ID AMPD2_HUMAN Reviewed; 825 AA. AC Q01433; A0A5F9UK94; B4DK50; B4DZI5; E9PNG0; Q14856; Q14857; Q16686; Q16687; AC Q16688; Q16729; Q5T693; Q5T695; Q96IA1; Q9UDX8; Q9UDX9; Q9UMU4; DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot. DT 13-SEP-2023, sequence version 3. DT 27-MAR-2024, entry version 208. DE RecName: Full=AMP deaminase 2 {ECO:0000305}; DE EC=3.5.4.6 {ECO:0000269|PubMed:23911318}; DE AltName: Full=AMP deaminase isoform L; GN Name=AMPD2 {ECO:0000312|HGNC:HGNC:469}; 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 [GENOMIC RNA] OF 73-825 (ISOFORM EX1B-2-3), AND RP NUCLEOTIDE SEQUENCE [MRNA] OF 73-825 (ISOFORM EX1B-2-3). RC TISSUE=Placenta; RX PubMed=1429593; DOI=10.1016/s0021-9258(18)41686-9; RA Bausch-Jurken M.T., Mahnke-Zizelman D.K., Morisaki T., Sabina R.L.; RT "Molecular cloning of AMP deaminase isoform L. Sequence and bacterial RT expression of human AMPD2 cDNA."; RL J. Biol. Chem. 267:22407-22413(1992). RN [2] RP NUCLEOTIDE SEQUENCE [MRNA] OF 1-202 (ISOFORM EX1A-2-3), NUCLEOTIDE SEQUENCE RP [MRNA] OF 1-202 (ISOFORM EX1B-2-3), AND NUCLEOTIDE SEQUENCE [GENOMIC RNA] RP OF 1-670 (ISOFORM EX1B-3). RX PubMed=8526848; DOI=10.1042/bj3120401; RA Van den Bergh F., Sabina R.L.; RT "Characterization of human AMP deaminase 2 (AMPD2) gene expression reveals RT alternative transcripts encoding variable N-terminal extensions of isoform RT L."; RL Biochem. J. 312:401-410(1995). RN [3] RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] (ISOFORMS EX1B-3; EX1A-2-3 AND EX1B-2-3). RX PubMed=8764830; DOI=10.1016/0167-4781(96)00089-9; RA Mahnke-Zizelman D.K., van den Bergh F., Bausch-Jurken M.T., Eddy R., RA Sait S., Shows T.B., Sabina R.L.; RT "Cloning, sequence and characterization of the human AMPD2 gene: evidence RT for transcriptional regulation by two closely spaced promoters."; RL Biochim. Biophys. Acta 1308:122-132(1996). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS EX1B-3 AND 5), AND VARIANT RP VAL-468. RC TISSUE=Testis, and Thalamus; 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 [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16710414; DOI=10.1038/nature04727; RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K., RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.; RT "The DNA sequence and biological annotation of human chromosome 1."; RL Nature 441:315-321(2006). RN [6] 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [7] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM EX1A-2-3). RC TISSUE=Brain; 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 [8] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling RT networks."; RL Cell 127:635-648(2006). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Platelet; RX PubMed=18088087; DOI=10.1021/pr0704130; RA Zahedi R.P., Lewandrowski U., Wiesner J., Wortelkamp S., Moebius J., RA Schuetz C., Walter U., Gambaryan S., Sickmann A.; RT "Phosphoproteome of resting human platelets."; RL J. Proteome Res. 7:526-534(2008). RN [10] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64; SER-97; THR-134 AND RP SER-136, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [11] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-22 AND SER-136, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-114 AND SER-136, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [13] 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., Buerckstuemmer T., RA 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 [14] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-136, AND IDENTIFICATION BY RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21406692; DOI=10.1126/scisignal.2001570; RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.; RT "System-wide temporal characterization of the proteome and phosphoproteome RT of human embryonic stem cell differentiation."; RL Sci. Signal. 4:RS3-RS3(2011). RN [15] RP FUNCTION, TISSUE SPECIFICITY, VARIANTS PCH9 HIS-620; ASP-724 AND TYR-739, RP AND CATALYTIC ACTIVITY. RX PubMed=23911318; DOI=10.1016/j.cell.2013.07.005; RA Akizu N., Cantagrel V., Schroth J., Cai N., Vaux K., McCloskey D., RA Naviaux R.K., Van Vleet J., Fenstermaker A.G., Silhavy J.L., Scheliga J.S., RA Toyama K., Morisaki H., Sonmez F.M., Celep F., Oraby A., Zaki M.S., RA Al-Baradie R., Faqeih E.A., Saleh M.A., Spencer E., Rosti R.O., Scott E., RA Nickerson E., Gabriel S., Morisaki T., Holmes E.W., Gleeson J.G.; RT "AMPD2 regulates GTP synthesis and is mutated in a potentially treatable RT neurodegenerative brainstem disorder."; RL Cell 154:505-517(2013). RN [16] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-64; SER-80; SER-114; RP SER-136 AND SER-138, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE RP ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [17] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-46; SER-114 AND SER-136, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Liver; RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014; RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., RA Ye M., Zou H.; RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver RT phosphoproteome."; RL J. Proteomics 96:253-262(2014). RN [18] RP INVOLVEMENT IN SPG63. RX PubMed=24482476; DOI=10.1126/science.1247363; RA Novarino G., Fenstermaker A.G., Zaki M.S., Hofree M., Silhavy J.L., RA Heiberg A.D., Abdellateef M., Rosti B., Scott E., Mansour L., Masri A., RA Kayserili H., Al-Aama J.Y., Abdel-Salam G.M., Karminejad A., Kara M., RA Kara B., Bozorgmehri B., Ben-Omran T., Mojahedi F., Mahmoud I.G., RA Bouslam N., Bouhouche A., Benomar A., Hanein S., Raymond L., Forlani S., RA Mascaro M., Selim L., Shehata N., Al-Allawi N., Bindu P.S., Azam M., RA Gunel M., Caglayan A., Bilguvar K., Tolun A., Issa M.Y., Schroth J., RA Spencer E.G., Rosti R.O., Akizu N., Vaux K.K., Johansen A., Koh A.A., RA Megahed H., Durr A., Brice A., Stevanin G., Gabriel S.B., Ideker T., RA Gleeson J.G.; RT "Exome sequencing links corticospinal motor neuron disease to common RT neurodegenerative disorders."; RL Science 343:506-511(2014). CC -!- FUNCTION: AMP deaminase plays a critical role in energy metabolism. CC Catalyzes the deamination of AMP to IMP and plays an important role in CC the purine nucleotide cycle. {ECO:0000269|PubMed:23911318}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + H(+) + H2O = IMP + NH4(+); Xref=Rhea:RHEA:14777, CC ChEBI:CHEBI:15377, ChEBI:CHEBI:15378, ChEBI:CHEBI:28938, CC ChEBI:CHEBI:58053, ChEBI:CHEBI:456215; EC=3.5.4.6; CC Evidence={ECO:0000269|PubMed:23911318}; CC -!- COFACTOR: CC Name=Zn(2+); Xref=ChEBI:CHEBI:29105; Evidence={ECO:0000250}; CC Note=Binds 1 zinc ion per subunit. {ECO:0000250}; CC -!- PATHWAY: Purine metabolism; IMP biosynthesis via salvage pathway; IMP CC from AMP: step 1/1. {ECO:0000269|PubMed:23911318}. CC -!- SUBUNIT: Homotetramer. CC -!- INTERACTION: CC Q01433; O95273: CCNDBP1; NbExp=4; IntAct=EBI-8796759, EBI-748961; CC Q01433; P54274: TERF1; NbExp=2; IntAct=EBI-8796759, EBI-710997; CC Q01433-2; P23109: AMPD1; NbExp=3; IntAct=EBI-11957578, EBI-2959675; CC Q01433-2; Q01433-2: AMPD2; NbExp=3; IntAct=EBI-11957578, EBI-11957578; CC Q01433-2; Q96HA8: NTAQ1; NbExp=3; IntAct=EBI-11957578, EBI-741158; CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=4; CC Name=Ex1B-2-3; CC IsoId=Q01433-1; Sequence=Displayed; CC Name=Ex1A-2-3; CC IsoId=Q01433-2; Sequence=VSP_001271, VSP_001272; CC Name=Ex1B-3; CC IsoId=Q01433-4; Sequence=VSP_001273; CC Name=5; CC IsoId=Q01433-5; Sequence=VSP_045975; CC -!- TISSUE SPECIFICITY: Highly expressed in cerebellum. CC {ECO:0000269|PubMed:23911318}. CC -!- DISEASE: Pontocerebellar hypoplasia 9 (PCH9) [MIM:615809]: A form of CC pontocerebellar hypoplasia, a disorder characterized by structural CC defects of the pons and cerebellum, evident upon brain imaging. PCH9 CC features include severely delayed psychomotor development, progressive CC microcephaly, spasticity, seizures, and brain abnormalities, including CC brain atrophy, thin corpus callosum, and delayed myelination. CC {ECO:0000269|PubMed:23911318}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- DISEASE: Spastic paraplegia 63, autosomal recessive (SPG63) CC [MIM:615686]: A form of spastic paraplegia, a neurodegenerative CC disorder characterized by a slow, gradual, progressive weakness and CC spasticity of the lower limbs. Rate of progression and the severity of CC symptoms are quite variable. Initial symptoms may include difficulty CC with balance, weakness and stiffness in the legs, muscle spasms, and CC dragging the toes when walking. In some forms of the disorder, bladder CC symptoms (such as incontinence) may appear, or the weakness and CC stiffness may spread to other parts of the body. CC {ECO:0000269|PubMed:24482476}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the metallo-dependent hydrolases superfamily. CC Adenosine and AMP deaminases family. {ECO:0000305}. CC -!- SEQUENCE CAUTION: CC Sequence=AAA11725.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=AAA62127.1; Type=Miscellaneous discrepancy; Note=Intron retention.; Evidence={ECO:0000305}; CC Sequence=AAC50307.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=AAD56302.1; Type=Erroneous initiation; Note=Extended N-terminus.; Evidence={ECO:0000305}; CC Sequence=EAW56396.1; Type=Erroneous gene model prediction; Evidence={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; M91029; AAA62126.1; -; Genomic_RNA. DR EMBL; M91029; AAA62127.1; ALT_SEQ; Genomic_RNA. DR EMBL; S47833; AAA11725.1; ALT_SEQ; mRNA. DR EMBL; U16267; AAC50306.1; -; mRNA. DR EMBL; U16268; AAC50307.1; ALT_INIT; mRNA. DR EMBL; U16269; AAB06511.1; -; Genomic_RNA. DR EMBL; U16270; AAC50308.1; -; mRNA. DR EMBL; U16272; AAC50309.2; -; Genomic_DNA. DR EMBL; U16271; AAC50309.2; JOINED; Genomic_DNA. DR EMBL; U16272; AAD56302.1; ALT_INIT; Genomic_DNA. DR EMBL; U16271; AAD56302.1; JOINED; Genomic_DNA. DR EMBL; U16272; AAD56303.1; -; Genomic_DNA. DR EMBL; U16271; AAD56303.1; JOINED; Genomic_DNA. DR EMBL; AK296394; BAG59062.1; -; mRNA. DR EMBL; AK302939; BAG64097.1; -; mRNA. DR EMBL; AL355310; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471122; EAW56396.1; ALT_SEQ; Genomic_DNA. DR EMBL; CH471122; EAW56399.1; -; Genomic_DNA. DR EMBL; CH471122; EAW56401.1; -; Genomic_DNA. DR EMBL; BC007711; AAH07711.1; -; mRNA. DR EMBL; BC075844; AAH75844.1; -; mRNA. DR CCDS; CCDS58016.1; -. [Q01433-5] DR CCDS; CCDS804.1; -. [Q01433-2] DR CCDS; CCDS805.2; -. [Q01433-1] DR PIR; A44313; A44313. DR PIR; S59994; S59994. DR PIR; S59995; S59995. DR PIR; S59998; S59998. DR PIR; S59999; S59999. DR PIR; S60000; S60000. DR RefSeq; NP_001244289.1; NM_001257360.1. DR RefSeq; NP_001244290.1; NM_001257361.1. [Q01433-5] DR RefSeq; NP_001295099.1; NM_001308170.1. [Q01433-4] DR RefSeq; NP_004028.3; NM_004037.7. [Q01433-1] DR RefSeq; NP_631895.1; NM_139156.3. [Q01433-2] DR RefSeq; NP_981949.1; NM_203404.1. DR PDB; 4NO3; X-ray; 1.70 A; C=111-119. DR PDB; 4NO5; X-ray; 2.10 A; C=111-119. DR PDB; 8HU6; X-ray; 2.33 A; A/B/C/D=157-825. DR PDB; 8HUB; X-ray; 3.25 A; A/B/C/D=157-825. DR PDBsum; 4NO3; -. DR PDBsum; 4NO5; -. DR PDBsum; 8HU6; -. DR PDBsum; 8HUB; -. DR AlphaFoldDB; Q01433; -. DR SMR; Q01433; -. DR BioGRID; 106768; 128. DR IntAct; Q01433; 30. DR MINT; Q01433; -. DR STRING; 9606.ENSP00000499465; -. DR BindingDB; Q01433; -. DR ChEMBL; CHEMBL2997; -. DR GlyCosmos; Q01433; 1 site, 2 glycans. DR GlyGen; Q01433; 2 sites, 2 O-linked glycans (2 sites). DR iPTMnet; Q01433; -. DR MetOSite; Q01433; -. DR PhosphoSitePlus; Q01433; -. DR BioMuta; AMPD2; -. DR DMDM; 12644375; -. DR EPD; Q01433; -. DR jPOST; Q01433; -. DR MassIVE; Q01433; -. DR MaxQB; Q01433; -. DR PaxDb; 9606-ENSP00000256578; -. DR PeptideAtlas; Q01433; -. DR ProteomicsDB; 22402; -. DR ProteomicsDB; 57950; -. [Q01433-1] DR ProteomicsDB; 57951; -. [Q01433-2] DR ProteomicsDB; 57953; -. [Q01433-4] DR Pumba; Q01433; -. DR Antibodypedia; 33766; 246 antibodies from 31 providers. DR DNASU; 271; -. DR Ensembl; ENST00000256578.8; ENSP00000256578.4; ENSG00000116337.20. [Q01433-1] DR Ensembl; ENST00000342115.8; ENSP00000345498.4; ENSG00000116337.20. [Q01433-2] DR Ensembl; ENST00000528454.5; ENSP00000437164.1; ENSG00000116337.20. [Q01433-5] DR Ensembl; ENST00000528667.7; ENSP00000436541.2; ENSG00000116337.20. [Q01433-1] DR Ensembl; ENST00000531203.6; ENSP00000431975.2; ENSG00000116337.20. [Q01433-5] DR Ensembl; ENST00000531734.6; ENSP00000433739.2; ENSG00000116337.20. [Q01433-2] DR GeneID; 271; -. DR KEGG; hsa:271; -. DR MANE-Select; ENST00000528667.7; ENSP00000436541.2; NM_001368809.2; NP_001355738.1. DR UCSC; uc001dyb.3; human. [Q01433-1] DR AGR; HGNC:469; -. DR CTD; 271; -. DR DisGeNET; 271; -. DR GeneCards; AMPD2; -. DR HGNC; HGNC:469; AMPD2. DR HPA; ENSG00000116337; Tissue enhanced (choroid). DR MalaCards; AMPD2; -. DR MIM; 102771; gene. DR MIM; 615686; phenotype. DR MIM; 615809; phenotype. DR neXtProt; NX_Q01433; -. DR OpenTargets; ENSG00000116337; -. DR Orphanet; 401805; Autosomal recessive spastic paraplegia type 63. DR Orphanet; 369920; Pontocerebellar hypoplasia type 9. DR PharmGKB; PA24777; -. DR VEuPathDB; HostDB:ENSG00000116337; -. DR eggNOG; KOG1096; Eukaryota. DR GeneTree; ENSGT00950000183011; -. DR HOGENOM; CLU_003782_4_0_1; -. DR InParanoid; Q01433; -. DR OMA; FHRKFPY; -. DR OrthoDB; 20951at2759; -. DR PhylomeDB; Q01433; -. DR TreeFam; TF300439; -. DR BioCyc; MetaCyc:HS04008-MONOMER; -. DR BRENDA; 3.5.4.6; 2681. DR PathwayCommons; Q01433; -. DR Reactome; R-HSA-74217; Purine salvage. DR SABIO-RK; Q01433; -. DR SignaLink; Q01433; -. DR UniPathway; UPA00591; UER00663. DR BioGRID-ORCS; 271; 24 hits in 1161 CRISPR screens. DR ChiTaRS; AMPD2; human. DR GeneWiki; AMPD2; -. DR GenomeRNAi; 271; -. DR Pharos; Q01433; Tchem. DR PRO; PR:Q01433; -. DR Proteomes; UP000005640; Chromosome 1. DR RNAct; Q01433; Protein. DR Bgee; ENSG00000116337; Expressed in adenohypophysis and 178 other cell types or tissues. DR ExpressionAtlas; Q01433; baseline and differential. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0003876; F:AMP deaminase activity; IGI:MGI. DR GO; GO:0042802; F:identical protein binding; IPI:IntAct. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0046033; P:AMP metabolic process; IBA:GO_Central. DR GO; GO:0052652; P:cyclic purine nucleotide metabolic process; IMP:UniProtKB. DR GO; GO:0097009; P:energy homeostasis; IGI:MGI. DR GO; GO:0006188; P:IMP biosynthetic process; IGI:MGI. DR GO; GO:0032264; P:IMP salvage; IEA:UniProtKB-UniPathway. DR CDD; cd01319; AMPD; 1. DR Gene3D; 4.10.800.20; -; 1. DR Gene3D; 3.20.20.140; Metal-dependent hydrolases; 1. DR InterPro; IPR006650; A/AMP_deam_AS. DR InterPro; IPR006329; AMPD. DR InterPro; IPR032466; Metal_Hydrolase. DR NCBIfam; TIGR01429; AMP_deaminase; 1. DR PANTHER; PTHR11359; AMP DEAMINASE; 1. DR PANTHER; PTHR11359:SF3; AMP DEAMINASE 2; 1. DR Pfam; PF19326; AMP_deaminase; 1. DR PIRSF; PIRSF001251; AMP_deaminase_met; 1. DR SUPFAM; SSF51556; Metallo-dependent hydrolases; 1. DR PROSITE; PS00485; A_DEAMINASE; 1. DR Genevisible; Q01433; HS. PE 1: Evidence at protein level; KW 3D-structure; Alternative splicing; Disease variant; KW Hereditary spastic paraplegia; Hydrolase; Metal-binding; Methylation; KW Neurodegeneration; Nucleotide metabolism; Phosphoprotein; KW Reference proteome; Zinc. FT CHAIN 1..825 FT /note="AMP deaminase 2" FT /id="PRO_0000194407" FT REGION 1..49 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT ACT_SITE 655 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104" FT BINDING 364 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 366 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 366 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 435..440 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 633 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 636 FT /ligand="substrate" FT /evidence="ECO:0000250" FT BINDING 710 FT /ligand="Zn(2+)" FT /ligand_id="ChEBI:CHEBI:29105" FT /ligand_note="catalytic" FT /evidence="ECO:0000250" FT BINDING 711..714 FT /ligand="substrate" FT /evidence="ECO:0000250" FT MOD_RES 22 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:19690332" FT MOD_RES 45 FT /note="Omega-N-methylarginine" FT /evidence="ECO:0000250|UniProtKB:Q9DBT5" FT MOD_RES 46 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 80 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 91 FT /note="Phosphotyrosine" FT /evidence="ECO:0000250|UniProtKB:Q9DBT5" FT MOD_RES 97 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 114 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:17081983, FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 134 FT /note="Phosphothreonine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 136 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:19690332, ECO:0007744|PubMed:20068231, FT ECO:0007744|PubMed:21406692, ECO:0007744|PubMed:23186163, FT ECO:0007744|PubMed:24275569" FT MOD_RES 138 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT VAR_SEQ 1..74 FT /note="MASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAP FT CLKHFPLDLRTSMDGKCKEIAE -> MWQSQAPAGAAQTPPLSPPWSQPWHPIHLALAS FT PRPNIPLRSGPACRPPLQLQ (in isoform Ex1B-3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_001273" FT VAR_SEQ 1..64 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_045975" FT VAR_SEQ 1..27 FT /note="Missing (in isoform Ex1A-2-3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_001271" FT VAR_SEQ 28..30 FT /note="AAP -> MAS (in isoform Ex1A-2-3)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_001272" FT VARIANT 468 FT /note="I -> V (in dbSNP:rs201254826)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_069105" FT VARIANT 620 FT /note="R -> H (in PCH9; dbSNP:rs587777395)" FT /evidence="ECO:0000269|PubMed:23911318" FT /id="VAR_071158" FT VARIANT 724 FT /note="E -> D (in PCH9; dbSNP:rs587777392)" FT /evidence="ECO:0000269|PubMed:23911318" FT /id="VAR_071193" FT VARIANT 739 FT /note="D -> Y (in PCH9; dbSNP:rs587777394)" FT /evidence="ECO:0000269|PubMed:23911318" FT /id="VAR_071159" FT CONFLICT 153 FT /note="R -> G (in Ref. 1; AAA11725)" FT /evidence="ECO:0000305" FT CONFLICT 757 FT /note="V -> I (in Ref. 4; BAG59062)" FT /evidence="ECO:0000305" SQ SEQUENCE 825 AA; 94890 MW; F79EAD41CBA771AC CRC64; MASYPSGSGK PKAKYPFKKR ASLQASTAAP EARGGLGAPP LQSARSLPGP APCLKHFPLD LRTSMDGKCK EIAEELFTRS LAESELRSAP YEFPEESPIE QLEERRQRLE RQISQDVKLE PDILLRAKQD FLKTDSDSDL QLYKEQGEGQ GDRSLRERDV LEREFQRVTI SGEEKCGVPF TDLLDAAKSV VRALFIREKY MALSLQSFCP TTRRYLQQLA EKPLETRTYE QGPDTPVSAD APVHPPALEQ HPYEHCEPST MPGDLGLGLR MVRGVVHVYT RREPDEHCSE VELPYPDLQE FVADVNVLMA LIINGPIKSF CYRRLQYLSS KFQMHVLLNE MKELAAQKKV PHRDFYNIRK VDTHIHASSC MNQKHLLRFI KRAMKRHLEE IVHVEQGREQ TLREVFESMN LTAYDLSVDT LDVHADRNTF HRFDKFNAKY NPIGESVLRE IFIKTDNRVS GKYFAHIIKE VMSDLEESKY QNAELRLSIY GRSRDEWDKL ARWAVMHRVH SPNVRWLVQV PRLFDVYRTK GQLANFQEML ENIFLPLFEA TVHPASHPEL HLFLEHVDGF DSVDDESKPE NHVFNLESPL PEAWVEEDNP PYAYYLYYTF ANMAMLNHLR RQRGFHTFVL RPHCGEAGPI HHLVSAFMLA ENISHGLLLR KAPVLQYLYY LAQIGIAMSP LSNNSLFLSY HRNPLPEYLS RGLMVSLSTD DPLQFHFTKE PLMEEYSIAT QVWKLSSCDM CELARNSVLM SGFSHKVKSH WLGPNYTKEG PEGNDIRRTN VPDIRVGYRY ETLCQELALI TQAVQSEMLE TIPEEAGITM SPGPQ //