PHOP2_HUMAN
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 03-AUG-2022, entry version 147.
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=H2O + pyridoxal 5'-phosphate = phosphate + pyridoxal;
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}.
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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_001008489.3.
DR RefSeq; NP_001186214.1; NM_001199285.1.
DR RefSeq; NP_001186215.1; NM_001199286.1.
DR RefSeq; NP_001186216.1; NM_001199287.1.
DR RefSeq; NP_001186217.1; NM_001199288.1.
DR AlphaFoldDB; Q8TCD6; -.
DR BioGRID; 138930; 25.
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; Q8TCD6; -.
DR PeptideAtlas; Q8TCD6; -.
DR PRIDE; Q8TCD6; -.
DR ProteomicsDB; 74123; -.
DR Antibodypedia; 33816; 100 antibodies from 24 providers.
DR DNASU; 493911; -.
DR Ensembl; ENST00000359744.8; ENSP00000352782.3; ENSG00000144362.12.
DR Ensembl; ENST00000616481.4; ENSP00000481680.1; ENSG00000144362.12.
DR Ensembl; ENST00000616524.4; ENSP00000481046.1; ENSG00000144362.12.
DR Ensembl; ENST00000617738.4; ENSP00000481857.1; ENSG00000144362.12.
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 CTD; 493911; -.
DR GeneCards; PHOSPHO2; -.
DR HGNC; HGNC:28316; PHOSPHO2.
DR HPA; ENSG00000144362; Low tissue specificity.
DR neXtProt; NX_Q8TCD6; -.
DR OpenTargets; ENSG00000144362; -.
DR PharmGKB; PA134947617; -.
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; 1454608at2759; -.
DR PhylomeDB; Q8TCD6; -.
DR TreeFam; TF300112; -.
DR BioCyc; MetaCyc:HS07168-MON; -.
DR PathwayCommons; Q8TCD6; -.
DR SABIO-RK; Q8TCD6; -.
DR SignaLink; Q8TCD6; -.
DR BioGRID-ORCS; 493911; 8 hits in 1069 CRISPR screens.
DR GenomeRNAi; 493911; -.
DR Pharos; Q8TCD6; Tdark.
DR PRO; PR:Q8TCD6; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; Q8TCD6; protein.
DR Bgee; ENSG00000144362; Expressed in secondary oocyte and 171 other tissues.
DR ExpressionAtlas; Q8TCD6; baseline and differential.
DR Genevisible; Q8TCD6; HS.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0016791; F:phosphatase activity; IBA:GO_Central.
DR GO; GO:0033883; F:pyridoxal phosphatase activity; IEA:UniProtKB-EC.
DR Gene3D; 3.40.50.1000; -; 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 PANTHER; PTHR20889; PTHR20889; 1.
DR Pfam; PF06888; Put_Phosphatase; 1.
DR PIRSF; PIRSF031051; PyrdxlP_Pase_PHOSPHO2; 1.
DR SUPFAM; SSF56784; SSF56784; 1.
DR TIGRFAMs; TIGR01489; DKMTPPase-SF; 1.
PE 1: Evidence at protein level;
KW Hydrolase; Magnesium; Metal-binding; Pyridoxal phosphate;
KW 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
