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   02-SEP-2026, entry version 173.
DE   RecName: Full=Adenylate kinase 9 {ECO:0000303|PubMed:23416111};
DE            EC=2.7.4.4 {ECO:0000269|PubMed:23416111};
DE            EC=2.7.4.6 {ECO:0000269|PubMed:23416111};
DE   AltName: Full=Adenylate kinase domain-containing protein 1 {ECO:0000312|HGNC:HGNC:33814};
DE   AltName: Full=Adenylate kinase domain-containing protein 2 {ECO:0000312|HGNC:HGNC:33814};
GN   Name=AK9 {ECO:0000303|PubMed:23416111, ECO:0000312|HGNC:HGNC:33814};
GN   Synonyms=AKD1 {ECO:0000312|HGNC:HGNC:33814}, AKD2
GN   {ECO:0000312|HGNC:HGNC:33814}, C6orf199 {ECO:0000312|HGNC:HGNC:33814},
GN   C6orf224 {ECO:0000312|HGNC:HGNC:33814};
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,
RC   Testis, and 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).
RN   [6]
RP   VARIANTS SPGF89 203-GLU--GLU-205 DEL; LEU-815; GLU-1086 DEL; LYS-1131 AND
RP   MET-1692, AND INVOLVEMENT IN SPGF89.
RX   PubMed=37713809; DOI=10.1016/j.ebiom.2023.104798;
RA   Sha Y., Liu W., Li S., Osadchuk L.V., Chen Y., Nie H., Gao S., Xie L.,
RA   Qin W., Zhou H., Li L.;
RT   "Deficiency in AK9 causes asthenozoospermia and male infertility by
RT   destabilising sperm nucleotide homeostasis.";
RL   EBioMedicine 96:104798-104798(2023).
RN   [7]
RP   ERRATUM OF PUBMED:37713809.
RX   PubMed=38171079; DOI=10.1016/j.ebiom.2023.104957;
RA   Sha Y., Liu W., Li S., Osadchuk L.V., Chen Y., Nie H., Gao S., Xie L.,
RA   Qin W., Zhou H., Li L.;
RL   EBioMedicine 99:104957-104957(2024).
CC   -!- FUNCTION: Broad-specificity nucleoside phosphate kinase involved in
CC       cellular nucleotide homeostasis by catalyzing nucleoside-phosphate
CC       interconversions. Similar to other adenylate kinases, preferentially
CC       catalyzes the phosphorylation of the nucleoside monophosphate AMP with
CC       ATP as phosphate donor to produce ADP. In vitro, can also catalyze the
CC       phosphorylation of CMP, dAMP and dCMP and use GTP as an alternate
CC       phosphate donor. Moreover, exhibits a diphosphate kinase activity,
CC       producing ATP, CTP, GTP, UTP, TTP, dATP, dCTP and dGTP from the
CC       corresponding diphosphate substrates with either ATP or GTP as
CC       phosphate donors. For this activity shows the following substrate
CC       preference CDP > UDP > ADP > 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=AMP + ATP = 2 ADP; Xref=Rhea:RHEA:12973, ChEBI:CHEBI:30616,
CC         ChEBI:CHEBI:456215, ChEBI:CHEBI:456216;
CC         Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + AMP = GDP + ADP; Xref=Rhea:RHEA:29863,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:456215,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CMP + ATP = CDP + ADP; Xref=Rhea:RHEA:11600,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58069, ChEBI:CHEBI:60377,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + CMP = CDP + GDP; Xref=Rhea:RHEA:79855,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58069, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:60377; Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dAMP + ATP = dADP + ADP; Xref=Rhea:RHEA:23100,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57667, ChEBI:CHEBI:58245,
CC         ChEBI:CHEBI:456216; Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCMP + ATP = dCDP + ADP; Xref=Rhea:RHEA:25094,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:57566, ChEBI:CHEBI:58593,
CC         ChEBI:CHEBI:456216; 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   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP + ATP = CTP + ADP; Xref=Rhea:RHEA:25237,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37563, ChEBI:CHEBI:58069,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=CDP + GTP = CTP + GDP; Xref=Rhea:RHEA:79859,
CC         ChEBI:CHEBI:37563, ChEBI:CHEBI:37565, ChEBI:CHEBI:58069,
CC         ChEBI:CHEBI:58189; Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GDP + ATP = GTP + ADP; Xref=Rhea:RHEA:27686,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37565, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=UDP + ATP = UTP + ADP; Xref=Rhea:RHEA:25098,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:46398, ChEBI:CHEBI:58223,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=GTP + UDP = UTP + GDP; Xref=Rhea:RHEA:79863,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:46398, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58223; Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP + GTP = dTTP + GDP; Xref=Rhea:RHEA:79867,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:37568, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58369; Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCDP + ATP = dCTP + ADP; Xref=Rhea:RHEA:27678,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58593, ChEBI:CHEBI:61481,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dCDP + GTP = dCTP + GDP; Xref=Rhea:RHEA:79875,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:58189, ChEBI:CHEBI:58593,
CC         ChEBI:CHEBI:61481; Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dGDP + ATP = dGTP + ADP; Xref=Rhea:RHEA:27690,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:58595, ChEBI:CHEBI:61429,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dTDP + ATP = dTTP + ADP; Xref=Rhea:RHEA:27682,
CC         ChEBI:CHEBI:30616, ChEBI:CHEBI:37568, ChEBI:CHEBI:58369,
CC         ChEBI:CHEBI:456216; EC=2.7.4.6;
CC         Evidence={ECO:0000269|PubMed:23416111};
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=dADP + GTP = dATP + GDP; Xref=Rhea:RHEA:79871,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:57667, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:61404; 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}. Cell projection, cilium, flagellum
CC       {ECO:0000250|UniProtKB:G3UYQ4}.
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; Sequence=VSP_039638, VSP_039642,
CC                                            VSP_039643;
CC       Name=6;
CC         IsoId=Q5TCS8-6; Sequence=VSP_039641, VSP_039644;
CC   -!- DISEASE: Spermatogenic failure 89 (SPGF89) [MIM:620705]: An autosomal
CC       recessive male infertility disorder due to severely reduced progressive
CC       motility of sperm. {ECO:0000269|PubMed:37713809}. Note=The disease may
CC       be caused by variants affecting the gene represented in this entry.
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_001145128.3. [Q5TCS8-4]
DR   RefSeq; NP_001316531.1; NM_001329602.2. [Q5TCS8-2]
DR   RefSeq; NP_659462.1; NM_145025.5. [Q5TCS8-2]
DR   AlphaFoldDB; Q5TCS8; -.
DR   SMR; Q5TCS8; -.
DR   BioGRID; 128702; 23.
DR   FunCoup; Q5TCS8; 2011.
DR   IntAct; Q5TCS8; 14.
DR   NDEx; IQUERY-CP-AK9; 1 NDEx IQuery Curated Pathway.
DR   STRING; 9606.ENSP00000410186; -.
DR   GlyGen; Q5TCS8; 2 sites, 1 O-linked glycan (2 sites).
DR   iPTMnet; Q5TCS8; -.
DR   PhosphoSitePlus; Q5TCS8; -.
DR   BioMuta; AK9; -.
DR   DMDM; 302393675; -.
DR   jPOST; Q5TCS8; -.
DR   MassIVE; Q5TCS8; -.
DR   PaxDb; 9606-ENSP00000410186; -.
DR   PeptideAtlas; 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; 126 antibodies from 17 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   AGR; HGNC:33814; -.
DR   ClinPGx; PA164715271; -.
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   MIM; 620705; phenotype.
DR   OpenTargets; ENSG00000155085; -.
DR   Orphanet; 719880; Congenital myasthenic syndrome due to acetylcholine receptor clustering defect.
DR   Orphanet; 276234; Non-syndromic male infertility due to sperm motility disorder.
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; MESVCGT; -.
DR   OrthoDB; 439792at2759; -.
DR   PAN-GO; Q5TCS8; 6 GO annotations based on evolutionary models.
DR   PhylomeDB; Q5TCS8; -.
DR   PathwayCommons; Q5TCS8; -.
DR   Reactome; R-HSA-499943; Interconversion of nucleotide di- and triphosphates.
DR   SABIO-RK; Q5TCS8; -.
DR   SignaLink; Q5TCS8; -.
DR   Agora; ENSG00000155085; -.
DR   BioGRID-ORCS; 221264; 13 hits in 1147 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 150 other cell types or tissues.
DR   ExpressionAtlas; Q5TCS8; baseline and differential.
DR   GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR   GO; GO:0005829; C:cytosol; IDA:HPA.
DR   GO; GO:0031514; C:motile cilium; IEA:UniProtKB-SubCell.
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:AMP kinase activity; EXP:UniProtKB.
DR   GO; GO:0005524; F:ATP binding; IEA:InterPro.
DR   GO; GO:0036430; F:CMP kinase activity; EXP:UniProtKB.
DR   GO; GO:0047506; F:dAMP kinase activity; EXP:UniProtKB.
DR   GO; GO:0036431; F:dCMP kinase activity; EXP:UniProtKB.
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:0046899; F:nucleoside triphosphate adenylate kinase activity; IEA:RHEA.
DR   GO; GO:0046705; P:CDP biosynthetic process; IBA:GO_Central.
DR   GO; GO:0009123; P:nucleoside monophosphate metabolic process; IEA:UniProtKB-ARBA.
DR   GO; GO:0006225; P:UDP biosynthetic process; IBA:GO_Central.
DR   CDD; cd01428; ADK; 2.
DR   FunFam; 3.40.50.300:FF:001757; Adenylate kinase 9; 1.
DR   FunFam; 3.40.50.300:FF:004704; Adenylate kinase 9; 1.
DR   Gene3D; 3.40.50.300; P-loop containing nucleotide triphosphate hydrolases; 4.
DR   InterPro; IPR003593; AAA+_ATPase.
DR   InterPro; IPR000850; Adenylat/UMP-CMP_kin.
DR   InterPro; IPR027417; P-loop_NTPase.
DR   PANTHER; PTHR23359; NUCLEOTIDE KINASE; 1.
DR   Pfam; PF13238; AAA_18; 1.
DR   Pfam; PF00406; ADK; 2.
DR   SMART; SM00382; AAA; 3.
DR   SUPFAM; SSF52540; P-loop containing nucleoside triphosphate hydrolases; 6.
PE   1: Evidence at protein level;
KW   Alternative splicing; ATP-binding; Cell projection; Cilium; Coiled coil;
KW   Cytoplasm; Flagellum; Kinase; Nucleotide metabolism; Nucleotide-binding;
KW   Nucleus; Proteomics identification; Reference proteome; 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="NMP 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        197..210
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        733..750
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        751..761
FT                   /note="Basic and acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        767..791
FT                   /note="Acidic residues"
FT                   /evidence="ECO:0000256|SAM:MobiDB-lite"
FT   COMPBIAS        892..919
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   VARIANT         203..205
FT                   /note="Missing (in SPGF89; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:37713809"
FT                   /id="VAR_089392"
FT   VARIANT         815
FT                   /note="P -> L (in SPGF89; uncertain significance;
FT                   dbSNP:rs1204130200)"
FT                   /evidence="ECO:0000269|PubMed:37713809"
FT                   /id="VAR_089393"
FT   VARIANT         1086
FT                   /note="Missing (in SPGF89; uncertain significance)"
FT                   /evidence="ECO:0000269|PubMed:37713809"
FT                   /id="VAR_089394"
FT   VARIANT         1131
FT                   /note="E -> K (in SPGF89; uncertain significance;
FT                   dbSNP:rs574889890)"
FT                   /evidence="ECO:0000269|PubMed:37713809"
FT                   /id="VAR_089395"
FT   VARIANT         1692
FT                   /note="V -> M (in SPGF89; uncertain significance;
FT                   dbSNP:rs746832146)"
FT                   /evidence="ECO:0000269|PubMed:37713809"
FT                   /id="VAR_089396"
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
//