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Q96M32 (KAD7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 108. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Adenylate kinase 7

Short name=AK 7
EC=2.7.4.3
EC=2.7.4.6
Alternative name(s):
ATP-AMP transphosphorylase 7
Gene names
Name:AK7
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length723 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

Nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. Has highest activity toward AMP, and weaker activity toward dAMP, CMP and dCMP. Also displays broad nucleoside diphosphate kinase activity. Involved in maintaining ciliary structure and function. Ref.3 Ref.4

Catalytic activity

ATP + AMP = 2 ADP. Ref.3 Ref.4

ATP + nucleoside diphosphate = ADP + nucleoside triphosphate. Ref.3 Ref.4

Subcellular location

Cytoplasmcytosol Ref.3.

Sequence similarities

In the central section; belongs to the adenylate kinase family.

In the C-terminal section; belongs to the dpy-30 family.

Biophysicochemical properties

Kinetic parameters:

KM=1.0 µM for AMP Ref.3

KM=28 µM for dAMP

KM=1.2 µM for CMP

Vmax=1130 pmol/min/µg enzyme with AMP as substrate

Vmax=860 pmol/min/µg enzyme with dAMP as substrate

Vmax=150 pmol/min/µg enzyme with CMP as substrate

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 723723Adenylate kinase 7
PRO_0000158952

Regions

Nucleotide binding377 – 3826ATP By similarity
Nucleotide binding432 – 45524AMP By similarity
Nucleotide binding482 – 4854AMP By similarity
Region367 – 612246Adenylate kinase
Region397 – 45559NMPbind By similarity
Region537 – 54711LID By similarity
Region679 – 72345DPY-30
Coiled coil46 – 458413 Potential
Coiled coil609 – 67769 Potential
Compositional bias3 – 64Poly-Glu
Compositional bias51 – 588Poly-Glu
Compositional bias420 – 43213Poly-Glu
Compositional bias497 – 5026Poly-Glu
Compositional bias616 – 67459Glu-rich

Sites

Binding site4891AMP By similarity
Binding site5551AMP By similarity
Binding site5871ATP; via carbonyl oxygen By similarity

Natural variations

Natural variant1021R → Q. Ref.1
Corresponds to variant rs2275554 [ dbSNP | Ensembl ].
VAR_017059
Natural variant3891N → K. Ref.1
Corresponds to variant rs2369679 [ dbSNP | Ensembl ].
VAR_057950

Experimental info

Sequence conflict2721P → L in BAB71480. Ref.1
Sequence conflict4101E → G in BAB71480. Ref.1

Sequences

Sequence LengthMass (Da)Tools
Q96M32 [UniParc].

Last modified November 24, 2009. Version 3.
Checksum: 7A9E2BF11A4CEEF8

FASTA72382,658
        10         20         30         40         50         60 
MAEEEETAAL TEKVIRTQRV FINLLDSYSS GNIGKFLSNC VVGASLEEIT EEEEEEDENK 

        70         80         90        100        110        120 
SAMLEASSTK VKEGTFQIVG TLSKPDSPRP DFAVETYSAI SREDLLMRLL ECDVIIYNIT 

       130        140        150        160        170        180 
ESSQQMEEAI WAVSALSEEV SHFEKRKLFI LLSTVMTWAR SKALDPEDSE VPFTEEDYRR 

       190        200        210        220        230        240 
RKSHPNFLDH INAEKMVLKF GKKARKFAAY VVAAGLQYGA EGGMLHTFFK MAWLGEIPAL 

       250        260        270        280        290        300 
PVFGDGTNVI PTIHVLDLAG VIQNVIDHVP KPHYLVAVDE SVHTLEDIVK CISKNTGPGK 

       310        320        330        340        350        360 
IQKIPRENAY LTKDLTQDCL DHLLVNLRME ALFVKENFNI RWAAQTGFVE NINTILKEYK 

       370        380        390        400        410        420 
QSRGLMPIKI CILGPPAVGK SSIAKELANY YKLHHIQLKD VISEAIAKLE AIVAPNDVGE 

       430        440        450        460        470        480 
GEEEVEEEEE EENVEDAQEL LDGIKESMEQ NAGQLDDQYI IRFMKEKLKS MPCRNQGYIL 

       490        500        510        520        530        540 
DGFPKTYDQA KDLFNQEDEE EEDDVRGRMF PFDKLIIPEF VCALDASDEF LKERVINLPE 

       550        560        570        580        590        600 
SIVAGTHYSQ DRFLRALSNY RDINIDDETV FNYFDELEIH PIHIDVGKLE DAQNRLAIKQ 

       610        620        630        640        650        660 
LIKEIGEPRN YGLTDEEKAE EERKAAEERL AREAAEEAER EHQEAVEMAE KIARWEEWNK 

       670        680        690        700        710        720 
RLEEVKREER ELLEAQSIPL RNYLMTYVMP TLIQGLNECC NVRPEDPVDF LAEYLFKNNP 


EAQ 

« Hide

References

« Hide 'large scale' references
[1]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANTS GLN-102 AND LYS-389.
Tissue: Testis.
[2]"The DNA sequence and analysis of human chromosome 14."
Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C., Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A., Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H., Du H. expand/collapse author list , Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T., Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B., Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D., Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R., Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S., Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C., Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S., Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C., Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P., Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M., Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V., Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J., Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F., Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F., Waterston R., Hood L., Weissenbach J.
Nature 421:601-607(2003) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]"The characterization of human adenylate kinases 7 and 8 demonstrates differences in kinetic parameters and structural organization among the family of adenylate kinase isoenzymes."
Panayiotou C., Solaroli N., Xu Y., Johansson M., Karlsson A.
Biochem. J. 433:527-534(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, CATALYTIC ACTIVITY.
[4]"The human adenylate kinase 9 is a nucleoside mono- and diphosphate kinase."
Amiri M., Conserva F., Panayiotou C., Karlsson A., Solaroli N.
Int. J. Biochem. Cell Biol. 45:925-931(2013) [PubMed] [Europe PMC] [Abstract]
Cited for: FUNCTION, CATALYTIC ACTIVITY.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
AK057426 mRNA. Translation: BAB71480.1.
AL163051 Genomic DNA. No translation available.
AL359240 Genomic DNA. No translation available.
RefSeqNP_689540.2. NM_152327.3.
UniGeneHs.667462.

3D structure databases

ProteinModelPortalQ96M32.
SMRQ96M32. Positions 368-517, 673-723.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid125773. 1 interaction.
STRING9606.ENSP00000267584.

PTM databases

PhosphoSiteQ96M32.

Polymorphism databases

DMDM269849674.

Proteomic databases

PaxDbQ96M32.
PRIDEQ96M32.

Protocols and materials databases

DNASU122481.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000267584; ENSP00000267584; ENSG00000140057.
GeneID122481.
KEGGhsa:122481.
UCSCuc001yfn.3. human.

Organism-specific databases

CTD122481.
GeneCardsGC14P096858.
H-InvDBHIX0011951.
HGNCHGNC:20091. AK7.
HPAHPA003543.
MIM615364. gene.
neXtProtNX_Q96M32.
PharmGKBPA134963502.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG267062.
HOGENOMHOG000007764.
HOVERGENHBG045568.
InParanoidQ96M32.
KOK00939.
OMAKMAWLGE.
OrthoDBEOG786H2R.
PhylomeDBQ96M32.
TreeFamTF313982.

Gene expression databases

ArrayExpressQ96M32.
BgeeQ96M32.
CleanExHS_AK7.
GenevestigatorQ96M32.

Family and domain databases

Gene3D3.40.50.300. 1 hit.
3.40.50.720. 1 hit.
InterProIPR000850. Adenylat/UMP-CMP_kin.
IPR007858. Dpy-30_motif.
IPR016040. NAD(P)-bd_dom.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERPTHR23359. PTHR23359. 1 hit.
PfamPF05186. Dpy-30. 1 hit.
[Graphical view]
SUPFAMSSF52540. SSF52540. 1 hit.
ProtoNetSearch...

Other

ChiTaRSAK7. human.
GenomeRNAi122481.
NextBio80898.
PROQ96M32.
SOURCESearch...

Entry information

Entry nameKAD7_HUMAN
AccessionPrimary (citable) accession number: Q96M32
Secondary accession number(s): Q8IYP6
Entry history
Integrated into UniProtKB/Swiss-Prot: October 3, 2003
Last sequence update: November 24, 2009
Last modified: April 16, 2014
This is version 108 of the entry and version 3 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Relevant documents

SIMILARITY comments

Index of protein domains and families

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 14

Human chromosome 14: entries, gene names and cross-references to MIM