O60256; -.
DR PRIDE; O60256; -.
DR Ensembl; ENST00000268835; ENSP00000268835; ENSG00000141127.
DR Ensembl; ENST00000419071; ENSP00000392536; ENSG00000141127.
DR Ensembl; ENST00000542013; ENSP00000439129; ENSG00000141127.
DR GeneID; 5636; -.
DR KEGG; hsa:5636; -.
DR UCSC; uc010vyk.2; human.
DR CTD; 5636; -.
DR GeneCards; GC17P018702; -.
DR HGNC; HGNC:9467; PRPSAP2.
DR HPA; HPA021881; -.
DR MIM; 603762; gene.
DR neXtProt; NX_O60256; -.
DR PharmGKB; PA33822; -.
DR eggNOG; COG0462; -.
DR HOGENOM; HOG000210451; -.
DR HOVERGEN; HBG001520; -.
DR InParanoid; O60256; -.
DR OMA; KLLAKMM; -.
DR PhylomeDB; O60256; -.
DR ChiTaRS; PRPSAP2; human.
DR EvolutionaryTrace; O60256; -.
DR GeneWiki; PRPSAP2; -.
DR GenomeRNAi; 5636; -.
DR NextBio; 21902; -.
DR PRO; PR:O60256; -.
DR ArrayExpress; O60256; -.
DR Bgee; O60256; -.
DR CleanEx; HS_PRPSAP2; -.
DR Genevestigator; O60256; -.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:Ensembl.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Nucleotide biosynthesis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 369 Phosphoribosyl pyrophosphate synthase-
FT associated protein 2.
FT /FTId=PRO_0000141082.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 227 227 Phosphoserine.
FT VAR_SEQ 41 80 Missing (in isoform 2).
FT /FTId=VSP_044731.
FT VAR_SEQ 269 317 Missing (in isoform 3).
FT /FTId=VSP_046462.
FT CONFLICT 121 121 K -> R (in Ref. 2; BAG64840).
FT STRAND 21 24
FT HELIX 29 32
FT HELIX 33 42
FT STRAND 49 53
FT STRAND 59 63
FT STRAND 71 75
FT HELIX 82 98
FT STRAND 102 107
FT HELIX 126 136
FT STRAND 141 146
FT HELIX 150 155
FT STRAND 156 158
FT STRAND 160 163
FT HELIX 166 176
FT HELIX 180 182
FT STRAND 183 189
FT HELIX 190 192
FT HELIX 193 202
FT STRAND 206 210
FT STRAND 256 258
FT STRAND 263 272
FT HELIX 276 287
FT STRAND 292 300
FT HELIX 306 312
FT STRAND 317 324
FT HELIX 327 331
FT STRAND 336 339
FT HELIX 342 354
FT STRAND 362 364
SQ SEQUENCE 369 AA; 40926 MW; 12A0E46BD4AC55BF CRC64;
MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR
VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR
KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY
RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS
LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG
LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY
LFRNIGLDD
//
ID KPRB_HUMAN Reviewed; 369 AA.
AC O60256; B4E1M8; B7ZKZ1; E7EMY2; Q6IAS2;
DT 25-OCT-2002, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-AUG-1998, sequence version 1.
DT 22-JAN-2014, entry version 105.
DE RecName: Full=Phosphoribosyl pyrophosphate synthase-associated protein 2;
DE Short=PRPP synthase-associated protein 2;
DE AltName: Full=41 kDa phosphoribosypyrophosphate synthetase-associated protein;
DE Short=PAP41;
GN Name=PRPSAP2;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=9545573; DOI=10.1016/S0167-4781(97)00217-0;
RA Katashima R., Iwahana H., Fujimura M., Yamaoka T., Ishizuka T.,
RA Tatibana M., Itakura M.;
RT "Molecular cloning of a human cDNA for the 41-kDa
RT phosphoribosylpyrophosphate synthetase-associated protein.";
RL Biochim. Biophys. Acta 1396:245-250(1998).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Trachea;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
RT "Cloning of human full open reading frames in Gateway(TM) system entry
RT vector (pDONR201).";
RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16625196; DOI=10.1038/nature04689;
RA Zody M.C., Garber M., Adams D.J., Sharpe T., Harrow J., Lupski J.R.,
RA Nicholson C., Searle S.M., Wilming L., Young S.K., Abouelleil A.,
RA Allen N.R., Bi W., Bloom T., Borowsky M.L., Bugalter B.E., Butler J.,
RA Chang J.L., Chen C.-K., Cook A., Corum B., Cuomo C.A., de Jong P.J.,
RA DeCaprio D., Dewar K., FitzGerald M., Gilbert J., Gibson R.,
RA Gnerre S., Goldstein S., Grafham D.V., Grocock R., Hafez N.,
RA Hagopian D.S., Hart E., Norman C.H., Humphray S., Jaffe D.B.,
RA Jones M., Kamal M., Khodiyar V.K., LaButti K., Laird G., Lehoczky J.,
RA Liu X., Lokyitsang T., Loveland J., Lui A., Macdonald P., Major J.E.,
RA Matthews L., Mauceli E., McCarroll S.A., Mihalev A.H., Mudge J.,
RA Nguyen C., Nicol R., O'Leary S.B., Osoegawa K., Schwartz D.C.,
RA Shaw-Smith C., Stankiewicz P., Steward C., Swarbreck D.,
RA Venkataraman V., Whittaker C.A., Yang X., Zimmer A.R., Bradley A.,
RA Hubbard T., Birren B.W., Rogers J., Lander E.S., Nusbaum C.;
RT "DNA sequence of human chromosome 17 and analysis of rearrangement in
RT the human lineage.";
RL Nature 440:1045-1049(2006).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 3).
RC TISSUE=Brain, and Uterus;
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
RT project: the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [6]
RP PROTEIN SEQUENCE OF 18-36; 49-57; 61-97; 103-115; 137-181; 205-232;
RP 250-288; 293-330; 338-350 AND 352-363, PHOSPHORYLATION AT SER-227, AND
RP MASS SPECTROMETRY.
RC TISSUE=Embryonic kidney;
RA Bienvenut W.V., Waridel P., Quadroni M.;
RL Submitted (MAR-2009) to UniProtKB.
RN [7]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P.,
RA Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in
RT signaling networks.";
RL Cell 127:635-648(2006).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, AND MASS SPECTROMETRY.
RX PubMed=19413330; DOI=10.1021/ac9004309;
RA Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
RA Mohammed S.;
RT "Lys-N and trypsin cover complementary parts of the phosphoproteome in
RT a refined SCX-based approach.";
RL Anal. Chem. 81:4493-4501(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RC TISSUE=Leukemic T-cell;
RX PubMed=19690332; DOI=10.1126/scisignal.2000007;
RA Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K.,
RA Rodionov V., Han D.K.;
RT "Quantitative phosphoproteomic analysis of T cell receptor signaling
RT reveals system-wide modulation of protein-protein interactions.";
RL Sci. Signal. 2:RA46-RA46(2009).
RN [11]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S.,
RA Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full
RT phosphorylation site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-227, AND MASS
RP SPECTROMETRY.
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
RA Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
RA Blagoev B.;
RT "System-wide temporal characterization of the proteome and
RT phosphoproteome of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.55 ANGSTROMS) OF 13-369.
RG Structural genomics consortium (SGC);
RT "Human phosphoribosylpyrophosphate synthetase-associated protein 41
RT (Pap41).";
RL Submitted (FEB-2009) to the PDB data bank.
CC -!- FUNCTION: Seems to play a negative regulatory role in 5-
CC phosphoribose 1-diphosphate synthesis.
CC -!- SUBUNIT: Binds to PRPS1 and PRPS2.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=O60256-1; Sequence=Displayed;
CC Name=2;
CC IsoId=O60256-2; Sequence=VSP_044731;
CC Note=No experimental confirmation available;
CC Name=3;
CC IsoId=O60256-3; Sequence=VSP_046462;
CC Note=No experimental confirmation available;
CC -!- TISSUE SPECIFICITY: Ubiquitous.
CC -!- SIMILARITY: Belongs to the ribose-phosphate pyrophosphokinase
CC family.
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DR EMBL; AB007851; BAA25435.1; -; mRNA.
DR EMBL; AK303911; BAG64840.1; -; mRNA.
DR EMBL; CR457082; CAG33363.1; -; mRNA.
DR EMBL; AC090286; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC107982; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC106050; AAI06051.1; -; mRNA.
DR EMBL; BC101670; AAI01671.1; -; mRNA.
DR EMBL; BC101672; AAI01673.1; -; mRNA.
DR EMBL; BC143475; AAI43476.1; -; mRNA.
DR RefSeq; NP_001230865.1; NM_001243936.1.
DR RefSeq; NP_001230869.1; NM_001243940.1.
DR RefSeq; NP_001230870.1; NM_001243941.1.
DR RefSeq; NP_001230871.1; NM_001243942.1.
DR RefSeq; NP_002758.1; NM_002767.3.
DR RefSeq; XP_005256781.1; XM_005256724.1.
DR RefSeq; XP_005256782.1; XM_005256725.1.
DR RefSeq; XP_005256783.1; XM_005256726.1.
DR UniGene; Hs.632236; -.
DR PDB; 2JI4; X-ray; 2.55 A; A=13-369.
DR PDBsum; 2JI4; -.
DR ProteinModelPortal; O60256; -.
DR SMR; O60256; 19-368.
DR IntAct; O60256; 1.
DR MINT; MINT-5003869; -.
DR STRING; 9606.ENSP00000268835; -.
DR BindingDB; O60256; -.
DR ChEMBL; CHEMBL2646; -.
DR PhosphoSite; O60256; -.
DR PaxDb; O60256; -.
DR PeptideAtlas; O60256; -.
DR PRIDE; O60256; -.
DR Ensembl; ENST00000268835; ENSP00000268835; ENSG00000141127.
DR Ensembl; ENST00000419071; ENSP00000392536; ENSG00000141127.
DR Ensembl; ENST00000542013; ENSP00000439129; ENSG00000141127.
DR GeneID; 5636; -.
DR KEGG; hsa:5636; -.
DR UCSC; uc010vyk.2; human.
DR CTD; 5636; -.
DR GeneCards; GC17P018702; -.
DR HGNC; HGNC:9467; PRPSAP2.
DR HPA; HPA021881; -.
DR MIM; 603762; gene.
DR neXtProt; NX_O60256; -.
DR PharmGKB; PA33822; -.
DR eggNOG; COG0462; -.
DR HOGENOM; HOG000210451; -.
DR HOVERGEN; HBG001520; -.
DR InParanoid; O60256; -.
DR OMA; KLLAKMM; -.
DR PhylomeDB; O60256; -.
DR ChiTaRS; PRPSAP2; human.
DR EvolutionaryTrace; O60256; -.
DR GeneWiki; PRPSAP2; -.
DR GenomeRNAi; 5636; -.
DR NextBio; 21902; -.
DR PRO; PR:O60256; -.
DR ArrayExpress; O60256; -.
DR Bgee; O60256; -.
DR CleanEx; HS_PRPSAP2; -.
DR Genevestigator; O60256; -.
DR GO; GO:0002189; C:ribose phosphate diphosphokinase complex; IEA:Ensembl.
DR GO; GO:0004857; F:enzyme inhibitor activity; TAS:ProtInc.
DR GO; GO:0000287; F:magnesium ion binding; IEA:InterPro.
DR GO; GO:0004749; F:ribose phosphate diphosphokinase activity; IEA:InterPro.
DR GO; GO:0060348; P:bone development; IEA:Ensembl.
DR GO; GO:0006139; P:nucleobase-containing compound metabolic process; TAS:ProtInc.
DR GO; GO:0009165; P:nucleotide biosynthetic process; IEA:UniProtKB-KW.
DR InterPro; IPR005946; Rib-P_diPkinase.
DR Pfam; PF14572; Pribosyl_synth; 1.
DR TIGRFAMs; TIGR01251; ribP_PPkin; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Complete proteome;
KW Direct protein sequencing; Nucleotide biosynthesis; Phosphoprotein;
KW Reference proteome.
FT CHAIN 1 369 Phosphoribosyl pyrophosphate synthase-
FT associated protein 2.
FT /FTId=PRO_0000141082.
FT MOD_RES 1 1 N-acetylmethionine.
FT MOD_RES 227 227 Phosphoserine.
FT VAR_SEQ 41 80 Missing (in isoform 2).
FT /FTId=VSP_044731.
FT VAR_SEQ 269 317 Missing (in isoform 3).
FT /FTId=VSP_046462.
FT CONFLICT 121 121 K -> R (in Ref. 2; BAG64840).
FT STRAND 21 24
FT HELIX 29 32
FT HELIX 33 42
FT STRAND 49 53
FT STRAND 59 63
FT STRAND 71 75
FT HELIX 82 98
FT STRAND 102 107
FT HELIX 126 136
FT STRAND 141 146
FT HELIX 150 155
FT STRAND 156 158
FT STRAND 160 163
FT HELIX 166 176
FT HELIX 180 182
FT STRAND 183 189
FT HELIX 190 192
FT HELIX 193 202
FT STRAND 206 210
FT STRAND 256 258
FT STRAND 263 272
FT HELIX 276 287
FT STRAND 292 300
FT HELIX 306 312
FT STRAND 317 324
FT HELIX 327 331
FT STRAND 336 339
FT HELIX 342 354
FT STRAND 362 364
SQ SEQUENCE 369 AA; 40926 MW; 12A0E46BD4AC55BF CRC64;
MFCVTPPELE TKMNITKGGL VLFSANSNSS CMELSKKIAE RLGVEMGKVQ VYQEPNRETR
VQIQESVRGK DVFIIQTVSK DVNTTIMELL IMVYACKTSC AKSIIGVIPY FPYSKQCKMR
KRGSIVSKLL ASMMCKAGLT HLITMDLHQK EIQGFFNIPV DNLRASPFLL QYIQEEIPDY
RNAVIVAKSP ASAKRAQSFA ERLRLGIAVI HGEAQDAESD LVDGRHSPPM VRSVAAIHPS
LEIPMLIPKE KPPITVVGDV GGRIAIIVDD IIDDVDSFLA AAETLKERGA YKIFVMATHG
LLSSDAPRRI EESAIDEVVV TNTIPHEVQK LQCPKIKTVD ISMILSEAIR RIHNGESMSY
LFRNIGLDD
//
MIM
603762
*RECORD*
*FIELD* NO
603762
*FIELD* TI
*603762 PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE-ASSOCIATED PROTEIN 2; PRPSAP2
;;PAP41
read more*FIELD* TX
CLONING
Phosphoribosylpyrophosphate (PRPP) is a primary substrate and a critical
control factor for de novo synthesis of purine and pyrimidine
nucleotides, histidine, tryptophan, and NAD. The enzyme PRPP synthetase
(PRPS), which catalyzes the formation of PRPP, exists in an aggregate
composed of 2 catalytic subunits, PRPS I (PRPS1; 311850) and PRPS II
(PRPS2; 311860), and 2 associated subunits, PAP39 (601249) and PAP41. By
searching an EST database for sequences related to PAP39, Katashima et
al. (1998) identified cDNAs encoding PAP41. The predicted 369-amino acid
protein exhibited 72%, 51%, and 50% sequence identity with PAP39, PRPS2,
and PRPS2, respectively. The rat and human PAP41 proteins are 99%
identical. Northern blot analysis revealed that PAP41 is expressed as a
2.1-kb mRNA in several human cell lines.
MAPPING
By fluorescence in situ hybridization, Katashima et al. (1998) mapped
the PRPSAP2 gene to 17p12-p11.2.
*FIELD* RF
1. Katashima, R.; Iwahana, H.; Fujimura, M.; Yamaoka, T.; Ishizuka,
T.; Tatibana, M.; Itakura, M.: Molecular cloning of a human cDNA
for the 41-kDa phosphoribosylpyrophosphate synthetase-associated protein. Biochim.
Biophys. Acta 1396: 245-250, 1998.
2. Katashima, R.; Iwahana, H.; Fujimura, M.; Yamaoka, T.; Itakura,
M.: Assignment of the human phosphoribosylpyrophosphate synthetase-associated
protein 41 gene (PRPSAP2) to 17p11.2-p12. Genomics 54: 180-181,
1998.
*FIELD* CD
Rebekah S. Rasooly: 4/21/1999
*FIELD* ED
carol: 08/17/2007
alopez: 4/21/1999
*RECORD*
*FIELD* NO
603762
*FIELD* TI
*603762 PHOSPHORIBOSYLPYROPHOSPHATE SYNTHETASE-ASSOCIATED PROTEIN 2; PRPSAP2
;;PAP41
read more*FIELD* TX
CLONING
Phosphoribosylpyrophosphate (PRPP) is a primary substrate and a critical
control factor for de novo synthesis of purine and pyrimidine
nucleotides, histidine, tryptophan, and NAD. The enzyme PRPP synthetase
(PRPS), which catalyzes the formation of PRPP, exists in an aggregate
composed of 2 catalytic subunits, PRPS I (PRPS1; 311850) and PRPS II
(PRPS2; 311860), and 2 associated subunits, PAP39 (601249) and PAP41. By
searching an EST database for sequences related to PAP39, Katashima et
al. (1998) identified cDNAs encoding PAP41. The predicted 369-amino acid
protein exhibited 72%, 51%, and 50% sequence identity with PAP39, PRPS2,
and PRPS2, respectively. The rat and human PAP41 proteins are 99%
identical. Northern blot analysis revealed that PAP41 is expressed as a
2.1-kb mRNA in several human cell lines.
MAPPING
By fluorescence in situ hybridization, Katashima et al. (1998) mapped
the PRPSAP2 gene to 17p12-p11.2.
*FIELD* RF
1. Katashima, R.; Iwahana, H.; Fujimura, M.; Yamaoka, T.; Ishizuka,
T.; Tatibana, M.; Itakura, M.: Molecular cloning of a human cDNA
for the 41-kDa phosphoribosylpyrophosphate synthetase-associated protein. Biochim.
Biophys. Acta 1396: 245-250, 1998.
2. Katashima, R.; Iwahana, H.; Fujimura, M.; Yamaoka, T.; Itakura,
M.: Assignment of the human phosphoribosylpyrophosphate synthetase-associated
protein 41 gene (PRPSAP2) to 17p11.2-p12. Genomics 54: 180-181,
1998.
*FIELD* CD
Rebekah S. Rasooly: 4/21/1999
*FIELD* ED
carol: 08/17/2007
alopez: 4/21/1999