AMPD2_HUMAN
ID AMPD2_HUMAN Reviewed; 879 AA.
AC Q01433; B4DK50; B4DZI5; E9PNG0; Q14856; Q14857; Q16686; Q16687; Q16688;
AC Q16729; Q5T693; Q5T695; Q96IA1; Q9UDX8; Q9UDX9; Q9UMU4;
DT 01-JUL-1993, integrated into UniProtKB/Swiss-Prot.
DT 01-DEC-2000, sequence version 2.
DT 03-AUG-2022, entry version 199.
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 [MRNA].
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 [GENOMIC DNA / MRNA], AND ALTERNATIVE SPLICING.
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], AND ALTERNATIVE SPLICING.
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-522.
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-168, 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-118; SER-151; THR-188 AND
RP SER-190, 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-76 AND SER-190, 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-168 AND SER-190, 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-190, 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-674; ASP-778 AND TYR-793,
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-100; SER-118; SER-134;
RP SER-168; SER-190 AND SER-192, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE 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-100; SER-168 AND SER-190, 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).
RN [19]
RP METHYLATION AT GLN-6, AND MUTAGENESIS OF GLN-6.
RX PubMed=26797129; DOI=10.1074/jbc.m115.711952;
RA Kusevic D., Kudithipudi S., Jeltsch A.;
RT "Substrate specificity of the HEMK2 protein glutamine methyltransferase and
RT identification of novel substrates.";
RL J. Biol. Chem. 291:6124-6133(2016).
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=5;
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=Ex1A-3;
CC IsoId=Q01433-3; Sequence=VSP_001274;
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 -!- PTM: Methylated at Gln-6 by N6AMT1. {ECO:0000269|PubMed:26797129}.
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}.
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DR EMBL; M91029; AAA62127.1; -; mRNA.
DR EMBL; M91029; AAA62126.1; -; mRNA.
DR EMBL; S47833; AAA11725.1; -; mRNA.
DR EMBL; U16267; AAC50306.1; -; mRNA.
DR EMBL; U16268; AAC50307.1; -; mRNA.
DR EMBL; U16269; AAB06511.1; -; Genomic_RNA.
DR EMBL; U16270; AAC50308.1; -; mRNA.
DR EMBL; U16272; AAD56302.1; -; Genomic_DNA.
DR EMBL; U16271; AAD56302.1; JOINED; Genomic_DNA.
DR EMBL; U16272; AAC50309.2; -; Genomic_DNA.
DR EMBL; U16271; AAC50309.2; 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; -; 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; CCDS76186.1; -. [Q01433-4]
DR CCDS; CCDS804.1; -. [Q01433-2]
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.
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=165-173.
DR PDB; 4NO5; X-ray; 2.10 A; C=165-173.
DR PDBsum; 4NO3; -.
DR PDBsum; 4NO5; -.
DR AlphaFoldDB; Q01433; -.
DR SMR; Q01433; -.
DR BioGRID; 106768; 97.
DR IntAct; Q01433; 23.
DR STRING; 9606.ENSP00000256578; -.
DR BindingDB; Q01433; -.
DR ChEMBL; CHEMBL2997; -.
DR GlyGen; Q01433; 1 site, 2 O-linked glycans (1 site).
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; Q01433; -.
DR PeptideAtlas; Q01433; -.
DR PRIDE; Q01433; -.
DR ProteomicsDB; 22402; -.
DR ProteomicsDB; 57950; -. [Q01433-1]
DR ProteomicsDB; 57951; -. [Q01433-2]
DR ProteomicsDB; 57952; -. [Q01433-3]
DR ProteomicsDB; 57953; -. [Q01433-4]
DR Antibodypedia; 33766; 229 antibodies from 31 providers.
DR DNASU; 271; -.
DR Ensembl; ENST00000342115.8; ENSP00000345498.4; ENSG00000116337.20. [Q01433-2]
DR Ensembl; ENST00000528454.5; ENSP00000437164.1; ENSG00000116337.20. [Q01433-5]
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 UCSC; uc001dyb.3; human. [Q01433-1]
DR CTD; 271; -.
DR DisGeNET; 271; -.
DR GeneCards; AMPD2; -.
DR HGNC; HGNC:469; AMPD2.
DR HPA; ENSG00000116337; Low tissue specificity.
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 PhylomeDB; Q01433; -.
DR TreeFam; TF300439; -.
DR BioCyc; MetaCyc:HS04008-MON; -.
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; 21 hits in 1082 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 176 other tissues.
DR ExpressionAtlas; Q01433; baseline and differential.
DR Genevisible; Q01433; HS.
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 InterPro; IPR006650; A/AMP_deam_AS.
DR InterPro; IPR006329; AMPD.
DR InterPro; IPR029749; AMPD2.
DR InterPro; IPR032466; Metal_Hydrolase.
DR PANTHER; PTHR11359; PTHR11359; 1.
DR PANTHER; PTHR11359:SF3; PTHR11359:SF3; 1.
DR Pfam; PF19326; AMP_deaminase; 1.
DR PIRSF; PIRSF001251; AMP_deaminase_met; 1.
DR SUPFAM; SSF51556; SSF51556; 1.
DR TIGRFAMs; TIGR01429; AMP_deaminase; 1.
DR PROSITE; PS00485; A_DEAMINASE; 1.
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..879
FT /note="AMP deaminase 2"
FT /id="PRO_0000194407"
FT REGION 78..103
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT ACT_SITE 709
FT /note="Proton acceptor"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU10104"
FT BINDING 418
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 420
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 489..494
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 687
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 690
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT BINDING 764
FT /ligand="Zn(2+)"
FT /ligand_id="ChEBI:CHEBI:29105"
FT /ligand_note="catalytic"
FT /evidence="ECO:0000250"
FT BINDING 765..768
FT /ligand="substrate"
FT /evidence="ECO:0000250"
FT MOD_RES 6
FT /note="N5-methylglutamine"
FT /evidence="ECO:0000269|PubMed:26797129"
FT MOD_RES 76
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:19690332"
FT MOD_RES 99
FT /note="Omega-N-methylarginine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT5"
FT MOD_RES 100
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163,
FT ECO:0007744|PubMed:24275569"
FT MOD_RES 118
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 134
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 145
FT /note="Phosphotyrosine"
FT /evidence="ECO:0000250|UniProtKB:Q9DBT5"
FT MOD_RES 151
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 168
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 188
FT /note="Phosphothreonine"
FT /evidence="ECO:0007744|PubMed:18669648"
FT MOD_RES 190
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 192
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT VAR_SEQ 1..128
FT /note="MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVV
FT PAMASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHF
FT PLDLRTSMDGKCKEIAE -> MLTFLPSPQ (in isoform Ex1A-3)"
FT /evidence="ECO:0000305"
FT /id="VSP_001274"
FT VAR_SEQ 1..128
FT /note="MRNRGQGLFRLRSRCFLHQSLPLGAGRRKGLDVAEPGPSRCRSDSPAVAAVV
FT PAMASYPSGSGKPKAKYPFKKRASLQASTAAPEARGGLGAPPLQSARSLPGPAPCLKHF
FT PLDLRTSMDGKCKEIAE -> MWQSQAPAGAAQTPPLSPPWSQPWHPIHLALASPRPNI
FT PLRSGPACRPPLQLQ (in isoform Ex1B-3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_001273"
FT VAR_SEQ 1..118
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_045975"
FT VAR_SEQ 1..81
FT /note="Missing (in isoform Ex1A-2-3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001271"
FT VAR_SEQ 82..84
FT /note="AAP -> MAS (in isoform Ex1A-2-3)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_001272"
FT VARIANT 522
FT /note="I -> V (in dbSNP:rs201254826)"
FT /evidence="ECO:0000269|PubMed:14702039"
FT /id="VAR_069105"
FT VARIANT 674
FT /note="R -> H (in PCH9; dbSNP:rs587777395)"
FT /evidence="ECO:0000269|PubMed:23911318"
FT /id="VAR_071158"
FT VARIANT 778
FT /note="E -> D (in PCH9; dbSNP:rs587777392)"
FT /evidence="ECO:0000269|PubMed:23911318"
FT /id="VAR_071193"
FT VARIANT 793
FT /note="D -> Y (in PCH9; dbSNP:rs587777394)"
FT /evidence="ECO:0000269|PubMed:23911318"
FT /id="VAR_071159"
FT MUTAGEN 6
FT /note="Q->R: Abolishes methylation by N6AMT1."
FT /evidence="ECO:0000269|PubMed:26797129"
FT CONFLICT 207
FT /note="R -> G (in Ref. 1; AAA11725)"
FT /evidence="ECO:0000305"
FT CONFLICT 811
FT /note="V -> I (in Ref. 4; BAG59062)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 879 AA; 100688 MW; 5BD9BBF5AA41BE8F CRC64;
MRNRGQGLFR LRSRCFLHQS LPLGAGRRKG LDVAEPGPSR CRSDSPAVAA VVPAMASYPS
GSGKPKAKYP FKKRASLQAS TAAPEARGGL GAPPLQSARS LPGPAPCLKH FPLDLRTSMD
GKCKEIAEEL FTRSLAESEL RSAPYEFPEE SPIEQLEERR QRLERQISQD VKLEPDILLR
AKQDFLKTDS DSDLQLYKEQ GEGQGDRSLR ERDVLEREFQ RVTISGEEKC GVPFTDLLDA
AKSVVRALFI REKYMALSLQ SFCPTTRRYL QQLAEKPLET RTYEQGPDTP VSADAPVHPP
ALEQHPYEHC EPSTMPGDLG LGLRMVRGVV HVYTRREPDE HCSEVELPYP DLQEFVADVN
VLMALIINGP IKSFCYRRLQ YLSSKFQMHV LLNEMKELAA QKKVPHRDFY NIRKVDTHIH
ASSCMNQKHL LRFIKRAMKR HLEEIVHVEQ GREQTLREVF ESMNLTAYDL SVDTLDVHAD
RNTFHRFDKF NAKYNPIGES VLREIFIKTD NRVSGKYFAH IIKEVMSDLE ESKYQNAELR
LSIYGRSRDE WDKLARWAVM HRVHSPNVRW LVQVPRLFDV YRTKGQLANF QEMLENIFLP
LFEATVHPAS HPELHLFLEH VDGFDSVDDE SKPENHVFNL ESPLPEAWVE EDNPPYAYYL
YYTFANMAML NHLRRQRGFH TFVLRPHCGE AGPIHHLVSA FMLAENISHG LLLRKAPVLQ
YLYYLAQIGI AMSPLSNNSL FLSYHRNPLP EYLSRGLMVS LSTDDPLQFH FTKEPLMEEY
SIATQVWKLS SCDMCELARN SVLMSGFSHK VKSHWLGPNY TKEGPEGNDI RRTNVPDIRV
GYRYETLCQE LALITQAVQS EMLETIPEEA GITMSPGPQ
