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Protein

Adenylate kinase isoenzyme 6

Gene

AK6

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Broad-specificity nucleoside monophosphate (NMP) kinase that catalyzes the reversible transfer of the terminal phosphate group between nucleoside triphosphates and monophosphates. AMP and dAMP are the preferred substrates, but CMP and dCMP are also good substrates. IMP is phosphorylated to a much lesser extent. All nucleoside triphosphates ATP, GTP, UTP, CTP, dATP, dCTP, dGTP, and TTP are accepted as phosphate donors. CTP is the best phosphate donor, followed by UTP, ATP, GTP and dCTP. May have a role in nuclear energy homeostasis. Has also ATPase activity. May be involved in regulation of Cajal body (CB) formation.1 Publication

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation1 Publication

Kineticsi

kcat is 6.3 sec(-1) for adenylate kinase activity. kcat is 4.8 sec(-1) for ATPase activity.

  1. KM=192 µM for AMP3 Publications
  2. KM=45 µM for ATP (for adenylate kinase activity)3 Publications
  3. KM=332 µM for ATP (for ATPase activity)3 Publications
  1. Vmax=1.27 µmol/min/mg enzyme for ATPase activity3 Publications
  2. Vmax=982 nmol/min/mg enzyme for the forward adenylate kinase reaction3 Publications
  3. Vmax=955 nmol/min/mg enzyme for the reverse adenylate kinase reaction3 Publications

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391AMPCurated
Binding sitei79 – 791ATP
Binding sitei105 – 1051ATP
Binding sitei109 – 1091ATP

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi13 – 186ATP
Nucleotide bindingi148 – 1492ATP

GO - Molecular functioni

  • adenylate kinase activity Source: UniProtKB
  • ATPase activity Source: UniProtKB-HAMAP
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

  • nucleotide phosphorylation Source: GOC
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.4.3. 2681.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase isoenzyme 6UniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AK6UniRule annotation
Alternative name(s):
Adrenal gland protein AD-004
Coilin-interacting nuclear ATPase proteinUniRule annotation
Short name:
hCINAP
Dual activity adenylate kinase/ATPaseUniRule annotation
Short name:
AK/ATPaseUniRule annotation
Gene namesi
Name:AK6UniRule annotation
Synonyms:CINAPUniRule annotation
ORF Names:AD-004, CGI-137
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Unplaced

Organism-specific databases

HGNCiHGNC:49151. AK6.

Subcellular locationi

  • Nucleusnucleoplasm
  • NucleusCajal body

  • Note: Displays widespread diffuse nucleoplasmic distribution but not detected in nucleoli. Detected in Cajal bodies but not in all cells.

GO - Cellular componenti

  • Cajal body Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleoplasm Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi79 – 791H → G: Induces homodimerization. Reduces adenylate kinase activity by 72% and ATPase activity by 76%. Significantly changes Cajal body organization in the nucleus, resulting in enhanced apoptosis and reduced proliferation. 1 Publication

Organism-specific databases

PharmGKBiPA36317.

Polymorphism and mutation databases

BioMutaiCCDC125.
DMDMi6831735.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 172172Adenylate kinase isoenzyme 6PRO_0000153896Add
BLAST

Proteomic databases

MaxQBiQ9Y3D8.
PaxDbiQ9Y3D8.
PeptideAtlasiQ9Y3D8.
PRIDEiQ9Y3D8.

Expressioni

Tissue specificityi

Expressed in heart, brain, placenta, lung, liver, skeletal muscle, kidney, pancreas, chorionic villi and the central nervous system.1 Publication

Gene expression databases

BgeeiQ9Y3D8.
ExpressionAtlasiQ9Y3D8. baseline and differential.
GenevisibleiQ9Y3D8. HS.

Organism-specific databases

HPAiCAB005361.

Interactioni

Subunit structurei

Monomer and homodimer (By similarity). Interacts with COIL (via C-terminus).UniRule annotation3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
COILP384325EBI-2896123,EBI-945751
NDRG1Q92597-33EBI-2896123,EBI-10278703
RPS14P622633EBI-2896123,EBI-352783

Protein-protein interaction databases

IntActiQ9Y3D8. 6 interactions.
MINTiMINT-1389230.

Structurei

Secondary structure

1
172
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi6 – 94Combined sources
Helixi16 – 2712Combined sources
Beta strandi30 – 334Combined sources
Helixi34 – 418Combined sources
Beta strandi44 – 485Combined sources
Turni49 – 524Combined sources
Beta strandi53 – 564Combined sources
Helixi58 – 7114Combined sources
Beta strandi74 – 774Combined sources
Helixi86 – 883Combined sources
Beta strandi90 – 967Combined sources
Helixi99 – 10810Combined sources
Helixi113 – 12412Combined sources
Helixi127 – 1359Combined sources
Helixi138 – 1403Combined sources
Beta strandi141 – 1455Combined sources
Helixi149 – 16921Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RKBX-ray2.00A1-172[»]
3IIJX-ray1.76A1-172[»]
3IIKX-ray1.95A1-172[»]
3IILX-ray2.00A1-172[»]
3IIMX-ray2.00A1-172[»]
ProteinModelPortaliQ9Y3D8.
SMRiQ9Y3D8. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9Y3D8.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni33 – 5624NMPbindAdd
BLAST
Regioni108 – 11811LIDAdd
BLAST

Sequence similaritiesi

Belongs to the adenylate kinase family. AK6 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG1936.
GeneTreeiENSGT00390000015930.
HOGENOMiHOG000224472.
HOVERGENiHBG052207.
KOiK18532.
OMAiDNVQCEI.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00039. Adenylate_kinase_AK6.
InterProiIPR020618. Adenyl_kinase_AK6.
IPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9Y3D8-1) [UniParc]FASTAAdd to basket

Also known as: AK6

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MLLPNILLTG TPGVGKTTLG KELASKSGLK YINVGDLARE EQLYDGYDEE
60 70 80 90 100
YDCPILDEDR VVDELDNQMR EGGVIVDYHG CDFFPERWFH IVFVLRTDTN
110 120 130 140 150
VLYERLETRG YNEKKLTDNI QCEIFQVLYE EATASYKEEI VHQLPSNKPE
160 170
ELENNVDQIL KWIEQWIKDH NS
Length:172
Mass (Da):20,061
Last modified:November 1, 1999 - v1
Checksum:i33F62318FB434301
GO
Isoform 2 (identifier: Q9Y3D8-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     2-9: LLPNILLT → CHRKP

Note: Gene prediction based on EST data.
Show »
Length:169
Mass (Da):19,805
Checksum:i3F341AE6C5898C66
GO

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei2 – 98LLPNILLT → CHRKP in isoform 2. CuratedVSP_039714

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ878880 mRNA. Translation: CAI48030.1.
AJ878881 mRNA. Translation: CAI48031.1.
AF151895 mRNA. Translation: AAD34132.1.
AF110777 mRNA. Translation: AAF14860.1.
AC145132 Genomic DNA. No translation available.
CH471137 Genomic DNA. Translation: EAW51290.1.
CH471137 Genomic DNA. Translation: EAW51291.1.
CH471137 Genomic DNA. Translation: EAW51292.1.
CH471137 Genomic DNA. Translation: EAW51297.1.
BC007349 mRNA. Translation: AAH07349.1.
BC007426 mRNA. Translation: AAH07426.1.
CCDSiCCDS4001.1. [Q9Y3D8-1]
CCDS43324.1. [Q9Y3D8-2]
RefSeqiNP_001015891.1. NM_001015891.1. [Q9Y3D8-2]
NP_057367.1. NM_016283.4. [Q9Y3D8-1]
UniGeneiHs.653163.

Genome annotation databases

GeneIDi102157402.
KEGGihsa:102157402.
UCSCiuc003jwa.3. human. [Q9Y3D8-1]
uc003jwb.3. human. [Q9Y3D8-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AJ878880 mRNA. Translation: CAI48030.1.
AJ878881 mRNA. Translation: CAI48031.1.
AF151895 mRNA. Translation: AAD34132.1.
AF110777 mRNA. Translation: AAF14860.1.
AC145132 Genomic DNA. No translation available.
CH471137 Genomic DNA. Translation: EAW51290.1.
CH471137 Genomic DNA. Translation: EAW51291.1.
CH471137 Genomic DNA. Translation: EAW51292.1.
CH471137 Genomic DNA. Translation: EAW51297.1.
BC007349 mRNA. Translation: AAH07349.1.
BC007426 mRNA. Translation: AAH07426.1.
CCDSiCCDS4001.1. [Q9Y3D8-1]
CCDS43324.1. [Q9Y3D8-2]
RefSeqiNP_001015891.1. NM_001015891.1. [Q9Y3D8-2]
NP_057367.1. NM_016283.4. [Q9Y3D8-1]
UniGeneiHs.653163.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1RKBX-ray2.00A1-172[»]
3IIJX-ray1.76A1-172[»]
3IIKX-ray1.95A1-172[»]
3IILX-ray2.00A1-172[»]
3IIMX-ray2.00A1-172[»]
ProteinModelPortaliQ9Y3D8.
SMRiQ9Y3D8. Positions 1-172.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

IntActiQ9Y3D8. 6 interactions.
MINTiMINT-1389230.

Polymorphism and mutation databases

BioMutaiCCDC125.
DMDMi6831735.

Proteomic databases

MaxQBiQ9Y3D8.
PaxDbiQ9Y3D8.
PeptideAtlasiQ9Y3D8.
PRIDEiQ9Y3D8.

Protocols and materials databases

DNASUi6880.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

GeneIDi102157402.
KEGGihsa:102157402.
UCSCiuc003jwa.3. human. [Q9Y3D8-1]
uc003jwb.3. human. [Q9Y3D8-2]

Organism-specific databases

CTDi102157402.
GeneCardsiGC05M068647.
HGNCiHGNC:49151. AK6.
HPAiCAB005361.
neXtProtiNX_Q9Y3D8.
PharmGKBiPA36317.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG1936.
GeneTreeiENSGT00390000015930.
HOGENOMiHOG000224472.
HOVERGENiHBG052207.
KOiK18532.
OMAiDNVQCEI.

Enzyme and pathway databases

BRENDAi2.7.4.3. 2681.

Miscellaneous databases

EvolutionaryTraceiQ9Y3D8.
GenomeRNAii102157402.
NextBioi26873.
PROiQ9Y3D8.

Gene expression databases

BgeeiQ9Y3D8.
ExpressionAtlasiQ9Y3D8. baseline and differential.
GenevisibleiQ9Y3D8. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00039. Adenylate_kinase_AK6.
InterProiIPR020618. Adenyl_kinase_AK6.
IPR027417. P-loop_NTPase.
[Graphical view]
SUPFAMiSSF52540. SSF52540. 1 hit.
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of hCINAP, a novel coilin-interacting protein encoded by a transcript from the transcription factor TAFIID32 locus."
    Santama N., Ogg S.C., Malekkou A., Zographos S.E., Weis K., Lamond A.I.
    J. Biol. Chem. 280:36429-36441(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), BIOPHYSICOCHEMICAL PROPERTIES, INTERACTION WITH COIL, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, ALTERNATIVE SPLICING.
    Tissue: Cervix carcinoma and Placenta.
  2. "Identification of novel human genes evolutionarily conserved in Caenorhabditis elegans by comparative proteomics."
    Lai C.-H., Chou C.-Y., Ch'ang L.-Y., Liu C.-S., Lin W.-C.
    Genome Res. 10:703-713(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Adrenal gland.
  4. "The DNA sequence and comparative analysis of human chromosome 5."
    Schmutz J., Martin J., Terry A., Couronne O., Grimwood J., Lowry S., Gordon L.A., Scott D., Xie G., Huang W., Hellsten U., Tran-Gyamfi M., She X., Prabhakar S., Aerts A., Altherr M., Bajorek E., Black S.
    , Branscomb E., Caoile C., Challacombe J.F., Chan Y.M., Denys M., Detter J.C., Escobar J., Flowers D., Fotopulos D., Glavina T., Gomez M., Gonzales E., Goodstein D., Grigoriev I., Groza M., Hammon N., Hawkins T., Haydu L., Israni S., Jett J., Kadner K., Kimball H., Kobayashi A., Lopez F., Lou Y., Martinez D., Medina C., Morgan J., Nandkeshwar R., Noonan J.P., Pitluck S., Pollard M., Predki P., Priest J., Ramirez L., Retterer J., Rodriguez A., Rogers S., Salamov A., Salazar A., Thayer N., Tice H., Tsai M., Ustaszewska A., Vo N., Wheeler J., Wu K., Yang J., Dickson M., Cheng J.-F., Eichler E.E., Olsen A., Pennacchio L.A., Rokhsar D.S., Richardson P., Lucas S.M., Myers R.M., Rubin E.M.
    Nature 431:268-274(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
    The MGC Project Team
    Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Tissue: Lymph.
  7. "Protein preparation, crystallization and preliminary X-ray analysis of human adrenal gland protein AD-004."
    Ren H., Liang Y., Li R., Ding H., Qiu S., Lu S., An J., Li L., Luo M., Zheng X., Su X.D.
    Acta Crystallogr. D 60:1292-1294(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUBUNIT.
  8. "The crystal structure of human adenylate kinase 6: an adenylate kinase localized to the cell nucleus."
    Ren H., Wang L., Bennett M., Liang Y., Zheng X., Lu F., Li L., Nan J., Luo M., Eriksson S., Zhang C., Su X.-D.
    Proc. Natl. Acad. Sci. U.S.A. 102:303-308(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS), FUNCTION, CATALYTIC ACTIVITY, BIOPHYSICOCHEMICAL PROPERTIES, SUBCELLULAR LOCATION.
  9. "hCINAP is an atypical mammalian nuclear adenylate kinase with an ATPase motif: structural and functional studies."
    Drakou C.E., Malekkou A., Hayes J.M., Lederer C.W., Leonidas D.D., Oikonomakos N.G., Lamond A.I., Santama N., Zographos S.E.
    Proteins 80:206-220(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.76 ANGSTROMS) IN COMPLEX WITH ADP AND DADP, MUTAGENESIS OF HIS-79, BIOPHYSICOCHEMICAL PROPERTIES.

Entry informationi

Entry nameiKAD6_HUMAN
AccessioniPrimary (citable) accession number: Q9Y3D8
Secondary accession number(s): A8MSZ6, Q5F2S9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 30, 2000
Last sequence update: November 1, 1999
Last modified: June 24, 2015
This is version 138 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (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.

Miscellaneousi

Caution

AK6 and TAF9 were initially considered as products of the same gene since they share two exons. However, they are translated from different initiation codons and reading frames and encode unrelated proteins. This arrangement is conserved in some mammalian species.Curated

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 5
    Human chromosome 5: entries, gene names and cross-references to MIM
  2. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  3. SIMILARITY comments
    Index of protein domains and families
  4. Uncharacterized protein families (UPF)
    List of uncharacterized protein family (UPF) entries

External Data

Dasty 3

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into Uniref entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.