KAD9_HUMAN
ID KAD9_HUMAN Reviewed; 1911 AA.
AC Q5TCS8; A6NL75; B2RDJ0; B6ZDM7; Q3MIS4; Q5I0W8; Q6ZNF1; Q6ZVR7; Q8N7C6;
AC Q8WW00; Q96NF4;
DT 11-SEP-2007, integrated into UniProtKB/Swiss-Prot.
DT 10-AUG-2010, sequence version 2.
DT 03-AUG-2022, entry version 155.
DE RecName: Full=Adenylate kinase 9;
DE Short=AK 9;
DE EC=2.7.4.4;
DE EC=2.7.4.6;
DE AltName: Full=Adenylate kinase domain-containing protein 1;
DE AltName: Full=Adenylate kinase domain-containing protein 2;
GN Name=AK9; Synonyms=AKD1, AKD2, C6orf199, C6orf224;
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 2 AND 5), NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 431-1911 (ISOFORM 3), AND NUCLEOTIDE
RP SEQUENCE [LARGE SCALE MRNA] OF 1563-1911 (ISOFORM 4).
RC TISSUE=Caudate nucleus, Hair follicle dermal papilla, Placenta, Testis, and
RC Thymus;
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=14574404; DOI=10.1038/nature02055;
RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L.,
RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R.,
RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D.,
RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H.,
RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J.,
RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V.,
RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J.,
RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E.,
RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J.,
RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J.,
RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C.,
RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A.,
RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R.,
RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M.,
RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K.,
RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R.,
RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M.,
RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A.,
RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L.,
RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I.,
RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y.,
RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E.,
RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A.,
RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W.,
RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M.,
RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J.,
RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M.,
RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I.,
RA Rogers J., Beck S.;
RT "The DNA sequence and analysis of human chromosome 6.";
RL Nature 425:805-811(2003).
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] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1067-1911 (ISOFORM 6), AND NUCLEOTIDE SEQUENCE [LARGE
RP SCALE MRNA] OF 1587-1911 (ISOFORM 4).
RC TISSUE=Heart, Lung, Pituitary, and Testis;
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, BIOPHYSICOCHEMICAL PROPERTIES, AND
RP SUBCELLULAR LOCATION.
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).
CC -!- FUNCTION: Involved in maintaining the homeostasis of cellular
CC nucleotides by catalyzing the interconversion of nucleoside phosphates.
CC Has both nucleoside monophosphate and diphosphate kinase activities.
CC Catalyzes the phosphorylation of AMP, dAMP, CMP and dCMP with ATP as
CC phosphate donor and of CMP with GTP as phosphate donor. Also catalyzes
CC the production of ATP, CTP, GTP, UTP, dATP, dCTP, dGTP and TTP from the
CC corresponding diphosphate substrates with either ATP or GTP as
CC phosphate donor. Shows substrate preference of CDP > UDP > ADP > GDP >
CC TDP. {ECO:0000269|PubMed:23416111}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-phosphate + ATP = a ribonucleoside 5'-
CC diphosphate + ADP; Xref=Rhea:RHEA:24036, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:58043, ChEBI:CHEBI:456216; EC=2.7.4.4;
CC Evidence={ECO:0000269|PubMed:23416111};
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: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:23416111};
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=48 uM for AMP (with ATP as phosphate donor)
CC {ECO:0000269|PubMed:23416111};
CC KM=3600 uM for dAMP (with ATP as phosphate donor)
CC {ECO:0000269|PubMed:23416111};
CC KM=940 uM for CMP (with ATP as phosphate donor)
CC {ECO:0000269|PubMed:23416111};
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:23416111}. Nucleus
CC {ECO:0000269|PubMed:23416111}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=6;
CC Name=4;
CC IsoId=Q5TCS8-4; Sequence=Displayed;
CC Name=1;
CC IsoId=Q5TCS8-1; Sequence=VSP_039639, VSP_039640;
CC Name=2;
CC IsoId=Q5TCS8-2; Sequence=VSP_028008, VSP_028009;
CC Name=3;
CC IsoId=Q5TCS8-3; Sequence=VSP_028010, VSP_028011;
CC Name=5;
CC IsoId=Q5TCS8-5, Q6ZNF1-1;
CC Sequence=VSP_039638, VSP_039642, VSP_039643;
CC Name=6;
CC IsoId=Q5TCS8-6; Sequence=VSP_039641, VSP_039644;
CC -!- SIMILARITY: Belongs to the adenylate kinase family. {ECO:0000305}.
CC -!- SEQUENCE CAUTION:
CC Sequence=AAI01715.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=AAI11949.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
CC Sequence=BAC05368.1; Type=Erroneous initiation; Note=Truncated N-terminus.; Evidence={ECO:0000305};
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DR EMBL; AK055538; BAB70945.1; -; mRNA.
DR EMBL; AK098657; BAC05368.1; ALT_INIT; mRNA.
DR EMBL; AK124171; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AK131244; BAD18424.1; -; mRNA.
DR EMBL; AK315561; BAG37937.1; -; mRNA.
DR EMBL; AL121788; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL133472; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL109947; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL139391; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471051; EAW48333.1; -; Genomic_DNA.
DR EMBL; BC022031; AAH22031.1; -; mRNA.
DR EMBL; BC087860; AAH87860.1; -; mRNA.
DR EMBL; BC101714; AAI01715.1; ALT_INIT; mRNA.
DR EMBL; BC111948; AAI11949.1; ALT_INIT; mRNA.
DR CCDS; CCDS5077.1; -. [Q5TCS8-2]
DR CCDS; CCDS55048.1; -. [Q5TCS8-4]
DR RefSeq; NP_001138600.2; NM_001145128.2. [Q5TCS8-4]
DR RefSeq; NP_001316531.1; NM_001329602.1. [Q5TCS8-2]
DR RefSeq; NP_659462.1; NM_145025.4. [Q5TCS8-2]
DR AlphaFoldDB; Q5TCS8; -.
DR SMR; Q5TCS8; -.
DR BioGRID; 128702; 14.
DR IntAct; Q5TCS8; 11.
DR STRING; 9606.ENSP00000410186; -.
DR iPTMnet; Q5TCS8; -.
DR PhosphoSitePlus; Q5TCS8; -.
DR BioMuta; AK9; -.
DR DMDM; 302393675; -.
DR EPD; Q5TCS8; -.
DR jPOST; Q5TCS8; -.
DR MassIVE; Q5TCS8; -.
DR MaxQB; Q5TCS8; -.
DR PaxDb; Q5TCS8; -.
DR PeptideAtlas; Q5TCS8; -.
DR PRIDE; Q5TCS8; -.
DR ProteomicsDB; 64979; -. [Q5TCS8-4]
DR ProteomicsDB; 64980; -. [Q5TCS8-1]
DR ProteomicsDB; 64981; -. [Q5TCS8-2]
DR ProteomicsDB; 64982; -. [Q5TCS8-3]
DR ProteomicsDB; 64983; -. [Q5TCS8-5]
DR ProteomicsDB; 64984; -. [Q5TCS8-6]
DR Antibodypedia; 32270; 133 antibodies from 18 providers.
DR DNASU; 221264; -.
DR Ensembl; ENST00000285397.9; ENSP00000285397.4; ENSG00000155085.16. [Q5TCS8-2]
DR Ensembl; ENST00000355283.1; ENSP00000347431.1; ENSG00000155085.16. [Q5TCS8-5]
DR Ensembl; ENST00000424296.7; ENSP00000410186.2; ENSG00000155085.16. [Q5TCS8-4]
DR GeneID; 221264; -.
DR KEGG; hsa:221264; -.
DR MANE-Select; ENST00000424296.7; ENSP00000410186.2; NM_001145128.3; NP_001138600.2.
DR UCSC; uc003ptn.2; human. [Q5TCS8-4]
DR CTD; 221264; -.
DR DisGeNET; 221264; -.
DR GeneCards; AK9; -.
DR HGNC; HGNC:33814; AK9.
DR HPA; ENSG00000155085; Low tissue specificity.
DR MalaCards; AK9; -.
DR MIM; 615358; gene.
DR neXtProt; NX_Q5TCS8; -.
DR OpenTargets; ENSG00000155085; -.
DR Orphanet; 98913; Postsynaptic congenital myasthenic syndromes.
DR PharmGKB; PA164715271; -.
DR VEuPathDB; HostDB:ENSG00000155085; -.
DR eggNOG; KOG3078; Eukaryota.
DR eggNOG; KOG3079; Eukaryota.
DR GeneTree; ENSGT00740000115564; -.
DR HOGENOM; CLU_001764_0_0_1; -.
DR InParanoid; Q5TCS8; -.
DR OMA; GARKNHI; -.
DR OrthoDB; 362962at2759; -.
DR PhylomeDB; Q5TCS8; -.
DR TreeFam; TF330805; -.
DR PathwayCommons; Q5TCS8; -.
DR Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR SABIO-RK; Q5TCS8; -.
DR SignaLink; Q5TCS8; -.
DR BioGRID-ORCS; 221264; 13 hits in 1068 CRISPR screens.
DR ChiTaRS; AK9; human.
DR GenomeRNAi; 221264; -.
DR Pharos; Q5TCS8; Tbio.
DR PRO; PR:Q5TCS8; -.
DR Proteomes; UP000005640; Chromosome 6.
DR RNAct; Q5TCS8; protein.
DR Bgee; ENSG00000155085; Expressed in sural nerve and 148 other tissues.
DR ExpressionAtlas; Q5TCS8; baseline and differential.
DR Genevisible; Q5TCS8; HS.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005739; C:mitochondrion; IBA:GO_Central.
DR GO; GO:0031965; C:nuclear membrane; IDA:HPA.
DR GO; GO:0005654; C:nucleoplasm; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IDA:UniProtKB.
DR GO; GO:0004017; F:adenylate kinase activity; IBA:GO_Central.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0050145; F:nucleoside monophosphate kinase activity; IDA:UniProtKB.
DR GO; GO:0006756; P:AMP phosphorylation; IDA:UniProtKB.
DR GO; GO:0006757; P:ATP generation from ADP; IDA:UniProtKB.
DR GO; GO:0061508; P:CDP phosphorylation; IDA:UniProtKB.
DR GO; GO:0061566; P:CMP phosphorylation; IDA:UniProtKB.
DR GO; GO:0006174; P:dADP phosphorylation; IDA:UniProtKB.
DR GO; GO:0061565; P:dAMP phosphorylation; IDA:UniProtKB.
DR GO; GO:0061570; P:dCDP phosphorylation; IDA:UniProtKB.
DR GO; GO:0061567; P:dCMP phosphorylation; IDA:UniProtKB.
DR GO; GO:0006186; P:dGDP phosphorylation; IDA:UniProtKB.
DR GO; GO:0061568; P:GDP phosphorylation; IDA:UniProtKB.
DR GO; GO:0061571; P:TDP phosphorylation; IDA:UniProtKB.
DR GO; GO:0061569; P:UDP phosphorylation; IDA:UniProtKB.
DR CDD; cd01428; ADK; 3.
DR Gene3D; 3.40.50.300; -; 4.
DR InterPro; IPR003593; AAA+_ATPase.
DR InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR InterPro; IPR027417; P-loop_NTPase.
DR PANTHER; PTHR23359; PTHR23359; 3.
DR SMART; SM00382; AAA; 3.
DR SUPFAM; SSF52540; SSF52540; 6.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Coiled coil; Cytoplasm; Kinase;
KW Nucleotide metabolism; Nucleotide-binding; Nucleus; Reference proteome;
KW Transferase.
FT CHAIN 1..1911
FT /note="Adenylate kinase 9"
FT /id="PRO_0000304138"
FT REGION 31..285
FT /note="Adenylate kinase 1"
FT /evidence="ECO:0000305"
FT REGION 60..89
FT /note="NMP 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 160..205
FT /note="LID 1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 185..210
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 728..796
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 892..926
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 992..1203
FT /note="Adenylate kinase 2"
FT /evidence="ECO:0000305"
FT REGION 1021..1052
FT /note="NMP 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 1124..1144
FT /note="LID 2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 1412..1601
FT /note="Adenylate kinase 3"
FT /evidence="ECO:0000305"
FT REGION 1441..1472
FT /note="NMPbind 3"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT REGION 1536..1550
FT /note="LID 3"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT COILED 443..485
FT /evidence="ECO:0000255"
FT COILED 676..711
FT /evidence="ECO:0000255"
FT COMPBIAS 734..750
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 751..766
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 771..787
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 892..918
FT /note="Acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT BINDING 40..45
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 87..89
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 116..119
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 229
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="1"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1001..1006
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1050..1052
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1079..1082
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="2"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1421..1426
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1447
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1470..1472
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1499..1502
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1506
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT BINDING 1543
FT /ligand="AMP"
FT /ligand_id="ChEBI:CHEBI:456215"
FT /ligand_label="3"
FT /evidence="ECO:0000250|UniProtKB:P69441"
FT VAR_SEQ 1..921
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039638"
FT VAR_SEQ 420..421
FT /note="VD -> TN (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028008"
FT VAR_SEQ 422..1911
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_028009"
FT VAR_SEQ 703..751
FT /note="EARKATEEELRLEEENRRLLELMKVKAKEAEETDNEDEEEIEGDELEVH ->
FT KSHRRGIETRRRKSKATGTYESEGKRQAQIAMTDDVSWYCYCKQLQYFK (in
FT isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_039639"
FT VAR_SEQ 752..1911
FT /note="Missing (in isoform 1)"
FT /evidence="ECO:0000305"
FT /id="VSP_039640"
FT VAR_SEQ 989..1014
FT /note="APPLRICLVGPQGSGKTMCGRQLAEK -> VRQYSYLNDCSHRIFLGLITNH
FT HQFT (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028010"
FT VAR_SEQ 1015..1911
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_028011"
FT VAR_SEQ 1212..1283
FT /note="NVVRDDEEISEEELEEDNDDIENILEDEFPKDEEEMSGEEDEEQETDAIERL
FT RGELGEKFEADTHNLQIIQD -> PNKEKRKRGISENTTCYKCNHMSPWCEYAGLPYRG
FT LLILYSATATATAGTKHCRSGAKVIVALSKQNIHNQK (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039641"
FT VAR_SEQ 1212..1257
FT /note="NVVRDDEEISEEELEEDNDDIENILEDEFPKDEEEMSGEEDEEQET -> VS
FT SFVFFFKTGSHSVAQGRVQWHNHSSLQPRTPGLKGSSHLSLSKC (in isoform
FT 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039642"
FT VAR_SEQ 1258..1911
FT /note="Missing (in isoform 5)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_039643"
FT VAR_SEQ 1284..1911
FT /note="Missing (in isoform 6)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_039644"
FT CONFLICT 222
FT /note="I -> T (in Ref. 1; BAB70945)"
FT /evidence="ECO:0000305"
FT CONFLICT 1716
FT /note="K -> R (in Ref. 1; BAC05368)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 1911 AA; 221413 MW; 16A1888E727C51A4 CRC64;
MTSQEKTEEY PFADIFDEDE TERNFLLSKP VCFVVFGKPG VGKTTLARYI TQAWKCIRVE
ALPILEEQIA AETESGVMLQ SMLISGQSIP DELVIKLMLE KLNSPEVCHF GYIITEIPSL
SQDAMTTLQQ IELIKNLNLK PDVIINIKCP DYDLCQRISG QRQHNNTGYI YSRDQWDPEV
IENHRKKKKE AQKDGKGEEE EEEEEQEEEE AFIAEMQMVA EILHHLVQRP EDYLENVENI
VKLYKETILQ TLEEVMAEHN PQYLIELNGN KPAEELFMIV MDRLKYLNLK RAAILTKLQG
AEEEINDTME NDELFRTLAS YKLIAPRYRW QRSKWGRTCP VNLKDGNIYS GLPDYSVSFL
GKIYCLSSEE ALKPFLLNPR PYLLPPMPGP PCKVFILGPQ YSGKTTLCNM LAENYKGKVV
DYAQLVQPRF DKARETLVEN TIAEATAAAI KVVKEKLLRE LQARKQAETA LREFQRQYEK
MEFGVFPMEA THSSIDEEGY IQGSQRDRGS SLVDTEEAKT KSENVLHDQA AKVDKDDGKE
TGETFTFKRH SQDASQDVKL YSDTAPTEDL IEEVTADHPE VVTMIEETIK MSQDINFEQP
YEKHAEILQE VLGEVMEENK DRFPGAPKYG GWIVDNCPIV KELWMALIKK GIIPDLVIYL
SDTENNGKCL FNRIYLQKKS EIDSKILERL LEELQKKKKE EEEARKATEE ELRLEEENRR
LLELMKVKAK EAEETDNEDE EEIEGDELEV HEEPEASHDT RGSWLPEEFE ASEVPETEPE
AVSEPIEETT VETEIPKGSK EGLEIEKLSE TVVLPEFPED SYPDVPEMEP FKEKIGSFII
LWKQLEATIS EAYIKILNLE IADRTPQELL QKVVETMEKP FQYTAWELTG EDYEEETEDY
QTEAEVDEEL EEEEEEEGED KMKERKRHLG DTKHFCPVVL KENFILQPGN TEEAAKYREK
IYYFSSAEAK EKFLEHPEDY VAHEEPLKAP PLRICLVGPQ GSGKTMCGRQ LAEKLNIFHI
QFEEVLQEKL LLKTEKKVGP EFEEDSENEQ AAKQELEELA IQANVKVEEE NTKKQLPEVQ
LTEEEEVIKS SLMENEPLPP EILEVILSEW WLKEPIRSTG FILDGFPRYP EEAQFLGDRG
FFPDAAVFIQ VDDQDIFDRL LPAQIEKWKL KQKKKLERKK LIKDMKAKIR VDTIAKRRAE
LILERDKKRR ENVVRDDEEI SEEELEEDND DIENILEDEF PKDEEEMSGE EDEEQETDAI
ERLRGELGEK FEADTHNLQI IQDELERYLI PIISINGARR NHIVQYTLNM KLKPLVENRA
SIFEKCHPIP APLAQKMLTF TYKYISSFGY WDPVKLSEGE TIKPVENAEN PIYPVIHRQY
IYFLSSKETK EKFMKNPIKY IRQPKPKPTV PIRIIIVGPP KSGKTTVAKK ITSEYGLKHL
SIGGALRYVL NNHPETELAL MLNWHLHKGM TAPDELAIQA LELSLMESVC NTAGVVIDGY
PVTKHQMNLL EARSIIPMVI FELSVPSKEI FKRLLLEKEN EQRLPYPLHN SAQIVAVNNV
KYRKNIGEIR QYYQEQHQNW YVIDGFHSKW WVWNEVIKNV QMVNKYMQTY LERIKAGKAA
CIDKLCITPQ ELLSRLGEFE QFCPVSLAES QELFDCSATD SLEFAAEFRG HYYKMSSQEK
LNKFLENPEL YVPPLAPHPL PSADMIPKRL TLSELKSRFP KCAELQGYCP VTYKDGNQRY
EALVPGSINY ALEYHNRIYI CENKEKLQKF LRSPLKYWEQ KLPHKLPPLR EPILLTSLPL
PGYLEQGIAT SLIKAMNAAG CLKPKFPFLS IRRSALLYIA LHLKAFNPKG SEYTRKKYKK
KMEQFMESCE LITYLGAKMT RKYKEPQFRA IDFDHKLKTF LSLRNIDPIN G
