Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.
Entry version 75 (13 Nov 2019)
Sequence version 2 (03 Apr 2013)
Previous versions | rss
Help videoAdd a publicationFeedback
Protein

A-kinase anchor protein 13

Gene

Akap13

Organism
Rattus norvegicus (Rat)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>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 (PubMed:17537920). May also activate other Rho family members. 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 (PubMed:17537920, PubMed:23716597). 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 (PubMed:23090968). 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) (PubMed:20139090). Part of a signaling pathway that activates MAPK11 and/or MAPK14 and leads to increased transcription activation of the estrogen receptors ESR1 and ESR2 (By similarity). 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 (By similarity). 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 (By similarity). Plays a role in cardiomyocyte growth and cardiac hypertrophy in response to activation of the beta-adrenergic receptor by phenylephrine or isoproterenol (PubMed:17537920). Required for normal adaptive cardiac hypertrophy in response to pressure overload (By similarity). Plays a role in osteogenesis (By similarity).By similarity3 Publications

Regions

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section specifies the position(s) and type(s) of zinc fingers within the protein.<p><a href='/help/zn_fing' target='_top'>More...</a></p>Zinc fingeri1753 – 1800Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST48

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionGuanine-nucleotide releasing factor
LigandMetal-binding, Zinc

Enzyme and pathway databases

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-RNO-193648 NRAGE signals death through JNK
R-RNO-194840 Rho GTPase cycle
R-RNO-416482 G alpha (12/13) signalling events

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
A-kinase anchor protein 13
Short name:
AKAP-13
Alternative name(s):
AKAP-Lbc1 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Akap13Imported
Synonyms:Rt131 Publication
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiRattus norvegicus (Rat)Imported
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10116 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeRattus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000002494 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 1

Organism-specific databases

Rat genome database

More...
RGDi
727893 Akap13

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>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 & Seán O’Donoghue; Source: COMPARTMENTS

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00004363201 – 2760A-kinase anchor protein 13Add BLAST2760

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei776PhosphoserineBy similarity1
Modified residuei801PhosphothreonineBy similarity1
Modified residuei932PhosphothreonineBy similarity1
Modified residuei962PhosphoserineBy similarity1
Modified residuei1450PhosphoserineBy similarity1
Modified residuei1468PhosphoserineBy similarity1
Modified residuei1501PhosphoserineBy similarity1
Modified residuei1526PhosphoserineBy similarity1
Modified residuei1585PhosphoserineCombined sources1
Modified residuei1625PhosphoserineBy similarity1
Modified residuei1628PhosphoserineCombined sources1
Modified residuei1630PhosphoserineCombined sources1
Modified residuei1654N6-methyllysineBy similarity1
Modified residuei1838PhosphoserineBy similarity1
Modified residuei1857PhosphoserineBy similarity1
Modified residuei1891PhosphoserineCombined sources1
Modified residuei1892PhosphothreonineBy similarity1
Modified residuei1894PhosphoserineCombined sources1
Modified residuei1907PhosphoserineCombined sources1
Modified residuei2292PhosphoserineCombined sources1
Modified residuei2345PhosphoserineBy similarity1
Modified residuei2415PhosphothreonineBy similarity1
Modified residuei2511PhosphoserineCombined sources1
Modified residuei2514PhosphoserineBy similarity1
Modified residuei2676PhosphoserineCombined sources1

Keywords - PTMi

Methylation, Phosphoprotein

Proteomic databases

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
F1M3G7

PeptideAtlas

More...
PeptideAtlasi
F1M3G7

PRoteomics IDEntifications database

More...
PRIDEi
F1M3G7

PTM databases

iPTMnet integrated resource for PTMs in systems biology context

More...
iPTMneti
F1M3G7

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
F1M3G7

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms. By default, the information is derived from experiments at the mRNA level, unless specified ‘at protein level’. <br></br>Examples: <a href="http://www.uniprot.org/uniprot/P92958#expression">P92958</a>, <a href="http://www.uniprot.org/uniprot/Q8TDN4#expression">Q8TDN4</a>, <a href="http://www.uniprot.org/uniprot/O14734#expression">O14734</a><p><a href='/help/tissue_specificity' target='_top'>More...</a></p>Tissue specificityi

Detected in bone osteoblasts (at protein level).1 Publication

<p>This subsection of the ‘Expression’ section reports the experimentally proven effects of inducers and repressors (usually chemical compounds or environmental factors) on the level of protein (or mRNA) expression (up-regulation, down-regulation, constitutive expression).<p><a href='/help/induction' target='_top'>More...</a></p>Inductioni

Up-regulated in cardiomyocytes in response to phenylephrine (in vitro).1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSRNOG00000010964 Expressed in 9 organ(s), highest expression level in lung

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

<p>This subsection of the <a href="http://www.uniprot.org/help/interaction_section">'Interaction'</a> section provides information about the protein quaternary structure and interaction(s) with other proteins or protein complexes (with the exception of physiological receptor-ligand interactions which are annotated in the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section).<p><a href='/help/subunit_structure' target='_top'>More...</a></p>Subunit structurei

Interacts with the cAMP-dependent protein kinase (PKA) holoenzyme and with the regulatory subunit PRKAR2A (PubMed:11696353).

Interacts with RHOA (PubMed:11696353).

Interacts also with RHOB and RHOC.

Identified in a ternary complex with RHOA and PRKAR2A.

Identified in a complex with NR3C1 and RHOA.

Interacts with BRAF and KSR1.

Identified in a complex with BRAF and KSR1 (By similarity).

Component of a signaling complex containing at least AKAP13, PKN1, MAPK14, ZAK and MAP2K3 (PubMed:23716597). Within this complex, AKAP13 interacts directly with PKN1, which in turn recruits MAPK14, MAP2K3 and ZAK (By similarity).

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.

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.

Interacts (via the C-terminal domain after the PH domain) with PRKD1 (By similarity).

By similarity3 Publications

GO - Molecular functioni

Protein-protein interaction databases

STRING: functional protein association networks

More...
STRINGi
10116.ENSRNOP00000014802

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

More...
SMRi
F1M3G7

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/family_and_domains_section">Family and Domains</a> section describes the position and type of a domain, which is defined as a specific combination of secondary structures organized into a characteristic three-dimensional structure or fold.<p><a href='/help/domain' target='_top'>More...</a></p>Domaini1956 – 2153DHPROSITE-ProRule annotationAdd BLAST198
Domaini2176 – 2280PHPROSITE-ProRule annotationAdd BLAST105

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni482 – 504Important for interaction with PRKAR2ABy similarityAdd BLAST23
Regioni1213 – 1228Important for interaction with PRKAR2A1 PublicationAdd BLAST16
Regioni1546 – 1695Important for interaction with MAP2K3By similarityAdd BLAST150
Regioni1881 – 2760Interaction with ESR1By similarityAdd BLAST880

Coiled coil

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and domains’ section denotes the positions of regions of coiled coil within the protein.<p><a href='/help/coiled' target='_top'>More...</a></p>Coiled coili2292 – 2329Sequence analysisAdd BLAST38
Coiled coili2516 – 2632Sequence analysisAdd BLAST117

Compositional bias

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes the position of regions of compositional bias within the protein and the particular amino acids that are over-represented within those regions.<p><a href='/help/compbias' target='_top'>More...</a></p>Compositional biasi1432 – 1435Poly-SerSequence analysis4
Compositional biasi1493 – 1498Poly-GluSequence analysis6
Compositional biasi2725 – 2737Poly-LysSequence analysisAdd BLAST13

<p>This subsection of the ‘Family and domains’ section provides general information on the biological role of a domain. The term ‘domain’ is intended here in its wide acceptation, it may be a structural domain, a transmembrane region or a functional domain. Several domains are described in this subsection.<p><a href='/help/domain_cc' target='_top'>More...</a></p>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.By similarity

Zinc finger

Feature keyPosition(s)DescriptionActionsGraphical viewLength
Zinc fingeri1753 – 1800Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd BLAST48

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
ENOG410IR0Y Eukaryota
ENOG410XT68 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000154146

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
F1M3G7

KEGG Orthology (KO)

More...
KOi
K16529

Identification of Orthologs from Complete Genome Data

More...
OMAi
XDQKSTV

Database of Orthologous Groups

More...
OrthoDBi
69816at2759

TreeFam database of animal gene trees

More...
TreeFami
TF325887

Family and domain databases

Conserved Domains Database

More...
CDDi
cd00160 RhoGEF, 1 hit

Gene3D Structural and Functional Annotation of Protein Families

More...
Gene3Di
1.20.900.10, 1 hit
2.30.29.30, 1 hit

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR028852 AKAP13
IPR035899 DBL_dom_sf
IPR000219 DH-domain
IPR002219 PE/DAG-bd
IPR011993 PH-like_dom_sf
IPR041020 PH_16
IPR001849 PH_domain

The PANTHER Classification System

More...
PANTHERi
PTHR13944:SF18 PTHR13944:SF18, 1 hit

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF17838 PH_16, 1 hit
PF00621 RhoGEF, 1 hit

Simple Modular Architecture Research Tool; a protein domain database

More...
SMARTi
View protein in SMART
SM00109 C1, 1 hit
SM00233 PH, 1 hit
SM00325 RhoGEF, 1 hit

Superfamily database of structural and functional annotation

More...
SUPFAMi
SSF48065 SSF48065, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View 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

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

F1M3G7-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MKLSPQQAPL YGDCVVTVLL AEEDKVEDDA IFYLIFSGST LYHCTSTRKV
60 70 80 90 100
SSDTLETIAP GHDCCETVKV LLCASKEGLP VFVVAEEDFH FVQDEAYDAA
110 120 130 140 150
QFLATSAGNQ QALNFTRFLD RSGPPSGDVN SLDEKVALAF RHLKLPAEWN
160 170 180 190 200
VLGTDHTLHD GGPRETLMHF AVRLGLLRLT WFLLQKPGGR GALSIHNKEG
210 220 230 240 250
ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG DYSVRHHREL
260 270 280 290 300
DIYTLTSESE SHCEPHGDSC TGHISKLMNI QQQLMKTNLK QMDNLMPLMV
310 320 330 340 350
TTQDSSCVPC VPEPSDHQQL PFEETKSTVC CQGSPGRKDA SPCDLSSVVE
360 370 380 390 400
EENLICSHKK NKDTGRPGEG VEPASAVDSR SASHQDSCLQ SIPDCGVKGR
410 420 430 440 450
EGLPSCGNRN EVTGTQYSGV ATCQQPLSSE SSVPQDVLVT EPDARQHSSG
460 470 480 490 500
RELPDSSSTD AGAPEKAGEL EHSLLTPDAT TQNSKPQVGE SAKERLENSD
510 520 530 540 550
ISSAEATAVQ ALREPKQKAD VTNHVFAARA AGADAPAEAS PAWSPEEIPT
560 570 580 590 600
GKPGMETQER GCEGGITSDQ SSQVLPAAAA ATENKVLDGL ELETLPACPC
610 620 630 640 650
ETASSLDLTV SGPRPDGMPK QNSESSAQHA QSLNSQAPLC SIAGAGTPSA
660 670 680 690 700
ESACPQSTET SSGGSVIEHG SGEASLPEST AAQPEPQGLC TAPCPEDPQA
710 720 730 740 750
DTVTSDTAAH NQKSVGSCHL CALDAKNQEK DLRQDTPSVN TLEDVPHLPS
760 770 780 790 800
VVPQSEEKLE PDQVSPRGSS FSLASSPESE SVTKDDVLSL VSSQKEKGTA
810 820 830 840 850
TPQLHRAPAC SDGPDGRDLN DTDKVGDGAA SPPTPSAVEL QTSMGNTSPV
860 870 880 890 900
GVGEQEGSSL TATLEVLSDS LLQSVDKAAL VSDSLLPEEG GSIVVPESST
910 920 930 940 950
ALGQGGKDKA TKCPSVKEDV HSSEMSREDQ RTPPPGQEIS RLCEKPMSAL
960 970 980 990 1000
CAGEKALQHS NSPDTPSACL QTETKHNKEV APQSSPLMKG GAVQNLVPPK
1010 1020 1030 1040 1050
TSLSADSEQK TSSTEQSGSS LLPGGASEAL RCSQPSLSVS VESIQFQGKT
1060 1070 1080 1090 1100
SACKVSRNAM EDVTVADAFL ATAEPTKEDA LHHVKDISDL LNQEKKTTPG
1110 1120 1130 1140 1150
LPEALLDKGV TDLQEVITPE IEPLDCKREK LEGTDLSCPT SKSKETPNNE
1160 1170 1180 1190 1200
ETTQPPARDL PTETGLSAIN DNGPQADMKH VTQASVPGEE SNVTTVLGMV
1210 1220 1230 1240 1250
STQAADGPPG ADSIEETATR IVEAVIKQIK ASNTLRTQVE IQNPPLSSSE
1260 1270 1280 1290 1300
IKEIENTGSE SARVFLPGEP LQMENTQKET TGHCSVETEA PEKIILAVHR
1310 1320 1330 1340 1350
PEPAPEMPDT KTGGEVDLLS KRSAASEEEA IGNGAATPKM KQAPGTQVIN
1360 1370 1380 1390 1400
RESWCAIEPC PEAASLLASK QSSECRSFID VGLGTECATK EGVLQRESGS
1410 1420 1430 1440 1450
DSDLFHSPSD EMDSIIFSKP EEEQLLCDTT GSSSSTDDTA SLDRHSSHGS
1460 1470 1480 1490 1500
DVSLPQTSKL NRSRNHQSSN GFFSHGVDPE SREGESEPAG SGEMEEEEMD
1510 1520 1530 1540 1550
SITEVPANRS FLRNSMRSLS PFRRHSWGPG KNAASDAEMN QRSSMQVLGH
1560 1570 1580 1590 1600
VVRRPPIHRR SMSWCPSGVQ YSAALNADFN IRSFSLEGLT GGGGVGNKPS
1610 1620 1630 1640 1650
SSLEISSANS SELRNPFSGE EQRSSLMSLS EEHLEPDQRQ HHRMFDQQTC
1660 1670 1680 1690 1700
YRSKQQGFNY CTSAISSPLT KSISLMTISH PGLDNSRPFH SASANLTESI
1710 1720 1730 1740 1750
TEENCNFLPP SPSKKSFEEK SGTKVSRTFS YIRNKMSSSK KSKKEKDKKT
1760 1770 1780 1790 1800
LNGHTFSPIP IVGPINCSQC MKPFTNKDAY TCASCGAFVH KGCRENLASC
1810 1820 1830 1840 1850
AKVKMKQPKG SLQAHDTSSL PTVIMRNKSS QPKERPRSAV LLAEEAIAAP
1860 1870 1880 1890 1900
MFTNRRSQQS VSLSKSVSIQ NITGVGNDEN MSNTWKFLSH STDSLNKICK
1910 1920 1930 1940 1950
VNESTESLTD EGVGTDMNEG QLMGDFESDS KQLEAESWSR TVDSKFLKQQ
1960 1970 1980 1990 2000
KKDVVKRQEV IYELMQTELH HIRTLKIMSD VYSRGMMTDL LFEQQMVEKL
2010 2020 2030 2040 2050
FPCLDELISI HSQFFQRILE RKKESLVDKS EKNFLIKRIG DVLVSQFSGE
2060 2070 2080 2090 2100
NAERLKKTYG KFCGQHNQSV NYFKDLYTKD KRFQAFVKKK MSSSVVRRLG
2110 2120 2130 2140 2150
IPECILLVTQ RITKYPVLFQ RILQCTKDNE VEQEDLTQSL SLVKDVIGAV
2160 2170 2180 2190 2200
DSKVASYEKK VRLGEIYTKT DSKSIMRMKS GQMFAKEDLR RKKLVRDGSV
2210 2220 2230 2240 2250
FLKSATGRLK EKDQKYVFAS LDHKSTVISL KKLIVREVAH EEKGLFLISM
2260 2270 2280 2290 2300
GVKDPEMVEV HASSREERNS WIQIIQDTIN SLNRDEDEGI PSENEEEKRL
2310 2320 2330 2340 2350
LDTKARELKE QLQQKDQQIL LLLEEKEMIF RDMTECSTPL PEDCSPTHSP
2360 2370 2380 2390 2400
RMLFRSNTEE ALKGGPLMKS AISEVEILQG LVSGSLGGTL GQPISSPVEQ
2410 2420 2430 2440 2450
EVMAGPISLP RRAETFGGFD CHQLNASKGG EKEEGDDGQD LRRTESDSGL
2460 2470 2480 2490 2500
KKGGNANLVF MLKRNSEQVV QSIVHLHELL TMLQGVVLQQ DSYIEDQKLV
2510 2520 2530 2540 2550
LTEKVLTRSA SRPSSLIEQE KQRSLEKQRQ DLANLQKQQA QHLEEKRRRE
2560 2570 2580 2590 2600
REWEARELEL RDREAKLAER EETVRRRQQD LERDREELQQ KKGTYQCDLE
2610 2620 2630 2640 2650
RLRAAQKQLE REQEQLKRDA EQLSQRQMEQ DLCQVSNKHG RLMRVPSFLP
2660 2670 2680 2690 2700
NSDEFSLLST PSITKSGSLD SELSVSPKRN SISRTQKDKG PFHILSSASQ
2710 2720 2730 2740 2750
TKVPEGQSQA PSSTSTSTRL FGLSKPKEKK EKKKKSKGSR TQPGDGPAPE
2760
VPAEGEEIFC
Length:2,760
Mass (Da):301,403
Last modified:April 3, 2013 - v2
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iDC1C4A92AF76188C
GO

<p>This subsection of the ‘Sequence’ section reports difference(s) between the protein sequence shown in the UniProtKB entry and other available protein sequences derived from the same gene.<p><a href='/help/sequence_caution' target='_top'>More...</a></p>Sequence cautioni

The sequence AAL40924 differs from that shown. Reason: Erroneous initiation. Extended N-terminus.Curated

Experimental Info

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Sequence’ section reports difference(s) between the canonical sequence (displayed by default in the entry) and the different sequence submissions merged in the entry. These various submissions may originate from different sequencing projects, different types of experiments, or different biological samples. Sequence conflicts are usually of unknown origin.<p><a href='/help/conflict' target='_top'>More...</a></p>Sequence conflicti1348V → A in AAL40924 (PubMed:11696353).Curated1
Sequence conflicti1542 – 1559Missing in AAL40924 (PubMed:11696353).CuratedAdd BLAST18
Sequence conflicti1745 – 1747EKD → KKK in AAL40924 (PubMed:11696353).Curated3

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

More...
EMBLi

GenBank nucleotide sequence database

More...
GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AABR07004317 Genomic DNA No translation available.
AABR07004318 Genomic DNA No translation available.
AABR07004319 Genomic DNA No translation available.
CH473980 Genomic DNA Translation: EDM08537.1
AF387102 mRNA Translation: AAL40924.1 Different initiation.

NCBI Reference Sequences

More...
RefSeqi
NP_001099741.2, NM_001106271.2

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSRNOT00000014802; ENSRNOP00000014802; ENSRNOG00000010964

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
293024

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
rno:293024

UCSC genome browser

More...
UCSCi
RGD:727893 rat

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AABR07004317 Genomic DNA No translation available.
AABR07004318 Genomic DNA No translation available.
AABR07004319 Genomic DNA No translation available.
CH473980 Genomic DNA Translation: EDM08537.1
AF387102 mRNA Translation: AAL40924.1 Different initiation.
RefSeqiNP_001099741.2, NM_001106271.2

3D structure databases

SMRiF1M3G7
ModBaseiSearch...

Protein-protein interaction databases

STRINGi10116.ENSRNOP00000014802

PTM databases

iPTMnetiF1M3G7
PhosphoSitePlusiF1M3G7

Proteomic databases

PaxDbiF1M3G7
PeptideAtlasiF1M3G7
PRIDEiF1M3G7

Genome annotation databases

EnsembliENSRNOT00000014802; ENSRNOP00000014802; ENSRNOG00000010964
GeneIDi293024
KEGGirno:293024
UCSCiRGD:727893 rat

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
11214
RGDi727893 Akap13

Phylogenomic databases

eggNOGiENOG410IR0Y Eukaryota
ENOG410XT68 LUCA
GeneTreeiENSGT00940000154146
InParanoidiF1M3G7
KOiK16529
OMAiXDQKSTV
OrthoDBi69816at2759
TreeFamiTF325887

Enzyme and pathway databases

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

Miscellaneous databases

Protein Ontology

More...
PROi
PR:F1M3G7

Gene expression databases

BgeeiENSRNOG00000010964 Expressed in 9 organ(s), highest expression level in lung

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
IPR041020 PH_16
IPR001849 PH_domain
PANTHERiPTHR13944:SF18 PTHR13944:SF18, 1 hit
PfamiView protein in Pfam
PF17838 PH_16, 1 hit
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

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiAKP13_RAT
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: F1M3G7
Secondary accession number(s): Q8VHU6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: June 8, 2016
Last sequence update: April 3, 2013
Last modified: November 13, 2019
This is version 75 of the entry and version 2 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome
UniProt is an ELIXIR core data resource
Main funding by: National Institutes of Health

We'd like to inform you that we have updated our Privacy Notice to comply with Europe’s new General Data Protection Regulation (GDPR) that applies since 25 May 2018.

Do not show this banner again