Full text data of ADPGK
ADPGK
[Confidence: medium (present in either hRBCD or BSc_CH or PM22954596)]
ADP-dependent glucokinase; ADP-GK; ADPGK; 2.7.1.147 (RbBP-35; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
ADP-dependent glucokinase; ADP-GK; ADPGK; 2.7.1.147 (RbBP-35; Flags: Precursor)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Comments
Isoform Q9BRR6-2 was detected.
Isoform Q9BRR6-2 was detected.
UniProt
Q9BRR6
ID ADPGK_HUMAN Reviewed; 497 AA.
AC Q9BRR6; Q49AU7; Q8NBI1; Q8WZ90; Q96NF8; Q9H0A7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 104.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA 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
RT project: 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose
CC 6-phosphate using ADP as the phosphate donor. GDP and CDP can
CC replace ADP, but with reduced efficiency (By similarity).
CC -!- CATALYTIC ACTIVITY: ADP + D-glucose = AMP + D-glucose 6-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- PATHWAY: Carbohydrate degradation; glycolysis.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (Potential).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family.
CC -!- SIMILARITY: Contains 1 ADPK (ADP-dependent kinase) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_112574.3; NM_031284.4.
DR UniGene; Hs.654636; -.
DR ProteinModelPortal; Q9BRR6; -.
DR SMR; Q9BRR6; 156-488.
DR IntAct; Q9BRR6; 5.
DR MINT; MINT-1404876; -.
DR STRING; 9606.ENSP00000312250; -.
DR PhosphoSite; Q9BRR6; -.
DR DMDM; 62899887; -.
DR PaxDb; Q9BRR6; -.
DR PRIDE; Q9BRR6; -.
DR DNASU; 83440; -.
DR Ensembl; ENST00000311669; ENSP00000312250; ENSG00000159322.
DR Ensembl; ENST00000456471; ENSP00000397694; ENSG00000159322.
DR Ensembl; ENST00000562823; ENSP00000454367; ENSG00000159322.
DR Ensembl; ENST00000567941; ENSP00000458102; ENSG00000159322.
DR Ensembl; ENST00000569517; ENSP00000454304; ENSG00000159322.
DR GeneID; 83440; -.
DR KEGG; hsa:83440; -.
DR UCSC; uc002avg.4; human.
DR CTD; 83440; -.
DR GeneCards; GC15M073043; -.
DR H-InvDB; HIX0026868; -.
DR HGNC; HGNC:25250; ADPGK.
DR HPA; HPA045194; -.
DR MIM; 611861; gene.
DR neXtProt; NX_Q9BRR6; -.
DR PharmGKB; PA134971928; -.
DR eggNOG; COG4809; -.
DR HOGENOM; HOG000233731; -.
DR HOVERGEN; HBG050461; -.
DR InParanoid; Q9BRR6; -.
DR KO; K08074; -.
DR OMA; AVGVNAC; -.
DR UniPathway; UPA00109; -.
DR GeneWiki; ADP-specific_glucokinase; -.
DR GenomeRNAi; 83440; -.
DR NextBio; 72318; -.
DR PRO; PR:Q9BRR6; -.
DR ArrayExpress; Q9BRR6; -.
DR Bgee; Q9BRR6; -.
DR CleanEx; HS_ADPGK; -.
DR Genevestigator; Q9BRR6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043843; F:ADP-specific glucokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.
DR InterPro; IPR007666; ADP_PFK/GK.
DR PANTHER; PTHR21208; PTHR21208; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Polymorphism; Reference proteome; Secreted;
KW Signal; Transferase.
FT SIGNAL 1 22 Potential.
FT CHAIN 23 497 ADP-dependent glucokinase.
FT /FTId=PRO_0000184776.
FT DOMAIN 52 497 ADPK.
FT ACT_SITE 481 481 Proton acceptor (By similarity).
FT METAL 297 297 Magnesium (By similarity).
FT METAL 328 328 Magnesium (By similarity).
FT METAL 481 481 Magnesium (By similarity).
FT VAR_SEQ 1 274 Missing (in isoform 4).
FT /FTId=VSP_013550.
FT VAR_SEQ 1 239 Missing (in isoform 3).
FT /FTId=VSP_013549.
FT VAR_SEQ 1 122 Missing (in isoform 5).
FT /FTId=VSP_013548.
FT VAR_SEQ 79 497 Missing (in isoform 6).
FT /FTId=VSP_035014.
FT VAR_SEQ 275 280 RKRLLE -> MAASCR (in isoform 4).
FT /FTId=VSP_013551.
FT VAR_SEQ 313 313 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_013552.
FT VAR_SEQ 404 469 AAGARVAGTQACATETIDTSRVSLRAPQEFMTSHSEAGSRI
FT VLNPNKPVVEWHREGISFHFTPVLV -> LGSSCGWDTGLR
FT HRNHRHQPSVSEGTPRVHDFPFGGRLQDCIKPKQASSRMAQ
FT RGNILPLHTSIGV (in isoform 5).
FT /FTId=VSP_013553.
FT VAR_SEQ 470 497 Missing (in isoform 5).
FT /FTId=VSP_013554.
FT VARIANT 184 184 K -> R (in dbSNP:rs8024644).
FT /FTId=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
//
ID ADPGK_HUMAN Reviewed; 497 AA.
AC Q9BRR6; Q49AU7; Q8NBI1; Q8WZ90; Q96NF8; Q9H0A7;
DT 26-APR-2005, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-JUN-2001, sequence version 1.
DT 22-JAN-2014, entry version 104.
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;
OC Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
OC Catarrhini; Hominidae; 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.,
RA Lauber J., Duesterhoeft A., Beyer A., Koehrer K., Strack N.,
RA Mewes H.-W., Ottenwaelder B., Obermaier B., Tampe J., Heubner D.,
RA Wambutt R., Korn B., Klein M., Poustka A.;
RT "Towards a catalog of human genes and proteins: sequencing and
RT analysis of 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.,
RA Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
RA Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
RA Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
RA Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
RA Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
RA Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
RA Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
RA Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
RA Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
RA 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.,
RA Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
RA Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
RA Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
RA Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
RA Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
RA Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
RA Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
RA Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
RA Nakai K., Yada T., Nakamura Y., Ohara O., 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-
RT length human cDNAs encoding secretion or membrane proteins from oligo-
RT capped cDNA 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
RT project: 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.,
RA Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
CC -!- FUNCTION: Catalyzes the phosphorylation of D-glucose to D-glucose
CC 6-phosphate using ADP as the phosphate donor. GDP and CDP can
CC replace ADP, but with reduced efficiency (By similarity).
CC -!- CATALYTIC ACTIVITY: ADP + D-glucose = AMP + D-glucose 6-phosphate.
CC -!- COFACTOR: Binds 1 magnesium ion per subunit (By similarity).
CC -!- PATHWAY: Carbohydrate degradation; glycolysis.
CC -!- SUBUNIT: Monomer (By similarity).
CC -!- SUBCELLULAR LOCATION: Secreted (Potential).
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 Note=No experimental confirmation available;
CC -!- SIMILARITY: Belongs to the ADP-dependent glucokinase family.
CC -!- SIMILARITY: Contains 1 ADPK (ADP-dependent kinase) domain.
CC -----------------------------------------------------------------------
CC Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms
CC Distributed under the Creative Commons Attribution-NoDerivs 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 RefSeq; NP_112574.3; NM_031284.4.
DR UniGene; Hs.654636; -.
DR ProteinModelPortal; Q9BRR6; -.
DR SMR; Q9BRR6; 156-488.
DR IntAct; Q9BRR6; 5.
DR MINT; MINT-1404876; -.
DR STRING; 9606.ENSP00000312250; -.
DR PhosphoSite; Q9BRR6; -.
DR DMDM; 62899887; -.
DR PaxDb; Q9BRR6; -.
DR PRIDE; Q9BRR6; -.
DR DNASU; 83440; -.
DR Ensembl; ENST00000311669; ENSP00000312250; ENSG00000159322.
DR Ensembl; ENST00000456471; ENSP00000397694; ENSG00000159322.
DR Ensembl; ENST00000562823; ENSP00000454367; ENSG00000159322.
DR Ensembl; ENST00000567941; ENSP00000458102; ENSG00000159322.
DR Ensembl; ENST00000569517; ENSP00000454304; ENSG00000159322.
DR GeneID; 83440; -.
DR KEGG; hsa:83440; -.
DR UCSC; uc002avg.4; human.
DR CTD; 83440; -.
DR GeneCards; GC15M073043; -.
DR H-InvDB; HIX0026868; -.
DR HGNC; HGNC:25250; ADPGK.
DR HPA; HPA045194; -.
DR MIM; 611861; gene.
DR neXtProt; NX_Q9BRR6; -.
DR PharmGKB; PA134971928; -.
DR eggNOG; COG4809; -.
DR HOGENOM; HOG000233731; -.
DR HOVERGEN; HBG050461; -.
DR InParanoid; Q9BRR6; -.
DR KO; K08074; -.
DR OMA; AVGVNAC; -.
DR UniPathway; UPA00109; -.
DR GeneWiki; ADP-specific_glucokinase; -.
DR GenomeRNAi; 83440; -.
DR NextBio; 72318; -.
DR PRO; PR:Q9BRR6; -.
DR ArrayExpress; Q9BRR6; -.
DR Bgee; Q9BRR6; -.
DR CleanEx; HS_ADPGK; -.
DR Genevestigator; Q9BRR6; -.
DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-SubCell.
DR GO; GO:0043843; F:ADP-specific glucokinase activity; IEA:UniProtKB-EC.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0006096; P:glycolysis; IEA:UniProtKB-UniPathway.
DR InterPro; IPR007666; ADP_PFK/GK.
DR PANTHER; PTHR21208; PTHR21208; 1.
DR Pfam; PF04587; ADP_PFK_GK; 1.
DR PROSITE; PS51255; ADPK; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; Complete proteome; Glycolysis; Kinase;
KW Magnesium; Metal-binding; Polymorphism; Reference proteome; Secreted;
KW Signal; Transferase.
FT SIGNAL 1 22 Potential.
FT CHAIN 23 497 ADP-dependent glucokinase.
FT /FTId=PRO_0000184776.
FT DOMAIN 52 497 ADPK.
FT ACT_SITE 481 481 Proton acceptor (By similarity).
FT METAL 297 297 Magnesium (By similarity).
FT METAL 328 328 Magnesium (By similarity).
FT METAL 481 481 Magnesium (By similarity).
FT VAR_SEQ 1 274 Missing (in isoform 4).
FT /FTId=VSP_013550.
FT VAR_SEQ 1 239 Missing (in isoform 3).
FT /FTId=VSP_013549.
FT VAR_SEQ 1 122 Missing (in isoform 5).
FT /FTId=VSP_013548.
FT VAR_SEQ 79 497 Missing (in isoform 6).
FT /FTId=VSP_035014.
FT VAR_SEQ 275 280 RKRLLE -> MAASCR (in isoform 4).
FT /FTId=VSP_013551.
FT VAR_SEQ 313 313 Missing (in isoform 2 and isoform 4).
FT /FTId=VSP_013552.
FT VAR_SEQ 404 469 AAGARVAGTQACATETIDTSRVSLRAPQEFMTSHSEAGSRI
FT VLNPNKPVVEWHREGISFHFTPVLV -> LGSSCGWDTGLR
FT HRNHRHQPSVSEGTPRVHDFPFGGRLQDCIKPKQASSRMAQ
FT RGNILPLHTSIGV (in isoform 5).
FT /FTId=VSP_013553.
FT VAR_SEQ 470 497 Missing (in isoform 5).
FT /FTId=VSP_013554.
FT VARIANT 184 184 K -> R (in dbSNP:rs8024644).
FT /FTId=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
//
MIM
611861
*RECORD*
*FIELD* NO
611861
*FIELD* TI
*611861 ADP-DEPENDENT GLUCOKINASE; ADPGK
;;ADP-GK
*FIELD* TX
DESCRIPTION
ADPGK (EC 2.7.1.147) catalyzes the ADP-dependent phosphorylation of
read moreglucose to glucose-6-phosphate and may play a role in glycolysis,
possibly during ischemic conditions (Ronimus and Morgan, 2004).
CLONING
By database analysis, Ronimus and Morgan (2004) identified human ADPGK.
They obtained a mouse Adpgk cDNA derived from mammary tumor and
determined by SDS-PAGE that Adpgk has a molecular mass of 51.5 kD. Gel
filtration analysis showed that the protein likely is monomeric.
Database analysis showed expression in mammalian epithelial, endocrine,
lymphatic, muscular, and organ tissues, consistent with a housekeeping
function for Adpgk.
GENE FUNCTION
Using recombinant mouse Adpgk purified to homogeneity by SDS-PAGE,
Ronimus and Morgan (2004) showed that Adpgk exhibited ADP-dependent
glucokinase activity and had a bimodal optimal pH at 5.75 to 6.5 and
8.75 to 9.0. Activity was not inhibited by glucose-6-phosphate and other
known modulators of glycolytic enzymes; however, high concentrations of
glucose significantly inhibited enzyme activity. Mouse Adpgk displayed
high specificity for D-glucose, low Km for glucose and ADP, and
inhibition by glucose and AMP. Based on these characteristics, Ronimus
and Morgan (2004) concluded that Adpgk is a member of the mammalian
hexokinase/glucokinase family (see HK1; 142600)
GENE STRUCTURE
Ronimus and Morgan (2004) determined that the ADPGK gene contains 7
exons and 4 predicted alternative promoters.
MAPPING
By genomic sequence analysis, Ronimus and Morgan (2004) mapped the ADPGK
gene to chromosome 15. They mapped the corresponding mouse Adpgk gene to
mouse chromosome 9.
*FIELD* RF
1. Ronimus, R. S.; Morgan, H. W.: Cloning and biochemical characterization
of a novel mouse ADP-dependent glucokinase. Biochem. Biophys. Res.
Commun. 315: 652-658, 2004.
*FIELD* CD
Dorothy S. Reilly: 2/26/2008
*FIELD* ED
wwang: 02/26/2008
*RECORD*
*FIELD* NO
611861
*FIELD* TI
*611861 ADP-DEPENDENT GLUCOKINASE; ADPGK
;;ADP-GK
*FIELD* TX
DESCRIPTION
ADPGK (EC 2.7.1.147) catalyzes the ADP-dependent phosphorylation of
read moreglucose to glucose-6-phosphate and may play a role in glycolysis,
possibly during ischemic conditions (Ronimus and Morgan, 2004).
CLONING
By database analysis, Ronimus and Morgan (2004) identified human ADPGK.
They obtained a mouse Adpgk cDNA derived from mammary tumor and
determined by SDS-PAGE that Adpgk has a molecular mass of 51.5 kD. Gel
filtration analysis showed that the protein likely is monomeric.
Database analysis showed expression in mammalian epithelial, endocrine,
lymphatic, muscular, and organ tissues, consistent with a housekeeping
function for Adpgk.
GENE FUNCTION
Using recombinant mouse Adpgk purified to homogeneity by SDS-PAGE,
Ronimus and Morgan (2004) showed that Adpgk exhibited ADP-dependent
glucokinase activity and had a bimodal optimal pH at 5.75 to 6.5 and
8.75 to 9.0. Activity was not inhibited by glucose-6-phosphate and other
known modulators of glycolytic enzymes; however, high concentrations of
glucose significantly inhibited enzyme activity. Mouse Adpgk displayed
high specificity for D-glucose, low Km for glucose and ADP, and
inhibition by glucose and AMP. Based on these characteristics, Ronimus
and Morgan (2004) concluded that Adpgk is a member of the mammalian
hexokinase/glucokinase family (see HK1; 142600)
GENE STRUCTURE
Ronimus and Morgan (2004) determined that the ADPGK gene contains 7
exons and 4 predicted alternative promoters.
MAPPING
By genomic sequence analysis, Ronimus and Morgan (2004) mapped the ADPGK
gene to chromosome 15. They mapped the corresponding mouse Adpgk gene to
mouse chromosome 9.
*FIELD* RF
1. Ronimus, R. S.; Morgan, H. W.: Cloning and biochemical characterization
of a novel mouse ADP-dependent glucokinase. Biochem. Biophys. Res.
Commun. 315: 652-658, 2004.
*FIELD* CD
Dorothy S. Reilly: 2/26/2008
*FIELD* ED
wwang: 02/26/2008