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Protein

Adenylate kinase 2, mitochondrial

Gene

AK2

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

Functioni

Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism. Adenylate kinase activity is critical for regulation of the phosphate utilization and the AMP de novo biosynthesis pathways. Plays a key role in hematopoiesis.UniRule annotation1 Publication

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei46 – 461AMPUniRule annotation
Binding sitei51 – 511AMPUniRule annotation
Binding sitei107 – 1071AMPUniRule annotation
Binding sitei138 – 1381ATP
Binding sitei142 – 1421ATPUniRule annotation
Binding sitei175 – 1751AMP
Binding sitei186 – 1861AMPUniRule annotation
Binding sitei214 – 2141ATP; via carbonyl oxygen

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi25 – 306ATP
Nucleotide bindingi72 – 743AMPUniRule annotation
Nucleotide bindingi100 – 1034AMPUniRule annotation
Nucleotide bindingi151 – 1522ATP

GO - Molecular functioni

  • adenylate kinase activity Source: ProtInc
  • ATP binding Source: UniProtKB-KW

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase 2, mitochondrialUniRule annotation (EC:2.7.4.3UniRule annotation)
Short name:
AK 2UniRule annotation
Alternative name(s):
ATP-AMP transphosphorylase 2UniRule annotation
ATP:AMP phosphotransferaseUniRule annotation
Adenylate monophosphate kinaseUniRule annotation
Cleaved into the following chain:
Adenylate kinase 2, mitochondrial, N-terminally processedUniRule annotation
Gene namesi
Name:AK2UniRule annotation
Synonyms:ADK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640 Componenti: Chromosome 1

Organism-specific databases

HGNCiHGNC:362. AK2.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Reticular dysgenesis (RDYS)2 Publications

The disease is caused by mutations affecting the gene represented in this entry.

Disease descriptionMost severe form of inborn severe combined immunodeficiencies (SCID) and is characterized by absence of granulocytes and almost complete deficiency of lymphocytes in peripheral blood, hypoplasia of the thymus and secondary lymphoid organs, and lack of innate and adaptive humoral and cellular immune functions, leading to fatal septicemia within days after birth. In bone marrow of individuals with reticular dysgenesis, myeloid differentiation is blocked at the promyelocytic stage, whereas erythro- and megakaryocytic maturation is generally normal. In addition, affected newborns have bilateral sensorineural deafness. Defects may be due to its absence in leukocytes and inner ear, in which its absence can not be compensated by AK1.

See also OMIM:267500
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031R → W in RDYS. 1 Publication
VAR_054630
Natural varianti165 – 1651D → G in RDYS. 1 Publication
VAR_054631

Keywords - Diseasei

Disease mutation

Organism-specific databases

MIMi267500. phenotype.
Orphaneti33355. Reticular dysgenesis.
PharmGKBiPA24656.

Chemistry

DrugBankiDB00718. Adefovir Dipivoxil.
DB00300. Tenofovir.

Polymorphism and mutation databases

BioMutaiAK2.
DMDMi1708596.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Adenylate kinase 2, mitochondrialPRO_0000423212Add
BLAST
Initiator methioninei1 – 11Removed; alternateUniRule annotation1 Publication
Chaini2 – 239238Adenylate kinase 2, mitochondrial, N-terminally processedPRO_0000158917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Disulfide bondi42 ↔ 92UniRule annotation1 Publication
Modified residuei62 – 621N6-succinyllysineBy similarity
Modified residuei93 – 931N6-succinyllysineBy similarity
Modified residuei133 – 1331Phosphoserine1 Publication
Modified residuei181 – 1811N6-acetyllysineBy similarity

Keywords - PTMi

Acetylation, Disulfide bond, Phosphoprotein

Proteomic databases

MaxQBiP54819.
PaxDbiP54819.
PRIDEiP54819.

2D gel databases

OGPiP54819.
REPRODUCTION-2DPAGEIPI00218988.
UCD-2DPAGEP54819.

PTM databases

PhosphoSiteiP54819.

Expressioni

Tissue specificityi

Present in most tissues. Present at high level in heart, liver and kidney, and at low level in brain, skeletal muscle and skin. Present in thrombocytes but not in erythrocytes, which lack mitochondria. Present in all nucleated cell populations from blood, while AK1 is mostly absent. In spleen and lymph nodes, mononuclear cells lack AK1, whereas AK2 is readily detectable. These results indicate that leukocytes may be susceptible to defects caused by the lack of AK2, as they do not express AK1 in sufficient amounts to compensate for the AK2 functional deficits (at protein level).1 Publication

Gene expression databases

BgeeiP54819.
CleanExiHS_AK2.
ExpressionAtlasiP54819. baseline and differential.
GenevisibleiP54819. HS.

Organism-specific databases

HPAiHPA018479.

Interactioni

Subunit structurei

Monomer.UniRule annotation

Protein-protein interaction databases

BioGridi106707. 18 interactions.
IntActiP54819. 4 interactions.

Structurei

Secondary structure

1
239
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Beta strandi16 – 216Combined sources
Helixi28 – 3912Combined sources
Beta strandi42 – 454Combined sources
Helixi46 – 5611Combined sources
Helixi59 – 6911Combined sources
Helixi76 – 8712Combined sources
Helixi90 – 923Combined sources
Beta strandi95 – 1006Combined sources
Helixi105 – 11713Combined sources
Beta strandi124 – 1296Combined sources
Helixi132 – 1409Combined sources
Turni146 – 1483Combined sources
Beta strandi151 – 1533Combined sources
Turni154 – 1563Combined sources
Beta strandi166 – 1683Combined sources
Helixi180 – 20324Combined sources
Beta strandi207 – 2115Combined sources
Helixi216 – 23015Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9YX-ray2.10A1-239[»]
ProteinModelPortaliP54819.
SMRiP54819. Positions 15-232.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiP54819.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 7430NMPbindAdd
BLAST
Regioni141 – 17838LIDAdd
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 ATP binding. Assembling and dissambling the active center during each catalytic cycle provides an effective means to prevent ATP hydrolysis.

Sequence similaritiesi

Belongs to the adenylate kinase family. AK2 subfamily.UniRule annotation

Phylogenomic databases

eggNOGiCOG0563.
GeneTreeiENSGT00770000120643.
HOVERGENiHBG000458.
InParanoidiP54819.
KOiK00939.
OMAiKSTIAED.
OrthoDBiEOG74TX0R.
PhylomeDBiP54819.
TreeFamiTF300896.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028587. AK2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequences (6)i

Sequence statusi: Complete.

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

This entry describes 6 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: P54819-1) [UniParc]FASTAAdd to basket

Also known as: AK2A, AK2isoA

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
MAPSVPAAEP EYPKGIRAVL LGPPGAGKGT QAPRLAENFC VCHLATGDML
60 70 80 90 100
RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG
110 120 130 140 150
FPRTVRQAEM LDDLMEKRKE KLDSVIEFSI PDSLLIRRIT GRLIHPKSGR
160 170 180 190 200
SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY
210 220 230
YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI
Length:239
Mass (Da):26,478
Last modified:January 23, 2007 - v2
Checksum:i86FA94F9EE33629F
GO
Isoform 2 (identifier: P54819-2) [UniParc]FASTAAdd to basket

Also known as: AK2B, AK2isoB

The sequence of this isoform differs from the canonical sequence as follows:
     232-239: CKDLVMFI → S

Show »
Length:232
Mass (Da):25,615
Checksum:i64AEE1A97D81D401
GO
Isoform 3 (identifier: P54819-3) [UniParc]FASTAAdd to basket

Also known as: AK2C

The sequence of this isoform differs from the canonical sequence as follows:
     178-239: DNEKALKIRL...ATCKDLVMFI → IGQAKRSFLRLAKISFDVLIKKALA

Show »
Length:202
Mass (Da):22,265
Checksum:iAE7593A8ADBD00CF
GO
Isoform 4 (identifier: P54819-4) [UniParc]FASTAAdd to basket

Also known as: AK2D

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.
     177-178: DD → GL
     179-239: Missing.

Show »
Length:130
Mass (Da):14,709
Checksum:iC6FEB90B2BFF7845
GO
Isoform 5 (identifier: P54819-5) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     135-142: Missing.
     232-239: CKDLVMFI → S

Note: No experimental confirmation available.
Show »
Length:224
Mass (Da):24,648
Checksum:i1A769D71DDBB0B8A
GO
Isoform 6 (identifier: P54819-6) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-48: Missing.

Note: No experimental confirmation available.
Show »
Length:191
Mass (Da):21,636
Checksum:iA6535F6453550852
GO

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti103 – 1031R → W in RDYS. 1 Publication
VAR_054630
Natural varianti165 – 1651D → G in RDYS. 1 Publication
VAR_054631
Natural varianti209 – 2091A → T.
Corresponds to variant rs12116440 [ dbSNP | Ensembl ].
VAR_050032

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 4848Missing in isoform 4 and isoform 6. 2 PublicationsVSP_002792Add
BLAST
Alternative sequencei135 – 1428Missing in isoform 5. 1 PublicationVSP_036503
Alternative sequencei177 – 1782DD → GL in isoform 4. 1 PublicationVSP_002793
Alternative sequencei178 – 23962DNEKA…LVMFI → IGQAKRSFLRLAKISFDVLI KKALA in isoform 3. 1 PublicationVSP_002791Add
BLAST
Alternative sequencei179 – 23961Missing in isoform 4. 1 PublicationVSP_002794Add
BLAST
Alternative sequencei232 – 2398CKDLVMFI → S in isoform 2 and isoform 5. 5 PublicationsVSP_002790

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39945 mRNA. Translation: AAC52061.1.
U84371 mRNA. Translation: AAB41790.1.
U54645 mRNA. Translation: AAC13881.1.
AB005621 mRNA. Translation: BAC16747.1.
AB005622 mRNA. Translation: BAC16748.1.
AY080899 mRNA. Translation: AAL87027.1.
AY080900 mRNA. Translation: AAL87028.1.
AK291676 mRNA. Translation: BAF84365.1.
AK295105 mRNA. Translation: BAG58139.1.
AK296863 mRNA. Translation: BAG59426.1.
AB451267 mRNA. Translation: BAG70081.1.
AB451394 mRNA. Translation: BAG70208.1.
AL020995 Genomic DNA. Translation: CAI19351.1.
AL020995 Genomic DNA. Translation: CAI19352.1.
CH471059 Genomic DNA. Translation: EAX07484.1.
CH471059 Genomic DNA. Translation: EAX07486.1.
BC009405 mRNA. Translation: AAH09405.1.
BC070127 mRNA. Translation: AAH70127.1.
BC090040 mRNA. Translation: AAH90040.1.
CCDSiCCDS373.1. [P54819-2]
CCDS374.1. [P54819-1]
PIRiG02248.
JC5893.
RefSeqiNP_001186128.1. NM_001199199.1. [P54819-5]
NP_001616.1. NM_001625.3. [P54819-1]
NP_037543.1. NM_013411.4. [P54819-2]
UniGeneiHs.470907.

Genome annotation databases

EnsembliENST00000354858; ENSP00000346921; ENSG00000004455. [P54819-1]
ENST00000373449; ENSP00000362548; ENSG00000004455. [P54819-2]
GeneIDi204.
KEGGihsa:204.
UCSCiuc001bwo.2. human. [P54819-2]
uc001bwp.2. human. [P54819-1]
uc010ohq.2. human. [P54819-5]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
U39945 mRNA. Translation: AAC52061.1.
U84371 mRNA. Translation: AAB41790.1.
U54645 mRNA. Translation: AAC13881.1.
AB005621 mRNA. Translation: BAC16747.1.
AB005622 mRNA. Translation: BAC16748.1.
AY080899 mRNA. Translation: AAL87027.1.
AY080900 mRNA. Translation: AAL87028.1.
AK291676 mRNA. Translation: BAF84365.1.
AK295105 mRNA. Translation: BAG58139.1.
AK296863 mRNA. Translation: BAG59426.1.
AB451267 mRNA. Translation: BAG70081.1.
AB451394 mRNA. Translation: BAG70208.1.
AL020995 Genomic DNA. Translation: CAI19351.1.
AL020995 Genomic DNA. Translation: CAI19352.1.
CH471059 Genomic DNA. Translation: EAX07484.1.
CH471059 Genomic DNA. Translation: EAX07486.1.
BC009405 mRNA. Translation: AAH09405.1.
BC070127 mRNA. Translation: AAH70127.1.
BC090040 mRNA. Translation: AAH90040.1.
CCDSiCCDS373.1. [P54819-2]
CCDS374.1. [P54819-1]
PIRiG02248.
JC5893.
RefSeqiNP_001186128.1. NM_001199199.1. [P54819-5]
NP_001616.1. NM_001625.3. [P54819-1]
NP_037543.1. NM_013411.4. [P54819-2]
UniGeneiHs.470907.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9YX-ray2.10A1-239[»]
ProteinModelPortaliP54819.
SMRiP54819. Positions 15-232.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi106707. 18 interactions.
IntActiP54819. 4 interactions.

Chemistry

BindingDBiP54819.
ChEMBLiCHEMBL4938.
DrugBankiDB00718. Adefovir Dipivoxil.
DB00300. Tenofovir.

PTM databases

PhosphoSiteiP54819.

Polymorphism and mutation databases

BioMutaiAK2.
DMDMi1708596.

2D gel databases

OGPiP54819.
REPRODUCTION-2DPAGEIPI00218988.
UCD-2DPAGEP54819.

Proteomic databases

MaxQBiP54819.
PaxDbiP54819.
PRIDEiP54819.

Protocols and materials databases

DNASUi204.
Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000354858; ENSP00000346921; ENSG00000004455. [P54819-1]
ENST00000373449; ENSP00000362548; ENSG00000004455. [P54819-2]
GeneIDi204.
KEGGihsa:204.
UCSCiuc001bwo.2. human. [P54819-2]
uc001bwp.2. human. [P54819-1]
uc010ohq.2. human. [P54819-5]

Organism-specific databases

CTDi204.
GeneCardsiGC01M033476.
HGNCiHGNC:362. AK2.
HPAiHPA018479.
MIMi103020. gene.
267500. phenotype.
neXtProtiNX_P54819.
Orphaneti33355. Reticular dysgenesis.
PharmGKBiPA24656.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiCOG0563.
GeneTreeiENSGT00770000120643.
HOVERGENiHBG000458.
InParanoidiP54819.
KOiK00939.
OMAiKSTIAED.
OrthoDBiEOG74TX0R.
PhylomeDBiP54819.
TreeFamiTF300896.

Enzyme and pathway databases

ReactomeiREACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

EvolutionaryTraceiP54819.
GeneWikiiAK2.
GenomeRNAii204.
NextBioi812.
PROiP54819.
SOURCEiSearch...

Gene expression databases

BgeeiP54819.
CleanExiHS_AK2.
ExpressionAtlasiP54819. baseline and differential.
GenevisibleiP54819. HS.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProiIPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028587. AK2.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PfamiPF05191. ADK_lid. 1 hit.
[Graphical view]
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01351. adk. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Cloning and characterization of cDNA for human adenylate kinase 2A."
    Lee Y., Kim J.W., Lee I.A., Kang H.B., Choe Y.K., Lee H.G., Lim J.S., Kim H.J., Park C., Choe I.S.
    Biochem. Mol. Biol. Int. 39:833-842(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Liver.
  2. "Cloning and expression of human adenylate kinase 2 isozymes: differential expression of adenylate kinase 1 and 2 in human muscle tissues."
    Lee Y., Kim J.W., Lee S.M., Kim H.J., Lee K.S., Park C., Choe I.S.
    J. Biochem. 123:47-54(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2).
    Tissue: Fetal liver.
  3. "cDNA cloning and tissue-specific expression of the gene encoding human adenylate kinase isozyme 2."
    Noma T., Song S., Yoon Y.-S., Tanaka S., Nakazawa A.
    Biochim. Biophys. Acta 1395:34-39(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  4. "Novel isoforms of human adenylate kinase 2."
    Guo J.
    Submitted (FEB-2002) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 3 AND 4).
  5. "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; 5 AND 6).
    Tissue: Brain, Placenta and Tongue.
  6. "Human protein factory for converting the transcriptome into an in vitro-expressed proteome."
    Goshima N., Kawamura Y., Fukumoto A., Miura A., Honma R., Satoh R., Wakamatsu A., Yamamoto J., Kimura K., Nishikawa T., Andoh T., Iida Y., Ishikawa K., Ito E., Kagawa N., Kaminaga C., Kanehori K., Kawakami B.
    , Kenmochi K., Kimura R., Kobayashi M., Kuroita T., Kuwayama H., Maruyama Y., Matsuo K., Minami K., Mitsubori M., Mori M., Morishita R., Murase A., Nishikawa A., Nishikawa S., Okamoto T., Sakagami N., Sakamoto Y., Sasaki Y., Seki T., Sono S., Sugiyama A., Sumiya T., Takayama T., Takayama Y., Takeda H., Togashi T., Yahata K., Yamada H., Yanagisawa Y., Endo Y., Imamoto F., Kisu Y., Tanaka S., Isogai T., Imai J., Watanabe S., Nomura N.
    Nat. Methods 5:1011-1017(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
  7. "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].
  8. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  9. "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] (ISOFORMS 1 AND 2).
    Tissue: Placenta and Uterus.
  10. Bienvenut W.V., Heiserich L., Gottlieb E.
    Submitted (MAR-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-14; 18-34; 73-85; 94-103; 107-117 AND 120-138, CLEAVAGE OF INITIATOR METHIONINE, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Colon carcinoma.
  11. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  12. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  13. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT MET-1, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  14. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-133, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  15. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP4A, DISULFIDE BOND.
  16. "Reticular dysgenesis (aleukocytosis) is caused by mutations in the gene encoding mitochondrial adenylate kinase 2."
    Pannicke U., Hoenig M., Hess I., Friesen C., Holzmann K., Rump E.-M., Barth T.F., Rojewski M.T., Schulz A., Boehm T., Friedrich W., Schwarz K.
    Nat. Genet. 41:101-105(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INVOLVEMENT IN RDYS, TISSUE SPECIFICITY.
  17. Cited for: VARIANTS RDYS TRP-103 AND GLY-165, FUNCTION.

Entry informationi

Entry nameiKAD2_HUMAN
AccessioniPrimary (citable) accession number: P54819
Secondary accession number(s): A8K6L1
, B4DHH7, B4DL64, Q16856, Q5EB54, Q5TIF7, Q8TCY2, Q8TCY3
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: January 23, 2007
Last modified: June 24, 2015
This is version 159 of the entry and version 2 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, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 1
    Human chromosome 1: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. 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.