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Protein

A-kinase anchor protein 13

Gene

AKAP13

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 out of 5-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 (PubMed:11546812, PubMed:15229649, PubMed:23090968, PubMed:25186459, PubMed:24993829). May also activate other Rho family members (PubMed:11546812). 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, PubMed:21224381). 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 (PubMed:16469733). 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 (PubMed:9627117, PubMed:11579095). 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 (PubMed:21102438). 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 (PubMed:11546812). 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, PubMed:23090968). Required for normal adaptive cardiac hypertrophy in response to pressure overload (PubMed:23716597). Plays a role in osteogenesis (By similarity).By similarity9 Publications

Regions

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

GO - Molecular functioni

  • cAMP-dependent protein kinase activity Source: InterPro
  • guanyl-nucleotide exchange factor activity Source: Reactome
  • MAP-kinase scaffold activity Source: UniProtKB
  • metal ion binding Source: UniProtKB-KW
  • protein complex scaffold Source: UniProtKB
  • protein kinase A binding Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB
  • Rho guanyl-nucleotide exchange factor activity Source: UniProtKB
  • signal transducer activity Source: ProtInc

GO - Biological processi

Complete GO annotation...

Keywords - Molecular functioni

Guanine-nucleotide releasing factor

Keywords - Ligandi

Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-193648. NRAGE signals death through JNK.
R-HSA-194840. Rho GTPase cycle.
R-HSA-416482. G alpha (12/13) signalling events.
SignaLinkiQ12802.
SIGNORiQ12802.

Names & Taxonomyi

Protein namesi
Recommended name:
A-kinase anchor protein 13
Short name:
AKAP-13
Alternative name(s):
AKAP-Lbc1 Publication
Breast cancer nuclear receptor-binding auxiliary protein1 Publication
Guanine nucleotide exchange factor Lbc
Human thyroid-anchoring protein 311 Publication
Lymphoid blast crisis oncogene1 Publication
Short name:
LBC oncogene1 Publication
Non-oncogenic Rho GTPase-specific GTP exchange factor
Protein kinase A-anchoring protein 13
Short name:
PRKA13
p47
Gene namesi
Name:AKAP13
Synonyms:BRX1 Publication, HT311 Publication, LBC
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 15

Organism-specific databases

HGNCiHGNC:371. AKAP13.

Subcellular locationi

GO - Cellular componenti

  • cell cortex Source: UniProtKB
  • cytoplasm Source: HPA
  • cytosol Source: UniProtKB
  • membrane Source: UniProtKB
  • nucleus Source: UniProtKB-SubCell
  • perinuclear region of cytoplasm Source: Ensembl
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Membrane, Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi1251 – 12511A → P: Abolishes interaction with PRKAR2A and leads to constitutive activation of RHOA; when associated with P-1260. 2 Publications
Mutagenesisi1260 – 12601I → P: Abolishes interaction with PRKAR2Aand leads to constitutive activation of RHOA; when associated with P-1251. 2 Publications
Mutagenesisi1265 – 12651A → P: Abolishes interaction with PRKAR2A. 1 Publication
Mutagenesisi1565 – 15651S → A: Abolishes interaction with YWHAB, leading to constitutive activation of RHOA and MAPK14. 2 Publications
Mutagenesisi2001 – 20011E → A: Decreases guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2136 – 21361R → G: Decreases guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2148 – 21481Q → Y: Abolishes guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2152 – 21521K → Y: Abolishes guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2153 – 21531Y → F: Loss of guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2189 – 21891D → A: Reduces guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2189 – 21891D → Y: Abolishes guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2289 – 22891R → A: Decreases guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2299 – 22991F → A: Decreases guanyl nucleotide exchange activity toward RHOA. 1 Publication
Mutagenesisi2324 – 23241W → L: Impairs interaction with IKBKB. 1 Publication

Keywords - Diseasei

Proto-oncogene

Organism-specific databases

PharmGKBiPA24665.

Polymorphism and mutation databases

DMDMi134048676.

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 – 7901PhosphoserineCombined sources
Modified residuei815 – 8151PhosphothreonineCombined sources
Modified residuei953 – 9531PhosphothreonineBy similarity
Modified residuei983 – 9831PhosphoserineCombined sources
Modified residuei1489 – 14891PhosphoserineCombined sources
Modified residuei1507 – 15071PhosphoserineCombined sources
Modified residuei1540 – 15401PhosphoserineCombined sources
Modified residuei1565 – 15651PhosphoserineCombined sources1 Publication
Modified residuei1602 – 16021PhosphoserineBy similarity
Modified residuei1642 – 16421PhosphoserineCombined sources
Modified residuei1645 – 16451PhosphoserineCombined sources
Modified residuei1647 – 16471PhosphoserineCombined sources
Modified residuei1876 – 18761PhosphoserineCombined sources
Modified residuei1895 – 18951PhosphoserineCombined sources
Modified residuei1929 – 19291PhosphoserineCombined sources
Modified residuei1930 – 19301PhosphothreonineCombined sources
Modified residuei1932 – 19321PhosphoserineCombined sources
Modified residuei1945 – 19451PhosphoserineBy similarity
Modified residuei2345 – 23451PhosphoserineBy similarity
Modified residuei2398 – 23981PhosphoserineCombined sources
Modified residuei2467 – 24671PhosphothreonineCombined sources
Modified residuei2473 – 24731PhosphoserineCombined sources
Modified residuei2563 – 25631PhosphoserineCombined sources
Modified residuei2566 – 25661PhosphoserineBy similarity
Modified residuei2703 – 27031PhosphoserineCombined sources
Modified residuei2709 – 27091PhosphoserineCombined sources
Modified residuei2728 – 27281PhosphoserineCombined sources

Keywords - PTMi

Phosphoprotein

Proteomic databases

EPDiQ12802.
MaxQBiQ12802.
PaxDbiQ12802.
PeptideAtlasiQ12802.
PRIDEiQ12802.

PTM databases

iPTMnetiQ12802.
PhosphoSiteiQ12802.

Expressioni

Tissue specificityi

Detected in mammary gland (PubMed:9627117). Detected in heart (at protein level) (PubMed:11546812). 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

BgeeiQ12802.
ExpressionAtlasiQ12802. baseline and differential.
GenevisibleiQ12802. HS.

Organism-specific databases

HPAiHPA019773.

Interactioni

Subunit structurei

Interacts with the cAMP-dependent protein kinase (PKA) holoenzyme and with the regulatory subunit PRKAR2A (PubMed:11546812, PubMed:1618839, PubMed:15229649, PubMed:21102438, PubMed:11285229). Interacts with RHOA (PubMed:11546812, PubMed:17537920, PubMed:25186459, PubMed:24993829). Interacts also with RHOB and RHOC (PubMed:11546812). Identified in a ternary complex with RHOA and PRKAR2A (PubMed:11546812). Identified in a complex with NR3C1 and RHOA (PubMed:16469733). Interacts with BRAF and KSR1 (PubMed:21102438). 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 (PubMed:21224381). Interacts (phosphorylated form) with YWHAB and YWHAZ (PubMed:15229649, PubMed:21224381). Interaction with YWHAB inhibits activation of RHOA, interferes with PKN1 binding and activation of MAP kinases (PubMed:15229649, PubMed:21224381). Interacts with GNA12 (PubMed:11546812). Interacts with IKBKB (PubMed:23090968). Interacts with ESR1, THRA, PPARA and NME2 (PubMed:9627117, PubMed:15249197). 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 similarity12 Publications

Binary interactionsi

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

GO - Molecular functioni

  • MAP-kinase scaffold activity Source: UniProtKB
  • protein complex scaffold Source: UniProtKB
  • protein kinase A binding Source: UniProtKB
  • Rho GTPase binding Source: UniProtKB

Protein-protein interaction databases

BioGridi116383. 31 interactions.
DIPiDIP-180N.
IntActiQ12802. 26 interactions.
MINTiMINT-3308570.
STRINGi9606.ENSP00000354718.

Structurei

Secondary structure

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

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DRNNMR-C1246-1269[»]
2LG1NMR-A2164-2346[»]
4D0NX-ray2.10B1968-2338[»]
4D0OX-ray2.75A/B1972-2207[»]
ProteinModelPortaliQ12802.
SMRiQ12802. Positions 1968-2336.
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 – 51623Important for interaction with PRKAR2AAdd
BLAST
Regioni1585 – 1715131Important for interaction with MAP2K31 PublicationAdd
BLAST
Regioni1919 – 2813895Interaction with ESR11 PublicationAdd
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

The DH domain is sufficient for interaction with RHOA, and for guanine nucleotide exchange (GEF) activity with RHOA (PubMed:24993829). Forms that lack C-terminal regulatory domains have transforming activity and function as oncogenes (PubMed:9891067).1 Publication2 Publications
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).1 Publication
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

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

eggNOGiKOG3520. Eukaryota.
COG5422. LUCA.
GeneTreeiENSGT00760000119193.
HOVERGENiHBG080828.
InParanoidiQ12802.
KOiK16529.
OMAiQQLMKTN.
PhylomeDBiQ12802.
TreeFamiTF325887.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR028852. AKAP13.
IPR000219. DH-domain.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR018459. RII_binding_1.
[Graphical view]
PANTHERiPTHR13944:SF12. PTHR13944:SF12. 1 hit.
PfamiPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF10522. RII_binding_1. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 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. AlignAdd to basket

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

        10         20         30         40         50
MKLNPQQAPL YGDCVVTVLL AEEDKAEDDV VFYLVFLGST LRHCTSTRKV
60 70 80 90 100
SSDTLETIAP GHDCCETVKV QLCASKEGLP VFVVAEEDFH FVQDEAYDAA
110 120 130 140 150
QFLATSAGNQ QALNFTRFLD QSGPPSGDVN SLDKKLVLAF RHLKLPTEWN
160 170 180 190 200
VLGTDQSLHD AGPRETLMHF AVRLGLLRLT WFLLQKPGGR GALSIHNQEG
210 220 230 240 250
ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG DCSVRHHREL
260 270 280 290 300
DIYTLTSESD SHHEHPFPGD GCTGPIFKLM NIQQQLMKTN LKQMDSLMPL
310 320 330 340 350
MMTAQDPSSA PETDGQFLPC APEPTDPQRL SSSEETESTQ CCPGSPVAQT
360 370 380 390 400
ESPCDLSSIV EEENTDRSCR KKNKGVERKG EEVEPAPIVD SGTVSDQDSC
410 420 430 440 450
LQSLPDCGVK GTEGLSSCGN RNEETGTKSS GMPTDQESLS SGDAVLQRDL
460 470 480 490 500
VMEPGTAQYS SGGELGGIST TNVSTPDTAG EMEHGLMNPD ATVWKNVLQG
510 520 530 540 550
GESTKERFEN SNIGTAGASD VHVTSKPVDK ISVPNCAPAA SSLDGNKPAE
560 570 580 590 600
SSLAFSNEET STEKTAETET SRSREESADA PVDQNSVVIP AAAKDKISDG
610 620 630 640 650
LEPYTLLAAG IGEAMSPSDL ALLGLEEDVM PHQNSETNSS HAQSQKGKSS
660 670 680 690 700
PICSTTGDDK LCADSACQQN TVTSSGDLVA KLCDNIVSES ESTTARQPSS
710 720 730 740 750
QDPPDASHCE DPQAHTVTSD PVRDTQERAD FCPFKVVDNK GQRKDVKLDK
760 770 780 790 800
PLTNMLEVVS HPHPVVPKME KELVPDQAVI SDSTFSLANS PGSESVTKDD
810 820 830 840 850
ALSFVPSQKE KGTATPELHT ATDYRDGPDG NSNEPDTRPL EDRAVGLSTS
860 870 880 890 900
STAAELQHGM GNTSLTGLGG EHEGPAPPAI PEALNIKGNT DSSLQSVGKA
910 920 930 940 950
TLALDSVLTE EGKLLVVSES SAAQEQDKDK AVTCSSIKEN ALSSGTLQEE
960 970 980 990 1000
QRTPPPGQDT QQFHEKSISA DCAKDKALQL SNSPGASSAF LKAETEHNKE
1010 1020 1030 1040 1050
VAPQVSLLTQ GGAAQSLVPP GASLATESRQ EALGAEHNSS ALLPCLLPDG
1060 1070 1080 1090 1100
SDGSDALNCS QPSPLDVGVK NTQSQGKTSA CEVSGDVTVD VTGVNALQGM
1110 1120 1130 1140 1150
AEPRRENISH NTQDILIPNV LLSQEKNAVL GLPVALQDKA VTDPQGVGTP
1160 1170 1180 1190 1200
EMIPLDWEKG KLEGADHSCT MGDAEEAQID DEAHPVLLQP VAKELPTDME
1210 1220 1230 1240 1250
LSAHDDGAPA GVREVMRAPP SGRERSTPSL PCMVSAQDAP LPKGADLIEE
1260 1270 1280 1290 1300
AASRIVDAVI EQVKAAGALL TEGEACHMSL SSPELGPLTK GLESAFTEKV
1310 1320 1330 1340 1350
STFPPGESLP MGSTPEEATG SLAGCFAGRE EPEKIILPVQ GPEPAAEMPD
1360 1370 1380 1390 1400
VKAEDEVDFR ASSISEEVAV GSIAATLKMK QGPMTQAINR ENWCTIEPCP
1410 1420 1430 1440 1450
DAASLLASKQ SPECENFLDV GLGRECTSKQ GVLKRESGSD SDLFHSPSDD
1460 1470 1480 1490 1500
MDSIIFPKPE EEHLACDITG SSSSTDDTAS LDRHSSHGSD VSLSQILKPN
1510 1520 1530 1540 1550
RSRDRQSLDG FYSHGMGAEG RESESEPADP GDVEEEEMDS ITEVPANCSV
1560 1570 1580 1590 1600
LRSSMRSLSP FRRHSWGPGK NAASDAEMNH RSSMRVLGDV VRRPPIHRRS
1610 1620 1630 1640 1650
FSLEGLTGGA GVGNKPSSSL EVSSANAEEL RHPFSGEERV DSLVSLSEED
1660 1670 1680 1690 1700
LESDQREHRM FDQQICHRSK QQGFNYCTSA ISSPLTKSIS LMTISHPGLD
1710 1720 1730 1740 1750
NSRPFHSTFH NTSANLTESI TEENYNFLPH SPSKKDSEWK SGTKVSRTFS
1760 1770 1780 1790 1800
YIKNKMSSSK KSKEKEKEKD KIKEKEKDSK DKEKDKKTVN GHTFSSIPVV
1810 1820 1830 1840 1850
GPISCSQCMK PFTNKDAYTC ANCSAFVHKG CRESLASCAK VKMKQPKGSL
1860 1870 1880 1890 1900
QAHDTSSLPT VIMRNKPSQP KERPRSAVLL VDETATTPIF ANRRSQQSVS
1910 1920 1930 1940 1950
LSKSVSIQNI TGVGNDENMS NTWKFLSHST DSLNKISKVN ESTESLTDEG
1960 1970 1980 1990 2000
VGTDMNEGQL LGDFEIESKQ LEAESWSRII DSKFLKQQKK DVVKRQEVIY
2010 2020 2030 2040 2050
ELMQTEFHHV RTLKIMSGVY SQGMMADLLF EQQMVEKLFP CLDELISIHS
2060 2070 2080 2090 2100
QFFQRILERK KESLVDKSEK NFLIKRIGDV LVNQFSGENA ERLKKTYGKF
2110 2120 2130 2140 2150
CGQHNQSVNY FKDLYAKDKR FQAFVKKKMS SSVVRRLGIP ECILLVTQRI
2160 2170 2180 2190 2200
TKYPVLFQRI LQCTKDNEVE QEDLAQSLSL VKDVIGAVDS KVASYEKKVR
2210 2220 2230 2240 2250
LNEIYTKTDS KSIMRMKSGQ MFAKEDLKRK KLVRDGSVFL KNAAGRLKEV
2260 2270 2280 2290 2300
QAVLLTDILV FLQEKDQKYI FASLDQKSTV ISLKKLIVRE VAHEEKGLFL
2310 2320 2330 2340 2350
ISMGMTDPEM VEVHASSKEE RNSWIQIIQD TINTLNRDED EGIPSENEEE
2360 2370 2380 2390 2400
KKMLDTRARE LKEQLHQKDQ KILLLLEEKE MIFRDMAECS TPLPEDCSPT
2410 2420 2430 2440 2450
HSPRVLFRSN TEEALKGGPL MKSAINEVEI LQGLVSGNLG GTLGPTVSSP
2460 2470 2480 2490 2500
IEQDVVGPVS LPRRAETFGG FDSHQMNASK GGEKEEGDDG QDLRRTESDS
2510 2520 2530 2540 2550
GLKKGGNANL VFMLKRNSEQ VVQSVVHLYE LLSALQGVVL QQDSYIEDQK
2560 2570 2580 2590 2600
LVLSERALTR SLSRPSSLIE QEKQRSLEKQ RQDLANLQKQ QAQYLEEKRR
2610 2620 2630 2640 2650
REREWEARER ELREREALLA QREEEVQQGQ QDLEKEREEL QQKKGTYQYD
2660 2670 2680 2690 2700
LERLRAAQKQ LEREQEQLRR EAERLSQRQT ERDLCQVSHP HTKLMRIPSF
2710 2720 2730 2740 2750
FPSPEEPPSP SAPSIAKSGS LDSELSVSPK RNSISRTHKD KGPFHILSST
2760 2770 2780 2790 2800
SQTNKGPEGQ SQAPASTSAS TRLFGLTKPK EKKEKKKKNK TSRSQPGDGP
2810
ASEVSAEGEE IFC
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.Probable cloning artifact.Curated
The sequence AAC50065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAD21311.1 differs from that shown. Reason: Frameshift at positions 2614 and 2647. Curated
The sequence AAD40799.1 differs from that shown.Intron retention.Curated
The sequence AAD40799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated
The sequence AAL40923.1 differs from that shown. Reason: Frameshift at positions 2614 and 2647. Curated

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 (Ref. 9) Curated
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 (Ref. 3) Curated
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:
EMBLi
GenBanki
DDBJi
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]
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.5. human. [Q12802-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
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]
UniGeneiHs.459211.
Hs.710656.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
2DRNNMR-C1246-1269[»]
2LG1NMR-A2164-2346[»]
4D0NX-ray2.10B1968-2338[»]
4D0OX-ray2.75A/B1972-2207[»]
ProteinModelPortaliQ12802.
SMRiQ12802. Positions 1968-2336.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi116383. 31 interactions.
DIPiDIP-180N.
IntActiQ12802. 26 interactions.
MINTiMINT-3308570.
STRINGi9606.ENSP00000354718.

PTM databases

iPTMnetiQ12802.
PhosphoSiteiQ12802.

Polymorphism and mutation databases

DMDMi134048676.

Proteomic databases

EPDiQ12802.
MaxQBiQ12802.
PaxDbiQ12802.
PeptideAtlasiQ12802.
PRIDEiQ12802.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

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

Organism-specific databases

CTDi11214.
GeneCardsiAKAP13.
H-InvDBHIX0021561.
HIX0172808.
HGNCiHGNC:371. AKAP13.
HPAiHPA019773.
MIMi604686. gene.
neXtProtiNX_Q12802.
PharmGKBiPA24665.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3520. Eukaryota.
COG5422. LUCA.
GeneTreeiENSGT00760000119193.
HOVERGENiHBG080828.
InParanoidiQ12802.
KOiK16529.
OMAiQQLMKTN.
PhylomeDBiQ12802.
TreeFamiTF325887.

Enzyme and pathway databases

ReactomeiR-HSA-193648. NRAGE signals death through JNK.
R-HSA-194840. Rho GTPase cycle.
R-HSA-416482. G alpha (12/13) signalling events.
SignaLinkiQ12802.
SIGNORiQ12802.

Miscellaneous databases

ChiTaRSiAKAP13. human.
EvolutionaryTraceiQ12802.
GeneWikiiAKAP13.
GenomeRNAii11214.
PROiQ12802.
SOURCEiSearch...

Gene expression databases

BgeeiQ12802.
ExpressionAtlasiQ12802. baseline and differential.
GenevisibleiQ12802. HS.

Family and domain databases

Gene3Di1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProiIPR028852. AKAP13.
IPR000219. DH-domain.
IPR002219. PE/DAG-bd.
IPR011993. PH_dom-like.
IPR001849. PH_domain.
IPR018459. RII_binding_1.
[Graphical view]
PANTHERiPTHR13944:SF12. PTHR13944:SF12. 1 hit.
PfamiPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
PF10522. RII_binding_1. 1 hit.
[Graphical view]
SMARTiSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMiSSF48065. SSF48065. 1 hit.
SSF50729. SSF50729. 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]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  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), SUBCELLULAR LOCATION, 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 PKA HOLOENZYME; PRKAR2A; GNA12; RHOA; RHOB AND RHOC, IDENTIFICATION IN A COMPLEX WITH RHOA AND PRKAR2A, 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, INTERACTION WITH PKA HOLOENZYME AND PRKAR2A, 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 IN ACTIVATION OF 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. "Anchoring of both PKA and 14-3-3 inhibits the Rho-GEF activity of the AKAP-Lbc signaling complex."
    Diviani D., Abuin L., Cotecchia S., Pansier L.
    EMBO J. 23:2811-2820(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH YWHAB; YWHAZ AND PKA, PHOSPHORYLATION AT SER-1565, MUTAGENESIS OF ALA-1251; ILE-1260 AND SER-1565.
  14. "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.
  15. "Rho family Guanine nucleotide exchange factor Brx couples extracellular signals to the glucocorticoid signaling system."
    Kino T., Souvatzoglou E., Charmandari E., Ichijo T., Driggers P., Mayers C., Alatsatianos A., Manoli I., Westphal H., Chrousos G.P., Segars J.H.
    J. Biol. Chem. 281:9118-9126(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, IDENTIFICATION IN A COMPLEX WITH NR3C1 AND RHOA.
  16. "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.
  17. "The A-kinase anchoring protein (AKAP)-Lbc-signaling complex mediates alpha1 adrenergic receptor-induced cardiomyocyte hypertrophy."
    Appert-Collin A., Cotecchia S., Nenniger-Tosato M., Pedrazzini T., Diviani D.
    Proc. Natl. Acad. Sci. U.S.A. 104:10140-10145(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH RHOA.
  18. "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.
  19. 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.
  20. "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].
  21. "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.
  22. Cited for: FUNCTION, INTERACTION WITH KSR1; BRAF; PKA CATALYTIC SUBUNIT AND PRKAR2A.
  23. "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.
  24. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "A-kinase anchoring protein (AKAP)-Lbc anchors a PKN-based signaling complex involved in alpha1-adrenergic receptor-induced p38 activation."
    Cariolato L., Cavin S., Diviani D.
    J. Biol. Chem. 286:7925-7937(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH PKN1; YWHAB; MAPK14 AND ZAK, IDENTIFICATION IN A COMPLEX WITH PKN1; MAPK14; MAP2K3 AND ZAK, REGION, MUTAGENESIS OF SER-1565.
  26. "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].
  27. "Toward a comprehensive characterization of a human cancer cell phosphoproteome."
    Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S.
    J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-815; SER-983; SER-1507; SER-1876; SER-1929; SER-1932; THR-2467; SER-2709 AND SER-2728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  28. "A-kinase-anchoring protein-Lbc anchors IkappaB kinase beta to support interleukin-6-mediated cardiomyocyte hypertrophy."
    del Vescovo C.D., Cotecchia S., Diviani D.
    Mol. Cell. Biol. 33:14-27(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH IKBKB, MUTAGENESIS OF TRP-2324.
  29. "A-kinase anchoring protein Lbc coordinates a p38 activating signaling complex controlling compensatory cardiac hypertrophy."
    Perez Lopez I., Cariolato L., Maric D., Gillet L., Abriel H., Diviani D.
    Mol. Cell. Biol. 33:2903-2917(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  30. "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver phosphoproteome."
    Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L., Ye M., Zou H.
    J. Proteomics 96:253-262(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1489; SER-1540; THR-2467; SER-2473 AND SER-2728, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Liver.
  31. "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 IN COMPLEX WITH PRKAR2A PEPTIDE, INTERACTION WITH PRKAR2A.
  32. "The crystal structure of the RhoA-AKAP-Lbc DH-PH domain complex."
    Abdul Azeez K.R., Knapp S., Fernandes J.M., Klussmann E., Elkins J.M.
    Biochem. J. 464:231-239(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.10 ANGSTROMS) OF 1968-2338 IN COMPLEX WITH RHOA, FUNCTION, INTERACTION WITH RHOA, DOMAIN, MUTAGENESIS OF GLN-2148; LYS-2152 AND ASP-2189.
  33. "Structural insights into the activation of the RhoA GTPase by the lymphoid blast crisis (Lbc) oncoprotein."
    Lenoir M., Sugawara M., Kaur J., Ball L.J., Overduin M.
    J. Biol. Chem. 289:23992-24004(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 2164-2346, FUNCTION, INTERACTION WITH RHOA, DOMAIN, MUTAGENESIS OF GLU-2001; ARG-2136; ARG-2289 AND PHE-2299.

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: July 6, 2016
This is version 151 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

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.