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Protein

Adenylate kinase 4, mitochondrial

Gene

AK4

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

Functioni

Involved in maintaining the homeostasis of cellular nucleotides by catalyzing the interconversion of nucleoside phosphates. Efficiently phosphorylates AMP and dAMP using ATP as phosphate donor, but phosphorylates only AMP when using GTP as phosphate donor. Also displays broad nucleoside diphosphate kinase activity.3 PublicationsUniRule annotation

Catalytic activityi

NTP + AMP = NDP + ADP.UniRule annotation
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

Kineticsi

  1. KM=5.3 µM for AMP with ATP as phosphate donor1 Publication
  2. KM=1.4 µM for AMP with GTP as phosphate donor1 Publication
  3. KM=507 µM for dAMP with ATP as phosphate donor1 Publication

Vmax=90 pmol/min/µg enzyme with AMP as substrate and ATP as phosphate donor1 Publication

Vmax=80 pmol/min/µg enzyme with AMP as substrate and GTP as phosphate donor1 Publication

Vmax=88 pmol/min/µg enzyme with dAMP as substrate and ATP as phosphate donor1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei36 – 361AMP
Binding sitei41 – 411AMPUniRule annotation
Binding sitei96 – 961AMPUniRule annotation
Binding sitei126 – 1261NTP
Binding sitei170 – 1701AMP
Binding sitei199 – 1991NTP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi15 – 206NTP
Nucleotide bindingi62 – 643AMP
Nucleotide bindingi89 – 924AMP
Nucleotide bindingi135 – 1362NTPUniRule annotation

GO - Molecular functioni

  1. adenylate kinase activity Source: BHF-UCL
  2. ATP binding Source: UniProtKB-KW
  3. GTP binding Source: UniProtKB-KW
  4. nucleoside diphosphate kinase activity Source: UniProtKB
  5. nucleoside triphosphate adenylate kinase activity Source: BHF-UCL

GO - Biological processi

  1. ADP biosynthetic process Source: UniProtKB-HAMAP
  2. AMP metabolic process Source: BHF-UCL
  3. ATP metabolic process Source: BHF-UCL
  4. brain development Source: Ensembl
  5. GTP metabolic process Source: BHF-UCL
  6. liver development Source: Ensembl
  7. nucleoside diphosphate phosphorylation Source: UniProtKB
  8. nucleoside triphosphate biosynthetic process Source: UniProtKB
  9. response to drug Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, GTP-binding, Nucleotide-binding

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase 4, mitochondrialUniRule annotation (EC:2.7.4.10UniRule annotation, EC:2.7.4.6UniRule annotation)
Short name:
AK 4UniRule annotation
Alternative name(s):
Adenylate kinase 3-likeUniRule annotation
GTP:AMP phosphotransferase AK4UniRule annotation
Gene namesi
Name:AK4UniRule annotation
Synonyms:AK3, AK3L1UniRule annotation
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:363. AK4.

Subcellular locationi

Mitochondrion matrix 2 PublicationsUniRule annotation

GO - Cellular componenti

  1. extracellular vesicular exosome Source: UniProtKB
  2. mitochondrial matrix Source: BHF-UCL
  3. mitochondrion Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi4 – 41K → G: Abolishes mitochondrial import; when associated with G-7. 1 Publication
Mutagenesisi7 – 71R → G: Abolishes mitochondrial import; when associated with G-4. 1 Publication

Organism-specific databases

PharmGKBiPA165750325.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 223223Adenylate kinase 4, mitochondrialPRO_0000158926Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei60 – 601N6-succinyllysineBy similarity
Modified residuei175 – 1751N6-acetyllysineBy similarity
Modified residuei179 – 1791N6-acetyllysine; alternateBy similarity
Modified residuei179 – 1791N6-succinyllysine; alternateBy similarity
Modified residuei186 – 1861N6-acetyllysine; alternateBy similarity
Modified residuei186 – 1861N6-succinyllysine; alternateBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiP27144.
PaxDbiP27144.
PRIDEiP27144.

2D gel databases

UCD-2DPAGEP27144.

PTM databases

PhosphoSiteiP27144.

Expressioni

Tissue specificityi

Highly expressed in kidney, moderately expressed in heart and liver and weakly expressed in brain.1 Publication

Gene expression databases

BgeeiP27144.
CleanExiHS_AK3.
HS_AK3L1.
ExpressionAtlasiP27144. baseline and differential.
GenevestigatoriP27144.

Organism-specific databases

HPAiHPA042753.
HPA049461.

Interactioni

Subunit structurei

Monomer.1 PublicationUniRule annotation

Protein-protein interaction databases

BioGridi106708. 11 interactions.
IntActiP27144. 3 interactions.

Structurei

Secondary structure

1
223
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi7 – 115Combined sources
Helixi18 – 2912Combined sources
Beta strandi32 – 343Combined sources
Helixi36 – 4510Combined sources
Helixi49 – 5911Combined sources
Helixi66 – 7813Combined sources
Turni79 – 824Combined sources
Beta strandi85 – 895Combined sources
Helixi94 – 1018Combined sources
Beta strandi108 – 1136Combined sources
Helixi116 – 1249Combined sources
Beta strandi126 – 1294Combined sources
Turni130 – 1334Combined sources
Beta strandi134 – 1374Combined sources
Turni138 – 1403Combined sources
Turni150 – 1523Combined sources
Helixi160 – 1623Combined sources
Helixi164 – 18724Combined sources
Beta strandi191 – 1955Combined sources
Helixi199 – 21113Combined sources
Helixi217 – 2193Combined sources
Helixi220 – 2223Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AR7X-ray2.15A/B1-223[»]
2BBWX-ray2.05A/B1-223[»]
3NDPX-ray2.30A/B1-223[»]
ProteinModelPortaliP27144.
SMRiP27144. Positions 4-223.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP27144.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni35 – 6430NMPbindAdd
BLAST
Regioni125 – 16238LIDAdd
BLAST

Domaini

Consists of three domains, a large central CORE domain and two small peripheral domains, NMPbind and LID, which undergo movements during catalysis. The LID domain closes over the site of phosphoryl transfer upon GTP/ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP/ATP hydrolysis.

Sequence similaritiesi

Belongs to the adenylate kinase family. AK3 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0563.
GeneTreeiENSGT00550000074679.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP27144.
KOiK00939.
OMAiIWPYINS.
PhylomeDBiP27144.
TreeFamiTF312916.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
MF_03170. Adenylate_kinase_AK4.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/Ak4_mitochondrial.
IPR028585. AK4_mitochondrial.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF57774. SSF57774. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

P27144-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MASKLLRAVI LGPPGSGKGT VCQRIAQNFG LQHLSSGHFL RENIKASTEV
60 70 80 90 100
GEMAKQYIEK SLLVPDHVIT RLMMSELENR RGQHWLLDGF PRTLGQAEAL
110 120 130 140 150
DKICEVDLVI SLNIPFETLK DRLSRRWIHP PSGRVYNLDF NPPHVHGIDD
160 170 180 190 200
VTGEPLVQQE DDKPEAVAAR LRQYKDVAKP VIELYKSRGV LHQFSGTETN
210 220
KIWPYVYTLF SNKITPIQSK EAY
Length:223
Mass (Da):25,268
Last modified:August 1, 1992 - v1
Checksum:i653341A8EB3BC723
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti22 – 221C → S in AAH40224 (PubMed:15489334).Curated
Sequence conflicti22 – 221C → S in AAI46654 (PubMed:15489334).Curated
Sequence conflicti23 – 231Q → R in AAH66944 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60673 mRNA. Translation: CAA43088.1.
CR456830 mRNA. Translation: CAG33111.1.
AK313611 mRNA. Translation: BAG36374.1.
AL356212, AC099680 Genomic DNA. Translation: CAI22412.1.
CH471059 Genomic DNA. Translation: EAX06538.1.
CH471059 Genomic DNA. Translation: EAX06540.1.
CH471059 Genomic DNA. Translation: EAX06544.1.
BC016180 mRNA. Translation: AAH16180.1.
BC040224 mRNA. Translation: AAH40224.1.
BC066944 mRNA. Translation: AAH66944.1.
BC136886 mRNA. Translation: AAI36887.1.
BC136887 mRNA. Translation: AAI36888.1.
BC148270 mRNA. Translation: AAI48271.1.
BC146653 mRNA. Translation: AAI46654.1.
CCDSiCCDS629.1.
PIRiA42820. KIHUA3.
RefSeqiNP_001005353.1. NM_001005353.2.
NP_037542.1. NM_013410.3.
NP_982289.1. NM_203464.2.
XP_003119578.1. XM_003119530.3.
UniGeneiHs.10862.

Genome annotation databases

EnsembliENST00000327299; ENSP00000322175; ENSG00000162433.
ENST00000395334; ENSP00000378743; ENSG00000162433.
ENST00000545314; ENSP00000445912; ENSG00000162433.
GeneIDi100507855.
205.
KEGGihsa:100507855.
hsa:205.
UCSCiuc001dby.3. human.

Polymorphism databases

DMDMi125157.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
X60673 mRNA. Translation: CAA43088.1.
CR456830 mRNA. Translation: CAG33111.1.
AK313611 mRNA. Translation: BAG36374.1.
AL356212, AC099680 Genomic DNA. Translation: CAI22412.1.
CH471059 Genomic DNA. Translation: EAX06538.1.
CH471059 Genomic DNA. Translation: EAX06540.1.
CH471059 Genomic DNA. Translation: EAX06544.1.
BC016180 mRNA. Translation: AAH16180.1.
BC040224 mRNA. Translation: AAH40224.1.
BC066944 mRNA. Translation: AAH66944.1.
BC136886 mRNA. Translation: AAI36887.1.
BC136887 mRNA. Translation: AAI36888.1.
BC148270 mRNA. Translation: AAI48271.1.
BC146653 mRNA. Translation: AAI46654.1.
CCDSiCCDS629.1.
PIRiA42820. KIHUA3.
RefSeqiNP_001005353.1. NM_001005353.2.
NP_037542.1. NM_013410.3.
NP_982289.1. NM_203464.2.
XP_003119578.1. XM_003119530.3.
UniGeneiHs.10862.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2AR7X-ray2.15A/B1-223[»]
2BBWX-ray2.05A/B1-223[»]
3NDPX-ray2.30A/B1-223[»]
ProteinModelPortaliP27144.
SMRiP27144. Positions 4-223.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106708. 11 interactions.
IntActiP27144. 3 interactions.

Chemistry

BindingDBiP27144.
ChEMBLiCHEMBL4926.
DrugBankiDB00718. Adefovir Dipivoxil.
DB00300. Tenofovir.

PTM databases

PhosphoSiteiP27144.

Polymorphism databases

DMDMi125157.

2D gel databases

UCD-2DPAGEP27144.

Proteomic databases

MaxQBiP27144.
PaxDbiP27144.
PRIDEiP27144.

Protocols and materials databases

DNASUi205.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000327299; ENSP00000322175; ENSG00000162433.
ENST00000395334; ENSP00000378743; ENSG00000162433.
ENST00000545314; ENSP00000445912; ENSG00000162433.
GeneIDi100507855.
205.
KEGGihsa:100507855.
hsa:205.
UCSCiuc001dby.3. human.

Organism-specific databases

CTDi205.
GeneCardsiGC01P065614.
HGNCiHGNC:363. AK4.
HPAiHPA042753.
HPA049461.
MIMi103030. gene.
neXtProtiNX_P27144.
PharmGKBiPA165750325.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0563.
GeneTreeiENSGT00550000074679.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiP27144.
KOiK00939.
OMAiIWPYINS.
PhylomeDBiP27144.
TreeFamiTF312916.

Miscellaneous databases

EvolutionaryTraceiP27144.
GeneWikiiAK3L1.
NextBioi818.
PROiP27144.
SOURCEiSearch...

Gene expression databases

BgeeiP27144.
CleanExiHS_AK3.
HS_AK3L1.
ExpressionAtlasiP27144. baseline and differential.
GenevestigatoriP27144.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
MF_03170. Adenylate_kinase_AK4.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/Ak4_mitochondrial.
IPR028585. AK4_mitochondrial.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 2 hits.
SSF57774. SSF57774. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene."
    Xu G., O'Connell P., Stevens J., White R.
    Genomics 13:537-542(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)."
    Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.
    Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
  3. "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.
    , 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].
    Tissue: Testis.
  4. "The DNA sequence and biological annotation of human chromosome 1."
    Gregory S.G., Barlow K.F., McLay K.E., Kaul R., Swarbreck D., Dunham A., Scott C.E., Howe K.L., Woodfine K., Spencer C.C.A., Jones M.C., Gillson C., Searle S., Zhou Y., Kokocinski F., McDonald L., Evans R., Phillips K.
    , Atkinson A., Cooper R., Jones C., Hall R.E., Andrews T.D., Lloyd C., Ainscough R., Almeida J.P., Ambrose K.D., Anderson F., Andrew R.W., Ashwell R.I.S., Aubin K., Babbage A.K., Bagguley C.L., Bailey J., Beasley H., Bethel G., Bird C.P., Bray-Allen S., Brown J.Y., Brown A.J., Buckley D., Burton J., Bye J., Carder C., Chapman J.C., Clark S.Y., Clarke G., Clee C., Cobley V., Collier R.E., Corby N., Coville G.J., Davies J., Deadman R., Dunn M., Earthrowl M., Ellington A.G., Errington H., Frankish A., Frankland J., French L., Garner P., Garnett J., Gay L., Ghori M.R.J., Gibson R., Gilby L.M., Gillett W., Glithero R.J., Grafham D.V., Griffiths C., Griffiths-Jones S., Grocock R., Hammond S., Harrison E.S.I., Hart E., Haugen E., Heath P.D., Holmes S., Holt K., Howden P.J., Hunt A.R., Hunt S.E., Hunter G., Isherwood J., James R., Johnson C., Johnson D., Joy A., Kay M., Kershaw J.K., Kibukawa M., Kimberley A.M., King A., Knights A.J., Lad H., Laird G., Lawlor S., Leongamornlert D.A., Lloyd D.M., Loveland J., Lovell J., Lush M.J., Lyne R., Martin S., Mashreghi-Mohammadi M., Matthews L., Matthews N.S.W., McLaren S., Milne S., Mistry S., Moore M.J.F., Nickerson T., O'Dell C.N., Oliver K., Palmeiri A., Palmer S.A., Parker A., Patel D., Pearce A.V., Peck A.I., Pelan S., Phelps K., Phillimore B.J., Plumb R., Rajan J., Raymond C., Rouse G., Saenphimmachak C., Sehra H.K., Sheridan E., Shownkeen R., Sims S., Skuce C.D., Smith M., Steward C., Subramanian S., Sycamore N., Tracey A., Tromans A., Van Helmond Z., Wall M., Wallis J.M., White S., Whitehead S.L., Wilkinson J.E., Willey D.L., Williams H., Wilming L., Wray P.W., Wu Z., Coulson A., Vaudin M., Sulston J.E., Durbin R.M., Hubbard T., Wooster R., Dunham I., Carter N.P., McVean G., Ross M.T., Harrow J., Olson M.V., Beck S., Rogers J., Bentley D.R.
    Nature 441:315-321(2006) [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].
    Tissue: Brain, Colon and Lung.
  7. "Structure and expression of human mitochondrial adenylate kinase targeted to the mitochondrial matrix."
    Noma T., Fujisawa K., Yamashiro Y., Shinohara M., Nakazawa A., Gondo T., Ishihara T., Yoshinobu K.
    Biochem. J. 358:225-232(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
  8. "Evidence of an intact N-terminal translocation sequence of human mitochondrial adenylate kinase 4."
    Panayiotou C., Solaroli N., Johansson M., Karlsson A.
    Int. J. Biochem. Cell Biol. 42:62-69(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, CATALYTIC ACTIVITY, SUBCELLULAR LOCATION, BIOPHYSICOCHEMICAL PROPERTIES, MUTAGENESIS OF LYS-4 AND ARG-7.
  9. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  10. "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.
  11. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  12. "Crystal structure of human adenylate kinase 4 (AK4) in complex with diguanosine pentaphosphate."
    Structural genomics consortium (SGC)
    Submitted (DEC-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS) IN COMPLEX WITH DIGUANOSINE PENTAPHOSPHATE.
  13. "Crystal structure of human adenylate kinase 4 (L171P) suggests the role of hinge region in protein domain motion."
    Liu R., Xu H., Wei Z., Wang Y., Lin Y., Gong W.
    Biochem. Biophys. Res. Commun. 379:92-97(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS), FUNCTION.

Entry informationi

Entry nameiKAD4_HUMAN
AccessioniPrimary (citable) accession number: P27144
Secondary accession number(s): B2R927
, D3DQ62, Q6IBH4, Q6NXQ5, Q8IUU9
Entry historyi
Integrated into UniProtKB/Swiss-Prot: August 1, 1992
Last sequence update: August 1, 1992
Last modified: March 4, 2015
This is version 152 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

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  3. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  4. SIMILARITY comments
    Index of protein domains and families

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.