ID   HYKK_HUMAN              Reviewed;         373 AA.
AC   A2RU49; B7ZMA5; F8W6X5; Q6ZTN0;
DT   18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT   18-MAR-2008, sequence version 2.
DT   24-JAN-2024, entry version 131.
DE   RecName: Full=Hydroxylysine kinase;
DE            Short=5-hydroxy-L-lysine kinase;
DE            EC=2.7.1.81;
DE   AltName: Full=Aminoglycoside phosphotransferase domain-containing protein 1;
GN   Name=HYKK; Synonyms=AGPHD1;
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] (ISOFORM 2).
RC   TISSUE=Uterus;
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=16572171; DOI=10.1038/nature04601;
RA   Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
RA   Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
RA   FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
RA   Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
RA   Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
RA   DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J.,
RA   Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E.,
RA   Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B.,
RA   Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R.,
RA   O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M.B.,
RA   Stewart S., Sougnez C., Stone S.M., Topham K., Vincent D., Wang S.,
RA   Zimmer A.R., Birren B.W., Hood L., Lander E.S., Nusbaum C.;
RT   "Analysis of the DNA sequence and duplication history of human chromosome
RT   15.";
RL   Nature 440:671-675(2006).
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 (DEC-2006) to the EMBL/GenBank/DDBJ databases.
RN   [4]
RP   NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 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   [5]
RP   FUNCTION, CATALYTIC ACTIVITY, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX   PubMed=22241472; DOI=10.1074/jbc.m111.323485;
RA   Veiga-da-Cunha M., Hadi F., Balligand T., Stroobant V., Van Schaftingen E.;
RT   "Molecular identification of hydroxylysine kinase and of
RT   ammoniophospholyases acting on 5-phosphohydroxy-L-lysine and
RT   phosphoethanolamine.";
RL   J. Biol. Chem. 287:7246-7255(2012).
CC   -!- FUNCTION: Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-
CC       lysine. {ECO:0000269|PubMed:22241472}.
CC   -!- CATALYTIC ACTIVITY:
CC       Reaction=(5R)-5-hydroxy-L-lysine + GTP = (5R)-5-phosphooxy-L-lysine +
CC         GDP + H(+); Xref=Rhea:RHEA:19049, ChEBI:CHEBI:15378,
CC         ChEBI:CHEBI:37565, ChEBI:CHEBI:57882, ChEBI:CHEBI:58189,
CC         ChEBI:CHEBI:58357; EC=2.7.1.81;
CC         Evidence={ECO:0000269|PubMed:22241472};
CC   -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC       Kinetic parameters:
CC         KM=280 uM for (5R)-5-hydroxy-L-lysine (in the presence of 2 mM ATP)
CC         {ECO:0000269|PubMed:22241472};
CC         KM=7.6 uM for (5R)-5-hydroxy-L-lysine (in the presence of 0.2 mM GTP)
CC         {ECO:0000269|PubMed:22241472};
CC         KM=810 uM for ATP (in the presence of 0.5 mM (5R)-5-hydroxy-L-lysine)
CC         {ECO:0000269|PubMed:22241472};
CC         KM=3.5 uM for GTP (in the presence of 0.5 mM (5R)-5-hydroxy-L-lysine)
CC         {ECO:0000269|PubMed:22241472};
CC         Vmax=4.95 umol/min/mg enzyme toward (5R)-5-hydroxy-L-lysine (in the
CC         presence of 2 mM ATP) {ECO:0000269|PubMed:22241472};
CC         Vmax=0.49 umol/min/mg enzyme toward (5R)-5-hydroxy-L-lysine (in the
CC         presence of 0.2 mM GTP) {ECO:0000269|PubMed:22241472};
CC         Vmax=5.28 umol/min/mg enzyme toward ATP (in the presence of 0.5 mM
CC         (5R)-5-hydroxy-L-lysine) {ECO:0000269|PubMed:22241472};
CC         Vmax=0.57 umol/min/mg enzyme toward GTP (in the presence of 0.5 mM
CC         (5R)-5-hydroxy-L-lysine) {ECO:0000269|PubMed:22241472};
CC   -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC   -!- ALTERNATIVE PRODUCTS:
CC       Event=Alternative splicing; Named isoforms=3;
CC       Name=1;
CC         IsoId=A2RU49-1; Sequence=Displayed;
CC       Name=2;
CC         IsoId=A2RU49-2; Sequence=VSP_032517, VSP_032518;
CC       Name=3;
CC         IsoId=A2RU49-3; Sequence=VSP_032520;
CC   -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC       {ECO:0000305}.
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DR   EMBL; AK126453; BAC86556.1; -; mRNA.
DR   EMBL; AC027228; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR   EMBL; CH471136; EAW99167.1; -; Genomic_DNA.
DR   EMBL; BC132753; AAI32754.1; -; mRNA.
DR   EMBL; BC144383; AAI44384.1; -; mRNA.
DR   CCDS; CCDS42063.1; -. [A2RU49-1]
DR   CCDS; CCDS45318.1; -. [A2RU49-3]
DR   RefSeq; NP_001013641.2; NM_001013619.3. [A2RU49-1]
DR   RefSeq; NP_001077081.1; NM_001083612.1. [A2RU49-3]
DR   AlphaFoldDB; A2RU49; -.
DR   SMR; A2RU49; -.
DR   BioGRID; 125829; 8.
DR   IntAct; A2RU49; 3.
DR   STRING; 9606.ENSP00000373640; -.
DR   iPTMnet; A2RU49; -.
DR   PhosphoSitePlus; A2RU49; -.
DR   BioMuta; HYKK; -.
DR   EPD; A2RU49; -.
DR   MassIVE; A2RU49; -.
DR   MaxQB; A2RU49; -.
DR   PaxDb; 9606-ENSP00000455459; -.
DR   PeptideAtlas; A2RU49; -.
DR   ProteomicsDB; 29851; -.
DR   ProteomicsDB; 497; -. [A2RU49-1]
DR   ProteomicsDB; 498; -. [A2RU49-2]
DR   ProteomicsDB; 499; -. [A2RU49-3]
DR   Pumba; A2RU49; -.
DR   Antibodypedia; 51728; 49 antibodies from 14 providers.
DR   DNASU; 123688; -.
DR   Ensembl; ENST00000388988.9; ENSP00000373640.4; ENSG00000188266.14. [A2RU49-1]
DR   Ensembl; ENST00000408962.6; ENSP00000386197.2; ENSG00000188266.14. [A2RU49-3]
DR   Ensembl; ENST00000563233.2; ENSP00000454850.1; ENSG00000188266.14. [A2RU49-3]
DR   Ensembl; ENST00000566289.5; ENSP00000456614.1; ENSG00000188266.14. [A2RU49-2]
DR   Ensembl; ENST00000569878.5; ENSP00000455459.1; ENSG00000188266.14. [A2RU49-1]
DR   GeneID; 123688; -.
DR   KEGG; hsa:123688; -.
DR   MANE-Select; ENST00000388988.9; ENSP00000373640.4; NM_001013619.4; NP_001013641.2.
DR   UCSC; uc002bdt.4; human. [A2RU49-1]
DR   AGR; HGNC:34403; -.
DR   CTD; 123688; -.
DR   DisGeNET; 123688; -.
DR   GeneCards; HYKK; -.
DR   HGNC; HGNC:34403; HYKK.
DR   HPA; ENSG00000188266; Low tissue specificity.
DR   MIM; 614681; gene.
DR   neXtProt; NX_A2RU49; -.
DR   OpenTargets; ENSG00000188266; -.
DR   PharmGKB; PA165478483; -.
DR   VEuPathDB; HostDB:ENSG00000188266; -.
DR   eggNOG; ENOG502QT7T; Eukaryota.
DR   GeneTree; ENSGT00390000011314; -.
DR   HOGENOM; CLU_042971_1_1_1; -.
DR   InParanoid; A2RU49; -.
DR   OMA; AAHSCQL; -.
DR   OrthoDB; 5398335at2759; -.
DR   PhylomeDB; A2RU49; -.
DR   TreeFam; TF324471; -.
DR   BRENDA; 2.7.1.81; 2681.
DR   PathwayCommons; A2RU49; -.
DR   Reactome; R-HSA-71064; Lysine catabolism.
DR   SABIO-RK; A2RU49; -.
DR   SignaLink; A2RU49; -.
DR   BioGRID-ORCS; 123688; 9 hits in 1114 CRISPR screens.
DR   ChiTaRS; HYKK; human.
DR   GenomeRNAi; 123688; -.
DR   Pharos; A2RU49; Tbio.
DR   PRO; PR:A2RU49; -.
DR   Proteomes; UP000005640; Chromosome 15.
DR   RNAct; A2RU49; Protein.
DR   Bgee; ENSG00000188266; Expressed in olfactory segment of nasal mucosa and 102 other cell types or tissues.
DR   ExpressionAtlas; A2RU49; baseline and differential.
DR   GO; GO:0005759; C:mitochondrial matrix; TAS:Reactome.
DR   GO; GO:0019202; F:amino acid kinase activity; IBA:GO_Central.
DR   GO; GO:0047992; F:hydroxylysine kinase activity; IDA:FlyBase.
DR   GO; GO:0006554; P:lysine catabolic process; TAS:Reactome.
DR   GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR   Gene3D; 3.90.1200.10; -; 1.
DR   InterPro; IPR002575; Aminoglycoside_PTrfase.
DR   InterPro; IPR011009; Kinase-like_dom_sf.
DR   PANTHER; PTHR21064:SF1; HYDROXYLYSINE KINASE; 1.
DR   PANTHER; PTHR21064; UNCHARACTERIZED; 1.
DR   Pfam; PF01636; APH; 1.
DR   SUPFAM; SSF56112; Protein kinase-like (PK-like); 1.
DR   Genevisible; A2RU49; HS.
PE   1: Evidence at protein level;
KW   Alternative splicing; Cytoplasm; Kinase; Reference proteome; Transferase.
FT   CHAIN           1..373
FT                   /note="Hydroxylysine kinase"
FT                   /id="PRO_0000326044"
FT   ACT_SITE        226
FT                   /note="Proton acceptor"
FT                   /evidence="ECO:0000250"
FT   VAR_SEQ         160..172
FT                   /note="RFHHPKLSSLHRE -> EGKPRVTPLLAKN (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_032517"
FT   VAR_SEQ         173..373
FT                   /note="Missing (in isoform 2)"
FT                   /evidence="ECO:0000303|PubMed:14702039"
FT                   /id="VSP_032518"
FT   VAR_SEQ         221..373
FT                   /note="Missing (in isoform 3)"
FT                   /evidence="ECO:0000303|PubMed:15489334"
FT                   /id="VSP_032520"
FT   VARIANT         A2RU49-2:165
FT                   /note="V -> I (in dbSNP:4380026)"
FT                   /evidence="ECO:0000305"
FT                   /id="VAR_082892"
SQ   SEQUENCE   373 AA;  41933 MW;  C8BF3521D8D980A2 CRC64;
     MSSGNYQQSE ALSKPTFSEE QASALVESVF GLKVSKVRPL PSYDDQNFHV YVSKTKDGPT
     EYVLKISNTK ASKNPDLIEV QNHIIMFLKA AGFPTASVCH TKGDNTASLV SVDSGSEIKS
     YLVRLLTYLP GRPIAELPVS PQLLYEIGKL AAKLDKTLQR FHHPKLSSLH RENFIWNLKN
     VPLLEKYLYA LGQNRNREIV EHVIHLFKEE VMTKLSHFRE CINHGDLNDH NILIESSKSA
     SGNAEYQVSG ILDFGDMSYG YYVFEVAITI MYMMIESKSP IQVGGHVLAG FESITPLTAV
     EKGALFLLVC SRFCQSLVMA AYSCQLYPEN KDYLMVTAKT GWKHLQQMFD MGQKAVEEIW
     FETAKSYESG ISM
//