HYKK_MOUSE
ID HYKK_MOUSE Reviewed; 376 AA.
AC Q5U5V2; Q3TQ48; Q3TRW8; Q3UU28; Q8C3L8;
DT 18-MAR-2008, integrated into UniProtKB/Swiss-Prot.
DT 18-MAR-2008, sequence version 2.
DT 03-AUG-2022, entry version 118.
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 Mus musculus (Mouse).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Glires; Rodentia; Myomorpha; Muroidea; Muridae;
OC Murinae; Mus; Mus.
OX NCBI_TaxID=10090;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC STRAIN=C57BL/6J; TISSUE=Cerebellum, Embryoid bodies, Kidney, and Thymus;
RX PubMed=16141072; DOI=10.1126/science.1112014;
RA Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N.,
RA Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K.,
RA Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.,
RA Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R.,
RA Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T.,
RA Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A.,
RA Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B.,
RA Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M.,
RA Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S.,
RA Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E.,
RA Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D.,
RA Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M.,
RA Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H.,
RA Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V.,
RA Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S.,
RA Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H.,
RA Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N.,
RA Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F.,
RA Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G.,
RA Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z.,
RA Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C.,
RA Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y.,
RA Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S.,
RA Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K.,
RA Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R.,
RA van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H.,
RA Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M.,
RA Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C.,
RA Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S.,
RA Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K.,
RA Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M.,
RA Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C.,
RA Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A.,
RA Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.;
RT "The transcriptional landscape of the mammalian genome.";
RL Science 309:1559-1563(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC STRAIN=FVB/N; TISSUE=Kidney;
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 [3]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Kidney, and Liver;
RX PubMed=21183079; DOI=10.1016/j.cell.2010.12.001;
RA Huttlin E.L., Jedrychowski M.P., Elias J.E., Goswami T., Rad R.,
RA Beausoleil S.A., Villen J., Haas W., Sowa M.E., Gygi S.P.;
RT "A tissue-specific atlas of mouse protein phosphorylation and expression.";
RL Cell 143:1174-1189(2010).
CC -!- FUNCTION: Catalyzes the GTP-dependent phosphorylation of 5-hydroxy-L-
CC lysine. {ECO:0000250}.
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 -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000305}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q5U5V2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q5U5V2-2; Sequence=VSP_032521, VSP_032522;
CC -!- SIMILARITY: Belongs to the aminoglycoside phosphotransferase family.
CC {ECO:0000305}.
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DR EMBL; AK085527; BAC39464.1; -; mRNA.
DR EMBL; AK138851; BAE23801.1; -; mRNA.
DR EMBL; AK162425; BAE36908.1; -; mRNA.
DR EMBL; AK163926; BAE37537.1; -; mRNA.
DR EMBL; BC038618; AAH38618.1; -; mRNA.
DR CCDS; CCDS23197.1; -. [Q5U5V2-1]
DR RefSeq; NP_796325.2; NM_177351.4. [Q5U5V2-1]
DR AlphaFoldDB; Q5U5V2; -.
DR SMR; Q5U5V2; -.
DR STRING; 10090.ENSMUSP00000039980; -.
DR iPTMnet; Q5U5V2; -.
DR PhosphoSitePlus; Q5U5V2; -.
DR jPOST; Q5U5V2; -.
DR MaxQB; Q5U5V2; -.
DR PaxDb; Q5U5V2; -.
DR PeptideAtlas; Q5U5V2; -.
DR PRIDE; Q5U5V2; -.
DR ProteomicsDB; 273241; -. [Q5U5V2-1]
DR ProteomicsDB; 273242; -. [Q5U5V2-2]
DR Antibodypedia; 51728; 42 antibodies from 14 providers.
DR Ensembl; ENSMUST00000039742; ENSMUSP00000039980; ENSMUSG00000035878. [Q5U5V2-1]
DR GeneID; 235386; -.
DR KEGG; mmu:235386; -.
DR UCSC; uc009prr.2; mouse. [Q5U5V2-2]
DR UCSC; uc009prs.2; mouse. [Q5U5V2-1]
DR CTD; 123688; -.
DR MGI; MGI:2443139; Hykk.
DR VEuPathDB; HostDB:ENSMUSG00000035878; -.
DR eggNOG; ENOG502QT7T; Eukaryota.
DR GeneTree; ENSGT00390000011314; -.
DR HOGENOM; CLU_042971_1_1_1; -.
DR InParanoid; Q5U5V2; -.
DR OMA; QNFHVHI; -.
DR OrthoDB; 1519192at2759; -.
DR PhylomeDB; Q5U5V2; -.
DR TreeFam; TF324471; -.
DR Reactome; R-MMU-71064; Lysine catabolism.
DR BioGRID-ORCS; 235386; 3 hits in 70 CRISPR screens.
DR ChiTaRS; Hykk; mouse.
DR PRO; PR:Q5U5V2; -.
DR Proteomes; UP000000589; Chromosome 9.
DR RNAct; Q5U5V2; protein.
DR Bgee; ENSMUSG00000035878; Expressed in adult mammalian kidney and 170 other tissues.
DR Genevisible; Q5U5V2; MM.
DR GO; GO:0005737; C:cytoplasm; IEA:UniProtKB-SubCell.
DR GO; GO:0019202; F:amino acid kinase activity; IBA:GO_Central.
DR GO; GO:0047992; F:hydroxylysine kinase activity; ISO:MGI.
DR GO; GO:0016310; P:phosphorylation; IEA:UniProtKB-KW.
DR InterPro; IPR002575; Aminoglycoside_PTrfase.
DR InterPro; IPR011009; Kinase-like_dom_sf.
DR Pfam; PF01636; APH; 1.
DR SUPFAM; SSF56112; SSF56112; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Cytoplasm; Kinase; Reference proteome; Transferase.
FT CHAIN 1..376
FT /note="Hydroxylysine kinase"
FT /id="PRO_0000326045"
FT ACT_SITE 229
FT /note="Proton acceptor"
FT /evidence="ECO:0000250"
FT VAR_SEQ 163
FT /note="E -> L (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032521"
FT VAR_SEQ 164..376
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:16141072"
FT /id="VSP_032522"
FT CONFLICT 46
FT /note="Q -> P (in Ref. 1; BAC39464)"
FT /evidence="ECO:0000305"
FT CONFLICT 76
FT /note="Q -> P (in Ref. 1; BAC39464)"
FT /evidence="ECO:0000305"
FT CONFLICT 217
FT /note="K -> Q (in Ref. 1; BAC39464)"
FT /evidence="ECO:0000305"
FT CONFLICT 236
FT /note="L -> S (in Ref. 1; BAE23801)"
FT /evidence="ECO:0000305"
FT CONFLICT 239
FT /note="L -> F (in Ref. 2; AAH38618)"
FT /evidence="ECO:0000305"
SQ SEQUENCE 376 AA; 42357 MW; 0A22A0B70C6B7D2D CRC64;
MSSGAGWQSQ ASAKPVFTEA QASALVESVF GFKVSKIQPL PSYEDQNFRV HIARGKETTD
DPVEYVLKIS NTESSQTPEL IEMQNHVIMF LRAAGFPTAS VCRTKGDNTI SLISIDSGSG
VKSYLVRMLT YLPGRPIAEV AISHQQLYEI GRLAAQLDKA LEEFHHPKLS LFHRENFIWN
LKNVPLLEKY MGALSQSRNR EIVEQVIRMF KEEVMTKLSH FRECINHGDL NDHNILVDLS
KSASGEGVHQ VSGILDFGDM SYGYYVFEVA IVIMYMMIES TNPIQVGGHI LAGFESVIPL
TAVERQALFL LVCSRFSQSL VMAAYSCQLY PENKEYLMIT AKTGWKHLQQ LFDMGQKAVE
EIWFETAKSY ESEISM
