Full text data of AK6
AK6
(CINAP)
[Confidence: low (only semi-automatic identification from reviews)]
Adenylate kinase isoenzyme 6; AK6; 2.7.4.3 (Adrenal gland protein AD-004; Coilin-interacting nuclear ATPase protein; hCINAP; Dual activity adenylate kinase/ATPase; AK/ATPase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
Adenylate kinase isoenzyme 6; AK6; 2.7.4.3 (Adrenal gland protein AD-004; Coilin-interacting nuclear ATPase protein; hCINAP; Dual activity adenylate kinase/ATPase; AK/ATPase)
Note: presumably soluble (membrane word is not in UniProt keywords or features)
UniProt
Q9Y3D8
ID KAD6_HUMAN Reviewed; 172 AA.
AC Q9Y3D8; A8MSZ6; Q5F2S9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Adenylate kinase isoenzyme 6;
DE Short=AK6;
DE EC=2.7.4.3;
DE AltName: Full=Adrenal gland protein AD-004;
DE AltName: Full=Coilin-interacting nuclear ATPase protein;
DE Short=hCINAP;
DE AltName: Full=Dual activity adenylate kinase/ATPase;
DE Short=AK/ATPase;
GN Name=AK6; Synonyms=CINAP; ORFNames=AD-004, CGI-137;
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 1), BIOPHYSICOCHEMICAL PROPERTIES,
RP INTERACTION WITH COIL, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RC TISSUE=Cervix carcinoma, and Placenta;
RX PubMed=16079131; DOI=10.1074/jbc.M501982200;
RA Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K.,
RA Lamond A.I.;
RT "Characterization of hCINAP, a novel coilin-interacting protein
RT encoded by a transcript from the transcription factor TAFIID32
RT locus.";
RL J. Biol. Chem. 280:36429-36441(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 SUBUNIT.
RX PubMed=15213396; DOI=10.1107/S0907444904010467;
RA Ren H., Liang Y., Li R., Ding H., Qiu S., Lu S., An J., Li L., Luo M.,
RA Zheng X., Su X.D.;
RT "Protein preparation, crystallization and preliminary X-ray analysis
RT of human adrenal gland protein AD-004.";
RL Acta Crystallogr. D 60:1292-1294(2004).
RN [8]
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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=15630091; DOI=10.1073/pnas.0407459102;
RA Ren H., Wang L., Bennett M., Liang Y., Zheng X., Lu F., Li L., Nan J.,
RA Luo M., Eriksson S., Zhang C., Su X.-D.;
RT "The crystal structure of human adenylate kinase 6: an adenylate
RT kinase localized to the cell nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:303-308(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH ADP AND DADP,
RP MUTAGENESIS OF HIS-79, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22038794; DOI=10.1002/prot.23186;
RA Drakou C.E., Malekkou A., Hayes J.M., Lederer C.W., Leonidas D.D.,
RA Oikonomakos N.G., Lamond A.I., Santama N., Zographos S.E.;
RT "hCINAP is an atypical mammalian nuclear adenylate kinase with an
RT ATPase motif: structural and functional studies.";
RL Proteins 80:206-220(2012).
CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase
CC that catalyzes the reversible transfer of the terminal phosphate
CC group between nucleoside triphosphates and monophosphates. AMP and
CC dAMP are the preferred substrates, but CMP and dCMP are also good
CC substrates. IMP is phosphorylated to a much lesser extent. All
CC nucleoside triphosphates ATP, GTP, UTP, CTP, dATP, dCTP, dGTP, and
CC TTP are accepted as phosphate donors. CTP is the best phosphate
CC donor, followed by UTP, ATP, GTP and dCTP. May have a role in
CC nuclear energy homeostasis. Has also ATPase activity. May be
CC involved in regulation of Cajal body (CB) formation.
CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=192 uM for AMP;
CC KM=45 uM for ATP (for adenylate kinase activity);
CC KM=332 uM for ATP (for ATPase activity);
CC Vmax=1.27 umol/min/mg enzyme for ATPase activity;
CC Vmax=982 nmol/min/mg enzyme for the forward adenylate kinase
CC reaction;
CC Vmax=955 nmol/min/mg enzyme for the reverse adenylate kinase
CC reaction;
CC Note=kcat is 6.3 sec(-1) for adenylate kinase activity. kcat is
CC 4.8 sec(-1) for ATPase activity;
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with
CC COIL (via C-terminus).
CC -!- INTERACTION:
CC P38432:COIL; NbExp=5; IntAct=EBI-2896123, EBI-945751;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, Cajal body.
CC Note=Displays widespread diffuse nucleoplasmic distribution but
CC not detected in nucleoli. Detected in Cajal bodies but not in all
CC cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AK6;
CC IsoId=Q9Y3D8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3D8-2; Sequence=VSP_039714;
CC Note=Gene prediction based on EST data;
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC -!- CAUTION: Together with TAF9, were initially considered as products
CC of the same gene since they are sharing exons. However, they are
CC translated from different initiation codons and reading frames and
CC encode unrelated proteins. This arrangement is conserved in
CC mammals but these proteins are produced by separate genes in non-
CC mammalian species.
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DR EMBL; AJ878880; CAI48030.1; -; mRNA.
DR EMBL; AJ878881; CAI48031.1; -; mRNA.
DR EMBL; AF151895; AAD34132.1; -; mRNA.
DR EMBL; AF110777; AAF14860.1; -; mRNA.
DR EMBL; AC145132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471137; EAW51290.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51291.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51292.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51297.1; -; Genomic_DNA.
DR EMBL; BC007349; AAH07349.1; -; mRNA.
DR EMBL; BC007426; AAH07426.1; -; mRNA.
DR RefSeq; NP_001015891.1; NM_001015891.1.
DR RefSeq; NP_057367.1; NM_016283.4.
DR UniGene; Hs.653163; -.
DR PDB; 1RKB; X-ray; 2.00 A; A=1-172.
DR PDB; 3IIJ; X-ray; 1.76 A; A=1-172.
DR PDB; 3IIK; X-ray; 1.95 A; A=1-172.
DR PDB; 3IIL; X-ray; 2.00 A; A=1-172.
DR PDB; 3IIM; X-ray; 2.00 A; A=1-172.
DR PDBsum; 1RKB; -.
DR PDBsum; 3IIJ; -.
DR PDBsum; 3IIK; -.
DR PDBsum; 3IIL; -.
DR PDBsum; 3IIM; -.
DR ProteinModelPortal; Q9Y3D8; -.
DR SMR; Q9Y3D8; 1-172.
DR IntAct; Q9Y3D8; 4.
DR MINT; MINT-1389230; -.
DR STRING; 9606.ENSP00000370201; -.
DR DMDM; 6831735; -.
DR PaxDb; Q9Y3D8; -.
DR PeptideAtlas; Q9Y3D8; -.
DR PRIDE; Q9Y3D8; -.
DR DNASU; 6880; -.
DR Ensembl; ENST00000380818; ENSP00000370197; ENSG00000085231.
DR Ensembl; ENST00000380822; ENSP00000370201; ENSG00000085231.
DR Ensembl; ENST00000575603; ENSP00000459871; ENSG00000263302.
DR Ensembl; ENST00000576354; ENSP00000461237; ENSG00000263302.
DR GeneID; 102157402; -.
DR KEGG; hsa:6880; -.
DR UCSC; uc003jwa.3; human.
DR CTD; 6880; -.
DR GeneCards; GC05M068646; -.
DR GeneCards; GC05M068647; -.
DR HGNC; HGNC:49151; AK6.
DR HPA; CAB005361; -.
DR neXtProt; NX_Q9Y3D8; -.
DR PharmGKB; PA36317; -.
DR eggNOG; COG1936; -.
DR HOGENOM; HOG000224472; -.
DR HOVERGEN; HBG052207; -.
DR InParanoid; Q9Y3D8; -.
DR KO; K14535; -.
DR OMA; DNVQCEI; -.
DR ChiTaRS; TAF9; human.
DR EvolutionaryTrace; Q9Y3D8; -.
DR GenomeRNAi; 6880; -.
DR NextBio; 26873; -.
DR ArrayExpress; Q9Y3D8; -.
DR Bgee; Q9Y3D8; -.
DR Genevestigator; Q9Y3D8; -.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1; -.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Kinase; Nucleotide-binding; Nucleus; Reference proteome; Transferase.
FT CHAIN 1 172 Adenylate kinase isoenzyme 6.
FT /FTId=PRO_0000153896.
FT NP_BIND 13 18 ATP.
FT NP_BIND 148 149 ATP.
FT REGION 33 56 NMPbind.
FT REGION 108 118 LID.
FT BINDING 39 39 AMP (Probable).
FT BINDING 79 79 ATP.
FT BINDING 105 105 ATP.
FT BINDING 109 109 ATP.
FT VAR_SEQ 2 9 LLPNILLT -> CHRKP (in isoform 2).
FT /FTId=VSP_039714.
FT MUTAGEN 79 79 H->G: Induces homodimerization. Reduces
FT adenylate kinase activity by 72% and
FT ATPase activity by 76%. Significantly
FT changes Cajal body organization in the
FT nucleus, resulting in enhanced apoptosis
FT and reduced proliferation.
FT STRAND 6 9
FT HELIX 16 27
FT STRAND 30 33
FT HELIX 34 41
FT STRAND 44 48
FT TURN 49 52
FT STRAND 53 56
FT HELIX 58 71
FT STRAND 74 77
FT HELIX 86 88
FT STRAND 90 96
FT HELIX 99 108
FT HELIX 113 124
FT HELIX 127 135
FT HELIX 138 140
FT STRAND 141 145
FT HELIX 149 169
SQ SEQUENCE 172 AA; 20061 MW; 33F62318FB434301 CRC64;
MLLPNILLTG TPGVGKTTLG KELASKSGLK YINVGDLARE EQLYDGYDEE YDCPILDEDR
VVDELDNQMR EGGVIVDYHG CDFFPERWFH IVFVLRTDTN VLYERLETRG YNEKKLTDNI
QCEIFQVLYE EATASYKEEI VHQLPSNKPE ELENNVDQIL KWIEQWIKDH NS
//
ID KAD6_HUMAN Reviewed; 172 AA.
AC Q9Y3D8; A8MSZ6; Q5F2S9;
DT 30-MAY-2000, integrated into UniProtKB/Swiss-Prot.
read moreDT 01-NOV-1999, sequence version 1.
DT 22-JAN-2014, entry version 122.
DE RecName: Full=Adenylate kinase isoenzyme 6;
DE Short=AK6;
DE EC=2.7.4.3;
DE AltName: Full=Adrenal gland protein AD-004;
DE AltName: Full=Coilin-interacting nuclear ATPase protein;
DE Short=hCINAP;
DE AltName: Full=Dual activity adenylate kinase/ATPase;
DE Short=AK/ATPase;
GN Name=AK6; Synonyms=CINAP; ORFNames=AD-004, CGI-137;
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 1), BIOPHYSICOCHEMICAL PROPERTIES,
RP INTERACTION WITH COIL, SUBCELLULAR LOCATION, AND ALTERNATIVE SPLICING.
RC TISSUE=Cervix carcinoma, and Placenta;
RX PubMed=16079131; DOI=10.1074/jbc.M501982200;
RA Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K.,
RA Lamond A.I.;
RT "Characterization of hCINAP, a novel coilin-interacting protein
RT encoded by a transcript from the transcription factor TAFIID32
RT locus.";
RL J. Biol. Chem. 280:36429-36441(2005).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RX PubMed=10810093; DOI=10.1101/gr.10.5.703;
RA Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.;
RT "Identification of novel human genes evolutionarily conserved in
RT Caenorhabditis elegans by comparative proteomics.";
RL Genome Res. 10:703-713(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Adrenal gland;
RX PubMed=10931946; DOI=10.1073/pnas.160270997;
RA Hu R.-M., Han Z.-G., Song H.-D., Peng Y.-D., Huang Q.-H., Ren S.-X.,
RA Gu Y.-J., Huang C.-H., Li Y.-B., Jiang C.-L., Fu G., Zhang Q.-H.,
RA Gu B.-W., Dai M., Mao Y.-F., Gao G.-F., Rong R., Ye M., Zhou J.,
RA Xu S.-H., Gu J., Shi J.-X., Jin W.-R., Zhang C.-K., Wu T.-M.,
RA Huang G.-Y., Chen Z., Chen M.-D., Chen J.-L.;
RT "Gene expression profiling in the human hypothalamus-pituitary-adrenal
RT axis and full-length cDNA cloning.";
RL Proc. Natl. Acad. Sci. U.S.A. 97:9543-9548(2000).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15372022; DOI=10.1038/nature02919;
RA Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S.,
RA Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M.,
RA She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.,
RA Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M.,
RA Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T.,
RA Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M.,
RA Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K.,
RA Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C.,
RA Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M.,
RA Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A.,
RA Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M.,
RA Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M.,
RA Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S.,
RA Richardson P., Lucas S.M., Myers R.M., Rubin E.M.;
RT "The DNA sequence and comparative analysis of human chromosome 5.";
RL Nature 431:268-274(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
RA Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
RA Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
RA Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
RA Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
RA Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
RA Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
RA Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 SUBUNIT.
RX PubMed=15213396; DOI=10.1107/S0907444904010467;
RA Ren H., Liang Y., Li R., Ding H., Qiu S., Lu S., An J., Li L., Luo M.,
RA Zheng X., Su X.D.;
RT "Protein preparation, crystallization and preliminary X-ray analysis
RT of human adrenal gland protein AD-004.";
RL Acta Crystallogr. D 60:1292-1294(2004).
RN [8]
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).
RN [9]
RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY,
RP BIOPHYSICOCHEMICAL PROPERTIES, AND SUBCELLULAR LOCATION.
RX PubMed=15630091; DOI=10.1073/pnas.0407459102;
RA Ren H., Wang L., Bennett M., Liang Y., Zheng X., Lu F., Li L., Nan J.,
RA Luo M., Eriksson S., Zhang C., Su X.-D.;
RT "The crystal structure of human adenylate kinase 6: an adenylate
RT kinase localized to the cell nucleus.";
RL Proc. Natl. Acad. Sci. U.S.A. 102:303-308(2005).
RN [10]
RP X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH ADP AND DADP,
RP MUTAGENESIS OF HIS-79, AND BIOPHYSICOCHEMICAL PROPERTIES.
RX PubMed=22038794; DOI=10.1002/prot.23186;
RA Drakou C.E., Malekkou A., Hayes J.M., Lederer C.W., Leonidas D.D.,
RA Oikonomakos N.G., Lamond A.I., Santama N., Zographos S.E.;
RT "hCINAP is an atypical mammalian nuclear adenylate kinase with an
RT ATPase motif: structural and functional studies.";
RL Proteins 80:206-220(2012).
CC -!- FUNCTION: Broad-specificity nucleoside monophosphate (NMP) kinase
CC that catalyzes the reversible transfer of the terminal phosphate
CC group between nucleoside triphosphates and monophosphates. AMP and
CC dAMP are the preferred substrates, but CMP and dCMP are also good
CC substrates. IMP is phosphorylated to a much lesser extent. All
CC nucleoside triphosphates ATP, GTP, UTP, CTP, dATP, dCTP, dGTP, and
CC TTP are accepted as phosphate donors. CTP is the best phosphate
CC donor, followed by UTP, ATP, GTP and dCTP. May have a role in
CC nuclear energy homeostasis. Has also ATPase activity. May be
CC involved in regulation of Cajal body (CB) formation.
CC -!- CATALYTIC ACTIVITY: ATP + AMP = 2 ADP.
CC -!- BIOPHYSICOCHEMICAL PROPERTIES:
CC Kinetic parameters:
CC KM=192 uM for AMP;
CC KM=45 uM for ATP (for adenylate kinase activity);
CC KM=332 uM for ATP (for ATPase activity);
CC Vmax=1.27 umol/min/mg enzyme for ATPase activity;
CC Vmax=982 nmol/min/mg enzyme for the forward adenylate kinase
CC reaction;
CC Vmax=955 nmol/min/mg enzyme for the reverse adenylate kinase
CC reaction;
CC Note=kcat is 6.3 sec(-1) for adenylate kinase activity. kcat is
CC 4.8 sec(-1) for ATPase activity;
CC -!- SUBUNIT: Monomer and homodimer (By similarity). Interacts with
CC COIL (via C-terminus).
CC -!- INTERACTION:
CC P38432:COIL; NbExp=5; IntAct=EBI-2896123, EBI-945751;
CC -!- SUBCELLULAR LOCATION: Nucleus, nucleoplasm. Nucleus, Cajal body.
CC Note=Displays widespread diffuse nucleoplasmic distribution but
CC not detected in nucleoli. Detected in Cajal bodies but not in all
CC cells.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1; Synonyms=AK6;
CC IsoId=Q9Y3D8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y3D8-2; Sequence=VSP_039714;
CC Note=Gene prediction based on EST data;
CC -!- SIMILARITY: Belongs to the adenylate kinase family. AK6 subfamily.
CC -!- CAUTION: Together with TAF9, were initially considered as products
CC of the same gene since they are sharing exons. However, they are
CC translated from different initiation codons and reading frames and
CC encode unrelated proteins. This arrangement is conserved in
CC mammals but these proteins are produced by separate genes in non-
CC mammalian species.
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DR EMBL; AJ878880; CAI48030.1; -; mRNA.
DR EMBL; AJ878881; CAI48031.1; -; mRNA.
DR EMBL; AF151895; AAD34132.1; -; mRNA.
DR EMBL; AF110777; AAF14860.1; -; mRNA.
DR EMBL; AC145132; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471137; EAW51290.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51291.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51292.1; -; Genomic_DNA.
DR EMBL; CH471137; EAW51297.1; -; Genomic_DNA.
DR EMBL; BC007349; AAH07349.1; -; mRNA.
DR EMBL; BC007426; AAH07426.1; -; mRNA.
DR RefSeq; NP_001015891.1; NM_001015891.1.
DR RefSeq; NP_057367.1; NM_016283.4.
DR UniGene; Hs.653163; -.
DR PDB; 1RKB; X-ray; 2.00 A; A=1-172.
DR PDB; 3IIJ; X-ray; 1.76 A; A=1-172.
DR PDB; 3IIK; X-ray; 1.95 A; A=1-172.
DR PDB; 3IIL; X-ray; 2.00 A; A=1-172.
DR PDB; 3IIM; X-ray; 2.00 A; A=1-172.
DR PDBsum; 1RKB; -.
DR PDBsum; 3IIJ; -.
DR PDBsum; 3IIK; -.
DR PDBsum; 3IIL; -.
DR PDBsum; 3IIM; -.
DR ProteinModelPortal; Q9Y3D8; -.
DR SMR; Q9Y3D8; 1-172.
DR IntAct; Q9Y3D8; 4.
DR MINT; MINT-1389230; -.
DR STRING; 9606.ENSP00000370201; -.
DR DMDM; 6831735; -.
DR PaxDb; Q9Y3D8; -.
DR PeptideAtlas; Q9Y3D8; -.
DR PRIDE; Q9Y3D8; -.
DR DNASU; 6880; -.
DR Ensembl; ENST00000380818; ENSP00000370197; ENSG00000085231.
DR Ensembl; ENST00000380822; ENSP00000370201; ENSG00000085231.
DR Ensembl; ENST00000575603; ENSP00000459871; ENSG00000263302.
DR Ensembl; ENST00000576354; ENSP00000461237; ENSG00000263302.
DR GeneID; 102157402; -.
DR KEGG; hsa:6880; -.
DR UCSC; uc003jwa.3; human.
DR CTD; 6880; -.
DR GeneCards; GC05M068646; -.
DR GeneCards; GC05M068647; -.
DR HGNC; HGNC:49151; AK6.
DR HPA; CAB005361; -.
DR neXtProt; NX_Q9Y3D8; -.
DR PharmGKB; PA36317; -.
DR eggNOG; COG1936; -.
DR HOGENOM; HOG000224472; -.
DR HOVERGEN; HBG052207; -.
DR InParanoid; Q9Y3D8; -.
DR KO; K14535; -.
DR OMA; DNVQCEI; -.
DR ChiTaRS; TAF9; human.
DR EvolutionaryTrace; Q9Y3D8; -.
DR GenomeRNAi; 6880; -.
DR NextBio; 26873; -.
DR ArrayExpress; Q9Y3D8; -.
DR Bgee; Q9Y3D8; -.
DR Genevestigator; Q9Y3D8; -.
DR GO; GO:0015030; C:Cajal body; IDA:UniProtKB.
DR GO; GO:0004017; F:adenylate kinase activity; IDA:UniProtKB.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR HAMAP; MF_00039; Adenylate_kinase_AK6; 1; -.
DR InterPro; IPR020618; Adenyl_kinase_AK6.
DR InterPro; IPR027417; P-loop_NTPase.
DR SUPFAM; SSF52540; SSF52540; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Alternative splicing; ATP-binding; Complete proteome;
KW Kinase; Nucleotide-binding; Nucleus; Reference proteome; Transferase.
FT CHAIN 1 172 Adenylate kinase isoenzyme 6.
FT /FTId=PRO_0000153896.
FT NP_BIND 13 18 ATP.
FT NP_BIND 148 149 ATP.
FT REGION 33 56 NMPbind.
FT REGION 108 118 LID.
FT BINDING 39 39 AMP (Probable).
FT BINDING 79 79 ATP.
FT BINDING 105 105 ATP.
FT BINDING 109 109 ATP.
FT VAR_SEQ 2 9 LLPNILLT -> CHRKP (in isoform 2).
FT /FTId=VSP_039714.
FT MUTAGEN 79 79 H->G: Induces homodimerization. Reduces
FT adenylate kinase activity by 72% and
FT ATPase activity by 76%. Significantly
FT changes Cajal body organization in the
FT nucleus, resulting in enhanced apoptosis
FT and reduced proliferation.
FT STRAND 6 9
FT HELIX 16 27
FT STRAND 30 33
FT HELIX 34 41
FT STRAND 44 48
FT TURN 49 52
FT STRAND 53 56
FT HELIX 58 71
FT STRAND 74 77
FT HELIX 86 88
FT STRAND 90 96
FT HELIX 99 108
FT HELIX 113 124
FT HELIX 127 135
FT HELIX 138 140
FT STRAND 141 145
FT HELIX 149 169
SQ SEQUENCE 172 AA; 20061 MW; 33F62318FB434301 CRC64;
MLLPNILLTG TPGVGKTTLG KELASKSGLK YINVGDLARE EQLYDGYDEE YDCPILDEDR
VVDELDNQMR EGGVIVDYHG CDFFPERWFH IVFVLRTDTN VLYERLETRG YNEKKLTDNI
QCEIFQVLYE EATASYKEEI VHQLPSNKPE ELENNVDQIL KWIEQWIKDH NS
//