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Q12802

- AKP13_HUMAN

UniProt

Q12802 - AKP13_HUMAN

Protein

A-kinase anchor protein 13

Gene

AKAP13

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 131 (01 Oct 2014)
      Sequence version 2 (06 Mar 2007)
      Previous versions | rss
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    Functioni

    Anchors cAMP-dependent protein kinase (PKA) and acts as an adapter protein to selectively couple G alpha-13 and Rho. Augments gene activation by the estrogen receptor in an element-specific and ligand-dependent manner. Activates estrogen receptor beta by a p38 MAPK-dependent pathway. Stimulates exchange activity on Rho proteins in vitro, but not on CDC42, Ras or Rac and may bind calcium ions.4 Publications

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1791 – 183848Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    GO - Molecular functioni

    1. cAMP-dependent protein kinase activity Source: UniProtKB
    2. metal ion binding Source: UniProtKB-KW
    3. protein binding Source: IntAct
    4. Rho guanyl-nucleotide exchange factor activity Source: InterPro
    5. signal transducer activity Source: ProtInc

    GO - Biological processi

    1. apoptotic signaling pathway Source: Reactome
    2. neurotrophin TRK receptor signaling pathway Source: Reactome
    3. nuclear export Source: Ensembl
    4. positive regulation of apoptotic process Source: Reactome
    5. protein phosphorylation Source: GOC
    6. regulation of cardiac muscle hypertrophy Source: Ensembl
    7. regulation of glucocorticoid mediated signaling pathway Source: Ensembl
    8. regulation of protein kinase activity Source: Ensembl
    9. regulation of small GTPase mediated signal transduction Source: Reactome
    10. small GTPase mediated signal transduction Source: Reactome

    Keywords - Molecular functioni

    Guanine-nucleotide releasing factor

    Keywords - Ligandi

    Metal-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18407. G alpha (12/13) signalling events.
    SignaLinkiQ12802.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    A-kinase anchor protein 13
    Short name:
    AKAP-13
    Alternative name(s):
    AKAP-Lbc
    Breast cancer nuclear receptor-binding auxiliary protein
    Guanine nucleotide exchange factor Lbc
    Human thyroid-anchoring protein 31
    Lymphoid blast crisis oncogene
    Short name:
    LBC oncogene
    Non-oncogenic Rho GTPase-specific GTP exchange factor
    Protein kinase A-anchoring protein 13
    Short name:
    PRKA13
    p47
    Gene namesi
    Name:AKAP13
    Synonyms:BRX, HT31, LBC
    OrganismiHomo sapiens (Human)
    Taxonomic identifieri9606 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
    ProteomesiUP000005640: Chromosome 15

    Organism-specific databases

    HGNCiHGNC:371. AKAP13.

    Subcellular locationi

    GO - Cellular componenti

    1. cytoplasm Source: HPA
    2. cytosol Source: Reactome
    3. membrane Source: UniProtKB
    4. nucleus Source: UniProtKB-SubCell
    5. perinuclear region of cytoplasm Source: Ensembl

    Keywords - Cellular componenti

    Cytoplasm, Membrane, Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi1251 – 12511A → P: Loss of PKA anchoring; when associated with P-1260. 1 Publication
    Mutagenesisi1260 – 12601I → P: Loss of PKA anchoring; when associated with P-1251. 1 Publication
    Mutagenesisi1265 – 12651A → P: Abolishes RII-binding. 1 Publication
    Mutagenesisi2153 – 21531Y → F: Loss of interaction with RHOA. 1 Publication

    Keywords - Diseasei

    Proto-oncogene

    Organism-specific databases

    PharmGKBiPA24665.

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Chaini1 – 28132813A-kinase anchor protein 13PRO_0000080963Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei790 – 7901Phosphoserine1 Publication
    Modified residuei983 – 9831Phosphoserine5 Publications
    Modified residuei1565 – 15651Phosphoserine1 Publication
    Modified residuei1642 – 16421Phosphoserine2 Publications
    Modified residuei1645 – 16451Phosphoserine3 Publications
    Modified residuei1647 – 16471Phosphoserine3 Publications
    Modified residuei1876 – 18761Phosphoserine2 Publications
    Modified residuei1895 – 18951Phosphoserine1 Publication
    Modified residuei1929 – 19291Phosphoserine3 Publications
    Modified residuei1930 – 19301Phosphothreonine1 Publication
    Modified residuei1932 – 19321Phosphoserine2 Publications
    Modified residuei2398 – 23981Phosphoserine1 Publication
    Modified residuei2563 – 25631Phosphoserine1 Publication
    Modified residuei2703 – 27031Phosphoserine1 Publication
    Modified residuei2709 – 27091Phosphoserine1 Publication
    Modified residuei2728 – 27281Phosphoserine4 Publications

    Keywords - PTMi

    Phosphoprotein

    Proteomic databases

    MaxQBiQ12802.
    PaxDbiQ12802.
    PRIDEiQ12802.

    PTM databases

    PhosphoSiteiQ12802.

    Expressioni

    Tissue specificityi

    Expressed as a 5.3 kb transcript in hematopoietic cells, skeletal muscle, lung, heart, estrogen-responsive reproductive tissues, including breast ductal epithelium. Also found in testis and breast cancer cell lines. Predominantly expressed as a 10 kb transcript in the heart and at lower levels in the lung, placenta, kidney, pancreas, skeletal muscle and liver. Transcripts of between 6-9 kb are also expressed in myeloid and lymphoid lineages, a variety of epithelial tissues, and in skeletal muscle.3 Publications

    Gene expression databases

    ArrayExpressiQ12802.
    BgeeiQ12802.
    GenevestigatoriQ12802.

    Organism-specific databases

    HPAiHPA019773.

    Interactioni

    Subunit structurei

    Binds cAMP-dependent protein kinase (PKA) and to the RII-alpha regulatory subunit of PKA. Interacts with ESR1, ESR2, THRA, PPARA, RHOA and NME2.5 Publications

    Binary interactionsi

    WithEntry#Exp.IntActNotes
    ESR1P033723EBI-1373806,EBI-78473
    TGM2P219804EBI-1373806,EBI-727668

    Protein-protein interaction databases

    BioGridi116383. 17 interactions.
    DIPiDIP-180N.
    IntActiQ12802. 22 interactions.
    MINTiMINT-3308570.

    Structurei

    Secondary structure

    1
    2813
    Legend: HelixTurnBeta strand
    Show more details
    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Helixi1248 – 126316
    Turni1264 – 12685
    Beta strandi1973 – 19753
    Helixi1976 – 19794
    Helixi1982 – 19865
    Helixi1990 – 201829
    Helixi2020 – 20278
    Helixi2032 – 20387
    Helixi2042 – 206120
    Helixi2078 – 20847
    Helixi2087 – 211731
    Helixi2119 – 213113
    Helixi2135 – 21373
    Helixi2139 – 214911
    Helixi2150 – 21523
    Helixi2153 – 216311
    Helixi2168 – 220740
    Beta strandi2213 – 22153
    Beta strandi2221 – 22233
    Helixi2224 – 22263
    Beta strandi2232 – 224110
    Beta strandi2247 – 226519
    Beta strandi2268 – 22714
    Beta strandi2275 – 22773
    Beta strandi2279 – 22824
    Beta strandi2286 – 22905
    Beta strandi2297 – 23026
    Beta strandi2304 – 23074
    Beta strandi2310 – 23145
    Helixi2318 – 233518

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    EntryMethodResolution (Å)ChainPositionsPDBsum
    2DRNNMR-C1246-1269[»]
    2LG1NMR-A2164-2346[»]
    4D0NX-ray2.10B1968-2338[»]
    4D0OX-ray2.75A/B1972-2207[»]
    ProteinModelPortaliQ12802.
    SMRiQ12802. Positions 1988-2357.
    ModBaseiSearch...
    MobiDBiSearch...

    Miscellaneous databases

    EvolutionaryTraceiQ12802.

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini1994 – 2191198DHPROSITE-ProRule annotationAdd
    BLAST
    Domaini2231 – 2333103PHPROSITE-ProRule annotationAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni494 – 51623RII-bindingAdd
    BLAST
    Regioni1919 – 2813895Interaction with ESR1Add
    BLAST

    Coiled coil

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Coiled coili1758 – 179033Sequence AnalysisAdd
    BLAST
    Coiled coili2345 – 238137Sequence AnalysisAdd
    BLAST
    Coiled coili2568 – 2683116Sequence AnalysisAdd
    BLAST

    Compositional bias

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Compositional biasi1471 – 14744Poly-Ser
    Compositional biasi1534 – 15374Poly-Glu
    Compositional biasi2778 – 279013Poly-LysAdd
    BLAST

    Domaini

    Both the DH and PH domains are required for transforming activity.1 Publication

    Sequence similaritiesi

    Contains 1 DH (DBL-homology) domain.PROSITE-ProRule annotation
    Contains 1 PH domain.PROSITE-ProRule annotation
    Contains 1 phorbol-ester/DAG-type zinc finger.PROSITE-ProRule annotation

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri1791 – 183848Phorbol-ester/DAG-typePROSITE-ProRule annotationAdd
    BLAST

    Keywords - Domaini

    Coiled coil, Zinc-finger

    Phylogenomic databases

    eggNOGiCOG5422.
    HOVERGENiHBG080828.
    KOiK16529.
    OMAiGNDENMS.
    PhylomeDBiQ12802.
    TreeFamiTF325887.

    Family and domain databases

    Gene3Di1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProiIPR028852. AKAP13.
    IPR000219. DH-domain.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    [Graphical view]
    PANTHERiPTHR13944:SF4. PTHR13944:SF4. 1 hit.
    PfamiPF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    [Graphical view]
    SMARTiSM00109. C1. 1 hit.
    SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    [Graphical view]
    SUPFAMiSSF48065. SSF48065. 1 hit.
    PROSITEiPS50010. DH_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view]

    Sequences (4)i

    Sequence statusi: Complete.

    This entry describes 4 isoformsi produced by alternative splicing. Align

    Isoform 1 (identifier: Q12802-1) [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

    MKLNPQQAPL YGDCVVTVLL AEEDKAEDDV VFYLVFLGST LRHCTSTRKV     50
    SSDTLETIAP GHDCCETVKV QLCASKEGLP VFVVAEEDFH FVQDEAYDAA 100
    QFLATSAGNQ QALNFTRFLD QSGPPSGDVN SLDKKLVLAF RHLKLPTEWN 150
    VLGTDQSLHD AGPRETLMHF AVRLGLLRLT WFLLQKPGGR GALSIHNQEG 200
    ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG DCSVRHHREL 250
    DIYTLTSESD SHHEHPFPGD GCTGPIFKLM NIQQQLMKTN LKQMDSLMPL 300
    MMTAQDPSSA PETDGQFLPC APEPTDPQRL SSSEETESTQ CCPGSPVAQT 350
    ESPCDLSSIV EEENTDRSCR KKNKGVERKG EEVEPAPIVD SGTVSDQDSC 400
    LQSLPDCGVK GTEGLSSCGN RNEETGTKSS GMPTDQESLS SGDAVLQRDL 450
    VMEPGTAQYS SGGELGGIST TNVSTPDTAG EMEHGLMNPD ATVWKNVLQG 500
    GESTKERFEN SNIGTAGASD VHVTSKPVDK ISVPNCAPAA SSLDGNKPAE 550
    SSLAFSNEET STEKTAETET SRSREESADA PVDQNSVVIP AAAKDKISDG 600
    LEPYTLLAAG IGEAMSPSDL ALLGLEEDVM PHQNSETNSS HAQSQKGKSS 650
    PICSTTGDDK LCADSACQQN TVTSSGDLVA KLCDNIVSES ESTTARQPSS 700
    QDPPDASHCE DPQAHTVTSD PVRDTQERAD FCPFKVVDNK GQRKDVKLDK 750
    PLTNMLEVVS HPHPVVPKME KELVPDQAVI SDSTFSLANS PGSESVTKDD 800
    ALSFVPSQKE KGTATPELHT ATDYRDGPDG NSNEPDTRPL EDRAVGLSTS 850
    STAAELQHGM GNTSLTGLGG EHEGPAPPAI PEALNIKGNT DSSLQSVGKA 900
    TLALDSVLTE EGKLLVVSES SAAQEQDKDK AVTCSSIKEN ALSSGTLQEE 950
    QRTPPPGQDT QQFHEKSISA DCAKDKALQL SNSPGASSAF LKAETEHNKE 1000
    VAPQVSLLTQ GGAAQSLVPP GASLATESRQ EALGAEHNSS ALLPCLLPDG 1050
    SDGSDALNCS QPSPLDVGVK NTQSQGKTSA CEVSGDVTVD VTGVNALQGM 1100
    AEPRRENISH NTQDILIPNV LLSQEKNAVL GLPVALQDKA VTDPQGVGTP 1150
    EMIPLDWEKG KLEGADHSCT MGDAEEAQID DEAHPVLLQP VAKELPTDME 1200
    LSAHDDGAPA GVREVMRAPP SGRERSTPSL PCMVSAQDAP LPKGADLIEE 1250
    AASRIVDAVI EQVKAAGALL TEGEACHMSL SSPELGPLTK GLESAFTEKV 1300
    STFPPGESLP MGSTPEEATG SLAGCFAGRE EPEKIILPVQ GPEPAAEMPD 1350
    VKAEDEVDFR ASSISEEVAV GSIAATLKMK QGPMTQAINR ENWCTIEPCP 1400
    DAASLLASKQ SPECENFLDV GLGRECTSKQ GVLKRESGSD SDLFHSPSDD 1450
    MDSIIFPKPE EEHLACDITG SSSSTDDTAS LDRHSSHGSD VSLSQILKPN 1500
    RSRDRQSLDG FYSHGMGAEG RESESEPADP GDVEEEEMDS ITEVPANCSV 1550
    LRSSMRSLSP FRRHSWGPGK NAASDAEMNH RSSMRVLGDV VRRPPIHRRS 1600
    FSLEGLTGGA GVGNKPSSSL EVSSANAEEL RHPFSGEERV DSLVSLSEED 1650
    LESDQREHRM FDQQICHRSK QQGFNYCTSA ISSPLTKSIS LMTISHPGLD 1700
    NSRPFHSTFH NTSANLTESI TEENYNFLPH SPSKKDSEWK SGTKVSRTFS 1750
    YIKNKMSSSK KSKEKEKEKD KIKEKEKDSK DKEKDKKTVN GHTFSSIPVV 1800
    GPISCSQCMK PFTNKDAYTC ANCSAFVHKG CRESLASCAK VKMKQPKGSL 1850
    QAHDTSSLPT VIMRNKPSQP KERPRSAVLL VDETATTPIF ANRRSQQSVS 1900
    LSKSVSIQNI TGVGNDENMS NTWKFLSHST DSLNKISKVN ESTESLTDEG 1950
    VGTDMNEGQL LGDFEIESKQ LEAESWSRII DSKFLKQQKK DVVKRQEVIY 2000
    ELMQTEFHHV RTLKIMSGVY SQGMMADLLF EQQMVEKLFP CLDELISIHS 2050
    QFFQRILERK KESLVDKSEK NFLIKRIGDV LVNQFSGENA ERLKKTYGKF 2100
    CGQHNQSVNY FKDLYAKDKR FQAFVKKKMS SSVVRRLGIP ECILLVTQRI 2150
    TKYPVLFQRI LQCTKDNEVE QEDLAQSLSL VKDVIGAVDS KVASYEKKVR 2200
    LNEIYTKTDS KSIMRMKSGQ MFAKEDLKRK KLVRDGSVFL KNAAGRLKEV 2250
    QAVLLTDILV FLQEKDQKYI FASLDQKSTV ISLKKLIVRE VAHEEKGLFL 2300
    ISMGMTDPEM VEVHASSKEE RNSWIQIIQD TINTLNRDED EGIPSENEEE 2350
    KKMLDTRARE LKEQLHQKDQ KILLLLEEKE MIFRDMAECS TPLPEDCSPT 2400
    HSPRVLFRSN TEEALKGGPL MKSAINEVEI LQGLVSGNLG GTLGPTVSSP 2450
    IEQDVVGPVS LPRRAETFGG FDSHQMNASK GGEKEEGDDG QDLRRTESDS 2500
    GLKKGGNANL VFMLKRNSEQ VVQSVVHLYE LLSALQGVVL QQDSYIEDQK 2550
    LVLSERALTR SLSRPSSLIE QEKQRSLEKQ RQDLANLQKQ QAQYLEEKRR 2600
    REREWEARER ELREREALLA QREEEVQQGQ QDLEKEREEL QQKKGTYQYD 2650
    LERLRAAQKQ LEREQEQLRR EAERLSQRQT ERDLCQVSHP HTKLMRIPSF 2700
    FPSPEEPPSP SAPSIAKSGS LDSELSVSPK RNSISRTHKD KGPFHILSST 2750
    SQTNKGPEGQ SQAPASTSAS TRLFGLTKPK EKKEKKKKNK TSRSQPGDGP 2800
    ASEVSAEGEE IFC 2813
    Length:2,813
    Mass (Da):307,550
    Last modified:March 6, 2007 - v2
    Checksum:i6A8FDAC9A3D3B1F2
    GO
    Isoform 2 (identifier: Q12802-2) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1583-1598: SMRVLGDVVRRPPIHR → MSWCPSGVQYSAGLSADFNY

    Show »
    Length:2,817
    Mass (Da):307,845
    Checksum:i4EA29B253C76698E
    GO
    Isoform 3 (identifier: Q12802-4) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         1581-1598: Missing.
         1950-1951: Missing.

    Show »
    Length:2,793
    Mass (Da):305,281
    Checksum:i117C84737CE9A79B
    GO
    Isoform 4 (identifier: Q12802-5) [UniParc]FASTAAdd to Basket

    The sequence of this isoform differs from the canonical sequence as follows:
         160-179: DAGPRETLMHFAVRLGLLRL → GENLYDLQTHFKFVIFLLFF
         180-2813: Missing.

    Show »
    Length:179
    Mass (Da):19,992
    Checksum:iD441A72053F1EBC5
    GO

    Sequence cautioni

    The sequence AAC50065.1 differs from that shown. Reason: Probable cloning artifact.
    The sequence AAD40799.1 differs from that shown. Reason: Intron retention.
    The sequence AAD21311.1 differs from that shown. Reason: Frameshift at positions 2614 and 2647.
    The sequence AAL40923.1 differs from that shown. Reason: Frameshift at positions 2614 and 2647.
    The sequence AAC50065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.
    The sequence AAD40799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti191 – 1911G → R in AAL40923. (PubMed:11696353)Curated
    Sequence conflicti354 – 3541C → R in AAL40923. (PubMed:11696353)Curated
    Sequence conflicti609 – 6091A → V in AAL40923. (PubMed:11696353)Curated
    Sequence conflicti614 – 6141A → T in AAL40923. (PubMed:11696353)Curated
    Sequence conflicti618 – 6181S → P in AAL40923. (PubMed:11696353)Curated
    Sequence conflicti619 – 6191D → A in AAL11723. (PubMed:11546812)Curated
    Sequence conflicti755 – 7551M → S in AAA58670. (PubMed:1618839)Curated
    Sequence conflicti1385 – 13873TQA → MLY in AAD21311. (PubMed:9627117)Curated
    Sequence conflicti1547 – 15471N → H in BAD92651. 1 PublicationCurated
    Sequence conflicti1766 – 17683EKE → KKK in AAA58670. (PubMed:1618839)Curated
    Sequence conflicti1877 – 18771A → G in AAD40799. (PubMed:9891067)Curated
    Sequence conflicti1897 – 18971Q → E in AAD40799. (PubMed:9891067)Curated
    Sequence conflicti2035 – 20351V → D in AAD21311. (PubMed:9627117)Curated
    Sequence conflicti2488 – 24881D → G in AAD21311. (PubMed:9627117)Curated
    Sequence conflicti2667 – 26682QL → HV in BAB62913. 1 PublicationCurated
    Sequence conflicti2667 – 26682QL → HV in AAD21311. (PubMed:9627117)Curated

    Natural variant

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Natural varianti452 – 4521M → T.1 Publication
    Corresponds to variant rs2061821 [ dbSNP | Ensembl ].
    VAR_030925
    Natural varianti494 – 4941W → R.1 Publication
    Corresponds to variant rs2061822 [ dbSNP | Ensembl ].
    VAR_030926
    Natural varianti526 – 5261K → Q.
    Corresponds to variant rs34434221 [ dbSNP | Ensembl ].
    VAR_051986
    Natural varianti574 – 5741R → C.2 Publications
    Corresponds to variant rs2061824 [ dbSNP | Ensembl ].
    VAR_030927
    Natural varianti624 – 6241G → V.1 Publication
    Corresponds to variant rs745191 [ dbSNP | Ensembl ].
    VAR_030928
    Natural varianti689 – 6891E → K.1 Publication
    Corresponds to variant rs7177107 [ dbSNP | Ensembl ].
    VAR_030929
    Natural varianti845 – 8451V → A.1 Publication
    Corresponds to variant rs4075256 [ dbSNP | Ensembl ].
    VAR_030930
    Natural varianti897 – 8971V → M.2 Publications
    Corresponds to variant rs4075254 [ dbSNP | Ensembl ].
    VAR_030931
    Natural varianti1062 – 10621P → A.1 Publication
    Corresponds to variant rs4843074 [ dbSNP | Ensembl ].
    VAR_030932
    Natural varianti1086 – 10861D → N.1 Publication
    Corresponds to variant rs4843075 [ dbSNP | Ensembl ].
    VAR_030933
    Natural varianti1216 – 12161M → T.1 Publication
    Corresponds to variant rs7162168 [ dbSNP | Ensembl ].
    VAR_030934
    Natural varianti1525 – 15251S → G.
    Corresponds to variant rs35079107 [ dbSNP | Ensembl ].
    VAR_051987
    Natural varianti2457 – 24571G → S.4 Publications
    Corresponds to variant rs2241268 [ dbSNP | Ensembl ].
    VAR_030935
    Natural varianti2801 – 28011A → T.
    Corresponds to variant rs2614668 [ dbSNP | Ensembl ].
    VAR_030936

    Alternative sequence

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Alternative sequencei160 – 17920DAGPR…GLLRL → GENLYDLQTHFKFVIFLLFF in isoform 4. 1 PublicationVSP_023486Add
    BLAST
    Alternative sequencei180 – 28132634Missing in isoform 4. 1 PublicationVSP_023487Add
    BLAST
    Alternative sequencei1581 – 159818Missing in isoform 3. 3 PublicationsVSP_023489Add
    BLAST
    Alternative sequencei1583 – 159816SMRVL…PPIHR → MSWCPSGVQYSAGLSADFNY in isoform 2. 1 PublicationVSP_023490Add
    BLAST
    Alternative sequencei1950 – 19512Missing in isoform 3. 3 PublicationsVSP_023491

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF387101 mRNA. Translation: AAL40923.1. Frameshift.
    AF406992 mRNA. Translation: AAL11723.1.
    AB055890 mRNA. Translation: BAB62913.1.
    BC050312 mRNA. Translation: AAH50312.1.
    AF126008 mRNA. Translation: AAD21311.1. Frameshift.
    AF127481 mRNA. Translation: AAD40799.1. Sequence problems.
    U03634 mRNA. Translation: AAC50065.1. Sequence problems.
    M90360 mRNA. Translation: AAA58670.1. Different termination.
    AB209414 mRNA. Translation: BAD92651.1.
    CCDSiCCDS32319.1. [Q12802-1]
    CCDS32320.1. [Q12802-2]
    PIRiA42915.
    I38434.
    RefSeqiNP_001257475.1. NM_001270546.1.
    NP_006729.4. NM_006738.5. [Q12802-2]
    NP_009131.2. NM_007200.4. [Q12802-1]
    XP_005254905.1. XM_005254848.1. [Q12802-4]
    UniGeneiHs.459211.
    Hs.710656.

    Genome annotation databases

    EnsembliENST00000361243; ENSP00000354718; ENSG00000170776. [Q12802-2]
    ENST00000394518; ENSP00000378026; ENSG00000170776. [Q12802-1]
    ENST00000560302; ENSP00000453634; ENSG00000170776. [Q12802-5]
    GeneIDi11214.
    KEGGihsa:11214.
    UCSCiuc002bls.4. human. [Q12802-5]
    uc002blu.2. human. [Q12802-2]
    uc002blv.2. human. [Q12802-1]

    Polymorphism databases

    DMDMi134048676.

    Keywords - Coding sequence diversityi

    Alternative splicing, Polymorphism

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    AF387101 mRNA. Translation: AAL40923.1 . Frameshift.
    AF406992 mRNA. Translation: AAL11723.1 .
    AB055890 mRNA. Translation: BAB62913.1 .
    BC050312 mRNA. Translation: AAH50312.1 .
    AF126008 mRNA. Translation: AAD21311.1 . Frameshift.
    AF127481 mRNA. Translation: AAD40799.1 . Sequence problems.
    U03634 mRNA. Translation: AAC50065.1 . Sequence problems.
    M90360 mRNA. Translation: AAA58670.1 . Different termination.
    AB209414 mRNA. Translation: BAD92651.1 .
    CCDSi CCDS32319.1. [Q12802-1 ]
    CCDS32320.1. [Q12802-2 ]
    PIRi A42915.
    I38434.
    RefSeqi NP_001257475.1. NM_001270546.1.
    NP_006729.4. NM_006738.5. [Q12802-2 ]
    NP_009131.2. NM_007200.4. [Q12802-1 ]
    XP_005254905.1. XM_005254848.1. [Q12802-4 ]
    UniGenei Hs.459211.
    Hs.710656.

    3D structure databases

    Select the link destinations:
    PDBe
    RCSB PDB
    PDBj
    Links Updated
    Entry Method Resolution (Å) Chain Positions PDBsum
    2DRN NMR - C 1246-1269 [» ]
    2LG1 NMR - A 2164-2346 [» ]
    4D0N X-ray 2.10 B 1968-2338 [» ]
    4D0O X-ray 2.75 A/B 1972-2207 [» ]
    ProteinModelPortali Q12802.
    SMRi Q12802. Positions 1988-2357.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 116383. 17 interactions.
    DIPi DIP-180N.
    IntActi Q12802. 22 interactions.
    MINTi MINT-3308570.

    PTM databases

    PhosphoSitei Q12802.

    Polymorphism databases

    DMDMi 134048676.

    Proteomic databases

    MaxQBi Q12802.
    PaxDbi Q12802.
    PRIDEi Q12802.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENST00000361243 ; ENSP00000354718 ; ENSG00000170776 . [Q12802-2 ]
    ENST00000394518 ; ENSP00000378026 ; ENSG00000170776 . [Q12802-1 ]
    ENST00000560302 ; ENSP00000453634 ; ENSG00000170776 . [Q12802-5 ]
    GeneIDi 11214.
    KEGGi hsa:11214.
    UCSCi uc002bls.4. human. [Q12802-5 ]
    uc002blu.2. human. [Q12802-2 ]
    uc002blv.2. human. [Q12802-1 ]

    Organism-specific databases

    CTDi 11214.
    GeneCardsi GC15P085925.
    H-InvDB HIX0021561.
    HIX0172808.
    HGNCi HGNC:371. AKAP13.
    HPAi HPA019773.
    MIMi 604686. gene.
    neXtProti NX_Q12802.
    PharmGKBi PA24665.
    GenAtlasi Search...

    Phylogenomic databases

    eggNOGi COG5422.
    HOVERGENi HBG080828.
    KOi K16529.
    OMAi GNDENMS.
    PhylomeDBi Q12802.
    TreeFami TF325887.

    Enzyme and pathway databases

    Reactomei REACT_11051. Rho GTPase cycle.
    REACT_13638. NRAGE signals death through JNK.
    REACT_18407. G alpha (12/13) signalling events.
    SignaLinki Q12802.

    Miscellaneous databases

    ChiTaRSi AKAP13. human.
    EvolutionaryTracei Q12802.
    GeneWikii AKAP13.
    GenomeRNAii 11214.
    NextBioi 42679.
    PROi Q12802.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi Q12802.
    Bgeei Q12802.
    Genevestigatori Q12802.

    Family and domain databases

    Gene3Di 1.20.900.10. 1 hit.
    2.30.29.30. 1 hit.
    InterProi IPR028852. AKAP13.
    IPR000219. DH-domain.
    IPR001849. PH_domain.
    IPR011993. PH_like_dom.
    IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
    [Graphical view ]
    PANTHERi PTHR13944:SF4. PTHR13944:SF4. 1 hit.
    Pfami PF00169. PH. 1 hit.
    PF00621. RhoGEF. 1 hit.
    [Graphical view ]
    SMARTi SM00109. C1. 1 hit.
    SM00233. PH. 1 hit.
    SM00325. RhoGEF. 1 hit.
    [Graphical view ]
    SUPFAMi SSF48065. SSF48065. 1 hit.
    PROSITEi PS50010. DH_2. 1 hit.
    PS50003. PH_DOMAIN. 1 hit.
    PS00479. ZF_DAG_PE_1. 1 hit.
    PS50081. ZF_DAG_PE_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling."
      Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V., Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.
      FEBS Lett. 507:264-268(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RHOA, VARIANTS CYS-574 AND SER-2457.
    2. "AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation."
      Diviani D., Soderling J., Scott J.D.
      J. Biol. Chem. 276:44247-44257(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH RHOA; RHOB AND RHOC, MUTAGENESIS OF ALA-1251; ILE-1260 AND TYR-2153, VARIANTS VAL-624; MET-897 AND SER-2457.
    3. Miyamoto M., Ono Y.
      Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANTS THR-452; ARG-494; CYS-574; LYS-689; ALA-845; MET-897; ALA-1062; ASN-1086 AND THR-1216.
      Tissue: Lung.
    4. "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
      The MGC Project Team
      Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 4).
      Tissue: Hippocampus.
    5. "Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action."
      Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J.
      Oncogene 16:2513-2526(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1385-2813 (ISOFORM 1), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ESR1; THRA AND PPARA, VARIANT SER-2457.
      Tissue: Testis.
    6. "Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting."
      Sterpetti P., Hack A.A., Bashar M.P., Park B., Cheng S.-D., Knoll J.H.M., Urano T., Feig L.A., Toksoz D.
      Mol. Cell. Biol. 19:1334-1345(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1827-2813 (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, DOMAIN, TISSUE SPECIFICITY.
      Tissue: Skeletal muscle.
    7. Erratum
      Sterpetti P., Hack A.A., Bashar M.P., Park B., Cheng S.D., Knoll J.H., Urano T., Feig L.A., Toksoz D.
      Mol. Cell. Biol. 19:3930-3930(1999)
    8. "Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products."
      Toksoz D., Williams D.A.
      Oncogene 9:621-628(1994) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 1913-2335 (ISOFORM 3).
    9. "Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain."
      Carr D.W., Hausken Z.E., Fraser I.D.C., Stofko-Hahn R.E., Scott J.D.
      J. Biol. Chem. 267:13376-13382(1992) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 754-1768, PKA AND RII BINDING, MUTAGENESIS OF ALA-1265.
      Tissue: Thyroid.
    10. Totoki Y., Toyoda A., Takeda T., Sakaki Y., Tanaka A., Yokoyama S., Ohara O., Nagase T., Kikuno R.F.
      Submitted (MAR-2005) to the EMBL/GenBank/DDBJ databases
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1486-2813 (ISOFORM 3), VARIANT SER-2457.
      Tissue: Brain.
    11. "The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway."
      Driggers P.H., Segars J.H., Rubino D.M.
      J. Biol. Chem. 276:46792-46797(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: FUNCTION, INTERACTION WITH ESR2.
    12. "Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2."
      Iwashita S., Fujii M., Mukai H., Ono Y., Miyamoto M.
      Biochem. Biophys. Res. Commun. 320:1063-1068(2004) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH NME2.
    13. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
      Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
      Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1565, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
      Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
      Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 AND SER-2728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    15. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
      Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
      Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    16. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983; SER-1645; SER-1647; SER-1876; SER-1929; SER-1932; SER-2398; SER-2703; SER-2709 AND SER-2728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    17. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
      Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
      Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    18. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
      Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
      Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983; SER-1642; SER-1645; SER-1647; SER-1876 AND SER-2728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Leukemic T-cell.
    19. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
      Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
      Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-790; SER-983 AND SER-1929, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Cervix carcinoma.
    20. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    21. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
      Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
      Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983; SER-1642; SER-1645; SER-1647; SER-1895; SER-1929; THR-1930; SER-1932; SER-2563 AND SER-2728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    22. "A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes."
      Newlon M.G., Roy M., Morikis D., Carr D.W., Westphal R., Scott J.D., Jennings P.A.
      EMBO J. 20:1651-1662(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: STRUCTURE BY NMR OF 493-516.

    Entry informationi

    Entry nameiAKP13_HUMAN
    AccessioniPrimary (citable) accession number: Q12802
    Secondary accession number(s): Q14572
    , Q59FP6, Q86W90, Q8WXQ6, Q96JP6, Q96P79, Q9Y5T0, Q9Y5T6
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: July 15, 1999
    Last sequence update: March 6, 2007
    Last modified: October 1, 2014
    This is version 131 of the entry and version 2 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program
    DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

    Miscellaneousi

    Keywords - Technical termi

    3D-structure, Complete proteome, Reference proteome

    Documents

    1. Human chromosome 15
      Human chromosome 15: entries, gene names and cross-references to MIM
    2. Human entries with polymorphisms or disease mutations
      List of human entries with polymorphisms or disease mutations
    3. Human polymorphisms and disease mutations
      Index of human polymorphisms and disease mutations
    4. MIM cross-references
      Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
    5. PDB cross-references
      Index of Protein Data Bank (PDB) cross-references
    6. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3