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UniProtKB - Q5U301 (AKAP2_RAT)
Protein
A-kinase anchor protein 2
Gene
Akap2
Organism
Rattus norvegicus (Rat)
Status
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 (By similarity).
By similarityGO - Molecular functioni
- protein-containing complex binding Source: RGD
- protein domain specific binding Source: RGD
- protein kinase A binding Source: RGD
GO - Biological processi
- actin filament organization Source: RGD
- protein localization Source: RGD
- transmembrane receptor protein serine/threonine kinase signaling pathway Source: RGD
Names & Taxonomyi
Protein namesi | Recommended name: A-kinase anchor protein 2Short name: AKAP-2 |
Gene namesi | Name:Akap2 |
Organismi | Rattus norvegicus (Rat) |
Taxonomic identifieri | 10116 [NCBI] |
Taxonomic lineagei | Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Glires › Rodentia › Myomorpha › Muroidea › Muridae › Murinae › Rattus |
Proteomesi |
|
Organism-specific databases
RGDi | 1305135, Akap2 |
PTM / Processingi
Molecule processing
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
ChainiPRO_0000380090 | 1 – 870 | A-kinase anchor protein 2Add BLAST | 870 |
Amino acid modifications
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Modified residuei | 122 | PhosphoserineCombined sources | 1 | |
Modified residuei | 152 | PhosphoserineBy similarity | 1 | |
Cross-linki | 174 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO1); alternateBy similarity | ||
Cross-linki | 174 | Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2); alternateBy similarity | ||
Modified residuei | 347 | PhosphoserineCombined sources | 1 | |
Modified residuei | 472 | PhosphoserineBy similarity | 1 | |
Modified residuei | 476 | PhosphoserineCombined sources | 1 | |
Modified residuei | 528 | PhosphoserineBy similarity | 1 | |
Modified residuei | 537 | PhosphothreonineBy similarity | 1 | |
Modified residuei | 641 | PhosphoserineCombined sources | 1 | |
Modified residuei | 730 | PhosphoserineCombined sources | 1 | |
Modified residuei | 758 | PhosphoserineBy similarity | 1 | |
Modified residuei | 789 | PhosphoserineBy similarity | 1 | |
Modified residuei | 796 | PhosphoserineBy similarity | 1 |
Keywords - PTMi
Isopeptide bond, Phosphoprotein, Ubl conjugationProteomic databases
PaxDbi | Q5U301 |
PeptideAtlasi | Q5U301 |
PRIDEi | Q5U301 |
PTM databases
iPTMneti | Q5U301 |
PhosphoSitePlusi | Q5U301 |
Interactioni
GO - Molecular functioni
- protein domain specific binding Source: RGD
- protein kinase A binding Source: RGD
Protein-protein interaction databases
CORUMi | Q5U301 |
STRINGi | 10116.ENSRNOP00000015576 |
Structurei
Family & Domainsi
Region
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Regioni | 14 – 43 | DisorderedSequence analysisAdd BLAST | 30 | |
Regioni | 103 – 165 | DisorderedSequence analysisAdd BLAST | 63 | |
Regioni | 233 – 324 | DisorderedSequence analysisAdd BLAST | 92 | |
Regioni | 409 – 436 | DisorderedSequence analysisAdd BLAST | 28 | |
Regioni | 506 – 577 | DisorderedSequence analysisAdd BLAST | 72 | |
Regioni | 576 – 589 | PKA-RII subunit binding domainBy similarityAdd BLAST | 14 | |
Regioni | 595 – 688 | DisorderedSequence analysisAdd BLAST | 94 | |
Regioni | 740 – 814 | DisorderedSequence analysisAdd BLAST | 75 |
Coiled coil
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Coiled coili | 213 – 307 | Sequence analysisAdd BLAST | 95 | |
Coiled coili | 720 – 755 | Sequence analysisAdd BLAST | 36 |
Compositional bias
Feature key | Position(s) | DescriptionActions | Graphical view | Length |
---|---|---|---|---|
Compositional biasi | 14 – 38 | Polar residuesSequence analysisAdd BLAST | 25 | |
Compositional biasi | 129 – 165 | Polar residuesSequence analysisAdd BLAST | 37 | |
Compositional biasi | 249 – 275 | Basic and acidic residuesSequence analysisAdd BLAST | 27 | |
Compositional biasi | 276 – 310 | Polar residuesSequence analysisAdd BLAST | 35 | |
Compositional biasi | 409 – 426 | Polar residuesSequence analysisAdd BLAST | 18 | |
Compositional biasi | 506 – 549 | Polar residuesSequence analysisAdd BLAST | 44 | |
Compositional biasi | 556 – 570 | Polar residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 650 – 664 | Basic and acidic residuesSequence analysisAdd BLAST | 15 | |
Compositional biasi | 752 – 773 | Polar residuesSequence analysisAdd BLAST | 22 |
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.By similarity
Keywords - Domaini
Coiled coilPhylogenomic databases
eggNOGi | ENOG502QR7I, Eukaryota |
InParanoidi | Q5U301 |
Family and domain databases
InterProi | View protein in InterPro IPR029304, AKAP2_C |
Pfami | View protein in Pfam PF15304, AKAP2_C, 1 hit |
(1+)i Sequence
Sequence statusi: Complete.
This entry has 1 described isoform and 2 potential isoforms that are computationally mapped.Show allAlign All
Q5U301-1 [UniParc]FASTAAdd to basket
10 20 30 40 50
MEIGVSVAEC KSVPGITSTP HSKDHSSPFY SPSHNGLLTD HHESLDNDVA
60 70 80 90 100
REIQYLDEVL EANCCDSSVD GTYNGISSPE PGAAILVSSL GSPAHSATKV
110 120 130 140 150
EPIEKASGRQ LPPHIELSRS PSDSMAEGER ANGHSTDQPQ DMLGNSLQAP
160 170 180 190 200
ASPSSSTSSH CSSRDGEFTL TTLKKEAKFE LRAFHEDKKP SKLFEEDEHE
210 220 230 240 250
KEQFCIRKVR PSEEMIELEK ERRELIRSQA VKKNPGIAAK WWNPPQKKTI
260 270 280 290 300
EEQLDEEHLE SHRKYKERKE KRAQQEQLQL QQQQQQQLQQ LQQLQQQQQQ
310 320 330 340 350
QLSTSQLCTA PAAHEHLDSI EHTKEDVVTE QIDFSAARKQ FQQMENSRQT
360 370 380 390 400
LAKGQSTPRL FSIKPFYKPL GSINSDKPPT ILRPATIGGT VEDSSTQAAK
410 420 430 440 450
EQKALCVSES QSAGAGTGNA ATQGKEGPYS EPSKRGPLSK LWAEDGEFTS
460 470 480 490 500
ARAVLTVVKD EDHGILDQFS RSVNVSLTQE ELDSGLDELS VRSQDTTVLE
510 520 530 540 550
TLSNDFSMDN ISDSGASNET PNALQENSLA DFSLPQTPQT DNPSEGREGV
560 570 580 590 600
SKSFSDHGFY SPSSTLGDSP SVDDPLEYQA GLLVQNAIQQ AIAEQVDKAE
610 620 630 640 650
VHTSKEGSEQ QEPGAMVEEA GSQAPGSEKP QGMFAPPQVS SPVQEKRDVL
660 670 680 690 700
PKILPGEDKT LREKGPSQPP TAVQPSGPVN MKETRPEGGY FSKYSEAAEL
710 720 730 740 750
RSTASLLATQ ESDVMVGPFK LRSRKQRTLS MIEEEIRAAQ EREEELKRQR
760 770 780 790 800
QVRQSTPSPR AQNAPSLPSR TTCYKTAPGK IEKVKPPPSP TTEGPSLQPD
810 820 830 840 850
LAPEEAAGAQ RPKNLMQTLM EDYETHKSKR RERMDDSSVL EATRVNRRKS
860 870
ALALRWEAGI YANQEEEDNE
Computationally mapped potential isoform sequencesi
There are 2 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basketF1LPQ9 | F1LPQ9_RAT | A-kinase anchor protein 2 | Akap2 | 870 | Annotation score: | ||
A0A096MJ48 | A0A096MJ48_RAT | A-kinase anchor protein 2 | Akap2 | 126 | Annotation score: |
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC085790 mRNA Translation: AAH85790.1 |
Genome annotation databases
UCSCi | RGD:1305135, rat |
Similar proteinsi
Cross-referencesi
Sequence databases
Select the link destinations: EMBLi GenBanki DDBJi Links Updated | BC085790 mRNA Translation: AAH85790.1 |
3D structure databases
ModBasei | Search... |
SWISS-MODEL-Workspacei | Submit a new modelling project... |
Protein-protein interaction databases
CORUMi | Q5U301 |
STRINGi | 10116.ENSRNOP00000015576 |
PTM databases
iPTMneti | Q5U301 |
PhosphoSitePlusi | Q5U301 |
Proteomic databases
PaxDbi | Q5U301 |
PeptideAtlasi | Q5U301 |
PRIDEi | Q5U301 |
Genome annotation databases
UCSCi | RGD:1305135, rat |
Organism-specific databases
RGDi | 1305135, Akap2 |
Phylogenomic databases
eggNOGi | ENOG502QR7I, Eukaryota |
InParanoidi | Q5U301 |
Miscellaneous databases
PROi | PR:Q5U301 |
Family and domain databases
InterProi | View protein in InterPro IPR029304, AKAP2_C |
Pfami | View protein in Pfam PF15304, AKAP2_C, 1 hit |
MobiDBi | Search... |
Entry informationi
Entry namei | AKAP2_RAT | |
Accessioni | Q5U301Primary (citable) accession number: Q5U301 | |
Entry historyi | Integrated into UniProtKB/Swiss-Prot: | July 28, 2009 |
Last sequence update: | December 7, 2004 | |
Last modified: | June 2, 2021 | |
This is version 89 of the entry and version 1 of the sequence. See complete history. | ||
Entry statusi | Reviewed (UniProtKB/Swiss-Prot) | |
Annotation program | Chordata Protein Annotation Program |