ID KAD8_HUMAN Reviewed; 479 AA. AC Q96MA6; A8K821; Q8N9W9; DT 06-MAR-2007, integrated into UniProtKB/Swiss-Prot. DT 01-DEC-2001, sequence version 1. DT 27-MAR-2024, entry version 176. DE RecName: Full=Adenylate kinase 8; DE Short=AK 8; DE EC=2.7.4.3 {ECO:0000269|PubMed:21080915}; DE EC=2.7.4.6 {ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111}; DE AltName: Full=ATP-AMP transphosphorylase 8; GN Name=AK8; Synonyms=C9orf98; 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] (ISOFORMS 1 AND 2). RC TISSUE=Testis; 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=15164053; DOI=10.1038/nature02465; RA Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., RA Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., RA Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., RA Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., RA Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., RA Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., RA Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., RA Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., RA Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., RA Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., RA Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., RA Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., RA Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., RA Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., RA Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., RA Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., RA Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., RA Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., RA McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., RA Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., RA Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., RA Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., RA Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., RA West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., RA Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., RA Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., RA Dunham I.; RT "DNA sequence and analysis of human chromosome 9."; RL Nature 429:369-374(2004). 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 (JUL-2005) to the EMBL/GenBank/DDBJ databases. RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). 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 [5] RP FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, AND RP CATALYTIC ACTIVITY. RX PubMed=21080915; DOI=10.1042/bj20101443; RA Panayiotou C., Solaroli N., Xu Y., Johansson M., Karlsson A.; RT "The characterization of human adenylate kinases 7 and 8 demonstrates RT differences in kinetic parameters and structural organization among the RT family of adenylate kinase isoenzymes."; RL Biochem. J. 433:527-534(2011). RN [6] RP FUNCTION, AND CATALYTIC ACTIVITY. RX PubMed=23416111; DOI=10.1016/j.biocel.2013.02.004; RA Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.; RT "The human adenylate kinase 9 is a nucleoside mono- and diphosphate RT kinase."; RL Int. J. Biochem. Cell Biol. 45:925-931(2013). RN [7] RP INTERACTION WITH CFAP45 AND CFAP52, AMP-BINDING, SUBCELLULAR LOCATION, AND RP TISSUE SPECIFICITY. RX PubMed=33139725; DOI=10.1038/s41467-020-19113-0; RA Dougherty G.W., Mizuno K., Noethe-Menchen T., Ikawa Y., Boldt K., RA Ta-Shma A., Aprea I., Minegishi K., Pang Y.P., Pennekamp P., Loges N.T., RA Raidt J., Hjeij R., Wallmeier J., Mussaffi H., Perles Z., Elpeleg O., RA Rabert F., Shiratori H., Letteboer S.J., Horn N., Young S., Struenker T., RA Stumme F., Werner C., Olbrich H., Takaoka K., Ide T., Twan W.K., RA Biebach L., Grosse-Onnebrink J., Klinkenbusch J.A., Praveen K., RA Bracht D.C., Hoeben I.M., Junger K., Guetzlaff J., Cindric S., Aviram M., RA Kaiser T., Memari Y., Dzeja P.P., Dworniczak B., Ueffing M., Roepman R., RA Bartscherer K., Katsanis N., Davis E.E., Amirav I., Hamada H., Omran H.; RT "CFAP45 deficiency causes situs abnormalities and asthenospermia by RT disrupting an axonemal adenine nucleotide homeostasis module."; RL Nat. Commun. 11:5520-5520(2020). CC -!- FUNCTION: Nucleoside monophosphate (NMP) kinase that catalyzes the CC reversible transfer of the terminal phosphate group between nucleoside CC triphosphates and monophosphates. Has highest activity toward AMP, and CC weaker activity toward dAMP, CMP and dCMP. Also displays broad CC nucleoside diphosphate kinase activity. {ECO:0000269|PubMed:21080915, CC ECO:0000269|PubMed:23416111}. CC -!- CATALYTIC ACTIVITY: CC Reaction=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; EC=2.7.4.3; CC Evidence={ECO:0000269|PubMed:21080915}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'- CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640, CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316, CC ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111}; CC -!- CATALYTIC ACTIVITY: CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'- CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616, CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6; CC Evidence={ECO:0000269|PubMed:21080915, ECO:0000269|PubMed:23416111}; CC -!- BIOPHYSICOCHEMICAL PROPERTIES: CC Kinetic parameters: CC KM=4.1 uM for AMP {ECO:0000269|PubMed:21080915}; CC KM=630 uM for dAMP {ECO:0000269|PubMed:21080915}; CC KM=1.4 uM for CMP {ECO:0000269|PubMed:21080915}; CC Vmax=2400 pmol/min/ug enzyme with AMP as substrate CC {ECO:0000269|PubMed:21080915}; CC Vmax=1360 pmol/min/ug enzyme with dAMP as substrate CC {ECO:0000269|PubMed:21080915}; CC Vmax=190 pmol/min/ug enzyme with CMP as substrate CC {ECO:0000269|PubMed:21080915}; CC -!- SUBUNIT: Interacts with CFAP45 and CFAP52; CFAP45 and AK8 dimerization CC may create a cavity at the interface of the dimer that can accommodate CC AMP. {ECO:0000269|PubMed:33139725}. CC -!- INTERACTION: CC Q96MA6; Q96Q83: ALKBH3; NbExp=3; IntAct=EBI-8466265, EBI-6658697; CC Q96MA6; P55212: CASP6; NbExp=3; IntAct=EBI-8466265, EBI-718729; CC Q96MA6; Q68D86: CCDC102B; NbExp=3; IntAct=EBI-8466265, EBI-10171570; CC Q96MA6; Q07002: CDK18; NbExp=3; IntAct=EBI-8466265, EBI-746238; CC Q96MA6; P26441: CNTF; NbExp=3; IntAct=EBI-8466265, EBI-1050897; CC Q96MA6; O14645: DNALI1; NbExp=3; IntAct=EBI-8466265, EBI-395638; CC Q96MA6; Q9C005: DPY30; NbExp=3; IntAct=EBI-8466265, EBI-744973; CC Q96MA6; O75460-2: ERN1; NbExp=3; IntAct=EBI-8466265, EBI-25852368; CC Q96MA6; Q0VDC6: FKBP1A; NbExp=3; IntAct=EBI-8466265, EBI-10226858; CC Q96MA6; Q96CS2: HAUS1; NbExp=3; IntAct=EBI-8466265, EBI-2514791; CC Q96MA6; O00291: HIP1; NbExp=3; IntAct=EBI-8466265, EBI-473886; CC Q96MA6; P54652: HSPA2; NbExp=3; IntAct=EBI-8466265, EBI-356991; CC Q96MA6; O14901: KLF11; NbExp=3; IntAct=EBI-8466265, EBI-948266; CC Q96MA6; P13473-2: LAMP2; NbExp=3; IntAct=EBI-8466265, EBI-21591415; CC Q96MA6; P57077-4: MAP3K7CL; NbExp=6; IntAct=EBI-8466265, EBI-10215880; CC Q96MA6; P33993: MCM7; NbExp=4; IntAct=EBI-8466265, EBI-355924; CC Q96MA6; Q9NPA3: MID1IP1; NbExp=3; IntAct=EBI-8466265, EBI-750096; CC Q96MA6; P62826: RAN; NbExp=3; IntAct=EBI-8466265, EBI-286642; CC Q96MA6; Q14498: RBM39; NbExp=3; IntAct=EBI-8466265, EBI-395290; CC Q96MA6; Q14498-3: RBM39; NbExp=3; IntAct=EBI-8466265, EBI-6654703; CC Q96MA6; Q9Y371: SH3GLB1; NbExp=3; IntAct=EBI-8466265, EBI-2623095; CC Q96MA6; Q9H0W8: SMG9; NbExp=3; IntAct=EBI-8466265, EBI-2872322; CC Q96MA6; Q9BSW7: SYT17; NbExp=3; IntAct=EBI-8466265, EBI-745392; CC Q96MA6; Q9H832: UBE2Z; NbExp=3; IntAct=EBI-8466265, EBI-720977; CC Q96MA6; Q96NC0: ZMAT2; NbExp=3; IntAct=EBI-8466265, EBI-2682299; CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytosol {ECO:0000269|PubMed:21080915}. CC Cytoplasm, cytoskeleton, cilium axoneme {ECO:0000269|PubMed:33139725}. CC Note=Located in the proximal region of respiratory cilia. CC {ECO:0000269|PubMed:33139725}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=2; CC Name=1; CC IsoId=Q96MA6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q96MA6-2; Sequence=VSP_023419; CC -!- TISSUE SPECIFICITY: Expressed in respiratory cells (at protein level). CC {ECO:0000269|PubMed:33139725}. CC -!- SIMILARITY: Belongs to the adenylate kinase 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; AK057266; BAB71402.1; -; mRNA. DR EMBL; AK093446; BAC04168.1; -; mRNA. DR EMBL; AK292186; BAF84875.1; -; mRNA. DR EMBL; AL160165; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; AL445645; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; CH471090; EAW88016.1; -; Genomic_DNA. DR EMBL; BC034776; AAH34776.1; -; mRNA. DR EMBL; BC050576; AAH50576.1; -; mRNA. DR CCDS; CCDS6954.1; -. [Q96MA6-1] DR RefSeq; NP_001304887.1; NM_001317958.1. [Q96MA6-2] DR RefSeq; NP_001304888.1; NM_001317959.1. DR RefSeq; NP_689785.1; NM_152572.2. [Q96MA6-1] DR AlphaFoldDB; Q96MA6; -. DR SMR; Q96MA6; -. DR BioGRID; 127645; 20. DR IntAct; Q96MA6; 26. DR MINT; Q96MA6; -. DR STRING; 9606.ENSP00000298545; -. DR DrugBank; DB01717; Bis(Adenosine)-5'-Pentaphosphate. DR iPTMnet; Q96MA6; -. DR PhosphoSitePlus; Q96MA6; -. DR BioMuta; AK8; -. DR DMDM; 74752032; -. DR EPD; Q96MA6; -. DR MassIVE; Q96MA6; -. DR PaxDb; 9606-ENSP00000298545; -. DR PeptideAtlas; Q96MA6; -. DR ProteomicsDB; 77326; -. [Q96MA6-1] DR ProteomicsDB; 77327; -. [Q96MA6-2] DR Antibodypedia; 18213; 132 antibodies from 27 providers. DR DNASU; 158067; -. DR Ensembl; ENST00000298545.4; ENSP00000298545.3; ENSG00000165695.10. [Q96MA6-1] DR GeneID; 158067; -. DR KEGG; hsa:158067; -. DR MANE-Select; ENST00000298545.4; ENSP00000298545.3; NM_152572.3; NP_689785.1. DR UCSC; uc004cbu.2; human. [Q96MA6-1] DR AGR; HGNC:26526; -. DR CTD; 158067; -. DR DisGeNET; 158067; -. DR GeneCards; AK8; -. DR HGNC; HGNC:26526; AK8. DR HPA; ENSG00000165695; Tissue enhanced (epididymis, fallopian tube, testis). DR MIM; 615365; gene. DR neXtProt; NX_Q96MA6; -. DR OpenTargets; ENSG00000165695; -. DR PharmGKB; PA134971772; -. DR VEuPathDB; HostDB:ENSG00000165695; -. DR eggNOG; KOG3078; Eukaryota. DR eggNOG; KOG3079; Eukaryota. DR GeneTree; ENSGT00940000161613; -. DR HOGENOM; CLU_044905_0_0_1; -. DR InParanoid; Q96MA6; -. DR OMA; DCIRRGW; -. DR OrthoDB; 314591at2759; -. DR PhylomeDB; Q96MA6; -. DR TreeFam; TF328560; -. DR BRENDA; 2.7.4.3; 2681. DR PathwayCommons; Q96MA6; -. DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates. DR SABIO-RK; Q96MA6; -. DR SignaLink; Q96MA6; -. DR BioGRID-ORCS; 158067; 9 hits in 1147 CRISPR screens. DR ChiTaRS; AK8; human. DR GenomeRNAi; 158067; -. DR Pharos; Q96MA6; Tbio. DR PRO; PR:Q96MA6; -. DR Proteomes; UP000005640; Chromosome 9. DR RNAct; Q96MA6; Protein. DR Bgee; ENSG00000165695; Expressed in right uterine tube and 136 other cell types or tissues. DR GO; GO:0097729; C:9+2 motile cilium; IDA:GO_Central. DR GO; GO:0005930; C:axoneme; IEA:Ensembl. DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central. DR GO; GO:0005829; C:cytosol; TAS:Reactome. DR GO; GO:0036126; C:sperm flagellum; IEA:Ensembl. DR GO; GO:0004017; F:adenylate kinase activity; IDA:UniProtKB. DR GO; GO:0016208; F:AMP binding; IDA:GO_Central. DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW. DR GO; GO:0004127; F:cytidylate kinase activity; IDA:UniProtKB. DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB. DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW. DR GO; GO:0021591; P:ventricular system development; IEA:Ensembl. DR CDD; cd01428; ADK; 2. DR CDD; cd22979; DD_AK8; 1. DR Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 2. DR HAMAP; MF_00235; Adenylate_kinase_Adk; 1. DR InterPro; IPR000850; Adenylat/UMP-CMP_kin. DR InterPro; IPR036193; ADK_active_lid_dom_sf. DR InterPro; IPR027417; P-loop_NTPase. DR PANTHER; PTHR23359:SF81; ADENYLATE KINASE 8; 1. DR PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1. DR Pfam; PF00406; ADK; 2. DR PRINTS; PR00094; ADENYLTKNASE. DR SUPFAM; SSF57774; Microbial and mitochondrial ADK, insert 'zinc finger' domain; 2. DR SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 2. DR Genevisible; Q96MA6; HS. PE 1: Evidence at protein level; KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm; KW Cytoskeleton; Kinase; Nucleotide-binding; Reference proteome; Transferase. FT CHAIN 1..479 FT /note="Adenylate kinase 8" FT /id="PRO_0000279383" FT REGION 58..258 FT /note="Adenylate kinase 1" FT /evidence="ECO:0000305|PubMed:21080915" FT REGION 87..113 FT /note="NMP 1" FT /evidence="ECO:0000250|UniProtKB:P69441" FT REGION 177..206 FT /note="LID 1" FT /evidence="ECO:0000250|UniProtKB:P69441" FT REGION 269..471 FT /note="Adenylate kinase 2" FT /evidence="ECO:0000305|PubMed:21080915" FT REGION 298..327 FT /note="NMP 2" FT /evidence="ECO:0000250|UniProtKB:P69441" FT REGION 391..424 FT /note="LID 2" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 67..72 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 140..143 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 147 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 203 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="1" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 278..283 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 325..327 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 354..357 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 361 FT /ligand="AMP" FT /ligand_id="ChEBI:CHEBI:456215" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P69441" FT BINDING 392 FT /ligand="ATP" FT /ligand_id="ChEBI:CHEBI:30616" FT /ligand_label="2" FT /evidence="ECO:0000250|UniProtKB:P69441" FT VAR_SEQ 1..204 FT /note="Missing (in isoform 2)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_023419" FT VARIANT 5 FT /note="I -> T (in dbSNP:rs2231400)" FT /id="VAR_030873" FT VARIANT 130 FT /note="D -> G (in dbSNP:rs17407084)" FT /id="VAR_030874" SQ SEQUENCE 479 AA; 54926 MW; 9E4EABA3F429B731 CRC64; MDATIAPHRI PPEMPQYGEE NHIFELMQNM LEQLLIHQPE DPIPFMIQHL HRDNDNVPRI VILGPPASGK TTIAMWLCKH LNSSLLTLEN LILNEFSYTA TEARRLYLQR KTVPSALLVQ LIQERLAEED CIKQGWILDG IPETREQALR IQTLGITPRH VIVLSAPDTV LIERNLGKRI DPQTGEIYHT TFDWPPESEI QNRLMVPEDI SELETAQKLL EYHRNIVRVI PSYPKILKVI SADQPCVDVF YQALTYVQSN HRTNAPFTPR VLLLGPVGSG KSLQAALLAQ KYRLVNVCCG QLLKEAVADR TTFGELIQPF FEKEMAVPDS LLMKVLSQRL DQQDCIQKGW VLHGVPRDLD QAHLLNRLGY NPNRVFFLNV PFDSIMERLT LRRIDPVTGE RYHLMYKPPP TMEIQARLLQ NPKDAEEQVK LKMDLFYRNS ADLEQLYGSA ITLNGDQDPY TVFEYIESGI INPLPKKIP //