AKAP10

Protein-coding gene in the species Homo sapiens
AKAP10
Available structures
PDBOrtholog search: PDBe RCSB
List of PDB id codes

3IM4, 3TMH

Identifiers
AliasesAKAP10, AKAP-10, D-AKAP-2, D-AKAP2, PRKA10, A-kinase anchoring protein 10
External IDsOMIM: 604694; MGI: 1890218; HomoloGene: 32452; GeneCards: AKAP10; OMA:AKAP10 - orthologs
Gene location (Mouse)
Chromosome 11 (mouse)
Chr.Chromosome 11 (mouse)[1]
Chromosome 11 (mouse)
Genomic location for AKAP10
Genomic location for AKAP10
Band11|11 B2Start61,762,133 bp[1]
End61,821,078 bp[1]
RNA expression pattern
Bgee
HumanMouse (ortholog)
Top expressed in
  • sural nerve

  • Achilles tendon

  • trabecular bone

  • monocyte

  • nipple

  • blood

  • optic nerve

  • bone marrow cells

  • visceral pleura

  • pancreatic ductal cell
Top expressed in
  • spermatid

  • endocardial cushion

  • zygote

  • secondary oocyte

  • renal corpuscle

  • medullary collecting duct

  • Rostral migratory stream

  • seminiferous tubule

  • spermatocyte

  • primary oocyte
More reference expression data
BioGPS


More reference expression data
Gene ontology
Molecular function
  • protein binding
  • protein kinase A binding
Cellular component
  • plasma membrane
  • membrane
  • mitochondrion
  • cytoplasm
  • cytosol
  • protein-containing complex
Biological process
  • blood coagulation
  • signal transduction
  • protein localization
Sources:Amigo / QuickGO
Orthologs
SpeciesHumanMouse
Entrez

11216

56697

Ensembl

n/a

ENSMUSG00000047804

UniProt

O43572

O88845

RefSeq (mRNA)

NM_007202
NM_001330152

NM_019921

RefSeq (protein)

NP_001317081
NP_009133

NP_064305

Location (UCSC)n/aChr 11: 61.76 – 61.82 Mb
PubMed search[2][3]
Wikidata
View/Edit HumanView/Edit Mouse

A kinase anchor protein 10, mitochondrial is an enzyme that in humans is encoded by the AKAP10 gene.[4][5]

Function

The A-kinase anchor proteins (AKAPs) are a group of structurally diverse proteins, which have the common function of binding to the regulatory subunit of protein kinase A (PKA) and confining the holoenzyme to discrete locations within the cell. This gene encodes a member of the AKAP family. The encoded protein interacts with both the type I and type II regulatory subunits of PKA; therefore, it is a dual-specific AKAP. This protein is highly enriched in mitochondria. It contains RGS (regulator of G protein signalling) domains, in addition to a PKA-RII subunit-binding domain. The mitochondrial localization and the presence of RGS domains may have important implications for the function of this protein in PKA and G protein signal transduction.[5]

Interactions

AKAP10 has been shown to interact with PDZK1[6] and PRKAR1A.[4][7]

References

  1. ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000047804 – Ensembl, May 2017
  2. ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  3. ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
  4. ^ a b Huang LJ, Durick K, Weiner JA, Chun J, Taylor SS (November 1997). "D-AKAP2, a novel protein kinase A anchoring protein with a putative RGS domain". Proc. Natl. Acad. Sci. U.S.A. 94 (21): 11184–9. Bibcode:1997PNAS...9411184H. doi:10.1073/pnas.94.21.11184. PMC 23409. PMID 9326583.
  5. ^ a b "Entrez Gene: AKAP10 A kinase (PRKA) anchor protein 10".
  6. ^ Gisler SM, Pribanic S, Bacic D, Forrer P, Gantenbein A, Sabourin LA, Tsuji A, Zhao ZS, Manser E, Biber J, Murer H (November 2003). "PDZK1: I. a major scaffolder in brush borders of proximal tubular cells". Kidney Int. 64 (5): 1733–45. doi:10.1046/j.1523-1755.2003.00266.x. PMID 14531806.
  7. ^ Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (October 2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.

External links

Further reading

  • Lester LB, Scott JD (1997). "Anchoring and scaffold proteins for kinases and phosphatases". Recent Prog. Horm. Res. 52: 409–29, discussion 429–30. PMID 9238861.
  • Michel JJ, Scott JD (2002). "AKAP mediated signal transduction". Annu. Rev. Pharmacol. Toxicol. 42: 235–57. doi:10.1146/annurev.pharmtox.42.083101.135801. PMID 11807172.
  • Epplen C, Epplen JT (1994). "Expression of (cac)n/(gtg)n simple repetitive sequences in mRNA of human lymphocytes". Hum. Genet. 93 (1): 35–41. doi:10.1007/BF00218910. PMID 7505766. S2CID 22998633.
  • Wang L, Sunahara RK, Krumins A, Perkins G, Crochiere ML, Mackey M, Bell S, Ellisman MH, Taylor SS (2001). "Cloning and mitochondrial localization of full-length D-AKAP2, a protein kinase A anchoring protein". Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3220–5. Bibcode:2001PNAS...98.3220W. doi:10.1073/pnas.051633398. PMC 30634. PMID 11248059.
  • Hamuro Y, Burns L, Canaves J, Hoffman R, Taylor S, Woods V (2002). "Domain organization of D-AKAP2 revealed by enhanced deuterium exchange-mass spectrometry (DXMS)". J. Mol. Biol. 321 (4): 703–14. CiteSeerX 10.1.1.477.4850. doi:10.1016/S0022-2836(02)00419-9. PMID 12206784.
  • Kammerer S, Burns-Hamuro LL, Ma Y, Hamon SC, Canaves JM, Shi MM, Nelson MR, Sing CF, Cantor CR, Taylor SS, Braun A (2003). "Amino acid variant in the kinase binding domain of dual-specific A kinase-anchoring protein 2: a disease susceptibility polymorphism". Proc. Natl. Acad. Sci. U.S.A. 100 (7): 4066–71. Bibcode:2003PNAS..100.4066K. doi:10.1073/pnas.2628028100. PMC 153049. PMID 12646697.
  • Gisler SM, Pribanic S, Bacic D, Forrer P, Gantenbein A, Sabourin LA, Tsuji A, Zhao ZS, Manser E, Biber J, Murer H (2003). "PDZK1: I. a major scaffolder in brush borders of proximal tubular cells". Kidney Int. 64 (5): 1733–45. doi:10.1046/j.1523-1755.2003.00266.x. PMID 14531806.
  • Burns-Hamuro LL, Barraclough DM, Taylor SS (2004). "Identification and Functional Analysis of Dual-Specific a Kinase-Anchoring Protein-2". Regulators of G-Protein Signaling, Part B. Methods in Enzymology. Vol. 390. Academic Press. pp. 354–74. doi:10.1016/S0076-6879(04)90022-5. ISBN 978-0-12-182795-3. PMID 15488188.
  • Rual JF, Venkatesan K, Hao T, Hirozane-Kishikawa T, Dricot A, Li N, Berriz GF, Gibbons FD, Dreze M, Ayivi-Guedehoussou N, Klitgord N, Simon C, Boxem M, Milstein S, Rosenberg J, Goldberg DS, Zhang LV, Wong SL, Franklin G, Li S, Albala JS, Lim J, Fraughton C, Llamosas E, Cevik S, Bex C, Lamesch P, Sikorski RS, Vandenhaute J, Zoghbi HY, Smolyar A, Bosak S, Sequerra R, Doucette-Stamm L, Cusick ME, Hill DE, Roth FP, Vidal M (2005). "Towards a proteome-scale map of the human protein-protein interaction network". Nature. 437 (7062): 1173–8. Bibcode:2005Natur.437.1173R. doi:10.1038/nature04209. PMID 16189514. S2CID 4427026.
  • Tingley WG, Pawlikowska L, Zaroff JG, Kim T, Nguyen T, Young SG, Vranizan K, Kwok PY, Whooley MA, Conklin BR (2007). "Gene-trapped mouse embryonic stem cell-derived cardiac myocytes and human genetics implicate AKAP10 in heart rhythm regulation". Proc. Natl. Acad. Sci. U.S.A. 104 (20): 8461–6. Bibcode:2007PNAS..104.8461T. doi:10.1073/pnas.0610393104. PMC 1866184. PMID 17485678.


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