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Q9R0Y5

- KAD1_MOUSE

UniProt

Q9R0Y5 - KAD1_MOUSE

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Protein

Adenylate kinase isoenzyme 1

Gene
Ak1
Organism
Mus musculus (Mouse)
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. Also possesses broad nucleoside diphosphate kinase activity. Plays an important role in cellular energy homeostasis and in adenine nucleotide metabolism By similarity. May provide a mechanism to buffer the adenylate energy charge for sperm motility.1 Publication

Catalytic activityi

ATP + AMP = 2 ADP.UniRule annotation
ATP + nucleoside diphosphate = ADP + nucleoside triphosphate.UniRule annotation

Sites

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Binding sitei39 – 391AMP By similarity
Binding sitei44 – 441AMP By similarity
Binding sitei101 – 1011AMP By similarity
Binding sitei132 – 1321ATP By similarity
Binding sitei138 – 1381AMP By similarity
Binding sitei149 – 1491AMP By similarity
Binding sitei177 – 1771ATP; via carbonyl oxygen By similarity

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi18 – 236ATP By similarity
Nucleotide bindingi65 – 673AMP By similarity
Nucleotide bindingi94 – 974AMP By similarity

GO - Molecular functioni

  1. adenylate kinase activity Source: MGI
  2. ATP binding Source: UniProtKB-KW
  3. nucleoside diphosphate kinase activity Source: UniProtKB

GO - Biological processi

  1. ATP metabolic process Source: InterPro
  2. cell cycle arrest Source: MGI
  3. nucleoside diphosphate phosphorylation Source: UniProtKB
  4. nucleoside triphosphate biosynthetic process Source: UniProtKB
Complete GO annotation...

Keywords - Molecular functioni

Kinase, Transferase

Keywords - Ligandi

ATP-binding, Nucleotide-binding

Enzyme and pathway databases

BRENDAi2.7.4.3. 3474.

Names & Taxonomyi

Protein namesi
Recommended name:
Adenylate kinase isoenzyme 1 (EC:2.7.4.3, EC:2.7.4.6)
Short name:
AK 1
Alternative name(s):
ATP-AMP transphosphorylase 1
ATP:AMP phosphotransferase
Adenylate monophosphate kinase
Myokinase
Gene namesi
Name:Ak1
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
ProteomesiUP000000589: Chromosome 2

Organism-specific databases

MGIiMGI:87977. Ak1.

Subcellular locationi

Cytoplasm By similarity UniRule annotation

GO - Cellular componenti

  1. cytoplasm Source: MGI
  2. outer dense fiber Source: MGI
  3. plasma membrane Source: MGI
  4. sperm flagellum Source: MGI
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 194194Adenylate kinase isoenzyme 1UniRule annotationPRO_0000158911Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei1 – 11N-acetylmethionine By similarity

Keywords - PTMi

Acetylation

Proteomic databases

MaxQBiQ9R0Y5.
PaxDbiQ9R0Y5.
PRIDEiQ9R0Y5.

2D gel databases

REPRODUCTION-2DPAGEIPI00128209.
Q9R0Y5.

PTM databases

PhosphoSiteiQ9R0Y5.

Expressioni

Developmental stagei

Up-regulated during late spermiogenesis, when the flagellum is being assembled.1 Publication

Gene expression databases

BgeeiQ9R0Y5.
CleanExiMM_AK1.
GenevestigatoriQ9R0Y5.

Interactioni

Subunit structurei

Monomer By similarity.UniRule annotation

Protein-protein interaction databases

BioGridi198045. 1 interaction.
IntActiQ9R0Y5. 3 interactions.
MINTiMINT-4130855.

Structurei

3D structure databases

ProteinModelPortaliQ9R0Y5.
SMRiQ9R0Y5. Positions 1-194.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni38 – 6730NMPbind By similarityAdd
BLAST
Regioni131 – 14111LID By similarityAdd
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 By similarity.UniRule annotation

Sequence similaritiesi

Phylogenomic databases

eggNOGiCOG0563.
GeneTreeiENSGT00390000016215.
HOGENOMiHOG000238771.
HOVERGENiHBG108060.
KOiK00939.
OMAiYKTINGE.
OrthoDBiEOG7060S3.
PhylomeDBiQ9R0Y5.
TreeFamiTF354283.

Family and domain databases

Gene3Di3.40.50.300. 1 hit.
HAMAPiMF_00235. Adenylate_kinase_Adk.
MF_03171. Adenylate_kinase_AK1.
InterProiIPR000850. Adenylat/UMP-CMP_kin.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR23359. PTHR23359. 1 hit.
PRINTSiPR00094. ADENYLTKNASE.
SUPFAMiSSF52540. SSF52540. 1 hit.
TIGRFAMsiTIGR01360. aden_kin_iso1. 1 hit.
PROSITEiPS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: Q9R0Y5-1) [UniParc]FASTAAdd to Basket

Also known as: Ak1a

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

MEEKLKKAKI IFVVGGPGSG KGTQCEKIVQ KYGYTHLSTG DLLRAEVSSG    50
SERGKKLSAI MEKGELVPLD TVLDMLRDAM LAKVDSSNGF LIDGYPREVK 100
QGEEFEQKIG QPTLLLYVDA GAETMTQRLL KRGETSGRVD DNEETIKKRL 150
ETYYNATEPV ISFYDKRGIV RKVNAEGTVD TVFSEVCTYL DSLK 194
Length:194
Mass (Da):21,540
Last modified:May 1, 2000 - v1
Checksum:i88E7862522967D14
GO
Isoform 2 (identifier: Q9R0Y5-2) [UniParc]FASTAAdd to Basket

Also known as: Ak1b

The sequence of this isoform differs from the canonical sequence as follows:
     1-2: ME → MGCCVSSEPQEEGGRKTG

Show »
Length:210
Mass (Da):23,116
Checksum:i5295189A6E7CB6D8
GO

Sequence cautioni

The sequence CAM16612.1 differs from that shown. Reason: Erroneous gene model prediction.

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 22ME → MGCCVSSEPQEEGGRKTG in isoform 2. VSP_024843

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ010108 mRNA. Translation: CAB52407.1.
AJ010109 mRNA. Translation: CAB52408.1.
DQ486026 mRNA. Translation: ABF46940.1.
AK046613 mRNA. Translation: BAC32808.1.
AK089270 mRNA. Translation: BAC40822.1.
AL772271 Genomic DNA. Translation: CAM16612.1. Sequence problems.
AL772271 Genomic DNA. Translation: CAM16613.1.
AL772271 Genomic DNA. Translation: CAM16614.1.
BC014802 mRNA. Translation: AAH14802.1.
BC054366 mRNA. Translation: AAH54366.1.
CCDSiCCDS15924.1. [Q9R0Y5-2]
CCDS57167.1. [Q9R0Y5-1]
RefSeqiNP_001185719.1. NM_001198790.1. [Q9R0Y5-1]
NP_001185720.1. NM_001198791.1. [Q9R0Y5-1]
NP_001185721.1. NM_001198792.1. [Q9R0Y5-1]
NP_067490.1. NM_021515.3. [Q9R0Y5-2]
XP_006497687.1. XM_006497624.1. [Q9R0Y5-1]
UniGeneiMm.29189.

Genome annotation databases

EnsembliENSMUST00000068271; ENSMUSP00000068479; ENSMUSG00000026817. [Q9R0Y5-2]
ENSMUST00000113277; ENSMUSP00000108902; ENSMUSG00000026817. [Q9R0Y5-1]
ENSMUST00000113278; ENSMUSP00000108903; ENSMUSG00000026817. [Q9R0Y5-1]
GeneIDi11636.
KEGGimmu:11636.
UCSCiuc008jgh.2. mouse. [Q9R0Y5-1]
uc008jgj.2. mouse. [Q9R0Y5-2]

Keywords - Coding sequence diversityi

Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
AJ010108 mRNA. Translation: CAB52407.1 .
AJ010109 mRNA. Translation: CAB52408.1 .
DQ486026 mRNA. Translation: ABF46940.1 .
AK046613 mRNA. Translation: BAC32808.1 .
AK089270 mRNA. Translation: BAC40822.1 .
AL772271 Genomic DNA. Translation: CAM16612.1 . Sequence problems.
AL772271 Genomic DNA. Translation: CAM16613.1 .
AL772271 Genomic DNA. Translation: CAM16614.1 .
BC014802 mRNA. Translation: AAH14802.1 .
BC054366 mRNA. Translation: AAH54366.1 .
CCDSi CCDS15924.1. [Q9R0Y5-2 ]
CCDS57167.1. [Q9R0Y5-1 ]
RefSeqi NP_001185719.1. NM_001198790.1. [Q9R0Y5-1 ]
NP_001185720.1. NM_001198791.1. [Q9R0Y5-1 ]
NP_001185721.1. NM_001198792.1. [Q9R0Y5-1 ]
NP_067490.1. NM_021515.3. [Q9R0Y5-2 ]
XP_006497687.1. XM_006497624.1. [Q9R0Y5-1 ]
UniGenei Mm.29189.

3D structure databases

ProteinModelPortali Q9R0Y5.
SMRi Q9R0Y5. Positions 1-194.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 198045. 1 interaction.
IntActi Q9R0Y5. 3 interactions.
MINTi MINT-4130855.

PTM databases

PhosphoSitei Q9R0Y5.

2D gel databases

REPRODUCTION-2DPAGE IPI00128209.
Q9R0Y5.

Proteomic databases

MaxQBi Q9R0Y5.
PaxDbi Q9R0Y5.
PRIDEi Q9R0Y5.

Protocols and materials databases

Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENSMUST00000068271 ; ENSMUSP00000068479 ; ENSMUSG00000026817 . [Q9R0Y5-2 ]
ENSMUST00000113277 ; ENSMUSP00000108902 ; ENSMUSG00000026817 . [Q9R0Y5-1 ]
ENSMUST00000113278 ; ENSMUSP00000108903 ; ENSMUSG00000026817 . [Q9R0Y5-1 ]
GeneIDi 11636.
KEGGi mmu:11636.
UCSCi uc008jgh.2. mouse. [Q9R0Y5-1 ]
uc008jgj.2. mouse. [Q9R0Y5-2 ]

Organism-specific databases

CTDi 203.
MGIi MGI:87977. Ak1.

Phylogenomic databases

eggNOGi COG0563.
GeneTreei ENSGT00390000016215.
HOGENOMi HOG000238771.
HOVERGENi HBG108060.
KOi K00939.
OMAi YKTINGE.
OrthoDBi EOG7060S3.
PhylomeDBi Q9R0Y5.
TreeFami TF354283.

Enzyme and pathway databases

BRENDAi 2.7.4.3. 3474.

Miscellaneous databases

NextBioi 279205.
PROi Q9R0Y5.
SOURCEi Search...

Gene expression databases

Bgeei Q9R0Y5.
CleanExi MM_AK1.
Genevestigatori Q9R0Y5.

Family and domain databases

Gene3Di 3.40.50.300. 1 hit.
HAMAPi MF_00235. Adenylate_kinase_Adk.
MF_03171. Adenylate_kinase_AK1.
InterProi IPR000850. Adenylat/UMP-CMP_kin.
IPR028582. AK1.
IPR006267. AK1/5.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR23359. PTHR23359. 1 hit.
PRINTSi PR00094. ADENYLTKNASE.
SUPFAMi SSF52540. SSF52540. 1 hit.
TIGRFAMsi TIGR01360. aden_kin_iso1. 1 hit.
PROSITEi PS00113. ADENYLATE_KINASE. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "wt p53 dependent expression of a membrane-associated isoform of adenylate kinase."
    Collavin L., Lazarevic D., Utrera R., Marzinotto S., Monte M., Schneider C.
    Oncogene 18:5879-5888(1999) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1 AND 2).
  2. "Adenylate kinases 1 and 2 are part of the accessory structures in the mouse sperm flagellum."
    Cao W., Haig-Ladewig L., Gerton G.L., Moss S.B.
    Biol. Reprod. 75:492-500(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), FUNCTION, DEVELOPMENTAL STAGE.
    Strain: CD-1.
  3. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
    Strain: C57BL/6J and NOD.
    Tissue: Adipose tissue.
  4. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  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] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORMS 1 AND 2).
    Strain: C57BL/6 and FVB/N.
    Tissue: Mammary tumor and Retina.
  6. Lubec G., Klug S.
    Submitted (MAR-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 32-44; 64-77; 84-97 AND 150-166, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Hippocampus.
  7. "Comprehensive identification of phosphorylation sites in postsynaptic density preparations."
    Trinidad J.C., Specht C.G., Thalhammer A., Schoepfer R., Burlingame A.L.
    Mol. Cell. Proteomics 5:914-922(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain.

Entry informationi

Entry nameiKAD1_MOUSE
AccessioniPrimary (citable) accession number: Q9R0Y5
Secondary accession number(s): A2AK80, Q542C5, Q9R0Y4
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 4, 2001
Last sequence update: May 1, 2000
Last modified: July 9, 2014
This is version 118 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3

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