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Reviewed, UniProtKB/Swiss-Prot O43572 (AKA10_HUMAN)

Last modified December 16, 2008. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (5) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    A kinase anchor protein 10, mitochondrial
Alternative name(s):
    Protein kinase A-anchoring protein 10
      Short name=PRKA10
    Dual specificity A kinase-anchoring protein 2
      Short name=D-AKAP-2
Gene names
Name: AKAP10
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length662 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Differentially targeted protein that binds to type I and II regulatory subunits of protein kinase A and anchors them to the mitochondria or the plasma membrane. Although the physiological relevance between PKA and AKAPS with mitochondria is not fully understood, one idea is that BAD, a proapoptotic member, is phosphorylated and inactivated by mitochondria-anchored PKA. It cannot be excluded too that it may facilitate PKA as well as G protein signal transduction, by acting as an adapter for assembling multiprotein complexes. With its RGS domain, it could lead to the interaction to G-alpha proteins, providing a link between the signaling machinery and the downstream kinase By similarity.

Subcellular location

Mitochondrion. Membrane. Cytoplasm. Note= Predominantly mitochondrial but also membrane associated and cytoplasmic. Ref.1

Domain

RII-alpha binding site, predicted to form an amphipathic helix, could participate in protein-protein interactions with a complementary surface on the R-subunit dimer.

Sequence similarities

Contains 2 RGS domains.

Ontologies

Keywords

   Cellular componentCytoplasm
Membrane
Mitochondrion
   Coding sequence diversityPolymorphism
   DomainRepeat
Transit peptide
   PTMPhosphoprotein

Gene Ontology (GO)

   Biological processprotein localization

Traceable author statement. Source: ProtInc

signal transduction

Traceable author statement. Source: ProtInc

   Cellular componentmembrane

Inferred from electronic annotation. Source: UniProtKB-KW

mitochondrion

Inferred from electronic annotation. Source: UniProtKB-KW

   Molecular functionprotein binding

Traceable author statement. Source: ProtInc

signal transducer activity

Inferred from electronic annotation. Source: InterPro

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Transit peptide1 – 2828Mitochondrion Potential
Chain29 – 662634A kinase anchor protein 10, mitochondrial
PRO_0000030404

Regions

Domain125 – 369245RGS 1
Domain379 – 505127RGS 2
Region634 – 64714PKA-RII subunit binding

Amino acid modifications

Modified residue521Phosphoserine Ref.4
Modified residue1871Phosphoserine Ref.4

Natural variations

Natural variant2491R → H: dbSNP rs2108978.
VAR_024607
Natural variant6461I → V: dbSNP rs203462.
VAR_024608

Experimental info

Sequence conflict1771V → M in AAB92260. Ref.2
Sequence conflict5241L → P in AAB92260. Ref.2

Sequences

Sequence LengthMass (Da)Tools
O43572-1 [UniParc].

Last modified July 19, 2005. Version 2.
Checksum: B7A6D92CA2D3D794

FASTA66273,818
        10         20         30         40         50         60 
MRGAGPSPRQ SPRTLRPDPG PAMSFFRRKV KGKEQEKTSD VKSIKASISV HSPQKSTKNH 

        70         80         90        100        110        120 
ALLEAAGPSH VAINAISANM DSFSSSRTAT LKKQPSHMEA AHFGDLGRSC LDYQTQETKS 

       130        140        150        160        170        180 
SLSKTLEQVL HDTIVLPYFI QFMELRRMEH LVKFWLEAES FHSTTWSRIR AHSLNTVKQS 

       190        200        210        220        230        240 
SLAEPVSPSK KHETTASFLT DSLDKRLEDS GSAQLFMTHS EGIDLNNRTN STQNHLLLSQ 

       250        260        270        280        290        300 
ECDSAHSLRL EMARAGTHQV SMETQESSST LTVASRNSPA SPLKELSGKL MKSIEQDAVN 

       310        320        330        340        350        360 
TFTKYISPDA AKPIPITEAM RNDIIARICG EDGQVDPNCF VLAQSIVFSA MEQEHFSEFL 

       370        380        390        400        410        420 
RSHHFCKYQI EVLTSGTVYL ADILFCESAL FYFSEYMEKE DAVNILQFWL AADNFQSQLA 

       430        440        450        460        470        480 
AKKGQYDGQE AQNDAMILYD KYFSLQATHP LGFDDVVRLE IESNICREGG PLPNCFTTPL 

       490        500        510        520        530        540 
RQAWTTMEKV FLPGFLSSNL YYKYLNDLIH SVRGDEFLGG NVSLTAPGSV GPPDESHPGS 

       550        560        570        580        590        600 
SDSSASQSSV KKASIKILKN FDEAIIVDAA SLDPESLYQR TYAGKMTFGR VSDLGQFIRE 

       610        620        630        640        650        660 
SEPEPDVRKS KGSMFSQAMK KWVQGNTDEA QEELAWKIAK MIVSDIMQQA QYDQPLEKST 


KL 

« Hide

References

« Hide 'large scale' references
[1]"Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein."
Wang L., Sunahara R.K., Krumins A., Perkins G., Crochiere M.L., Mackey M., Bell S., Ellisman M.H., Taylor S.S.
Proc. Natl. Acad. Sci. U.S.A. 98:3220-3225(2001) [PubMed: 11248059] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], SUBCELLULAR LOCATION.
Tissue: Brain.
[2]"Homo sapiens protein kinase A anchoring protein with an RGS domain."
Chatterjee T.K., Fisher R.A.
Submitted (DEC-1997) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]"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: Lung.
[4]"Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
Mol. Cell 31:438-448(2008) [PubMed: 18691976] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-52 AND SER-187, MASS SPECTROMETRY.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF037439 mRNA. Translation: AAB92260.1.
BC017055 mRNA. Translation: AAH17055.1.
RefSeqNP_009133.2.
UniGeneHs.694769

3D structure databases

ModBaseSearch...

Protein-protein interaction databases

IntActO43572. 1 interaction.

PTM databases

PhosphoSiteO43572.

Proteomic databases

PRIDEO43572.

Genome annotation databases

EnsemblENSG00000108599. Homo sapiens. [Contig view]
GeneID11216.
KEGGhsa:11216.

Organism-specific databases

GeneCardsGC17M019749.
H-InvDBHIX0017647.
HGNCHGNC:368. AKAP10.
MIM604694. gene.
PharmGKBPA24662.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO43572.
HOVERGENO43572.

Gene expression databases

ArrayExpressO43572.
CleanExHS_AKAP10.
GermOnlineENSG00000108599. Homo sapiens.

Family and domain databases

InterProIPR000342. Regulat_G_prot_signal.
[Graphical view]
SMARTSM00315. RGS. 2 hits.
[Graphical view]
PROSITEPS50132. RGS. 2 hits.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio42691.
SOURCESearch...

Entry information

Entry nameAKA10_HUMAN
AccessionPrimary (citable) accession number: O43572
Secondary accession number(s): Q96AJ7
Entry history
Integrated into UniProtKB/Swiss-Prot: February 21, 2001
Last sequence update: July 19, 2005
Last modified: December 16, 2008
This is version 65 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 17

Human chromosome 17: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents