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Protein

GTP:AMP phosphotransferase AK3, mitochondrial

Gene

AK3

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. Has GTP:AMP phosphotransferase and ITP:AMP phosphotransferase activities.UniRule annotation1 Publication

Catalytic activityi

NTP + AMP = NDP + ADP.UniRule annotation1 Publication

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei38 – 381AMPUniRule annotation
Binding sitei43 – 431AMPUniRule annotation
Binding sitei98 – 981AMPUniRule annotation
Binding sitei128 – 1281GTPUniRule annotation
Binding sitei161 – 1611AMPUniRule annotation
Binding sitei172 – 1721AMPUniRule annotation
Binding sitei201 – 2011GTP; via carbonyl oxygenUniRule annotation

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi17 – 226GTPUniRule annotation
Nucleotide bindingi64 – 663AMPUniRule annotation
Nucleotide bindingi91 – 944AMPUniRule annotation
Nucleotide bindingi137 – 1382GTPUniRule annotation

GO - Molecular functioni

  • ATP binding Source: InterPro
  • GTP binding Source: UniProtKB-KW
  • nucleoside triphosphate adenylate kinase activity Source: BHF-UCL

GO - Biological processi

  • ADP biosynthetic process Source: UniProtKB-HAMAP
  • AMP metabolic process Source: BHF-UCL
  • blood coagulation Source: Reactome
  • GTP metabolic process Source: BHF-UCL
  • ITP metabolic process Source: BHF-UCL
  • UTP metabolic process Source: BHF-UCL
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

GTP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Names & Taxonomyi

Protein namesi
Recommended name:
GTP:AMP phosphotransferase AK3, mitochondrialUniRule annotation (EC:2.7.4.10UniRule annotation)
Alternative name(s):
Adenylate kinase 3UniRule annotation
Short name:
AK 3UniRule annotation
Adenylate kinase 3 alpha-like 1UniRule annotation
Gene namesi
Name:AK3UniRule annotation
Synonyms:AK3L1, AK6, AKL3L
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 9

Organism-specific databases

HGNCiHGNC:17376. AK3.

Subcellular locationi

GO - Cellular componenti

  • mitochondrial matrix Source: BHF-UCL
  • mitochondrion Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA164741184.

Polymorphism and mutation databases

BioMutaiAK3.
DMDMi23831297.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11RemovedBy similarity
Chaini2 – 227226GTP:AMP phosphotransferase AK3, mitochondrialPRO_0000158922Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei20 – 201N6-succinyllysineBy similarity
Modified residuei34 – 341N6-acetyllysineBy similarity
Modified residuei57 – 571N6-succinyllysineBy similarity
Modified residuei64 – 641N6-acetyllysine; alternateBy similarity
Modified residuei64 – 641N6-succinyllysine; alternateBy similarity
Modified residuei80 – 801N6-acetyllysine; alternateBy similarity
Modified residuei80 – 801N6-succinyllysine; alternateBy similarity
Modified residuei174 – 1741N6-acetyllysine; alternateBy similarity
Modified residuei174 – 1741N6-succinyllysine; alternateBy similarity
Modified residuei189 – 1891N6-acetyllysine; alternateBy similarity
Modified residuei189 – 1891N6-succinyllysine; alternateBy similarity
Modified residuei203 – 2031N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9UIJ7.
PaxDbiQ9UIJ7.
PRIDEiQ9UIJ7.

2D gel databases

OGPiQ9UIJ7.
REPRODUCTION-2DPAGEIPI00465256.
UCD-2DPAGEQ9UIJ7.

PTM databases

PhosphoSiteiQ9UIJ7.

Expressioni

Tissue specificityi

Highly expressed in heart, skeletal muscle and liver, moderately expressed in pancreas and kidney, and weakly expressed in placenta, brain and lung.1 Publication

Gene expression databases

BgeeiQ9UIJ7.
CleanExiHS_AK3.
HS_AK3L1.
GenevisibleiQ9UIJ7. HS.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Binary interactionsi

WithEntry#Exp.IntActNotes
APPBP2Q926243EBI-3916527,EBI-743771

Protein-protein interaction databases

BioGridi119127. 6 interactions.
IntActiQ9UIJ7. 3 interactions.
STRINGi9606.ENSP00000371230.

Structurei

Secondary structure

1
227
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi9 – 146Combined sources
Helixi20 – 3011Combined sources
Beta strandi31 – 377Combined sources
Helixi38 – 4811Combined sources
Helixi51 – 6010Combined sources
Turni61 – 633Combined sources
Helixi68 – 8013Combined sources
Beta strandi87 – 915Combined sources
Helixi96 – 1038Combined sources
Beta strandi110 – 1156Combined sources
Helixi118 – 1258Combined sources
Beta strandi128 – 1314Combined sources
Turni132 – 1354Combined sources
Beta strandi136 – 1394Combined sources
Turni140 – 1423Combined sources
Turni152 – 1543Combined sources
Helixi162 – 1643Combined sources
Helixi166 – 18924Combined sources
Beta strandi193 – 1975Combined sources
Helixi201 – 21212Combined sources
Turni213 – 2153Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZD8X-ray1.48A1-227[»]
ProteinModelPortaliQ9UIJ7.
SMRiQ9UIJ7. Positions 7-218.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiQ9UIJ7.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni37 – 6630NMPbindAdd
BLAST
Regioni127 – 16438LIDAdd
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 binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent GTP hydrolysis.

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG0563.
GeneTreeiENSGT00550000074679.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiQ9UIJ7.
KOiK00944.
OMAiNVPFQTI.
OrthoDBiEOG74TX0R.
PhylomeDBiQ9UIJ7.
TreeFamiTF312916.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/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]

Sequences (3)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 3 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q9UIJ7-1) [UniParc]FASTAAdd to basket

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
MGASARLLRA VIMGAPGSGK GTVSSRITTH FELKHLSSGD LLRDNMLRGT
60 70 80 90 100
EIGVLAKAFI DQGKLIPDDV MTRLALHELK NLTQYSWLLD GFPRTLPQAE
110 120 130 140 150
ALDRAYQIDT VINLNVPFEV IKQRLTARWI HPASGRVYNI EFNPPKTVGI
160 170 180 190 200
DDLTGEPLIQ REDDKPETVI KRLKAYEDQT KPVLEYYQKK GVLETFSGTE
210 220
TNKIWPYVYA FLQTKVPQRS QKASVTP
Length:227
Mass (Da):25,565
Last modified:January 23, 2007 - v4
Checksum:i98A0EDF4FD9C9CEF
GO
Isoform 2 (identifier: Q9UIJ7-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-70: Missing.

Show »
Length:157
Mass (Da):18,192
Checksum:iF7D36803A8A241A4
GO
Isoform 3 (identifier: Q9UIJ7-3) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     51-90: Missing.

Note: No experimental confirmation available.
Show »
Length:187
Mass (Da):21,014
Checksum:i107B098298461090
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti5 – 51A → G in BAA87913 (PubMed:11485571).Curated
Sequence conflicti38 – 381S → R in BAA87913 (PubMed:11485571).Curated
Sequence conflicti57 – 571K → Q in BAA87913 (PubMed:11485571).Curated
Sequence conflicti69 – 713DVM → YVT in BAA87913 (PubMed:11485571).Curated
Sequence conflicti181 – 1811K → E in BAG60470 (PubMed:14702039).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 7070Missing in isoform 2. 2 PublicationsVSP_043090Add
BLAST
Alternative sequencei51 – 9040Missing in isoform 3. 1 PublicationVSP_044876Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021870 mRNA. Translation: BAA87913.1.
AF183419 mRNA. Translation: AAG09688.1.
AK001553 mRNA. Translation: BAA91753.1.
AK001951 mRNA. Translation: BAA91996.1.
AK027534 mRNA. Translation: BAB55183.1.
AK098205 mRNA. Translation: BAG53592.1.
AK298200 mRNA. Translation: BAG60470.1.
AL136231, AL353151 Genomic DNA. Translation: CAI41262.1.
AL353151, AL136231 Genomic DNA. Translation: CAH72282.1.
AL136231, AL353151 Genomic DNA. Translation: CAI41260.1.
AL353151, AL136231 Genomic DNA. Translation: CAH72283.1.
CH471071 Genomic DNA. Translation: EAW58779.1.
CH471071 Genomic DNA. Translation: EAW58780.1.
CH471071 Genomic DNA. Translation: EAW58781.1.
BC013771 mRNA. Translation: AAH13771.1.
CCDSiCCDS56561.1. [Q9UIJ7-2]
CCDS56562.1. [Q9UIJ7-3]
CCDS6455.1. [Q9UIJ7-1]
RefSeqiNP_001186781.1. NM_001199852.1. [Q9UIJ7-3]
NP_001186782.1. NM_001199853.1. [Q9UIJ7-2]
NP_001186784.1. NM_001199855.1. [Q9UIJ7-2]
NP_001186785.1. NM_001199856.1. [Q9UIJ7-2]
NP_057366.2. NM_016282.3. [Q9UIJ7-1]
UniGeneiHs.732022.

Genome annotation databases

EnsembliENST00000359883; ENSP00000352948; ENSG00000147853. [Q9UIJ7-2]
ENST00000381809; ENSP00000371230; ENSG00000147853.
ENST00000447596; ENSP00000413933; ENSG00000147853. [Q9UIJ7-3]
ENST00000611749; ENSP00000482308; ENSG00000147853. [Q9UIJ7-2]
GeneIDi50808.
KEGGihsa:50808.
UCSCiuc003ziq.2. human. [Q9UIJ7-1]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB021870 mRNA. Translation: BAA87913.1.
AF183419 mRNA. Translation: AAG09688.1.
AK001553 mRNA. Translation: BAA91753.1.
AK001951 mRNA. Translation: BAA91996.1.
AK027534 mRNA. Translation: BAB55183.1.
AK098205 mRNA. Translation: BAG53592.1.
AK298200 mRNA. Translation: BAG60470.1.
AL136231, AL353151 Genomic DNA. Translation: CAI41262.1.
AL353151, AL136231 Genomic DNA. Translation: CAH72282.1.
AL136231, AL353151 Genomic DNA. Translation: CAI41260.1.
AL353151, AL136231 Genomic DNA. Translation: CAH72283.1.
CH471071 Genomic DNA. Translation: EAW58779.1.
CH471071 Genomic DNA. Translation: EAW58780.1.
CH471071 Genomic DNA. Translation: EAW58781.1.
BC013771 mRNA. Translation: AAH13771.1.
CCDSiCCDS56561.1. [Q9UIJ7-2]
CCDS56562.1. [Q9UIJ7-3]
CCDS6455.1. [Q9UIJ7-1]
RefSeqiNP_001186781.1. NM_001199852.1. [Q9UIJ7-3]
NP_001186782.1. NM_001199853.1. [Q9UIJ7-2]
NP_001186784.1. NM_001199855.1. [Q9UIJ7-2]
NP_001186785.1. NM_001199856.1. [Q9UIJ7-2]
NP_057366.2. NM_016282.3. [Q9UIJ7-1]
UniGeneiHs.732022.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1ZD8X-ray1.48A1-227[»]
ProteinModelPortaliQ9UIJ7.
SMRiQ9UIJ7. Positions 7-218.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi119127. 6 interactions.
IntActiQ9UIJ7. 3 interactions.
STRINGi9606.ENSP00000371230.

PTM databases

PhosphoSiteiQ9UIJ7.

Polymorphism and mutation databases

BioMutaiAK3.
DMDMi23831297.

2D gel databases

OGPiQ9UIJ7.
REPRODUCTION-2DPAGEIPI00465256.
UCD-2DPAGEQ9UIJ7.

Proteomic databases

MaxQBiQ9UIJ7.
PaxDbiQ9UIJ7.
PRIDEiQ9UIJ7.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000359883; ENSP00000352948; ENSG00000147853. [Q9UIJ7-2]
ENST00000381809; ENSP00000371230; ENSG00000147853.
ENST00000447596; ENSP00000413933; ENSG00000147853. [Q9UIJ7-3]
ENST00000611749; ENSP00000482308; ENSG00000147853. [Q9UIJ7-2]
GeneIDi50808.
KEGGihsa:50808.
UCSCiuc003ziq.2. human. [Q9UIJ7-1]

Organism-specific databases

CTDi50808.
GeneCardsiGC09M004703.
HGNCiHGNC:17376. AK3.
MIMi609290. gene.
neXtProtiNX_Q9UIJ7.
PharmGKBiPA164741184.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0563.
GeneTreeiENSGT00550000074679.
HOGENOMiHOG000238772.
HOVERGENiHBG000458.
InParanoidiQ9UIJ7.
KOiK00944.
OMAiNVPFQTI.
OrthoDBiEOG74TX0R.
PhylomeDBiQ9UIJ7.
TreeFamiTF312916.

Enzyme and pathway databases

ReactomeiREACT_24970. Factors involved in megakaryocyte development and platelet production.

Miscellaneous databases

ChiTaRSiAK3. human.
EvolutionaryTraceiQ9UIJ7.
GenomeRNAii50808.
NextBioi53246.
PROiQ9UIJ7.
SOURCEiSearch...

Gene expression databases

BgeeiQ9UIJ7.
CleanExiHS_AK3.
HS_AK3L1.
GenevisibleiQ9UIJ7. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03169. Adenylate_kinase_AK3.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028586. AK3/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. "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: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, CATALYTIC ACTIVITY, TISSUE SPECIFICITY, SUBCELLULAR LOCATION.
    Tissue: Liver.
  2. "A novel gene expressed in human pheochromocytoma."
    Li Y., Peng Y., Jiang Z., Gu W., Han Z., Chen Z.
    Submitted (SEP-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Pheochromocytoma.
  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] (ISOFORMS 1; 2 AND 3).
    Tissue: Placenta.
  4. "DNA sequence and analysis of human chromosome 9."
    Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L.
    , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
    Nature 429:369-374(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. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "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.
  9. "Structure of human adenylate kinase 3-like 1."
    Structural genomics consortium (SGC)
    Submitted (MAY-2005) to the PDB data bank
    Cited for: X-RAY CRYSTALLOGRAPHY (1.48 ANGSTROMS).

Entry informationi

Entry nameiKAD3_HUMAN
AccessioniPrimary (citable) accession number: Q9UIJ7
Secondary accession number(s): B4DP58
, D3DRI1, E7ET30, Q5VYW6, Q9H576, Q9HC01, Q9NPB4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: December 1, 2000
Last sequence update: January 23, 2007
Last modified: July 22, 2015
This is version 147 of the entry and version 4 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 9
    Human chromosome 9: 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.