ID PHOP2_HUMAN Reviewed; 241 AA. AC Q8TCD6; B2RC30; D3DPC7; DT 10-JAN-2006, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2002, sequence version 1. DT 02-SEP-2026, entry version 165. DE RecName: Full=Pyridoxal phosphate phosphatase PHOSPHO2; DE EC=3.1.3.74 {ECO:0000269|PubMed:16054448}; GN Name=PHOSPHO2; 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 [LARGE SCALE MRNA]. RC TISSUE=Brain; 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., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., 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., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA 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 [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=15815621; DOI=10.1038/nature03466; RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P., RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C., RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L., RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A., RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J., RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M., RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T., RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S., RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K., RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C., RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S., RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C., RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M., RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C., RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J., RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E., RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X., RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M., RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C., RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S., RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H., RA Wilson R.K.; RT "Generation and annotation of the DNA sequences of human chromosomes 2 and RT 4."; RL Nature 434:724-731(2005). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., RA Hunkapiller M.W., Myers E.W., Venter J.C.; RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Bone, and Lung; 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 [5] RP FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES. RX PubMed=16054448; DOI=10.1016/j.bbapap.2005.06.009; RA Roberts S.J., Stewart A.J., Schmid R., Blindauer C.A., Bond S.R., RA Sadler P.J., Farquharson C.; RT "Probing the substrate specificities of human PHOSPHO1 and PHOSPHO2."; RL Biochim. Biophys. Acta 1752:73-82(2005). CC -!- FUNCTION: Phosphatase that has high activity toward pyridoxal 5'- CC phosphate (PLP). Also active at much lower level toward pyrophosphate, CC phosphoethanolamine (PEA), phosphocholine (PCho), phospho-l-tyrosine, CC fructose-6-phosphate, p-nitrophenyl phosphate, and h-glycerophosphate. CC {ECO:0000269|PubMed:16054448}. CC -!- CATALYTIC ACTIVITY: CC Reaction=pyridoxal 5'-phosphate + H2O = pyridoxal + phosphate; CC Xref=Rhea:RHEA:20533, ChEBI:CHEBI:15377, ChEBI:CHEBI:17310, CC ChEBI:CHEBI:43474, ChEBI:CHEBI:597326; EC=3.1.3.74; CC Evidence={ECO:0000269|PubMed:16054448}; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; CC Evidence={ECO:0000250|UniProtKB:Q8TCT1}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=45.5 uM for pyridoxal 5'-phosphate {ECO:0000269|PubMed:16054448}; CC Vmax=633 nmol/min/mg enzyme with pyridoxal 5'-phosphate as substrate CC {ECO:0000269|PubMed:16054448}; CC -!- INTERACTION: CC Q8TCD6; P18859: ATP5PF; NbExp=5; IntAct=EBI-2861380, EBI-2606700; CC Q8TCD6; Q9BXJ5: C1QTNF2; NbExp=3; IntAct=EBI-2861380, EBI-2817707; CC Q8TCD6; P21333-2: FLNA; NbExp=3; IntAct=EBI-2861380, EBI-9641086; CC Q8TCD6; Q5VSY0: GKAP1; NbExp=3; IntAct=EBI-2861380, EBI-743722; CC Q8TCD6; Q8WXH2: JPH3; NbExp=3; IntAct=EBI-2861380, EBI-1055254; CC Q8TCD6; Q15742: NAB2; NbExp=6; IntAct=EBI-2861380, EBI-8641936; CC Q8TCD6; Q8WW01: TSEN15; NbExp=5; IntAct=EBI-2861380, EBI-372432; CC Q8TCD6; P40337-2: VHL; NbExp=3; IntAct=EBI-2861380, EBI-12157263; CC Q8TCD6; Q9Y3C0: WASHC3; NbExp=5; IntAct=EBI-2861380, EBI-712969; CC -!- SIMILARITY: Belongs to the HAD-like hydrolase superfamily. PHOSPHO CC family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AK314915; BAG37427.1; -; mRNA. DR EMBL; AC016772; AAY24234.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11262.1; -; Genomic_DNA. DR EMBL; CH471058; EAX11263.1; -; Genomic_DNA. DR EMBL; BC022324; AAH22324.1; -; mRNA. DR EMBL; BC106013; AAI06014.1; -; mRNA. DR CCDS; CCDS33319.1; -. DR RefSeq; NP_001008489.1; NM_001008489.4. DR RefSeq; NP_001186214.1; NM_001199285.2. DR RefSeq; NP_001186215.1; NM_001199286.2. DR RefSeq; NP_001186216.1; NM_001199287.2. DR RefSeq; NP_001186217.1; NM_001199288.2. DR AlphaFoldDB; Q8TCD6; -. DR BioGRID; 138930; 25. DR FunCoup; Q8TCD6; 1227. DR IntAct; Q8TCD6; 14. DR STRING; 9606.ENSP00000481046; -. DR DEPOD; PHOSPHO2; -. DR iPTMnet; Q8TCD6; -. DR PhosphoSitePlus; Q8TCD6; -. DR BioMuta; PHOSPHO2; -. DR DMDM; 74730590; -. DR MassIVE; Q8TCD6; -. DR PaxDb; 9606-ENSP00000481046; -. DR PeptideAtlas; Q8TCD6; -. DR ProteomicsDB; 74123; -. DR Antibodypedia; 33816; 97 antibodies from 23 providers. DR DNASU; 493911; -. DR Ensembl; ENST00000359744.8; ENSP00000352782.3; ENSG00000144362.13. DR Ensembl; ENST00000616481.4; ENSP00000481680.1; ENSG00000144362.13. DR Ensembl; ENST00000616524.4; ENSP00000481046.1; ENSG00000144362.13. DR Ensembl; ENST00000617738.4; ENSP00000481857.1; ENSG00000144362.13. DR Ensembl; ENST00000857416.1; ENSP00000527475.1; ENSG00000144362.13. DR Ensembl; ENST00000857417.1; ENSP00000527476.1; ENSG00000144362.13. DR Ensembl; ENST00000857418.1; ENSP00000527477.1; ENSG00000144362.13. DR Ensembl; ENST00000857419.1; ENSP00000527478.1; ENSG00000144362.13. DR Ensembl; ENST00000857420.1; ENSP00000527479.1; ENSG00000144362.13. DR Ensembl; ENST00000857421.1; ENSP00000527480.1; ENSG00000144362.13. DR Ensembl; ENST00000857422.1; ENSP00000527481.1; ENSG00000144362.13. DR Ensembl; ENST00000857423.1; ENSP00000527482.1; ENSG00000144362.13. DR Ensembl; ENST00000857424.1; ENSP00000527483.1; ENSG00000144362.13. DR Ensembl; ENST00000931227.1; ENSP00000601286.1; ENSG00000144362.13. DR Ensembl; ENST00000931228.1; ENSP00000601287.1; ENSG00000144362.13. DR Ensembl; ENST00000931229.1; ENSP00000601288.1; ENSG00000144362.13. DR Ensembl; ENST00000931230.1; ENSP00000601289.1; ENSG00000144362.13. DR Ensembl; ENST00000931231.1; ENSP00000601290.1; ENSG00000144362.13. DR Ensembl; ENST00000931232.1; ENSP00000601291.1; ENSG00000144362.13. DR Ensembl; ENST00000931233.1; ENSP00000601292.1; ENSG00000144362.13. DR Ensembl; ENST00000931234.1; ENSP00000601293.1; ENSG00000144362.13. DR Ensembl; ENST00000931235.1; ENSP00000601294.1; ENSG00000144362.13. DR Ensembl; ENST00000931236.1; ENSP00000601295.1; ENSG00000144362.13. DR Ensembl; ENST00000931237.1; ENSP00000601296.1; ENSG00000144362.13. DR Ensembl; ENST00000931238.1; ENSP00000601297.1; ENSG00000144362.13. DR Ensembl; ENST00000931239.1; ENSP00000601298.1; ENSG00000144362.13. DR Ensembl; ENST00000931240.1; ENSP00000601299.1; ENSG00000144362.13. DR Ensembl; ENST00000961207.1; ENSP00000631266.1; ENSG00000144362.13. DR Ensembl; ENST00000961208.1; ENSP00000631267.1; ENSG00000144362.13. DR Ensembl; ENST00000961209.1; ENSP00000631268.1; ENSG00000144362.13. DR GeneID; 493911; -. DR KEGG; hsa:493911; -. DR MANE-Select; ENST00000359744.8; ENSP00000352782.3; NM_001008489.4; NP_001008489.1. DR UCSC; uc002ufg.4; human. DR AGR; HGNC:28316; -. DR ClinPGx; PA134947617; -. DR CTD; 493911; -. DR DisGeNET; 493911; -. DR GeneCards; PHOSPHO2; -. DR HGNC; HGNC:28316; PHOSPHO2. DR HPA; ENSG00000144362; Low tissue specificity. DR OpenTargets; ENSG00000144362; -. DR VEuPathDB; HostDB:ENSG00000144362; -. DR eggNOG; KOG3120; Eukaryota. DR GeneTree; ENSGT00390000007741; -. DR HOGENOM; CLU_068983_0_1_1; -. DR InParanoid; Q8TCD6; -. DR OMA; HNLADCF; -. DR OrthoDB; 10267182at2759; -. DR PAN-GO; Q8TCD6; 1 GO annotation based on evolutionary models. DR PhylomeDB; Q8TCD6; -. DR BioCyc; MetaCyc:HS07168-MONOMER; -. DR PathwayCommons; Q8TCD6; -. DR SABIO-RK; Q8TCD6; -. DR SignaLink; Q8TCD6; -. DR Agora; ENSG00000144362; -. DR BioGRID-ORCS; 493911; 8 hits in 1157 CRISPR screens. DR GenomeRNAi; 493911; -. DR Pharos; Q8TCD6; Tbio. DR PRO; PR:Q8TCD6; -. DR Proteomes; UP000005640; Chromosome 2. DR RNAct; Q8TCD6; protein. DR Bgee; ENSG00000144362; Expressed in secondary oocyte and 173 other cell types or tissues. DR ExpressionAtlas; Q8TCD6; baseline and differential. DR GO; GO:0033883; F:pyridoxal phosphatase activity; EXP:UniProtKB. DR CDD; cd16418; HAD_Pase; 1. DR Gene3D; 3.40.50.1000; HAD superfamily/HAD-like; 1. DR InterPro; IPR036412; HAD-like_sf. DR InterPro; IPR006384; HAD_hydro_PyrdxlP_Pase-like. DR InterPro; IPR023214; HAD_sf. DR InterPro; IPR016965; Pase_PHOSPHO-typ. DR NCBIfam; TIGR01489; DKMTPPase-SF; 1. DR NCBIfam; TIGR01488; HAD-SF-IB; 1. DR PANTHER; PTHR20889; PHOSPHATASE, ORPHAN 1, 2; 1. DR PANTHER; PTHR20889:SF1; PYRIDOXAL PHOSPHATE PHOSPHATASE PHOSPHO2; 1. DR Pfam; PF06888; Put_Phosphatase; 1. DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1. DR SUPFAM; SSF56784; HAD-like; 1. PE 1: Evidence at protein level; KW Hydrolase; Magnesium; Metal-binding; Proteomics identification; KW Pyridoxal phosphate; Reference proteome. FT CHAIN 1..241 FT /note="Pyridoxal phosphate phosphatase PHOSPHO2" FT /id="PRO_0000068833" FT ACT_SITE 8 FT /note="Nucleophile" FT /evidence="ECO:0000250|UniProtKB:Q8TCT1" FT ACT_SITE 10 FT /note="Proton donor" FT /evidence="ECO:0000250|UniProtKB:Q96GD0" FT BINDING 8 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q96GD0" FT BINDING 10 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q96GD0" FT BINDING 19 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8TCT1" FT BINDING 99 FT /ligand="substrate" FT /evidence="ECO:0000250|UniProtKB:Q8TCT1" FT BINDING 179 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000250|UniProtKB:Q96GD0" FT VARIANT 206 FT /note="K -> E (in dbSNP:rs56036676)" FT /id="VAR_062092" SQ SEQUENCE 241 AA; 27769 MW; C9F0447F2A1A5FFA CRC64; MKILLVFDFD NTIIDDNSDT WIVQCAPNKK LPIELRDSYR KGFWTEFMGR VFKYLGDKGV REHEMKRAVT SLPFTPGMVE LFNFIRKNKD KFDCIIISDS NSVFIDWVLE AASFHDIFDK VFTNPAAFNS NGHLTVENYH THSCNRCPKN LCKKVVLIEF VDKQLQQGVN YTQIVYIGDG GNDVCPVTFL KNDDVAMPRK GYTLQKTLSR MSQNLEPMEY SVVVWSSGVD IISHLQFLIK D //