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Protein

A-kinase anchor protein 13

Gene

Akap13

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

Functioni

Scaffold protein that plays an important role in assembling signaling complexes downstream of several types of G protein-coupled receptors. Activates RHOA in response to signaling via G protein-coupled receptors via its function as Rho guanine nucleotide exchange factor. May also activate other Rho family members (PubMed:23658642). Part of a kinase signaling complex that links ADRA1A and ADRA1B adrenergic receptor signaling to the activation of downstream p38 MAP kinases, such as MAPK11 and MAPK14. Part of a signaling complex that links ADRA1B signaling to the activation of RHOA and IKBKB/IKKB, leading to increased NF-kappa-B transcriptional activity. Part of a RHOA-dependent signaling cascade that mediates responses to lysophosphatidic acid (LPA), a signaling molecule that activates G-protein coupled receptors and potentiates transcriptional activation of the glucocorticoid receptor NR3C1 (By similarity). Part of a signaling cascade that stimulates MEF2C-dependent gene expression in response to lysophosphatidic acid (LPA) (By similarity). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2. Part of a signaling cascade that links cAMP and EGFR signaling to BRAF signaling and to PKA-mediated phosphorylation of KSR1, leading to the activation of downstream MAP kinases, such as MAPK1 or MAPK3 (By similarity). Functions as scaffold protein that anchors cAMP-dependent protein kinase (PKA) and PRKD1. This promotes activation of PRKD1, leading to increased phosphorylation of HDAC5 and ultimately cardiomyocyte hypertrophy (PubMed:24161911). Has no guanine nucleotide exchange activity on CDC42, Ras or Rac (By similarity). Required for normal embryonic heart development, and in particular for normal sarcomere formation in the developing cardiomyocytes (PubMed:20139090). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:23658642, PubMed:24161911). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:17537920, PubMed:24161911). Plays a role in osteogenesis (PubMed:25892096).By similarity5 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1754 – 1801Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST48

GO - Molecular functioni

GO - Biological processi

Keywordsi

Molecular functionGuanine-nucleotide releasing factor
LigandMetal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-193648 NRAGE signals death through JNK
R-MMU-194840 Rho GTPase cycle
R-MMU-416482 G alpha (12/13) signalling events

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 13
Short name:
AKAP-13
Alternative name(s):
AKAP-Lbc1 Publication
Gene namesi
Name:Akap13Imported
Synonyms:Brx1 Publication
OrganismiMus musculus (Mouse)Imported
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 7

Organism-specific databases

MGIiMGI:2676556 Akap13

Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Cytoskeleton, Membrane, Nucleus

Pathology & Biotechi

Disruption phenotypei

Complete embryonic lethality (PubMed:16469733, PubMed:20139090). Mutant embryos are present at the expected Mendelian rate and develop normally up to 8 dpc. At 10 dpc, mutant embryos appear smaller, have an enlarged heart and pericardiac effusion. The myocardium is thinner than normal and has reduced trabeculation. Sarcomeres are abnormal with incompleteley formed myofilaments that end blindly and do not form Z-disks, indicating a defect in cardiomyocyte differentiation (PubMed:20139090). Heterozygous mice are born at the expected Mendelian frequency and appear grossly normal (PubMed:16469733, PubMed:20139090). Heterozygous mice display a blunted response to glucocorticoids (PubMed:16469733). Heterozygous mice display reduced bone volume relative to body size, but no change of bone length. Heterozygous mice display reduced bone mineral density and reduced trabecular bone, similar to osteoporotic bone. The number of osteoblasts in trabecular bone is reduced (PubMed:25892096).3 Publications

PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
ChainiPRO_00004363191 – 2776A-kinase anchor protein 13Add BLAST2776

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Modified residuei784PhosphoserineBy similarity1
Modified residuei809PhosphothreonineBy similarity1
Modified residuei941PhosphothreonineCombined sources1
Modified residuei1455PhosphoserineBy similarity1
Modified residuei1473PhosphoserineBy similarity1
Modified residuei1507PhosphoserineBy similarity1
Modified residuei1532PhosphoserineBy similarity1
Modified residuei1569PhosphoserineBy similarity1
Modified residuei1608PhosphoserineCombined sources1
Modified residuei1611PhosphoserineCombined sources1
Modified residuei1613PhosphoserineCombined sources1
Modified residuei1637N6-methyllysineBy similarity1
Modified residuei1839PhosphoserineCombined sources1
Modified residuei1858PhosphoserineBy similarity1
Modified residuei1892PhosphoserineCombined sources1
Modified residuei1893PhosphothreonineBy similarity1
Modified residuei1895PhosphoserineCombined sources1
Modified residuei1908PhosphoserineBy similarity1
Modified residuei2308PhosphoserineBy similarity1
Modified residuei2361PhosphoserineCombined sources1
Modified residuei2431PhosphothreonineBy similarity1
Modified residuei2527PhosphoserineCombined sources1
Modified residuei2530PhosphoserineCombined sources1
Modified residuei2673PhosphoserineBy similarity1
Modified residuei2692PhosphoserineCombined sources1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

MaxQBiE9Q394
PaxDbiE9Q394
PeptideAtlasiE9Q394
PRIDEiE9Q394

PTM databases

iPTMnetiE9Q394
PhosphoSitePlusiE9Q394

Expressioni

Tissue specificityi

Detected in embryonic heart, limb bud, first branchial arch and forebrain (at protein level) (PubMed:20139090). Detected in heart (PubMed:20139090). Detected in perichondrium, but not in the bone growth plate (PubMed:25892096).2 Publications

Developmental stagei

Detected in head folds, notochord and somites at 8.5 dpc, with little or no expression in the looping heart. Detected in heart, vasculature, eye, ear, somites, gut and brain at 9.5 dpc. Expression in the heart increases by 10.5 dpc. Highly expressed in atrial and ventricular myocardium and endocardium, trabeculae and outflow tract at 14.5 dpc. Additionally, detected in skeletal muscle, tongue, gut, kidney, lung, urinary system and in the choroid plexus of the brain.1 Publication

Inductioni

Up-regulated in the left heart ventricle in response to phenylephrine.1 Publication

Gene expression databases

BgeeiENSMUSG00000066406 Expressed in 240 organ(s), highest expression level in mesenteric lymph node
ExpressionAtlasiE9Q394 baseline and differential
GenevisibleiE9Q394 MM

Interactioni

Subunit structurei

Interacts with the cAMP-dependent protein kinase (PKA) holoenzyme and with the regulatory subunit PRKAR2A (PubMed:21102438, PubMed:24161911, PubMed:23658642). Interacts with RHOA. Interacts also with RHOB and RHOC. Identified in a ternary complex with RHOA and PRKAR2A. Identified in a complex with NR3C1 and RHOA (By similarity). Interacts with BRAF and KSR1. Identified in a complex with BRAF and KSR1 (PubMed:21102438). Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3. Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK. Interacts (phosphorylated form) with YWHAB and YWHAZ. Interaction with YWHAB inhibits activation of RHOA, interferes with PKN1 binding and activation of MAP kinases. Interacts with GNA12 (By similarity). Interacts with IKBKB (PubMed:23090968). Interacts with ESR1, THRA, PPARA and NME2 (By similarity). Interacts (via the C-terminal domain after the PH domain) with MEF2C and RXRB (PubMed:20139090). Interacts (via the C-terminal domain after the PH domain) with PRKD1 (PubMed:23658642, PubMed:24161911).By similarity5 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000129784

Structurei

3D structure databases

ProteinModelPortaliE9Q394
SMRiE9Q394
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Domaini1957 – 2154DHPROSITE-ProRule annotationAdd BLAST198
Domaini2194 – 2296PHPROSITE-ProRule annotationAdd BLAST103

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Regioni493 – 515Important for interaction with PRKAR2ABy similarityAdd BLAST23
Regioni1552 – 1678Important for interaction with MAP2K3By similarityAdd BLAST127
Regioni1882 – 2776Interaction with ESR1By similarityAdd BLAST895

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Coiled coili2308 – 2345Sequence analysisAdd BLAST38
Coiled coili2532 – 2646Sequence analysisAdd BLAST115

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Compositional biasi1437 – 1440Poly-SerSequence analysis4
Compositional biasi1499 – 1504Poly-GluSequence analysis6
Compositional biasi1697 – 1750Lys-richPROSITE-ProRule annotationAdd BLAST54
Compositional biasi2741 – 2753Poly-LysSequence analysisAdd BLAST13

Domaini

The DH domain is sufficient for interaction with RHOA, and for guanine nucleotide exchange (GEF) activity with RHOA. Forms that lack C-terminal regulatory domains have transforming activity and function as oncogenes.By similarity
The PH domain does not play a role in lipid-binding. Instead, it inhibits the guanine nucleotide exchange (GEF) activity of the isolated DH domain (in vitro).By similarity
The C-terminal domain after the PH domain is involved in protein-protein interactions that are required for normal, compensatory cardiac hypertrophy in response to pressure overload.1 Publication

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1754 – 1801Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG3520 Eukaryota
COG5422 LUCA
GeneTreeiENSGT00760000119193
KOiK16529
OMAiHRELDVY

Family and domain databases

CDDicd00160 RhoGEF, 1 hit
Gene3Di1.20.900.10, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR028852 AKAP13
IPR035899 DBL_dom_sf
IPR000219 DH-domain
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
PANTHERiPTHR13944:SF18 PTHR13944:SF18, 1 hit
PfamiView protein in Pfam
PF00621 RhoGEF, 1 hit
SMARTiView protein in SMART
SM00109 C1, 1 hit
SM00233 PH, 1 hit
SM00325 RhoGEF, 1 hit
SUPFAMiSSF48065 SSF48065, 1 hit
PROSITEiView protein in PROSITE
PS50010 DH_2, 1 hit
PS50003 PH_DOMAIN, 1 hit
PS00479 ZF_DAG_PE_1, 1 hit
PS50081 ZF_DAG_PE_2, 1 hit

Sequences (2+)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

This entry has 2 described isoforms and 5 potential isoforms that are computationally mapped.Show allAlign All

Isoform 1 (identifier: E9Q394-1) [UniParc]FASTAAdd to basket

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
MKLSPQQAPL YGDCVVTVLL AEEDKVEDDA IFYLIFSGST LYHCTSTRKV
60 70 80 90 100
SSDTLETIAP GHDCCETVKV LLCASREGLP VFVVAEEDFH FVQDEAYDAA
110 120 130 140 150
QFLATSAGNQ QALNFTRFLD RSGPPSRDVN SLDEKVALAF RHLKLPAEWN
160 170 180 190 200
VLGTDHTLHD GGPRETLMHF AVRLGLLRLT WFLLQKPGGR GALSIHNKEG
210 220 230 240 250
ATPVSLALER GYHELHQLLT EENAGEPDSW SSLSYEIPYG DCSVRHHREL
260 270 280 290 300
DIYTLTSESE SHREPHGDSC TGHISKLMNI QQQLMKTNLK QMDNLMPLMV
310 320 330 340 350
TAQDSSCVPS VPETDGLFLP CVPEPSDHQH PPFEETKSTL CCQRSPGRMA
360 370 380 390 400
ESSCDLSSMV EEENVICSHK KNKDVGRKGE EAEPASAMDS GSASHQDSCL
410 420 430 440 450
QSVPDCGVKG REGLPSCGNR NEVTGTNYSG VATCQQPLSS RSSVLQDAMV
460 470 480 490 500
TEPDACQHSS GRELPDSSST DVGAPEKAGE LEHSLLTPDA TTQNNKPQVG
510 520 530 540 550
EGTKERLENS DSSTTETTAV QVLSEPMEKA DITNHVFATS AVGVNTPAEA
560 570 580 590 600
SPALSSEEIP TEKPGMETQE RGCEGGTTSD QSSPVLPAAA IENKVLGGQE
610 620 630 640 650
PDTSIAGFCK TASPLDLTMP GPSSDGMPEQ NSESHARPAQ SLSGQALLCS
660 670 680 690 700
TAEAGTPSAE ATHQPSTVTS SGRLEECGSG KASLPESTMV QPSTQELCTT
710 720 730 740 750
LCPEDPQADT VTSDTVKNTQ KSVGVCHLCV SDAKNQGNGL KQDTPLTNVL
760 770 780 790 800
EDVPRLPSVV SQTEKELAPD QVSPPASSFS LASSPESESV TKDDALSLVP
810 820 830 840 850
SQKEKGTATP QLHRTTACRD GPDGRDLSDT DKVGDGATDP PPSSAVELRT
860 870 880 890 900
SMGNTSPVGI GGEQEGSSPT ATLEVLSDSL LHNVDKAALV SDFTLPEEGV
910 920 930 940 950
SVVVPESSTA LGQDGKDRAM SCSSVKEDVH SSEMSREDQR TPPSGQEIPG
960 970 980 990 1000
LCEKPMSALC AEEKAQQHTP SACLKTETKD IKEVAPQVSL LTEGGAAKSL
1010 1020 1030 1040 1050
VPPRTSLSAD SKQKASSTEQ SGSSLLPSGL PGASEALHCN QPSALDVVVE
1060 1070 1080 1090 1100
NTQFQGETNA CEVSRSAMED VTVADASPAT AEPRKKDASH CIKDIPISEL
1110 1120 1130 1140 1150
LNQEKQMTPS LPEAFLDKGV TDLQEVITPE IEPLDCKRET LEGTDLNCAT
1160 1170 1180 1190 1200
SNSKETPIEK PMQPLARDLP TETGLSVINN NVPQADMKQV AQASIPAEES
1210 1220 1230 1240 1250
NATTVSTQAA DVPTRADSIE ETATRIVEAV IRQVRASNAL MAKVETQNPS
1260 1270 1280 1290 1300
LSSPETKQLE NAYTESACAF LPGETPQIEK THEDTTGQCG AETEEPEKII
1310 1320 1330 1340 1350
LPESAPGKQG KMPDTRTGDE VDLLSRISAA SEEEAVGNGA ATPKMKQGPG
1360 1370 1380 1390 1400
TQAINRESWC AIEPCPEAAS LLASKQSSEC RSFIDVGLGT ECASKEGMLQ
1410 1420 1430 1440 1450
RVSGSESDLF HSPSDEMDSI IFPKPEEEQL LCDTTGSSSS TDDTASLDRH
1460 1470 1480 1490 1500
SSHGSDVSLP QTSKLNRSRN HQSANGFFSP GVEAPESRES ESEPAGSGEM
1510 1520 1530 1540 1550
EEEEMDSITE VPANCSFLRS SMRSLSPFRR HSWGPGKNAA SDAEMNQRSS
1560 1570 1580 1590 1600
MRALGHVVRR PPIHRRSFSL EGLTGGGVGN KPSSSLEMSS ANSSELRNPF
1610 1620 1630 1640 1650
GGEEQRNSLM SLSEEHLEPD QRQHHRMFDQ QTCYRSKQQG FNYCTSAISS
1660 1670 1680 1690 1700
PLTKSISLMT ISHPGLDSSR PFHSTSANLT ESITEENCNF LPPSPSKKNF
1710 1720 1730 1740 1750
EEKSGTKVSR TFSYIRNKMS SSKKSKEKEK EKDKIKEKEK DSKEKEKDKK
1760 1770 1780 1790 1800
TLNGHTFSPI PIVGPISCSQ CMKPFTNKDA YTCAGCGAFV HKGCRENLAS
1810 1820 1830 1840 1850
CAKVKMKQPK GSLQAHDTSS LPTVIMRNKS SQPKERPRSA VLLADEATAA
1860 1870 1880 1890 1900
PMFTNRRSQQ SVSLSKSVSI QNITGVGNDE NMSNTWKFLS HSTDSLNKIC
1910 1920 1930 1940 1950
KVNESTESLT DEGVGTDMNE GQLMGDFESD SKQLEAESWS RTVDSKFLKQ
1960 1970 1980 1990 2000
QKKDVVKRQE VIYELMQTEL HHIRTLKIMS DVYSRGMMTD LLFEQQMVEK
2010 2020 2030 2040 2050
LFPCLDELIS IHSQFFQRIL ERKKESLVDK SEKNFLIKRI GDVLVSQFSG
2060 2070 2080 2090 2100
ESAERLKKTY GKFCGQHNQS VNYFKDLYTK DKRFQAFVKK KMSSSVVRRL
2110 2120 2130 2140 2150
GIPECILLVT QRITKYPVLF QRILQCTKDN EVEQEDLTQS LSLVKDVIGA
2160 2170 2180 2190 2200
VDSKVASYEK KVRLGEIYTK TDSKSIMRMK SGQMFAKEDL RRKKLVRDGS
2210 2220 2230 2240 2250
VFLKSTTGRL KEVQAVLLTD ILVFLQEKDQ KYVFASLDHK STVISLKKLI
2260 2270 2280 2290 2300
VREVAHEEKG LFLISMGVKD PEMVEVHASS REERNSWIQI IQDTINSLNR
2310 2320 2330 2340 2350
DEDEGIPSEN EEEKKLLDTK ARELKEQLQQ KDQQILLLLE EKEMIFRDMT
2360 2370 2380 2390 2400
ECSTPLPEDC SPTHSPRVLF RSNTEEALKG GPLMKSAINE VEILQSLVSG
2410 2420 2430 2440 2450
SLGGTLGQSI SSPVEQEVMA APISLPRRAE TFGGFDCHQM NASKGGEKEE
2460 2470 2480 2490 2500
GDDGQDLRRT ESDSGLKKGG NGNLVFMLKR NSEQVVQSIV HLHELLSMLQ
2510 2520 2530 2540 2550
GVVLQQDSYI EDQKLVLTEK VLTRSASRPS SLIEQEKQRS LEKQRQDLAN
2560 2570 2580 2590 2600
LQKQQAQHLE EKRRREREWE AREQELRDRE AKLAEREETV RRRQQDLERD
2610 2620 2630 2640 2650
REELQQKKGT YQCDLERLRA AQKQLEREQE QLRRDTERLS QRQMDQNLCQ
2660 2670 2680 2690 2700
VSNKHGRLMR IPSFLPNSDE FSSPSAPSVT KSGSLDSELS VSPKRNSISR
2710 2720 2730 2740 2750
TQKDKGPFHI LGSASQTKVP EGQSQAPSST STSTRLFGLS KPKEKKEKKK
2760 2770
KSKGSRTQPG DGPASEVPAE GEEIFC
Length:2,776
Mass (Da):303,976
Last modified:April 5, 2011 - v1
Checksum:i1A27E2B4986306EE
GO
Isoform 2 (identifier: E9Q394-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     1307-1311: GKQGK → E
     1548-1565: Missing.

Show »
Length:2,754
Mass (Da):301,499
Checksum:iFCB658ABA85C936A
GO

Computationally mapped potential isoform sequencesi

There are 5 potential isoforms mapped to this entry.BLASTAlignShow allAdd to basket
EntryEntry nameProtein names
Gene namesLengthAnnotation
A0A140LJJ5A0A140LJJ5_MOUSE
A-kinase anchor protein 13
Akap13
2,794Annotation score:
A0A140LHG3A0A140LHG3_MOUSE
A-kinase anchor protein 13
Akap13
607Annotation score:
A0A140LHQ3A0A140LHQ3_MOUSE
A-kinase anchor protein 13
Akap13
423Annotation score:
A0A140LIX0A0A140LIX0_MOUSE
A-kinase anchor protein 13
Akap13
870Annotation score:
A0A140LID7A0A140LID7_MOUSE
A-kinase anchor protein 13
Akap13
569Annotation score:

Alternative sequence

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Alternative sequenceiVSP_0583441307 – 1311GKQGK → E in isoform 2. 5
Alternative sequenceiVSP_0583451548 – 1565Missing in isoform 2. Add BLAST18

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC113019 Genomic DNA No translation available.
AC158749 Genomic DNA No translation available.
AK149507 mRNA Translation: BAE28926.1
CCDSiCCDS52276.1 [E9Q394-1]
RefSeqiNP_083608.1, NM_029332.1 [E9Q394-1]
XP_006541318.1, XM_006541255.3 [E9Q394-2]
UniGeneiMm.216107

Genome annotation databases

EnsembliENSMUST00000166315; ENSMUSP00000129784; ENSMUSG00000066406 [E9Q394-1]
GeneIDi75547
KEGGimmu:75547
UCSCiuc009hwq.1 mouse
uc009hwx.2 mouse [E9Q394-1]

Keywords - Coding sequence diversityi

Alternative splicing

Similar proteinsi

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AC113019 Genomic DNA No translation available.
AC158749 Genomic DNA No translation available.
AK149507 mRNA Translation: BAE28926.1
CCDSiCCDS52276.1 [E9Q394-1]
RefSeqiNP_083608.1, NM_029332.1 [E9Q394-1]
XP_006541318.1, XM_006541255.3 [E9Q394-2]
UniGeneiMm.216107

3D structure databases

ProteinModelPortaliE9Q394
SMRiE9Q394
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

STRINGi10090.ENSMUSP00000129784

PTM databases

iPTMnetiE9Q394
PhosphoSitePlusiE9Q394

Proteomic databases

MaxQBiE9Q394
PaxDbiE9Q394
PeptideAtlasiE9Q394
PRIDEiE9Q394

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000166315; ENSMUSP00000129784; ENSMUSG00000066406 [E9Q394-1]
GeneIDi75547
KEGGimmu:75547
UCSCiuc009hwq.1 mouse
uc009hwx.2 mouse [E9Q394-1]

Organism-specific databases

CTDi11214
MGIiMGI:2676556 Akap13

Phylogenomic databases

eggNOGiKOG3520 Eukaryota
COG5422 LUCA
GeneTreeiENSGT00760000119193
KOiK16529
OMAiHRELDVY

Enzyme and pathway databases

ReactomeiR-MMU-193648 NRAGE signals death through JNK
R-MMU-194840 Rho GTPase cycle
R-MMU-416482 G alpha (12/13) signalling events

Miscellaneous databases

ChiTaRSiAkap13 mouse
PROiPR:E9Q394
SOURCEiSearch...

Gene expression databases

BgeeiENSMUSG00000066406 Expressed in 240 organ(s), highest expression level in mesenteric lymph node
ExpressionAtlasiE9Q394 baseline and differential
GenevisibleiE9Q394 MM

Family and domain databases

CDDicd00160 RhoGEF, 1 hit
Gene3Di1.20.900.10, 1 hit
2.30.29.30, 1 hit
InterProiView protein in InterPro
IPR028852 AKAP13
IPR035899 DBL_dom_sf
IPR000219 DH-domain
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR001849 PH_domain
PANTHERiPTHR13944:SF18 PTHR13944:SF18, 1 hit
PfamiView protein in Pfam
PF00621 RhoGEF, 1 hit
SMARTiView protein in SMART
SM00109 C1, 1 hit
SM00233 PH, 1 hit
SM00325 RhoGEF, 1 hit
SUPFAMiSSF48065 SSF48065, 1 hit
PROSITEiView protein in PROSITE
PS50010 DH_2, 1 hit
PS50003 PH_DOMAIN, 1 hit
PS00479 ZF_DAG_PE_1, 1 hit
PS50081 ZF_DAG_PE_2, 1 hit
ProtoNetiSearch...

Entry informationi

Entry nameiAKP13_MOUSE
AccessioniPrimary (citable) accession number: E9Q394
Secondary accession number(s): Q3UEI5
Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 8, 2016
Last sequence update: April 5, 2011
Last modified: November 7, 2018
This is version 65 of the entry and version 1 of the sequence. See 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
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Main funding by: National Institutes of Health

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