Details for: AKAP13

Gene ID: 11214

Symbol: AKAP13

Ensembl ID: ENSG00000170776

Description: A-kinase anchoring protein 13

Associated with

Other Information

Genular Protein ID: 1452995007

Symbol: AKP13_HUMAN

Name: A-kinase anchor protein 13

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 11696353

Title: Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling.

PubMed ID: 11696353

DOI: 10.1016/s0014-5793(01)02995-7

PubMed ID: 11546812

Title: AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation.

PubMed ID: 11546812

DOI: 10.1074/jbc.m106629200

PubMed ID: 15489334

Title: The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).

PubMed ID: 15489334

DOI: 10.1101/gr.2596504

PubMed ID: 9627117

Title: Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action.

PubMed ID: 9627117

DOI: 10.1038/sj.onc.1201783

PubMed ID: 9891067

Title: Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting.

PubMed ID: 9891067

DOI: 10.1128/mcb.19.2.1334

PubMed ID: 8290273

Title: Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products.

PubMed ID: 8290273

PubMed ID: 1618839

Title: Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain.

PubMed ID: 1618839

DOI: 10.1016/s0021-9258(18)42221-1

PubMed ID: 11579095

Title: The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway.

PubMed ID: 11579095

DOI: 10.1074/jbc.m106927200

PubMed ID: 15249197

Title: Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2.

PubMed ID: 15249197

DOI: 10.1016/j.bbrc.2004.06.067

PubMed ID: 15229649

Title: Anchoring of both PKA and 14-3-3 inhibits the Rho-GEF activity of the AKAP-Lbc signaling complex.

PubMed ID: 15229649

DOI: 10.1038/sj.emboj.7600287

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16469733

Title: Rho family Guanine nucleotide exchange factor Brx couples extracellular signals to the glucocorticoid signaling system.

PubMed ID: 16469733

DOI: 10.1074/jbc.m509339200

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 17537920

Title: The A-kinase anchoring protein (AKAP)-Lbc-signaling complex mediates alpha1 adrenergic receptor-induced cardiomyocyte hypertrophy.

PubMed ID: 17537920

DOI: 10.1073/pnas.0701099104

PubMed ID: 18691976

Title: Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle.

PubMed ID: 18691976

DOI: 10.1016/j.molcel.2008.07.007

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 21102438

Title: AKAP-Lbc enhances cyclic AMP control of the ERK1/2 cascade.

PubMed ID: 21102438

DOI: 10.1038/ncb2130

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21224381

Title: A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling complex involved in alpha1-adrenergic receptor-induced p38 activation.

PubMed ID: 21224381

DOI: 10.1074/jbc.m110.185645

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

DOI: 10.1021/pr300630k

PubMed ID: 23090968

Title: A-kinase-anchoring protein-Lbc anchors IkappaB kinase beta to support interleukin-6-mediated cardiomyocyte hypertrophy.

PubMed ID: 23090968

DOI: 10.1128/mcb.00887-12

PubMed ID: 23716597

Title: A-kinase anchoring protein Lbc coordinates a p38 activating signaling complex controlling compensatory cardiac hypertrophy.

PubMed ID: 23716597

DOI: 10.1128/mcb.00031-13

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

DOI: 10.1074/mcp.o113.027870

PubMed ID: 11285229

Title: A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes.

PubMed ID: 11285229

DOI: 10.1093/emboj/20.7.1651

PubMed ID: 25186459

Title: The crystal structure of the RhoA-AKAP-Lbc DH-PH domain complex.

PubMed ID: 25186459

DOI: 10.1042/bj20140606

PubMed ID: 24993829

Title: Structural insights into the activation of the RhoA GTPase by the lymphoid blast crisis (Lbc) oncoprotein.

PubMed ID: 24993829

DOI: 10.1074/jbc.m114.561787

Sequence Information:

  • Length: 2813
  • Mass: 307550
  • Checksum: 6A8FDAC9A3D3B1F2
  • Sequence:
  • MKLNPQQAPL YGDCVVTVLL AEEDKAEDDV VFYLVFLGST LRHCTSTRKV SSDTLETIAP 
    GHDCCETVKV QLCASKEGLP VFVVAEEDFH FVQDEAYDAA QFLATSAGNQ QALNFTRFLD 
    QSGPPSGDVN SLDKKLVLAF RHLKLPTEWN VLGTDQSLHD AGPRETLMHF AVRLGLLRLT 
    WFLLQKPGGR GALSIHNQEG ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG 
    DCSVRHHREL DIYTLTSESD SHHEHPFPGD GCTGPIFKLM NIQQQLMKTN LKQMDSLMPL 
    MMTAQDPSSA PETDGQFLPC APEPTDPQRL SSSEETESTQ CCPGSPVAQT ESPCDLSSIV 
    EEENTDRSCR KKNKGVERKG EEVEPAPIVD SGTVSDQDSC LQSLPDCGVK GTEGLSSCGN 
    RNEETGTKSS GMPTDQESLS SGDAVLQRDL VMEPGTAQYS SGGELGGIST TNVSTPDTAG 
    EMEHGLMNPD ATVWKNVLQG GESTKERFEN SNIGTAGASD VHVTSKPVDK ISVPNCAPAA 
    SSLDGNKPAE SSLAFSNEET STEKTAETET SRSREESADA PVDQNSVVIP AAAKDKISDG 
    LEPYTLLAAG IGEAMSPSDL ALLGLEEDVM PHQNSETNSS HAQSQKGKSS PICSTTGDDK 
    LCADSACQQN TVTSSGDLVA KLCDNIVSES ESTTARQPSS QDPPDASHCE DPQAHTVTSD 
    PVRDTQERAD FCPFKVVDNK GQRKDVKLDK PLTNMLEVVS HPHPVVPKME KELVPDQAVI 
    SDSTFSLANS PGSESVTKDD ALSFVPSQKE KGTATPELHT ATDYRDGPDG NSNEPDTRPL 
    EDRAVGLSTS STAAELQHGM GNTSLTGLGG EHEGPAPPAI PEALNIKGNT DSSLQSVGKA 
    TLALDSVLTE EGKLLVVSES SAAQEQDKDK AVTCSSIKEN ALSSGTLQEE QRTPPPGQDT 
    QQFHEKSISA DCAKDKALQL SNSPGASSAF LKAETEHNKE VAPQVSLLTQ GGAAQSLVPP 
    GASLATESRQ EALGAEHNSS ALLPCLLPDG SDGSDALNCS QPSPLDVGVK NTQSQGKTSA 
    CEVSGDVTVD VTGVNALQGM AEPRRENISH NTQDILIPNV LLSQEKNAVL GLPVALQDKA 
    VTDPQGVGTP EMIPLDWEKG KLEGADHSCT MGDAEEAQID DEAHPVLLQP VAKELPTDME 
    LSAHDDGAPA GVREVMRAPP SGRERSTPSL PCMVSAQDAP LPKGADLIEE AASRIVDAVI 
    EQVKAAGALL TEGEACHMSL SSPELGPLTK GLESAFTEKV STFPPGESLP MGSTPEEATG 
    SLAGCFAGRE EPEKIILPVQ GPEPAAEMPD VKAEDEVDFR ASSISEEVAV GSIAATLKMK 
    QGPMTQAINR ENWCTIEPCP DAASLLASKQ SPECENFLDV GLGRECTSKQ GVLKRESGSD 
    SDLFHSPSDD MDSIIFPKPE EEHLACDITG SSSSTDDTAS LDRHSSHGSD VSLSQILKPN 
    RSRDRQSLDG FYSHGMGAEG RESESEPADP GDVEEEEMDS ITEVPANCSV LRSSMRSLSP 
    FRRHSWGPGK NAASDAEMNH RSSMRVLGDV VRRPPIHRRS FSLEGLTGGA GVGNKPSSSL 
    EVSSANAEEL RHPFSGEERV DSLVSLSEED LESDQREHRM FDQQICHRSK QQGFNYCTSA 
    ISSPLTKSIS LMTISHPGLD NSRPFHSTFH NTSANLTESI TEENYNFLPH SPSKKDSEWK 
    SGTKVSRTFS YIKNKMSSSK KSKEKEKEKD KIKEKEKDSK DKEKDKKTVN GHTFSSIPVV 
    GPISCSQCMK PFTNKDAYTC ANCSAFVHKG CRESLASCAK VKMKQPKGSL QAHDTSSLPT 
    VIMRNKPSQP KERPRSAVLL VDETATTPIF ANRRSQQSVS LSKSVSIQNI TGVGNDENMS 
    NTWKFLSHST DSLNKISKVN ESTESLTDEG VGTDMNEGQL LGDFEIESKQ LEAESWSRII 
    DSKFLKQQKK DVVKRQEVIY ELMQTEFHHV RTLKIMSGVY SQGMMADLLF EQQMVEKLFP 
    CLDELISIHS QFFQRILERK KESLVDKSEK NFLIKRIGDV LVNQFSGENA ERLKKTYGKF 
    CGQHNQSVNY FKDLYAKDKR FQAFVKKKMS SSVVRRLGIP ECILLVTQRI TKYPVLFQRI 
    LQCTKDNEVE QEDLAQSLSL VKDVIGAVDS KVASYEKKVR LNEIYTKTDS KSIMRMKSGQ 
    MFAKEDLKRK KLVRDGSVFL KNAAGRLKEV QAVLLTDILV FLQEKDQKYI FASLDQKSTV 
    ISLKKLIVRE VAHEEKGLFL ISMGMTDPEM VEVHASSKEE RNSWIQIIQD TINTLNRDED 
    EGIPSENEEE KKMLDTRARE LKEQLHQKDQ KILLLLEEKE MIFRDMAECS TPLPEDCSPT 
    HSPRVLFRSN TEEALKGGPL MKSAINEVEI LQGLVSGNLG GTLGPTVSSP IEQDVVGPVS 
    LPRRAETFGG FDSHQMNASK GGEKEEGDDG QDLRRTESDS GLKKGGNANL VFMLKRNSEQ 
    VVQSVVHLYE LLSALQGVVL QQDSYIEDQK LVLSERALTR SLSRPSSLIE QEKQRSLEKQ 
    RQDLANLQKQ QAQYLEEKRR REREWEARER ELREREALLA QREEEVQQGQ QDLEKEREEL 
    QQKKGTYQYD LERLRAAQKQ LEREQEQLRR EAERLSQRQT ERDLCQVSHP HTKLMRIPSF 
    FPSPEEPPSP SAPSIAKSGS LDSELSVSPK RNSISRTHKD KGPFHILSST SQTNKGPEGQ 
    SQAPASTSAS TRLFGLTKPK EKKEKKKKNK TSRSQPGDGP ASEVSAEGEE IFC

Genular Protein ID: 3741129032

Symbol: B0AZU4_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Sequence Information:

  • Length: 385
  • Mass: 42641
  • Checksum: 001849D7DA7107C9
  • Sequence:
  • MYERHKRRYS LCDISKVDRT VDVVLLKINR ENWCTIEPCP DAASLLASKQ SPECENFLDV 
    GLGRECTSKQ GVLKRESGSD SDLFHSPSDD MDSIIFPKPE EEHLACDITG SSSSTDDTAS 
    LDRHSSHGSD VSLSQILKPN RSRDRQSLDG FYSHGMGAEG RESESEPADP GDVEEEEMDS 
    ITEVPANCSV LRSSMRSLSP FRRHSWGPGK NAASDAEMNH RSFSLEGLTG GAGVGNKPSS 
    SLEVSSANAE ELRHPFSGEE RADSLVSLSE EDLESDQREH RMFDQQICHR SKQQGFNYCT 
    SAISSPLTKS ISLMTISHPG LDNSRPFHST FHNTSANLTE SITEENYNFL PHSPSKKDSE 
    WKSGTKVSRT FSYIKNKMSS SKKSK

Genular Protein ID: 3263593295

Symbol: A8MYJ1_HUMAN

Name: N/A

UniProtKB Accession Codes:

Database IDs:

Citations:

PubMed ID: 17081983

Title: Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.

PubMed ID: 17081983

DOI: 10.1016/j.cell.2006.09.026

PubMed ID: 16964243

Title: A probability-based approach for high-throughput protein phosphorylation analysis and site localization.

PubMed ID: 16964243

DOI: 10.1038/nbt1240

PubMed ID: 16572171

Title: Analysis of the DNA sequence and duplication history of human chromosome 15.

PubMed ID: 16572171

DOI: 10.1038/nature04601

PubMed ID: 18669648

Title: A quantitative atlas of mitotic phosphorylation.

PubMed ID: 18669648

DOI: 10.1073/pnas.0805139105

PubMed ID: 19413330

Title: Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach.

PubMed ID: 19413330

DOI: 10.1021/ac9004309

PubMed ID: 19690332

Title: Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions.

PubMed ID: 19690332

DOI: 10.1126/scisignal.2000007

PubMed ID: 20068231

Title: Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis.

PubMed ID: 20068231

DOI: 10.1126/scisignal.2000475

PubMed ID: 21269460

Title: Initial characterization of the human central proteome.

PubMed ID: 21269460

DOI: 10.1186/1752-0509-5-17

PubMed ID: 21406692

Title: System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation.

PubMed ID: 21406692

DOI: 10.1126/scisignal.2001570

PubMed ID: 23186163

Title: Toward a comprehensive characterization of a human cancer cell phosphoproteome.

PubMed ID: 23186163

PubMed ID: 24275569

Title: An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome.

PubMed ID: 24275569

DOI: 10.1016/j.jprot.2013.11.014

PubMed ID: 24129315

Title: Immunoaffinity enrichment and mass spectrometry analysis of protein methylation.

PubMed ID: 24129315

Sequence Information:

  • Length: 1434
  • Mass: 161841
  • Checksum: E181F9F0421C7CC6
  • Sequence:
  • MYERHKRRYS LCDISKVDRT VDVVLLKINR ENWCTIEPCP DAASLLASKQ SPECENFLDV 
    GLGRECTSKQ GVLKRESGSD SDLFHSPSDD MDSIIFPKPE EEHLACDITG SSSSTDDTAS 
    LDRHSSHGSD VSLSQILKPN RSRDRQSLDG FYSHGMGAEG RESESEPADP GDVEEEEMDS 
    ITEVPANCSV LRSSMRSLSP FRRHSWGPGK NAASDAEMNH RSFSLEGLTG GAGVGNKPSS 
    SLEVSSANAE ELRHPFSGEE RVDSLVSLSE EDLESDQREH RMFDQQICHR SKQQGFNYCT 
    SAISSPLTKS ISLMTISHPG LDNSRPFHST FHNTSANLTE SITEENYNFL PHSPSKKDSE 
    WKSGTKVSRT FSYIKNKMSS SKKSKEKEKE KDKIKEKEKD SKDKEKDKKT VNGHTFSSIP 
    VVGPISCSQC MKPFTNKDAY TCANCSAFVH KGCRESLASC AKVKMKPKGS LQAHDTSSLP 
    TVIMRNKPSQ PKERPRSAVL LVDETATTPI FANRRSQQSV SLSKSVSIQN ITGVGNDENM 
    SNTWKFLSHS TDSLNKISKV NESTESLTDE GVGTDMNEGQ LLGDFEIESK QLEAESWSRI 
    IDSKFLKQQK KDVVKRQEVI YELMQTEFHH VRTLKIMSGV YSQGMMADLL FEQQMVEKLF 
    PCLDELISIH SQFFQRILER KKESLVDKSE KNFLIKRIGD VLVNQFSGEN AERLKKTYGK 
    FCGQHNQSVN YFKDLYAKDK RFQAFVKKKM SSSVVRRLGI PECILLVTQR ITKYPVLFQR 
    ILQCTKDNEV EQEDLAQSLS LVKDVIGAVD SKVASYEKKV RLNEIYTKTD SKSIMRMKSG 
    QMFAKEDLKR KKLVRDGSVF LKNAAGRLKE VQAVLLTDIL VFLQEKDQKY IFASLDQKST 
    VISLKKLIVR EVAHEEKGLF LISMGMTDPE MVEVHASSKE ERNSWIQIIQ DTINTLNRDE 
    DEGIPSENEE EKKMLDTRAR ELKEQLHQKD QKILLLLEEK EMIFRDMAEC STPLPEDCSP 
    THSPRVLFRS NTEEALKGGP LMKSAINEVE ILQGLVSGNL GGTLGPTVSS PIEQDVVGPV 
    SLPRRAETFG GFDSHQMNAS KGGEKEEGDD GQDLRRTESD SGLKKGGNAN LVFMLKRNSE 
    QVVQSVVHLY ELLSALQGVV LQQDSYIEDQ KLVLSERALT RSLSRPSSLI EQEKQRSLEK 
    QRQDLANLQK QQAQYLEEKR RREREWEARE RELREREALL AQREEEVQQG QQDLEKEREE 
    LQQKKGTYQY DLERLRAAQK QLEREQEQLR REAERLSQRQ TERDLCQVSH PHTKLMRIPS 
    FFPSPEEPPS PSAPSIAKSG SLDSELSVSP KRNSISRTHK DKGPFHILSS TSQTNKGPEG 
    QSQAPASTSA STRLFGLTKP KEKKEKKKKN KTSRSQPGDG PASEVSAEGE EIFC

Database document:

This is a preview of the gene's schema. Only a few entries are kept for 'singleCellExpressions,' 'mRNAExpressions,' and other large data arrays for visualization purposes. You can zoom in with the mouse wheel for a closer view, and the text will adjust automatically if necessary. For the full schema, download it here.