ID ADPGK_HUMAN Reviewed; 497 AA. AC Q9BRR6; Q49AU7; Q8NBI1; Q8WZ90; Q96NF8; Q9H0A7; DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot. DT 01-JUN-2001, sequence version 1. DT 02-OCT-2024, entry version 174. DE RecName: Full=ADP-dependent glucokinase; DE Short=ADP-GK; DE Short=ADPGK; DE EC=2.7.1.147; DE AltName: Full=RbBP-35; DE Flags: Precursor; GN Name=ADPGK; ORFNames=PSEC0260; 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 [MRNA] (ISOFORM 5). RC TISSUE=Lymph node; RA Fan Z.S., Ao S.Z.; RT "RbBP-35 interacted with pRb."; RL Submitted (NOV-1999) to the EMBL/GenBank/DDBJ databases. RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RC TISSUE=Testis; RX PubMed=11230166; DOI=10.1101/gr.gr1547r; RA Wiemann S., Weil B., Wellenreuther R., Gassenhuber J., Glassl S., RA Ansorge W., Boecher M., Bloecker H., Bauersachs S., Blum H., Lauber J., RA Duesterhoeft A., Beyer A., Koehrer K., Strack N., Mewes H.-W., RA Ottenwaelder B., Obermaier B., Tampe J., Heubner D., Wambutt R., Korn B., RA Klein M., Poustka A.; RT "Towards a catalog of human genes and proteins: sequencing and analysis of RT 500 novel complete protein coding human cDNAs."; RL Genome Res. 11:422-435(2001). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3). RC TISSUE=Heart; 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 [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4). RA Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.; RT "Cloning of human full open reading frames in Gateway(TM) system entry RT vector (pDONR201)."; RL Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases. RN [5] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2). RC TISSUE=Teratocarcinoma; RX PubMed=16303743; DOI=10.1093/dnares/12.2.117; RA Otsuki T., Ota T., Nishikawa T., Hayashi K., Suzuki Y., Yamamoto J., RA Wakamatsu A., Kimura K., Sakamoto K., Hatano N., Kawai Y., Ishii S., RA Saito K., Kojima S., Sugiyama T., Ono T., Okano K., Yoshikawa Y., RA Aotsuka S., Sasaki N., Hattori A., Okumura K., Nagai K., Sugano S., RA Isogai T.; RT "Signal sequence and keyword trap in silico for selection of full-length RT human cDNAs encoding secretion or membrane proteins from oligo-capped cDNA RT libraries."; RL DNA Res. 12:117-126(2005). RN [6] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 6). RC TISSUE=Brain, and 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 [7] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=21269460; DOI=10.1186/1752-0509-5-17; RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., RA Bennett K.L., Superti-Furga G., Colinge J.; RT "Initial characterization of the human central proteome."; RL BMC Syst. Biol. 5:17-17(2011). RN [8] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; DOI=10.1002/pmic.201400617; RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D., RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.; RT "N-terminome analysis of the human mitochondrial proteome."; RL Proteomics 15:2519-2524(2015). CC -!- FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose 6- CC phosphate using ADP as the phosphate donor. GDP and CDP can replace CC ADP, but with reduced efficiency (By similarity). {ECO:0000250}. CC -!- CATALYTIC ACTIVITY: CC Reaction=ADP + D-glucose = AMP + D-glucose 6-phosphate + H(+); CC Xref=Rhea:RHEA:11460, ChEBI:CHEBI:4167, ChEBI:CHEBI:15378, CC ChEBI:CHEBI:61548, ChEBI:CHEBI:456215, ChEBI:CHEBI:456216; CC EC=2.7.1.147; CC -!- COFACTOR: CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000255|PROSITE- CC ProRule:PRU00584}; CC Note=Binds 1 Mg(2+) ion per subunit. {ECO:0000255|PROSITE- CC ProRule:PRU00584}; CC -!- PATHWAY: Carbohydrate degradation; glycolysis. {ECO:0000255|PROSITE- CC ProRule:PRU00584}. CC -!- SUBUNIT: Monomer. {ECO:0000250}. CC -!- SUBCELLULAR LOCATION: Secreted {ECO:0000305}. CC -!- ALTERNATIVE PRODUCTS: CC Event=Alternative splicing; Named isoforms=6; CC Name=1; CC IsoId=Q9BRR6-1; Sequence=Displayed; CC Name=2; CC IsoId=Q9BRR6-2; Sequence=VSP_013552; CC Name=3; CC IsoId=Q9BRR6-3; Sequence=VSP_013549; CC Name=4; CC IsoId=Q9BRR6-4; Sequence=VSP_013550, VSP_013551, VSP_013552; CC Name=5; CC IsoId=Q9BRR6-5; Sequence=VSP_013548, VSP_013553, VSP_013554; CC Name=6; CC IsoId=Q9BRR6-6; Sequence=VSP_035014; CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family. CC {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; AF204270; AAL31473.1; -; mRNA. DR EMBL; AL136873; CAB66807.1; -; mRNA. DR EMBL; AK055526; BAB70941.1; -; mRNA. DR EMBL; CR533447; CAG38478.1; -; mRNA. DR EMBL; AK075560; BAC11699.1; -; mRNA. DR EMBL; BC006112; AAH06112.1; -; mRNA. DR EMBL; BC018074; AAH18074.1; -; mRNA. DR CCDS; CCDS42057.1; -. [Q9BRR6-2] DR CCDS; CCDS92041.1; -. [Q9BRR6-1] DR RefSeq; NP_112574.3; NM_031284.4. [Q9BRR6-2] DR RefSeq; XP_006720775.1; XM_006720712.3. DR AlphaFoldDB; Q9BRR6; -. DR SMR; Q9BRR6; -. DR BioGRID; 123643; 102. DR IntAct; Q9BRR6; 62. DR MINT; Q9BRR6; -. DR STRING; 9606.ENSP00000312250; -. DR iPTMnet; Q9BRR6; -. DR MetOSite; Q9BRR6; -. DR PhosphoSitePlus; Q9BRR6; -. DR SwissPalm; Q9BRR6; -. DR BioMuta; ADPGK; -. DR DMDM; 62899887; -. DR jPOST; Q9BRR6; -. DR MassIVE; Q9BRR6; -. DR PaxDb; 9606-ENSP00000312250; -. DR PeptideAtlas; Q9BRR6; -. DR ProteomicsDB; 78812; -. [Q9BRR6-1] DR ProteomicsDB; 78813; -. [Q9BRR6-2] DR ProteomicsDB; 78814; -. [Q9BRR6-3] DR ProteomicsDB; 78815; -. [Q9BRR6-4] DR ProteomicsDB; 78816; -. [Q9BRR6-5] DR ProteomicsDB; 78817; -. [Q9BRR6-6] DR Pumba; Q9BRR6; -. DR Antibodypedia; 26747; 243 antibodies from 30 providers. DR DNASU; 83440; -. DR Ensembl; ENST00000311669.12; ENSP00000312250.8; ENSG00000159322.18. [Q9BRR6-2] DR Ensembl; ENST00000456471.3; ENSP00000397694.3; ENSG00000159322.18. [Q9BRR6-1] DR Ensembl; ENST00000562823.1; ENSP00000454367.1; ENSG00000159322.18. [Q9BRR6-6] DR Ensembl; ENST00000567941.5; ENSP00000458102.1; ENSG00000159322.18. [Q9BRR6-6] DR Ensembl; ENST00000569517.5; ENSP00000454304.1; ENSG00000159322.18. [Q9BRR6-6] DR GeneID; 83440; -. DR KEGG; hsa:83440; -. DR MANE-Select; ENST00000456471.3; ENSP00000397694.3; NM_001365225.1; NP_001352154.1. DR UCSC; uc002avf.5; human. [Q9BRR6-1] DR AGR; HGNC:25250; -. DR CTD; 83440; -. DR DisGeNET; 83440; -. DR GeneCards; ADPGK; -. DR HGNC; HGNC:25250; ADPGK. DR HPA; ENSG00000159322; Low tissue specificity. DR MIM; 611861; gene. DR neXtProt; NX_Q9BRR6; -. DR OpenTargets; ENSG00000159322; -. DR PharmGKB; PA134971928; -. DR VEuPathDB; HostDB:ENSG00000159322; -. DR eggNOG; KOG4184; Eukaryota. DR GeneTree; ENSGT00390000017953; -. DR HOGENOM; CLU_032362_0_0_1; -. DR InParanoid; Q9BRR6; -. DR OMA; MWRKASA; -. DR OrthoDB; 51859at2759; -. DR PhylomeDB; Q9BRR6; -. DR TreeFam; TF313401; -. DR BRENDA; 2.7.1.147; 2681. DR PathwayCommons; Q9BRR6; -. DR Reactome; R-HSA-70171; Glycolysis. DR SABIO-RK; Q9BRR6; -. DR SignaLink; Q9BRR6; -. DR UniPathway; UPA00109; -. DR BioGRID-ORCS; 83440; 16 hits in 1153 CRISPR screens. DR ChiTaRS; ADPGK; human. DR GeneWiki; ADP-specific_glucokinase; -. DR GenomeRNAi; 83440; -. DR Pharos; Q9BRR6; Tbio. DR PRO; PR:Q9BRR6; -. DR Proteomes; UP000005640; Chromosome 15. DR RNAct; Q9BRR6; protein. DR Bgee; ENSG00000159322; Expressed in oocyte and 177 other cell types or tissues. DR ExpressionAtlas; Q9BRR6; baseline and differential. DR GO; GO:0005783; C:endoplasmic reticulum; IDA:CACAO. DR GO; GO:0005789; C:endoplasmic reticulum membrane; TAS:Reactome. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell. DR GO; GO:0016020; C:membrane; HDA:UniProtKB. DR GO; GO:0043843; F:ADP-specific glucokinase activity; IDA:MGI. DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW. DR GO; GO:0006006; P:glucose metabolic process; IDA:MGI. DR GO; GO:0061620; P:glycolytic process through glucose-6-phosphate; TAS:Reactome. DR CDD; cd01938; ADPGK_ADPPFK; 1. DR Gene3D; 3.40.1190.20; -; 1. DR InterPro; IPR007666; ADP_PFK/GK. DR InterPro; IPR029056; Ribokinase-like. DR PANTHER; PTHR21208; ADP-DEPENDENT GLUCOKINASE; 1. DR PANTHER; PTHR21208:SF0; ADP-DEPENDENT GLUCOKINASE; 1. DR Pfam; PF04587; ADP_PFK_GK; 1. DR SUPFAM; SSF53613; Ribokinase-like; 1. DR PROSITE; PS51255; ADPK; 1. PE 1: Evidence at protein level; KW Alternative splicing; Glycolysis; Kinase; Magnesium; Metal-binding; KW Proteomics identification; Reference proteome; Secreted; Signal; KW Transferase. FT SIGNAL 1..22 FT /evidence="ECO:0000255" FT CHAIN 23..497 FT /note="ADP-dependent glucokinase" FT /id="PRO_0000184776" FT DOMAIN 52..497 FT /note="ADPK" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584" FT ACT_SITE 481 FT /note="Proton acceptor" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584" FT BINDING 297 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584" FT BINDING 328 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584" FT BINDING 481 FT /ligand="Mg(2+)" FT /ligand_id="ChEBI:CHEBI:18420" FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00584" FT VAR_SEQ 1..274 FT /note="Missing (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.4" FT /id="VSP_013550" FT VAR_SEQ 1..239 FT /note="Missing (in isoform 3)" FT /evidence="ECO:0000303|PubMed:14702039" FT /id="VSP_013549" FT VAR_SEQ 1..122 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_013548" FT VAR_SEQ 79..497 FT /note="Missing (in isoform 6)" FT /evidence="ECO:0000303|PubMed:15489334" FT /id="VSP_035014" FT VAR_SEQ 275..280 FT /note="RKRLLE -> MAASCR (in isoform 4)" FT /evidence="ECO:0000303|PubMed:11230166, ECO:0000303|Ref.4" FT /id="VSP_013551" FT VAR_SEQ 313 FT /note="Missing (in isoform 2 and isoform 4)" FT /evidence="ECO:0000303|PubMed:11230166, FT ECO:0000303|PubMed:16303743, ECO:0000303|Ref.4" FT /id="VSP_013552" FT VAR_SEQ 404..469 FT /note="AAGARVAGTQACATETIDTSRVSLRAPQEFMTSHSEAGSRIVLNPNKPVVEW FT HREGISFHFTPVLV -> LGSSCGWDTGLRHRNHRHQPSVSEGTPRVHDFPFGGRLQDC FT IKPKQASSRMAQRGNILPLHTSIGV (in isoform 5)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_013553" FT VAR_SEQ 470..497 FT /note="Missing (in isoform 5)" FT /evidence="ECO:0000303|Ref.1" FT /id="VSP_013554" FT VARIANT 184 FT /note="K -> R (in dbSNP:rs8024644)" FT /id="VAR_060085" SQ SEQUENCE 497 AA; 54089 MW; B758E977CDA88F8F CRC64; MALWRGSAYA GFLALAVGCV FLLEPELPGS ALRSLWSSLC LGPAPAPPGP VSPEGRLAAA WDALIVRPVR RWRRVAVGVN ACVDVVLSGV KLLQALGLSP GNGKDHSILH SRNDLEEAFI HFMGKGAAAE RFFSDKETFH DIAQVASEFP GAQHYVGGNA ALIGQKFAAN SDLKVLLCGP VGPKLHELLD DNVFVPPESL QEVDEFHLIL EYQAGEEWGQ LKAPHANRFI FSHDLSNGAM NMLEVFVSSL EEFQPDLVVL SGLHMMEGQS KELQRKRLLE VVTSISDIPT GIPVHLELAS MTNRELMSSI VHQQVFPAVT SLGLNEQELL FLTQSASGPH SSLSSWNGVP DVGMVSDILF WILKEHGRSK SRASDLTRIH FHTLVYHILA TVDGHWANQL AAVAAGARVA GTQACATETI DTSRVSLRAP QEFMTSHSEA GSRIVLNPNK PVVEWHREGI SFHFTPVLVC KDPIRTVGLG DAISAEGLFY SEVHPHY //