NDK7_HUMAN
ID NDK7_HUMAN Reviewed; 376 AA.
AC Q9Y5B8; A8K3T6; A8MY09; B3KSW9; Q5TGZ4;
DT 11-JAN-2001, integrated into UniProtKB/Swiss-Prot.
DT 01-NOV-1999, sequence version 1.
DT 03-AUG-2022, entry version 184.
DE RecName: Full=Nucleoside diphosphate kinase 7;
DE Short=NDK 7;
DE Short=NDP kinase 7;
DE EC=2.7.4.6;
DE AltName: Full=nm23-H7;
GN Name=NME7;
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 1).
RA Mehus J.G., Lambeth D.O.;
RT "Human nm23-H7 (NME7) mRNA.";
RL Submitted (MAY-1999) to the EMBL/GenBank/DDBJ databases.
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
RC TISSUE=Brain cortex, and Lung;
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 [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=16710414; DOI=10.1038/nature04727;
RA Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A.,
RA Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C.,
RA Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.,
RA Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C.,
RA Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W.,
RA Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J.,
RA Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J.,
RA Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y.,
RA Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J.,
RA Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H.,
RA Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L.,
RA Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J.,
RA Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S.,
RA Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K.,
RA Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R.,
RA Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M.,
RA Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S.,
RA Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J.,
RA Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W.,
RA McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N.,
RA Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V.,
RA Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J.,
RA Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E.,
RA Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S.,
RA Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M.,
RA White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H.,
RA Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E.,
RA Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G.,
RA Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.;
RT "The DNA sequence and biological annotation of human chromosome 1.";
RL Nature 441:315-321(2006).
RN [4]
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 (JUL-2005) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Urinary bladder;
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 [6]
RP IDENTIFICATION BY MASS SPECTROMETRY.
RC TISSUE=Lymphoblast;
RX PubMed=14654843; DOI=10.1038/nature02166;
RA Andersen J.S., Wilkinson C.J., Mayor T., Mortensen P., Nigg E.A., Mann M.;
RT "Proteomic characterization of the human centrosome by protein correlation
RT profiling.";
RL Nature 426:570-574(2003).
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).
CC -!- FUNCTION: Major role in the synthesis of nucleoside triphosphates other
CC than ATP. The ATP gamma phosphate is transferred to the NDP beta
CC phosphate via a ping-pong mechanism, using a phosphorylated active-site
CC intermediate. Microtubule inner protein (MIP) part of the dynein-
CC decorated doublet microtubules (DMTs) in cilia axoneme, which is
CC required for motile cilia beating (By similarity).
CC {ECO:0000250|UniProtKB:Q5E9Y9}.
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a 2'-deoxyribonucleoside 5'-diphosphate + ATP = a 2'-
CC deoxyribonucleoside 5'-triphosphate + ADP; Xref=Rhea:RHEA:44640,
CC ChEBI:CHEBI:30616, ChEBI:CHEBI:61560, ChEBI:CHEBI:73316,
CC ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- CATALYTIC ACTIVITY:
CC Reaction=a ribonucleoside 5'-diphosphate + ATP = a ribonucleoside 5'-
CC triphosphate + ADP; Xref=Rhea:RHEA:18113, ChEBI:CHEBI:30616,
CC ChEBI:CHEBI:57930, ChEBI:CHEBI:61557, ChEBI:CHEBI:456216; EC=2.7.4.6;
CC -!- COFACTOR:
CC Name=Mg(2+); Xref=ChEBI:CHEBI:18420; Evidence={ECO:0000250};
CC -!- INTERACTION:
CC Q9Y5B8; Q9Y2J4: AMOTL2; NbExp=3; IntAct=EBI-744782, EBI-746752;
CC Q9Y5B8; Q9BRR9: ARHGAP9; NbExp=3; IntAct=EBI-744782, EBI-750254;
CC Q9Y5B8; Q96KE9-2: BTBD6; NbExp=5; IntAct=EBI-744782, EBI-12012762;
CC Q9Y5B8; Q5VU69: C1orf189; NbExp=10; IntAct=EBI-744782, EBI-10247920;
CC Q9Y5B8; Q9BWT7: CARD10; NbExp=3; IntAct=EBI-744782, EBI-3866279;
CC Q9Y5B8; Q8NA61-2: CBY2; NbExp=3; IntAct=EBI-744782, EBI-11524851;
CC Q9Y5B8; A6NC98: CCDC88B; NbExp=3; IntAct=EBI-744782, EBI-347573;
CC Q9Y5B8; Q8TD31-3: CCHCR1; NbExp=6; IntAct=EBI-744782, EBI-10175300;
CC Q9Y5B8; O14613: CDC42EP2; NbExp=6; IntAct=EBI-744782, EBI-3438291;
CC Q9Y5B8; Q9P209: CEP72; NbExp=12; IntAct=EBI-744782, EBI-739498;
CC Q9Y5B8; Q96D03: DDIT4L; NbExp=3; IntAct=EBI-744782, EBI-742054;
CC Q9Y5B8; Q9NRI5-2: DISC1; NbExp=3; IntAct=EBI-744782, EBI-11988027;
CC Q9Y5B8; Q6TDU7: DNAI7; NbExp=3; IntAct=EBI-744782, EBI-5235378;
CC Q9Y5B8; Q5JST6: EFHC2; NbExp=3; IntAct=EBI-744782, EBI-2349927;
CC Q9Y5B8; O75344: FKBP6; NbExp=4; IntAct=EBI-744782, EBI-744771;
CC Q9Y5B8; O75955: FLOT1; NbExp=3; IntAct=EBI-744782, EBI-603643;
CC Q9Y5B8; P15407: FOSL1; NbExp=9; IntAct=EBI-744782, EBI-744510;
CC Q9Y5B8; P15408: FOSL2; NbExp=3; IntAct=EBI-744782, EBI-3893419;
CC Q9Y5B8; Q8WXI9: GATAD2B; NbExp=3; IntAct=EBI-744782, EBI-923440;
CC Q9Y5B8; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-744782, EBI-7251368;
CC Q9Y5B8; Q08379: GOLGA2; NbExp=6; IntAct=EBI-744782, EBI-618309;
CC Q9Y5B8; O15499: GSC2; NbExp=3; IntAct=EBI-744782, EBI-19954058;
CC Q9Y5B8; Q9BT25: HAUS8; NbExp=3; IntAct=EBI-744782, EBI-2558143;
CC Q9Y5B8; Q13422-7: IKZF1; NbExp=6; IntAct=EBI-744782, EBI-11522367;
CC Q9Y5B8; Q9UKT9: IKZF3; NbExp=3; IntAct=EBI-744782, EBI-747204;
CC Q9Y5B8; Q0VD86: INCA1; NbExp=5; IntAct=EBI-744782, EBI-6509505;
CC Q9Y5B8; Q9ULR0-1: ISY1; NbExp=3; IntAct=EBI-744782, EBI-18398632;
CC Q9Y5B8; P05783: KRT18; NbExp=4; IntAct=EBI-744782, EBI-297888;
CC Q9Y5B8; O95678: KRT75; NbExp=3; IntAct=EBI-744782, EBI-2949715;
CC Q9Y5B8; Q8TBB1: LNX1; NbExp=9; IntAct=EBI-744782, EBI-739832;
CC Q9Y5B8; Q9P086: MED11; NbExp=3; IntAct=EBI-744782, EBI-394704;
CC Q9Y5B8; Q96HR3: MED30; NbExp=5; IntAct=EBI-744782, EBI-394659;
CC Q9Y5B8; A8MW99: MEI4; NbExp=3; IntAct=EBI-744782, EBI-19944212;
CC Q9Y5B8; Q6FHY5: MEOX2; NbExp=3; IntAct=EBI-744782, EBI-16439278;
CC Q9Y5B8; Q9UBF9: MYOT; NbExp=3; IntAct=EBI-744782, EBI-296701;
CC Q9Y5B8; Q15742: NAB2; NbExp=6; IntAct=EBI-744782, EBI-8641936;
CC Q9Y5B8; I6L9F6: NEFL; NbExp=3; IntAct=EBI-744782, EBI-10178578;
CC Q9Y5B8; P07196: NEFL; NbExp=3; IntAct=EBI-744782, EBI-475646;
CC Q9Y5B8; Q9UBC1: NFKBIL1; NbExp=3; IntAct=EBI-744782, EBI-1043728;
CC Q9Y5B8; Q9GZT8: NIF3L1; NbExp=3; IntAct=EBI-744782, EBI-740897;
CC Q9Y5B8; O00746: NME4; NbExp=3; IntAct=EBI-744782, EBI-744871;
CC Q9Y5B8; P49902: NT5C2; NbExp=4; IntAct=EBI-744782, EBI-742084;
CC Q9Y5B8; O75665: OFD1; NbExp=3; IntAct=EBI-744782, EBI-716327;
CC Q9Y5B8; Q3KNR5: PAX4; NbExp=3; IntAct=EBI-744782, EBI-10240813;
CC Q9Y5B8; O75928-2: PIAS2; NbExp=3; IntAct=EBI-744782, EBI-348567;
CC Q9Y5B8; Q9NRD5: PICK1; NbExp=3; IntAct=EBI-744782, EBI-79165;
CC Q9Y5B8; P78424: POU6F2; NbExp=3; IntAct=EBI-744782, EBI-12029004;
CC Q9Y5B8; Q2NL68: PROSER3; NbExp=5; IntAct=EBI-744782, EBI-11336487;
CC Q9Y5B8; P25786: PSMA1; NbExp=3; IntAct=EBI-744782, EBI-359352;
CC Q9Y5B8; Q04864: REL; NbExp=3; IntAct=EBI-744782, EBI-307352;
CC Q9Y5B8; Q92622: RUBCN; NbExp=3; IntAct=EBI-744782, EBI-2952709;
CC Q9Y5B8; A0MZ66: SHTN1; NbExp=3; IntAct=EBI-744782, EBI-308778;
CC Q9Y5B8; A0MZ66-4: SHTN1; NbExp=3; IntAct=EBI-744782, EBI-12097232;
CC Q9Y5B8; O95295: SNAPIN; NbExp=3; IntAct=EBI-744782, EBI-296723;
CC Q9Y5B8; Q86XE0: SNX32; NbExp=5; IntAct=EBI-744782, EBI-8099743;
CC Q9Y5B8; Q8N0S2: SYCE1; NbExp=6; IntAct=EBI-744782, EBI-6872807;
CC Q9Y5B8; P15884: TCF4; NbExp=3; IntAct=EBI-744782, EBI-533224;
CC Q9Y5B8; P15884-3: TCF4; NbExp=3; IntAct=EBI-744782, EBI-13636688;
CC Q9Y5B8; Q9BT92: TCHP; NbExp=12; IntAct=EBI-744782, EBI-740781;
CC Q9Y5B8; Q969V4: TEKT1; NbExp=5; IntAct=EBI-744782, EBI-10180409;
CC Q9Y5B8; Q96N21: TEPSIN; NbExp=3; IntAct=EBI-744782, EBI-11139477;
CC Q9Y5B8; Q9P2Z0: THAP10; NbExp=3; IntAct=EBI-744782, EBI-745404;
CC Q9Y5B8; Q15025: TNIP1; NbExp=8; IntAct=EBI-744782, EBI-357849;
CC Q9Y5B8; P48788: TNNI2; NbExp=3; IntAct=EBI-744782, EBI-7746394;
CC Q9Y5B8; P14373: TRIM27; NbExp=3; IntAct=EBI-744782, EBI-719493;
CC Q9Y5B8; Q8IWZ4: TRIM48; NbExp=3; IntAct=EBI-744782, EBI-17555779;
CC Q9Y5B8; P10074: ZBTB48; NbExp=6; IntAct=EBI-744782, EBI-744864;
CC Q9Y5B8; P17027: ZNF23; NbExp=3; IntAct=EBI-744782, EBI-5657766;
CC Q9Y5B8; Q6P1L6: ZNF343; NbExp=3; IntAct=EBI-744782, EBI-10252492;
CC Q9Y5B8; Q8TF50: ZNF526; NbExp=3; IntAct=EBI-744782, EBI-11035148;
CC Q9Y5B8; Q6ZNG0: ZNF620; NbExp=3; IntAct=EBI-744782, EBI-4395669;
CC -!- SUBCELLULAR LOCATION: Cytoplasm, cytoskeleton, cilium axoneme
CC {ECO:0000250|UniProtKB:Q5E9Y9}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=Q9Y5B8-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q9Y5B8-2; Sequence=VSP_040996;
CC -!- SIMILARITY: Belongs to the NDK family. {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; AF153191; AAD34622.1; -; mRNA.
DR EMBL; AK094513; BAG52881.1; -; mRNA.
DR EMBL; AK290701; BAF83390.1; -; mRNA.
DR EMBL; AL031726; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; Z99758; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL356852; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471067; EAW90834.1; -; Genomic_DNA.
DR EMBL; CH471067; EAW90835.1; -; Genomic_DNA.
DR EMBL; BC006983; AAH06983.1; -; mRNA.
DR CCDS; CCDS1277.1; -. [Q9Y5B8-1]
DR CCDS; CCDS44274.1; -. [Q9Y5B8-2]
DR RefSeq; NP_037462.1; NM_013330.4. [Q9Y5B8-1]
DR RefSeq; NP_932076.1; NM_197972.2. [Q9Y5B8-2]
DR AlphaFoldDB; Q9Y5B8; -.
DR SMR; Q9Y5B8; -.
DR BioGRID; 118963; 167.
DR IntAct; Q9Y5B8; 118.
DR MINT; Q9Y5B8; -.
DR STRING; 9606.ENSP00000356785; -.
DR iPTMnet; Q9Y5B8; -.
DR PhosphoSitePlus; Q9Y5B8; -.
DR BioMuta; NME7; -.
DR DMDM; 12230353; -.
DR EPD; Q9Y5B8; -.
DR jPOST; Q9Y5B8; -.
DR MassIVE; Q9Y5B8; -.
DR MaxQB; Q9Y5B8; -.
DR PaxDb; Q9Y5B8; -.
DR PeptideAtlas; Q9Y5B8; -.
DR PRIDE; Q9Y5B8; -.
DR ProteomicsDB; 86336; -. [Q9Y5B8-1]
DR ProteomicsDB; 86337; -. [Q9Y5B8-2]
DR Antibodypedia; 34356; 163 antibodies from 25 providers.
DR DNASU; 29922; -.
DR Ensembl; ENST00000367811.8; ENSP00000356785.3; ENSG00000143156.14. [Q9Y5B8-1]
DR Ensembl; ENST00000472647.5; ENSP00000433341.1; ENSG00000143156.14. [Q9Y5B8-2]
DR GeneID; 29922; -.
DR KEGG; hsa:29922; -.
DR MANE-Select; ENST00000367811.8; ENSP00000356785.3; NM_013330.5; NP_037462.1.
DR UCSC; uc001gft.5; human. [Q9Y5B8-1]
DR CTD; 29922; -.
DR DisGeNET; 29922; -.
DR GeneCards; NME7; -.
DR HGNC; HGNC:20461; NME7.
DR HPA; ENSG00000143156; Low tissue specificity.
DR MalaCards; NME7; -.
DR MIM; 613465; gene.
DR neXtProt; NX_Q9Y5B8; -.
DR OpenTargets; ENSG00000143156; -.
DR Orphanet; 101063; Situs inversus totalis.
DR PharmGKB; PA134962167; -.
DR VEuPathDB; HostDB:ENSG00000143156; -.
DR eggNOG; KOG0888; Eukaryota.
DR GeneTree; ENSGT00940000158946; -.
DR HOGENOM; CLU_060216_3_1_1; -.
DR InParanoid; Q9Y5B8; -.
DR OMA; VCMCLEI; -.
DR OrthoDB; 1230088at2759; -.
DR PhylomeDB; Q9Y5B8; -.
DR TreeFam; TF106374; -.
DR PathwayCommons; Q9Y5B8; -.
DR Reactome; R-HSA-380270; Recruitment of mitotic centrosome proteins and complexes.
DR Reactome; R-HSA-380320; Recruitment of NuMA to mitotic centrosomes.
DR SignaLink; Q9Y5B8; -.
DR BioGRID-ORCS; 29922; 8 hits in 1076 CRISPR screens.
DR ChiTaRS; NME7; human.
DR GenomeRNAi; 29922; -.
DR Pharos; Q9Y5B8; Tbio.
DR PRO; PR:Q9Y5B8; -.
DR Proteomes; UP000005640; Chromosome 1.
DR RNAct; Q9Y5B8; protein.
DR Bgee; ENSG00000143156; Expressed in cerebellar vermis and 203 other tissues.
DR ExpressionAtlas; Q9Y5B8; baseline and differential.
DR Genevisible; Q9Y5B8; HS.
DR GO; GO:0005879; C:axonemal microtubule; ISS:UniProtKB.
DR GO; GO:0005813; C:centrosome; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; TAS:Reactome.
DR GO; GO:0005524; F:ATP binding; IEA:UniProtKB-KW.
DR GO; GO:0046872; F:metal ion binding; IEA:UniProtKB-KW.
DR GO; GO:0004550; F:nucleoside diphosphate kinase activity; IEA:UniProtKB-EC.
DR GO; GO:0006241; P:CTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006183; P:GTP biosynthetic process; IEA:InterPro.
DR GO; GO:0006165; P:nucleoside diphosphate phosphorylation; IEA:InterPro.
DR GO; GO:0006228; P:UTP biosynthetic process; IEA:InterPro.
DR CDD; cd04415; NDPk7A; 1.
DR CDD; cd04412; NDPk7B; 1.
DR Gene3D; 3.30.70.141; -; 2.
DR InterPro; IPR006602; DM10_dom.
DR InterPro; IPR034907; NDK-like_dom.
DR InterPro; IPR036850; NDK-like_dom_sf.
DR InterPro; IPR011410; NDPK7.
DR InterPro; IPR035525; NDPk7A.
DR InterPro; IPR037993; NDPk7B.
DR InterPro; IPR001564; Nucleoside_diP_kinase.
DR Pfam; PF00334; NDK; 2.
DR PIRSF; PIRSF036503; NDK7; 1.
DR PRINTS; PR01243; NUCDPKINASE.
DR SMART; SM00676; DM10; 1.
DR SMART; SM00562; NDK; 2.
DR SUPFAM; SSF54919; SSF54919; 2.
DR PROSITE; PS51336; DM10; 1.
PE 1: Evidence at protein level;
KW Alternative splicing; ATP-binding; Cell projection; Cytoplasm;
KW Cytoskeleton; Kinase; Magnesium; Metal-binding; Nucleotide metabolism;
KW Nucleotide-binding; Reference proteome; Transferase.
FT CHAIN 1..376
FT /note="Nucleoside diphosphate kinase 7"
FT /id="PRO_0000137130"
FT DOMAIN 3..91
FT /note="DM10"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00665"
FT ACT_SITE 206
FT /note="Pros-phosphohistidine intermediate"
FT /evidence="ECO:0000250"
FT BINDING 99
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 145
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 193
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT BINDING 203
FT /ligand="ATP"
FT /ligand_id="ChEBI:CHEBI:30616"
FT /evidence="ECO:0000250"
FT VAR_SEQ 1..36
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_040996"
SQ SEQUENCE 376 AA; 42492 MW; 67C121D6C36E7012 CRC64;
MNHSERFVFI AEWYDPNASL LRRYELLFYP GDGSVEMHDV KNHRTFLKRT KYDNLHLEDL
FIGNKVNVFS RQLVLIDYGD QYTARQLGSR KEKTLALIKP DAISKAGEII EIINKAGFTI
TKLKMMMLSR KEALDFHVDH QSRPFFNELI QFITTGPIIA MEILRDDAIC EWKRLLGPAN
SGVARTDASE SIRALFGTDG IRNAAHGPDS FASAAREMEL FFPSSGGCGP ANTAKFTNCT
CCIVKPHAVS EGLLGKILMA IRDAGFEISA MQMFNMDRVN VEEFYEVYKG VVTEYHDMVT
EMYSGPCVAM EIQQNNATKT FREFCGPADP EIARHLRPGT LRAIFGKTKI QNAVHCTDLP
EDGLLEVQYF FKILDN
