Reviewed, UniProtKB/Swiss-Prot P27144 (KAD4_HUMAN)

Names and origin

Protein names

Recommended name:
    Adenylate kinase isoenzyme 4, mitochondrial
    EC=2.7.4.3
Alternative name(s):
    Adenylate kinase 3-like
    ATP-AMP transphosphorylase

Gene names

Name:	AK3L1
Synonyms:	AK3, AK4
AND
Name:	AK3L2

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	223 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence at protein level.

General annotation (Comments)

Function	Catalyzes the reversible transfer of the terminal phosphate group between ATP and AMP. May also be active with GTP By similarity.
Catalytic activity	ATP + AMP = 2 ADP.
Subunit structure	Monomer.
Subcellular location	Mitochondrion matrix.
Sequence similarities	Belongs to the adenylate kinase family.

Ontologies

Keywords
Cellular component	Mitochondrion
Ligand	ATP-binding GTP-binding Nucleotide-binding
Molecular function	Kinase Transferase
Technical term	3D-structure
Gene Ontology (GO)
Biological process	nucleobase, nucleoside, nucleotide and nucleic acid metabolic process Inferred from electronic annotation. Source: InterPro
Cellular component	mitochondrial matrix Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW GTP binding Inferred from electronic annotation. Source: UniProtKB-KW adenylate kinase activity Inferred from electronic annotation. Source: EC
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 223

223

Adenylate kinase isoenzyme 4, mitochondrial

PRO_0000158926

Regions

Nucleotide binding

12 – 20

9

ATP

Nucleotide binding

89 – 96

8

AMP

Sites

Binding site

36

1

AMP

Experimental info

Sequence conflict

22

1

C → S in AAH40224. Ref.5

Sequence conflict

22

1

C → S in AAI46654. Ref.5

Sequence conflict

23

1

Q → R in AAH66944. Ref.5

Secondary structure

1

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223

Helix Strand Turn

Details...

Beta strand

7 – 11

5

Helix

18 – 29

12

Beta strand

32 – 34

3

Helix

36 – 45

10

Helix

49 – 61

13

Helix

66 – 78

13

Turn

79 – 82

4

Beta strand

85 – 89

5

Helix

94 – 101

8

Beta strand

108 – 112

5

Helix

116 – 123

8

Beta strand

126 – 128

3

Turn

130 – 132

3

Beta strand

135 – 137

3

Turn

138 – 140

3

Turn

150 – 152

3

Helix

160 – 162

3

Helix

164 – 187

24

Beta strand

191 – 194

4

Helix

199 – 201

3

Helix

202 – 211

10

Helix

220 – 222

3

Sequences

	Sequence		Length	Mass (Da)
	P27144-1 [UniParc]. Last modified August 1, 1992. Version 1. Checksum: 653341A8EB3BC723	FASTA	223	25,268
	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

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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: 1639383] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA] (AK3L2).
[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] (AK3L1).
[3]	"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: 16710414] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AK3L1).
[4]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA] (AK3L1).
[5]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Brain, Colon and Lung.
[6]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[7]	"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.
+	Additional computationally mapped references.

Cross-references

Sequence databases

EMBLGenBankDDBJ

X60673 mRNA. Translation: CAA43088.1.
CR456830 mRNA. Translation: CAG33111.1.
AL356212, AC099680 Genomic DNA. Translation: CAI22412.1.
CH471059 Genomic DNA. Translation: EAX06538.1.
BC016180 mRNA. Translation: AAH16180.1.
BC040224 mRNA. Translation: AAH40224.1.
BC066944 mRNA. Translation: AAH66944.1.
BC146653 mRNA. Translation: AAI46654.1.

IPI

IPI00016568.

PIR

KIHUA3. A42820.

RefSeq

NP_001005353.1.
NP_037542.1.
NP_982289.1.
XP_001725226.1.

UniGene

Hs.10862
Hs.592601

3D structure databases

PDBPDBe

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	[»]

ModBase

Search...

PTM databases

PhosphoSite

P27144.

Proteomic databases

PRIDE

P27144.

Genome annotation databases

Ensembl

ENSG00000162433. Homo sapiens. [Contig view]

GeneID

205.
645619.

KEGG

hsa:205.

Organism-specific databases

GeneCards

GC01P065385.
GC12M031658.

H-InvDB

HIX0000670.
HIX0059100.

HGNC

HGNC:363. AK3L1.
HGNC:21596. AK3L2.

MIM

103030. gene.

PharmGKB

PA134944695.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

P27144.

HOVERGEN

P27144.

OMA

P27144. HSFSGTE.

Enzyme and pathway databases

BRENDA

2.7.4.3. 247.

Gene expression databases

ArrayExpress

P27144.

Bgee

P27144.

CleanEx

HS_AK3.
HS_AK3L1.

GermOnline

ENSG00000162433. Homo sapiens.

Family and domain databases

InterPro

IPR006259. Adenyl_kin_sub.
IPR000850. Adenylate_kin.
IPR007862. Adenylate_kinase_Znf_lid.
[Graphical view]

PANTHER

PTHR23359. Adenylate_kin. 1 hit.

Pfam

PF00406. ADK. 1 hit.
PF05191. ADK_lid. 1 hit.
[Graphical view]

PRINTS

PR00094. ADENYLTKNASE.

ProDom

PD000657. Adenylate_kin. 1 hit.
[Graphical view] [Entries sharing at least one domain]

TIGRFAMs

TIGR01351. adk. 1 hit.

PROSITE

PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

818.

SOURCE

Search...

Entry information

Entry name

KAD4_HUMAN

Accession

Primary (citable) accession number: P27144
Secondary accession number(s): Q6IBH4, Q6NXQ5, Q8IUU9

Entry history

Integrated into UniProtKB/Swiss-Prot:	August 1, 1992
Last sequence update:	August 1, 1992
Last modified:	June 16, 2009
This is version 94 of the entry and version 1 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)