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P54819

- KAD2_HUMAN

UniProt

P54819 - KAD2_HUMAN

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Protein
Adenylate kinase 2, mitochondrial
Gene
AK2, ADK2
Organism
Homo sapiens (Human)
Status
Reviewed - 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.1 Publication

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation

Sites

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

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi25 – 306ATPUniRule annotation
Nucleotide bindingi72 – 743AMP By similarity
Nucleotide bindingi100 – 1034AMP By similarity
Nucleotide bindingi151 – 1522ATPUniRule annotation

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. adenylate kinase activity Source: ProtInc
Complete GO annotation...

GO - Biological processi

  1. ADP biosynthetic process Source: Ensembl
  2. AMP metabolic process Source: Ensembl
  3. brain development Source: Ensembl
  4. dATP metabolic process Source: Ensembl
  5. liver development Source: Ensembl
  6. nucleobase-containing small molecule interconversion Source: Reactome
  7. nucleobase-containing small molecule metabolic process Source: Reactome
  8. nucleotide phosphorylation Source: GOC
  9. oxidative phosphorylation Source: Ensembl
  10. response to thyroid hormone Source: Ensembl
  11. small molecule metabolic process Source: Reactome
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, mitochondrial (EC:2.7.4.3)
Short name:
AK 2
Alternative name(s):
ATP-AMP transphosphorylase 2
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Cleaved into the following chain:
Gene namesi
Name:AK2
Synonyms:ADK2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 1

Organism-specific databases

HGNCiHGNC:362. AK2.

Subcellular locationi

GO - Cellular componenti

  1. cytosol Source: Ensembl
  2. extracellular vesicular exosome Source: UniProt
  3. mitochondrial inner membrane Source: Ensembl
  4. mitochondrial intermembrane space Source: Reactome
  5. sperm mitochondrial sheath Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Mitochondrion

Pathology & Biotechi

Involvement in diseasei

Reticular dysgenesis (RDYS) [MIM:267500]: Most 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.
Note: The disease is caused by mutations affecting the gene represented in this entry.2 Publications
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.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 239239Adenylate kinase 2, mitochondrialUniRule annotation
PRO_0000423212Add
BLAST
Initiator methioninei1 – 11Removed; alternate1 Publication
Chaini2 – 239238Adenylate kinase 2, mitochondrial, N-terminally processedUniRule annotation
PRO_0000158917Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine2 Publications
Disulfide bondi42 ↔ 921 Publication
Modified residuei62 – 621N6-succinyllysine By similarity
Modified residuei93 – 931N6-succinyllysine By similarity
Modified residuei181 – 1811N6-acetyllysine By similarity

Keywords - PTMi

Acetylation, Disulfide bond

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

ArrayExpressiP54819.
BgeeiP54819.
CleanExiHS_AK2.
GenevestigatoriP54819.

Organism-specific databases

HPAiHPA018479.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi106707. 17 interactions.
IntActiP54819. 4 interactions.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2C9YX-ray2.10A1-239[»]
ProteinModelPortaliP54819.
SMRiP54819. Positions 15-232.

Miscellaneous databases

EvolutionaryTraceiP54819.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni45 – 7430NMPbindUniRule annotation
Add
BLAST
Regioni141 – 17838LIDUniRule annotation
Add
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.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0563.
HOVERGENiHBG000458.
InParanoidiP54819.
KOiK00939.
OMAiLENNKAC.
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. Align

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

MAPSVPAAEP EYPKGIRAVL LGPPGAGKGT QAPRLAENFC VCHLATGDML    50
RAMVASGSEL GKKLKATMDA GKLVSDEMVV ELIEKNLETP LCKNGFLLDG 100
FPRTVRQAEM LDDLMEKRKE KLDSVIEFSI PDSLLIRRIT GRLIHPKSGR 150
SYHEEFNPPK EPMKDDITGE PLIRRSDDNE KALKIRLQAY HTQTTPLIEY 200
YRKRGIHSAI DASQTPDVVF ASILAAFSKA TCKDLVMFI 239
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:
     2-48: Missing.
     177-178: DD → GL
     179-239: Missing.

Show »
Length:131
Mass (Da):14,840
Checksum:i99C780C24D0F7845
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:
     2-48: Missing.

Note: No experimental confirmation available.

Show »
Length:192
Mass (Da):21,767
Checksum:i599AC964FCA56E89
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 sequencei2 – 4847Missing in isoform 4 and isoform 6.
VSP_002792Add
BLAST
Alternative sequencei135 – 1428Missing in isoform 5.
VSP_036503
Alternative sequencei177 – 1782DD → GL in isoform 4.
VSP_002793
Alternative sequencei178 – 23962DNEKA…LVMFI → IGQAKRSFLRLAKISFDVLI KKALA in isoform 3.
VSP_002791Add
BLAST
Alternative sequencei179 – 23961Missing in isoform 4.
VSP_002794Add
BLAST
Alternative sequencei232 – 2398CKDLVMFI → S in isoform 2 and isoform 5.
VSP_002790

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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]

Polymorphism databases

DMDMi1708596.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
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 .
CCDSi CCDS373.1. [P54819-2 ]
CCDS374.1. [P54819-1 ]
PIRi G02248.
JC5893.
RefSeqi NP_001186128.1. NM_001199199.1. [P54819-5 ]
NP_001616.1. NM_001625.3. [P54819-1 ]
NP_037543.1. NM_013411.4. [P54819-2 ]
UniGenei Hs.470907.

3D structure databases

Select the link destinations:
PDBe
RCSB PDB
PDBj
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
2C9Y X-ray 2.10 A 1-239 [» ]
ProteinModelPortali P54819.
SMRi P54819. Positions 15-232.
ModBasei Search...

Protein-protein interaction databases

BioGridi 106707. 17 interactions.
IntActi P54819. 4 interactions.

Chemistry

BindingDBi P54819.
ChEMBLi CHEMBL4938.

PTM databases

PhosphoSitei P54819.

Polymorphism databases

DMDMi 1708596.

2D gel databases

OGPi P54819.
REPRODUCTION-2DPAGE IPI00218988.
UCD-2DPAGE P54819.

Proteomic databases

MaxQBi P54819.
PaxDbi P54819.
PRIDEi P54819.

Protocols and materials databases

DNASUi 204.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000354858 ; ENSP00000346921 ; ENSG00000004455 . [P54819-1 ]
ENST00000373449 ; ENSP00000362548 ; ENSG00000004455 . [P54819-2 ]
GeneIDi 204.
KEGGi hsa:204.
UCSCi uc001bwo.2. human. [P54819-2 ]
uc001bwp.2. human. [P54819-1 ]
uc010ohq.2. human. [P54819-5 ]

Organism-specific databases

CTDi 204.
GeneCardsi GC01M033476.
HGNCi HGNC:362. AK2.
HPAi HPA018479.
MIMi 103020. gene.
267500. phenotype.
neXtProti NX_P54819.
Orphaneti 33355. Reticular dysgenesis.
PharmGKBi PA24656.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG0563.
HOVERGENi HBG000458.
InParanoidi P54819.
KOi K00939.
OMAi LENNKAC.
OrthoDBi EOG74TX0R.
PhylomeDBi P54819.
TreeFami TF300896.

Enzyme and pathway databases

Reactomei REACT_21330. Synthesis and interconversion of nucleotide di- and triphosphates.

Miscellaneous databases

EvolutionaryTracei P54819.
GeneWikii AK2.
GenomeRNAii 204.
NextBioi 812.
PROi P54819.
SOURCEi Search...

Gene expression databases

ArrayExpressi P54819.
Bgeei P54819.
CleanExi HS_AK2.
Genevestigatori P54819.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
MF_03168. Adenylate_kinase_AK2.
InterProi IPR006259. Adenyl_kin_sub.
IPR000850. Adenylat/UMP-CMP_kin.
IPR007862. Adenylate_kinase_lid-dom.
IPR028587. AK2.
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. 1 hit.
TIGRFAMsi TIGR01351. adk. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

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. Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) IN COMPLEX WITH BI-SUBSTRATE ANALOG AP4A, DISULFIDE BOND.
  15. "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.
  16. 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: September 3, 2014
This is version 151 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

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