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Protein

A-kinase anchor protein 2

Gene

Akap2

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-Experimental evidence at protein leveli

Functioni

Binds to regulatory subunit (RII) of protein kinase A. May be involved in establishing polarity in signaling systems or in integrating PKA-RII isoforms with downstream effectors to capture, amplify and focus diffuse, trans-cellular signals carried by cAMP.

GO - Molecular functioni

  • protein kinase A binding Source: MGI

GO - Biological processi

  • actin filament organization Source: MGI
  • protein localization Source: MGI
  • transmembrane receptor protein serine/threonine kinase signaling pathway Source: MGI
Complete GO annotation...

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 2
Short name:
AKAP-2
Alternative name(s):
AKAP expressed in kidney and lung
Short name:
AKAP-KL
Protein kinase A-anchoring protein 2
Short name:
PRKA2
Gene namesi
Name:Akap2
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 4

Organism-specific databases

MGIiMGI:1306795. Akap2.

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi590 – 5901A → S: No effect on binding to RII. 1 Publication
Mutagenesisi598 – 5981I → A: Reduces binding to RII. 1 Publication

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 893893A-kinase anchor protein 2PRO_0000020657Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei33 – 331PhosphoserineCombined sources
Modified residuei44 – 441PhosphoserineCombined sources
Modified residuei122 – 1221PhosphoserineBy similarity
Modified residuei152 – 1521PhosphoserineBy similarity
Cross-linki174 – 174Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1)By similarity
Modified residuei357 – 3571PhosphoserineBy similarity
Modified residuei482 – 4821PhosphoserineCombined sources
Modified residuei486 – 4861PhosphoserineBy similarity
Modified residuei494 – 4941PhosphoserineCombined sources
Modified residuei538 – 5381PhosphoserineBy similarity
Modified residuei547 – 5471PhosphothreonineBy similarity
Modified residuei634 – 6341PhosphothreonineCombined sources
Modified residuei651 – 6511PhosphoserineCombined sources
Modified residuei740 – 7401PhosphoserineCombined sources
Modified residuei768 – 7681PhosphoserineBy similarity
Modified residuei799 – 7991PhosphoserineCombined sources
Modified residuei806 – 8061PhosphoserineBy similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiO54931.
MaxQBiO54931.
PaxDbiO54931.
PeptideAtlasiO54931.
PRIDEiO54931.

PTM databases

iPTMnetiO54931.
PhosphoSiteiO54931.

Expressioni

Tissue specificityi

Highly expressed in lung and weakly in thymus and cerebellum. Little or no expression in liver, heart and cerebral cortex. All isoforms are expressed in lung, but KL2A and KL2B isoforms are the principal isoforms in cerebellum.

Gene expression databases

BgeeiO54931.
CleanExiMM_AKAP2.
ExpressionAtlasiO54931. baseline and differential.
GenevisibleiO54931. MM.

Interactioni

Binary interactionsi

WithEntry#Exp.IntActNotes
Prkar2aP123673EBI-645828,EBI-645747

GO - Molecular functioni

  • protein kinase A binding Source: MGI

Protein-protein interaction databases

BioGridi198049. 1 interaction.
IntActiO54931. 3 interactions.
MINTiMINT-1734029.

Structurei

3D structure databases

ProteinModelPortaliO54931.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni586 – 59914PKA-RII subunit binding domainAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili255 – 31662Sequence analysisAdd
BLAST
Coiled coili729 – 76638Sequence analysisAdd
BLAST

Compositional bias

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Compositional biasi274 – 31138Gln-richAdd
BLAST

Domaini

The 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.

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiENOG410IG9A. Eukaryota.
ENOG410ZMFZ. LUCA.
GeneTreeiENSGT00530000063206.
HOGENOMiHOG000231745.
HOVERGENiHBG050477.
InParanoidiO54931.
KOiK16519.
PhylomeDBiO54931.
TreeFamiTF105402.

Family and domain databases

InterProiIPR029304. AKAP2_C.
[Graphical view]
PfamiPF15304. AKAP2_C. 1 hit.
[Graphical view]

Sequences (5)i

Sequence statusi: Complete.

This entry describes 5 isoformsi produced by alternative splicing and alternative initiation. AlignAdd to basket

Isoform 1 (identifier: O54931-1) [UniParc]FASTAAdd to basket

Also known as: KL1A

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

        10         20         30         40         50
MEIGVSVAEC KSVPGVTSTP HSKDHSSPFY SPSHNGLLAD HHESLDNDVA
60 70 80 90 100
REIQYLDEVL EANCCDSSVD GTYNGISSPE PGAAILVSSL GSPAHSVTEA
110 120 130 140 150
EPTEKASGRQ VPPHIELSRS PSDRMAEGER ANGHSTDQPQ DLLGNSLQAP
160 170 180 190 200
ASPSSSTSSH CSSRDGEFTL TTLKKEAKFE LRAFHEDKKP SKLFEEDERE
210 220 230 240 250
KEQFCVRKVR PSEEMIELEK ERRELIRSQA VKKNPGIAAK WWNPPQEKTI
260 270 280 290 300
EEQLDEEHLE SHRKYKERKE KRAQQEQLQL QQQQQQQLQQ QQLQQQQLQQ
310 320 330 340 350
QQLQQQLQQQ QLSTSQPCTA PAAHKHLDGI EHTKEDVVTE QIDFSAARKQ
360 370 380 390 400
FQLMENSRQT LAKGQSTPRL FSIKPYYKPL GSIHSDKPPT ILRPATVGGT
410 420 430 440 450
LEDGGTQAAK EQKAPCVSES QSAGAGPANA ATQGKEGPYS EPSKRGPLSK
460 470 480 490 500
LWAEDGEFTS ARAVLTVVKD EDHGILDQFS RSVNVSLTQE ELDSGLDELS
510 520 530 540 550
VRSQDTTVLE TLSNDFSMDN ISDSGASNET PSALQENSLA DFSLPQTPQT
560 570 580 590 600
DNPSEGREGV SKSFSDHGFY SPSSTLGDSP SVDDPLEYQA GLLVQNAIQQ
610 620 630 640 650
AIAEQVDKAE AHTSKEGSEQ QEPEATVEEA GSQTPGSEKP QGMFAPPQVS
660 670 680 690 700
SPVQEKRDIL PKNLPAEDRA LREKGPSQPP TAAQPSGPVN MEETRPEGGY
710 720 730 740 750
FSKYSEAAEL RSTASLLATQ ESDVMVGPFK LRSRKQRTLS MIEEEIRAAQ
760 770 780 790 800
EREEELKRQR QVRQSTPSPR AKNAPSLPSR TTCYKTAPGK IEKVKPPPSP
810 820 830 840 850
TTEGPSLQPD LAPEEAAGTQ RPKNLMQTLM EDYETHKSKR RERMDDSSYT
860 870 880 890
SKLLSCKVTS EVLEATRVNR RKSALALRWE AGIYANQEEE DNE
Length:893
Mass (Da):98,579
Last modified:July 28, 2009 - v3
Checksum:i4C9ADD7C4362EF49
GO
Isoform 2 (identifier: O54931-2) [UniParc]FASTAAdd to basket

Also known as: KL2A

The sequence of this isoform differs from the canonical sequence as follows:
     849-861: Missing.

Note: Produced by alternative splicing.
Show »
Length:880
Mass (Da):97,138
Checksum:i1CD1888BA492C55D
GO
Isoform 3 (identifier: O54931-3) [UniParc]FASTAAdd to basket

Also known as: KL3A

The sequence of this isoform differs from the canonical sequence as follows:
     790-795: KIEKVK → PGGHTG
     796-893: Missing.

Note: Produced by alternative splicing.
Show »
Length:795
Mass (Da):87,270
Checksum:i6BB58D5EABDF283A
GO
Isoform 4 (identifier: O54931-4) [UniParc]FASTAAdd to basket

Also known as: KL1B

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: Missing.

Note: Produced by alternative initiation at Met-125 of isoform KL1A.
Show »
Length:769
Mass (Da):85,517
Checksum:i6EF28D2ACAEFDB47
GO
Isoform 5 (identifier: O54931-5) [UniParc]FASTAAdd to basket

Also known as: KL2B

The sequence of this isoform differs from the canonical sequence as follows:
     1-124: Missing.
     849-861: Missing.

Note: Produced by alternative initiation at Met-125 of isoform KL2A.
Show »
Length:756
Mass (Da):84,077
Checksum:iC30DF3CEC4058A6A
GO

Sequence cautioni

The sequence AAC02206.1 differs from that shown. Reason: Frameshift at position 875. Curated
The sequence AAC02207.1 differs from that shown. Reason: Frameshift at position 875. Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti120 – 1201S → I in AAC02206 (PubMed:9497389).Curated
Sequence conflicti120 – 1201S → I in AAC02207 (PubMed:9497389).Curated
Sequence conflicti120 – 1201S → I in AAC02208 (PubMed:9497389).Curated
Sequence conflicti264 – 2641K → R in AAC02206 (PubMed:9497389).Curated
Sequence conflicti264 – 2641K → R in AAC02207 (PubMed:9497389).Curated
Sequence conflicti264 – 2641K → R in AAC02208 (PubMed:9497389).Curated
Sequence conflicti531 – 5311P → T in AAC02206 (PubMed:9497389).Curated
Sequence conflicti531 – 5311P → T in AAC02207 (PubMed:9497389).Curated
Sequence conflicti531 – 5311P → T in AAC02208 (PubMed:9497389).Curated

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 124124Missing in isoform 4 and isoform 5. CuratedVSP_018776Add
BLAST
Alternative sequencei790 – 7956KIEKVK → PGGHTG in isoform 3. 1 PublicationVSP_004097
Alternative sequencei796 – 89398Missing in isoform 3. 1 PublicationVSP_004098Add
BLAST
Alternative sequencei849 – 86113Missing in isoform 2 and isoform 5. 2 PublicationsVSP_004099Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033274 mRNA. Translation: AAC02206.1. Frameshift.
AF033275 mRNA. Translation: AAC02207.1. Frameshift.
AF033276 mRNA. Translation: AAC02208.1.
AK077020 mRNA. Translation: BAC36571.1.
AK147420 mRNA. Translation: BAE27901.1.
AL840629 Genomic DNA. Translation: CAM21291.1.
AL840629 Genomic DNA. Translation: CAM21292.1.
CCDSiCCDS18203.1. [O54931-2]
CCDS18204.1. [O54931-1]
CCDS18205.1. [O54931-3]
PIRiT09225.
RefSeqiNP_001030609.1. NM_001035532.2. [O54931-2]
NP_001030610.1. NM_001035533.2. [O54931-1]
NP_001291473.1. NM_001304544.1.
UniGeneiMm.331630.
Mm.467752.

Genome annotation databases

EnsembliENSMUST00000043456; ENSMUSP00000048678; ENSMUSG00000038729. [O54931-1]
ENSMUST00000098064; ENSMUSP00000095672; ENSMUSG00000038729. [O54931-2]
ENSMUST00000102902; ENSMUSP00000099966; ENSMUSG00000038729. [O54931-3]
ENSMUST00000102903; ENSMUSP00000099967; ENSMUSG00000038729. [O54931-3]
ENSMUST00000107598; ENSMUSP00000103224; ENSMUSG00000089945. [O54931-2]
GeneIDi11641.
677884.
KEGGimmu:11641.
mmu:677884.
UCSCiuc008syj.2. mouse. [O54931-2]
uc008syk.2. mouse. [O54931-3]
uc008syl.2. mouse. [O54931-1]

Keywords - Coding sequence diversityi

Alternative initiation, Alternative splicing

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AF033274 mRNA. Translation: AAC02206.1. Frameshift.
AF033275 mRNA. Translation: AAC02207.1. Frameshift.
AF033276 mRNA. Translation: AAC02208.1.
AK077020 mRNA. Translation: BAC36571.1.
AK147420 mRNA. Translation: BAE27901.1.
AL840629 Genomic DNA. Translation: CAM21291.1.
AL840629 Genomic DNA. Translation: CAM21292.1.
CCDSiCCDS18203.1. [O54931-2]
CCDS18204.1. [O54931-1]
CCDS18205.1. [O54931-3]
PIRiT09225.
RefSeqiNP_001030609.1. NM_001035532.2. [O54931-2]
NP_001030610.1. NM_001035533.2. [O54931-1]
NP_001291473.1. NM_001304544.1.
UniGeneiMm.331630.
Mm.467752.

3D structure databases

ProteinModelPortaliO54931.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi198049. 1 interaction.
IntActiO54931. 3 interactions.
MINTiMINT-1734029.

PTM databases

iPTMnetiO54931.
PhosphoSiteiO54931.

Proteomic databases

EPDiO54931.
MaxQBiO54931.
PaxDbiO54931.
PeptideAtlasiO54931.
PRIDEiO54931.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000043456; ENSMUSP00000048678; ENSMUSG00000038729. [O54931-1]
ENSMUST00000098064; ENSMUSP00000095672; ENSMUSG00000038729. [O54931-2]
ENSMUST00000102902; ENSMUSP00000099966; ENSMUSG00000038729. [O54931-3]
ENSMUST00000102903; ENSMUSP00000099967; ENSMUSG00000038729. [O54931-3]
ENSMUST00000107598; ENSMUSP00000103224; ENSMUSG00000089945. [O54931-2]
GeneIDi11641.
677884.
KEGGimmu:11641.
mmu:677884.
UCSCiuc008syj.2. mouse. [O54931-2]
uc008syk.2. mouse. [O54931-3]
uc008syl.2. mouse. [O54931-1]

Organism-specific databases

CTDi11217.
677884.
MGIiMGI:1306795. Akap2.

Phylogenomic databases

eggNOGiENOG410IG9A. Eukaryota.
ENOG410ZMFZ. LUCA.
GeneTreeiENSGT00530000063206.
HOGENOMiHOG000231745.
HOVERGENiHBG050477.
InParanoidiO54931.
KOiK16519.
PhylomeDBiO54931.
TreeFamiTF105402.

Miscellaneous databases

ChiTaRSiAkap2. mouse.
PROiO54931.
SOURCEiSearch...

Gene expression databases

BgeeiO54931.
CleanExiMM_AKAP2.
ExpressionAtlasiO54931. baseline and differential.
GenevisibleiO54931. MM.

Family and domain databases

InterProiIPR029304. AKAP2_C.
[Graphical view]
PfamiPF15304. AKAP2_C. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular characterization of a cDNA that encodes six isoforms of a novel murine A kinase anchor protein."
    Dong F., Feldmesser M., Casadevall A., Rubin C.S.
    J. Biol. Chem. 273:6533-6541(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORMS 1; 2 AND 3), ALTERNATIVE SPLICING (ISOFORMS 4 AND 5), MUTAGENESIS OF ALA-590 AND ILE-598.
    Tissue: Brain.
  2. "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 2).
    Strain: C57BL/6J.
    Tissue: Testis.
  3. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  4. "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.
  5. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
    Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
    Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-799, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-33; SER-44; SER-482; SER-494; THR-634; SER-651 AND SER-740, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Brain, Brown adipose tissue, Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.

Entry informationi

Entry nameiAKAP2_MOUSE
AccessioniPrimary (citable) accession number: O54931
Secondary accession number(s): A2APJ4
, O54932, O54933, Q8C5W1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: April 27, 2001
Last sequence update: July 28, 2009
Last modified: July 6, 2016
This is version 132 of the entry and version 3 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.