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P27144

- KAD4_HUMAN

UniProt

P27144 - KAD4_HUMAN

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Protein

Adenylate kinase 4, mitochondrial

Gene

AK4

Organism
Homo sapiens (Human)
Status
Reviewed - 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: UniProt
  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 – 115
Helixi18 – 2912
Beta strandi32 – 343
Helixi36 – 4510
Helixi49 – 5911
Helixi66 – 7813
Turni79 – 824
Beta strandi85 – 895
Helixi94 – 1018
Beta strandi108 – 1136
Helixi116 – 1249
Beta strandi126 – 1294
Turni130 – 1334
Beta strandi134 – 1374
Turni138 – 1403
Turni150 – 1523
Helixi160 – 1623
Helixi164 – 18724
Beta strandi191 – 1955
Helixi199 – 21113
Helixi217 – 2193
Helixi220 – 2223

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
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.
OMAiGDVAKQY.
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:
EMBL
GenBank
DDBJ
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:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS629.1.
PIRi A42820. KIHUA3.
RefSeqi NP_001005353.1. NM_001005353.2.
NP_037542.1. NM_013410.3.
NP_982289.1. NM_203464.2.
XP_003119578.1. XM_003119530.3.
UniGenei Hs.10862.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2AR7 X-ray 2.15 A/B 1-223 [» ]
2BBW X-ray 2.05 A/B 1-223 [» ]
3NDP X-ray 2.30 A/B 1-223 [» ]
ProteinModelPortali P27144.
SMRi P27144. Positions 4-223.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 106708. 11 interactions.
IntActi P27144. 3 interactions.

Chemistry

BindingDBi P27144.
ChEMBLi CHEMBL4926.
DrugBanki DB00718. Adefovir Dipivoxil.
DB00300. Tenofovir.

PTM databases

PhosphoSitei P27144.

Polymorphism databases

DMDMi 125157.

2D gel databases

UCD-2DPAGE P27144.

Proteomic databases

MaxQBi P27144.
PaxDbi P27144.
PRIDEi P27144.

Protocols and materials databases

DNASUi 205.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000327299 ; ENSP00000322175 ; ENSG00000162433 .
ENST00000395334 ; ENSP00000378743 ; ENSG00000162433 .
ENST00000545314 ; ENSP00000445912 ; ENSG00000162433 .
GeneIDi 100507855.
205.
KEGGi hsa:100507855.
hsa:205.
UCSCi uc001dby.3. human.

Organism-specific databases

CTDi 205.
GeneCardsi GC01P065614.
HGNCi HGNC:363. AK4.
HPAi HPA042753.
HPA049461.
MIMi 103030. gene.
neXtProti NX_P27144.
PharmGKBi PA165750325.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0563.
GeneTreei ENSGT00550000074679.
HOGENOMi HOG000238772.
HOVERGENi HBG000458.
InParanoidi P27144.
KOi K00939.
OMAi GDVAKQY.
PhylomeDBi P27144.
TreeFami TF312916.

Miscellaneous databases

EvolutionaryTracei P27144.
GeneWikii AK3L1.
NextBioi 818.
PROi P27144.
SOURCEi Search...

Gene expression databases

Bgeei P27144.
CleanExi HS_AK3.
HS_AK3L1.
ExpressionAtlasi P27144. baseline and differential.
Genevestigatori P27144.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
MF_03170. Adenylate_kinase_AK4.
InterProi IPR006259. 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 ]
PANTHERi PTHR23359. PTHR23359. 1 hit.
Pfami PF05191. ADK_lid. 1 hit.
[Graphical view ]
PRINTSi PR00094. ADENYLTKNASE.
SUPFAMi SSF52540. SSF52540. 2 hits.
SSF57774. SSF57774. 1 hit.
TIGRFAMsi TIGR01351. adk. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. "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.
  12. "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: October 29, 2014
This is version 149 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