ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!
Search for

UniProtKB/Swiss-Prot entry P27144


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

Note: most headings are clickable, even if they don't appear as links. They link to the user manual or other documents.
Entry information
Entry name KAD4_HUMAN
Primary accession number P27144
Secondary accession numbers Q6IBH4 Q6NXQ5 Q8IUU9
Integrated into Swiss-Prot on August 1, 1992
Sequence was last modified on August 1, 1992 (Sequence version 1)
Annotations were last modified on    November 25, 2008 (Entry version 87)
Name and origin of the protein
Protein name Adenylate kinase isoenzyme 4, mitochondrial
Synonyms EC 2.7.4.3
Adenylate kinase 3-like
ATP-AMP transphosphorylase
Gene names
Name: AK3L1
Synonyms: AK3, AK4
and
Name: AK3L2
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (AK3L2).
DOI=10.1016/0888-7543(92)90122-9; PubMed=1639383 [NCBI, ExPASy, EBI, Israel, Japan]
Xu G., O'Connell P., Stevens J., White R.;
"Characterization of human adenylate kinase 3 (AK3) cDNA and mapping of the AK3 pseudogene to an intron of the NF1 gene.";
Genomics 13:537-542(1992).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (AK3L1).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AK3L1).
DOI=10.1038/nature04727; PubMed=16710414 [NCBI, ExPASy, EBI, Israel, Japan]
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.;
"The DNA sequence and biological annotation of human chromosome 1.";
Nature 441:315-321(2006).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AK3L1).
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Brain, Colon, and Lung;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[6]
X-RAY CRYSTALLOGRAPHY (2.05 ANGSTROMS).
Structural genomics consortium (SGC);
"Crystal structure of human adenylate kinase 4 (ak4) in complex with diguanosine pentaphosphate.";
Submitted (DEC-2005) to the PDB data bank.
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
X60673; CAA43088.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CR456830; CAG33111.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AL356212; CAI22412.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AC099680; CAI22412.1; JOINED; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
CH471059; EAX06538.1; -; Genomic_DNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC016180; AAH16180.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC040224; AAH40224.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC066944; AAH66944.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC146653; AAI46654.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42820; KIHUA3.
RefSeq NP_001005353.1; -.
NP_037542.1; -.
NP_982289.1; -.
XP_001725226.1; -.
UniGene Hs.10862
3D structure databases
PDB
2AR7; X-ray; 2.15 A; A/B=1-223.[ExPASy / RCSB / EBI]
2BBW; X-ray; 2.05 A; A/B=1-223.[ExPASy / RCSB / EBI]
Detailed list of linked structures.
PDBsum 2AR7; -.
2BBW; -.
ModBase P27144.
PTM databases
PhosphoSite P27144; -.
Organism-specific databases
H-InvDB HIX0000670; -.
HIX0059100; -.
HGNC HGNC:363; AK3L1.
HGNC:21596; AK3L2.
GenAtlas AK3L1.
MIM 103030; gene. [NCBI / EBI]
PharmGKB PA134944695; -.
GeneCards P27144.
Gene expression databases
ArrayExpress P27144; -.
CleanEx HS_AK3; -.
HS_AK3L1; -.
GermOnline ENSG00000162433; Homo sapiens.
Ontologies
GO
GO:0005759; Cellular component: mitochondrial matrix (inferred from electronic annotation from UniProtKB-SubCell).
GO:0004017; Molecular function: adenylate kinase activity (inferred from electronic annotation from InterPro).
GO:0005524; Molecular function: ATP binding (inferred from electronic annotation from InterPro).
GO:0005525; Molecular function: GTP binding (inferred from electronic annotation from UniProtKB-KW).
GO:0006139; Biological process: nucleobase, nucleoside, nucleotide and nucleic acid metabolic process (inferred from electronic annotation from InterPro).
QuickGo view.
Family and domain databases
InterPro IPR006259; Adenyl_kin_sub.
IPR000850; Adenylate_kin.
IPR007862; Adenylate_kinase_Znf_lid.
Graphical view of domain structure.
PANTHER PTHR23359; Adenylate_kin; 1.
Pfam PF00406; ADK; 1.
PF05191; ADK_lid; 1.
Pfam graphical view of domain structure.
PRINTS PR00094; ADENYLTKNASE.
ProDom PD000657; Adenylate_kin; 1.
[Domain structure / List of seq. sharing at least 1 domain]
TIGRFAMs TIGR01351; adk; 1.
PROSITE PS00113; ADENYLATE_KINASE; 1.
BLOCKS P27144.
ProtoNet P27144.
Genome annotation databases
Ensembl ENSG00000162433; Homo sapiens. [Contig view]
GeneID 205; -.
645619; -.
KEGG hsa:205; -.
Phylogenomic databases
HOGENOM P27144; -.
HOVERGEN P27144; -.
Other
LinkHub P27144; -.
NextBio 818; -.
SOURCE AK3L1; Homo sapiens.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; GTP-binding; Kinase; Mitochondrion; Nucleotide-binding; Transferase.
Features
SEVIEWER logo Feature table viewer
KeyFrom   To Length Description FTId
CHAIN   1   223  223     Adenylate kinase isoenzyme 4, mitochondrial. PRO_0000158926
NP_BIND   12    20  9     GTP (By similarity). 
CONFLICT   22    22        C -> S (in Ref. 5; AAH40224/AAI46654). 
CONFLICT   23    23        Q -> R (in Ref. 5; AAH66944). 
STRAND   7    11  5      
HELIX   18    29  12      
STRAND   32    34  3      
HELIX   36    45  10      
HELIX   49    61  13      
HELIX   66    78  13      
TURN   79    82  4      
STRAND   85    89  5      
HELIX   94   101  8      
STRAND   108   112  5      
HELIX   116   123  8      
STRAND   126   128  3      
TURN   130   132  3      
STRAND   135   137  3      
TURN   138   140  3      
TURN   150   152  3      
HELIX   160   162  3      
HELIX   164   187  24      
STRAND   191   194  4      
HELIX   199   201  3      
HELIX   202   211  10      
HELIX   220   222  3      
Sequence information
Length: 223 AA [This is the length of the unprocessed precursor] Molecular weight: 25268 Da [This is the MW of the unprocessed precursor] CRC64: 653341A8EB3BC723 [This is a checksum on the sequence]
        10         20         30         40         50         60 
MASKLLRAVI LGPPGSGKGT VCQRIAQNFG LQHLSSGHFL RENIKASTEV GEMAKQYIEK 

        70         80         90        100        110        120 
SLLVPDHVIT RLMMSELENR RGQHWLLDGF PRTLGQAEAL DKICEVDLVI SLNIPFETLK 

       130        140        150        160        170        180 
DRLSRRWIHP PSGRVYNLDF NPPHVHGIDD VTGEPLVQQE DDKPEAVAAR LRQYKDVAKP 

       190        200        210        220 
VIELYKSRGV LHQFSGTETN KIWPYVYTLF SNKITPIQSK EAY 

P27144 in FASTA format

View entry in original UniProtKB/Swiss-Prot format
View entry in raw text format (no links)
Report form for errors/updates in this UniProtKB/Swiss-Prot entry

BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

ExPASy logo ExPASy Home page Site Map Search ExPASy Contact us Swiss-Prot
 Hosted by au flag APAF Australia Mirror sites: Brazil  Canada  China  Korea  Switzerland
Notice: This page will be replaced with www.uniprot.org. Please send us your feedback!