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Q12802 (AKP13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified March 19, 2014. Version 125. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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 names
Name:AKAP13
Synonyms:BRX, HT31, LBC
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length2813 AA.
Sequence statusComplete.
Protein existenceEvidence at protein level

General annotation (Comments)

Function

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. Ref.2 Ref.5 Ref.6 Ref.11

Subunit structure

Binds cAMP-dependent protein kinase (PKA) and to the RII-alpha regulatory subunit of PKA. Interacts with ESR1, ESR2, THRA, PPARA, RHOA and NME2. Ref.1 Ref.2 Ref.5 Ref.11 Ref.12

Subcellular location

Cytoplasm. Nucleus. Membrane Ref.2 Ref.5 Ref.6.

Tissue specificity

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. Ref.2 Ref.5 Ref.6

Domain

Both the DH and PH domains are required for transforming activity. Ref.6

Sequence similarities

Contains 1 DH (DBL-homology) domain.

Contains 1 PH domain.

Contains 1 phorbol-ester/DAG-type zinc finger.

Sequence caution

The sequence AAC50065.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAC50065.1 differs from that shown. Reason: Probable cloning artifact.

The sequence AAD21311.1 differs from that shown. Reason: Frameshift at positions 2614 and 2647.

The sequence AAD40799.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.

The sequence AAD40799.1 differs from that shown. Reason: Intron retention.

The sequence AAL40923.1 differs from that shown. Reason: Frameshift at positions 2614 and 2647.

Ontologies

Keywords
   Cellular componentCytoplasm
Membrane
Nucleus
   Coding sequence diversityAlternative splicing
Polymorphism
   DiseaseProto-oncogene
   DomainCoiled coil
Zinc-finger
   LigandMetal-binding
Zinc
   Molecular functionGuanine-nucleotide releasing factor
   PTMPhosphoprotein
   Technical term3D-structure
Complete proteome
Reference proteome
Gene Ontology (GO)
   Biological_processapoptotic signaling pathway

Traceable author statement. Source: Reactome

neurotrophin TRK receptor signaling pathway

Traceable author statement. Source: Reactome

nuclear export

Inferred from electronic annotation. Source: Ensembl

positive regulation of apoptotic process

Traceable author statement. Source: Reactome

regulation of Rho GTPase activity

Inferred from electronic annotation. Source: GOC

regulation of cardiac muscle hypertrophy

Inferred from electronic annotation. Source: Ensembl

regulation of glucocorticoid mediated signaling pathway

Inferred from electronic annotation. Source: Ensembl

regulation of protein kinase activity

Inferred from electronic annotation. Source: Ensembl

small GTPase mediated signal transduction

Traceable author statement. Source: Reactome

   Cellular_componentcytosol

Traceable author statement. Source: Reactome

membrane

Traceable author statement Ref.6. Source: ProtInc

nucleus

Inferred from electronic annotation. Source: UniProtKB-SubCell

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionRho guanyl-nucleotide exchange factor activity

Inferred from electronic annotation. Source: InterPro

cAMP-dependent protein kinase activity

Non-traceable author statement Ref.9. Source: UniProtKB

metal ion binding

Inferred from electronic annotation. Source: UniProtKB-KW

signal transducer activity

Traceable author statement Ref.8. Source: ProtInc

Complete GO annotation...

Binary interactions

Alternative products

This entry describes 4 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: Q12802-1)

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.
Isoform 2 (identifier: Q12802-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1583-1598: SMRVLGDVVRRPPIHR → MSWCPSGVQYSAGLSADFNY
Isoform 3 (identifier: Q12802-4)

The sequence of this isoform differs from the canonical sequence as follows:
     1581-1598: Missing.
     1950-1951: Missing.
Isoform 4 (identifier: Q12802-5)

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

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 28132813A-kinase anchor protein 13
PRO_0000080963

Regions

Domain1994 – 2191198DH
Domain2231 – 2333103PH
Zinc finger1791 – 183848Phorbol-ester/DAG-type
Region494 – 51623RII-binding
Region1919 – 2813895Interaction with ESR1
Coiled coil1758 – 179033 Potential
Coiled coil2345 – 238137 Potential
Coiled coil2568 – 2683116 Potential
Compositional bias1471 – 14744Poly-Ser
Compositional bias1534 – 15374Poly-Glu
Compositional bias2778 – 279013Poly-Lys

Amino acid modifications

Modified residue7901Phosphoserine Ref.19
Modified residue9831Phosphoserine Ref.14 Ref.16 Ref.18 Ref.19 Ref.21
Modified residue15651Phosphoserine Ref.13
Modified residue16421Phosphoserine Ref.18 Ref.21
Modified residue16451Phosphoserine Ref.16 Ref.18 Ref.21
Modified residue16471Phosphoserine Ref.16 Ref.18 Ref.21
Modified residue18761Phosphoserine Ref.16 Ref.18
Modified residue18951Phosphoserine Ref.21
Modified residue19291Phosphoserine Ref.16 Ref.19 Ref.21
Modified residue19301Phosphothreonine Ref.21
Modified residue19321Phosphoserine Ref.16 Ref.21
Modified residue23981Phosphoserine Ref.16
Modified residue25631Phosphoserine Ref.21
Modified residue27031Phosphoserine Ref.16
Modified residue27091Phosphoserine Ref.16
Modified residue27281Phosphoserine Ref.14 Ref.16 Ref.18 Ref.21

Natural variations

Alternative sequence160 – 17920DAGPR…GLLRL → GENLYDLQTHFKFVIFLLFF in isoform 4.
VSP_023486
Alternative sequence180 – 28132634Missing in isoform 4.
VSP_023487
Alternative sequence1581 – 159818Missing in isoform 3.
VSP_023489
Alternative sequence1583 – 159816SMRVL…PPIHR → MSWCPSGVQYSAGLSADFNY in isoform 2.
VSP_023490
Alternative sequence1950 – 19512Missing in isoform 3.
VSP_023491
Natural variant4521M → T. Ref.3
Corresponds to variant rs2061821 [ dbSNP | Ensembl ].
VAR_030925
Natural variant4941W → R. Ref.3
Corresponds to variant rs2061822 [ dbSNP | Ensembl ].
VAR_030926
Natural variant5261K → Q.
Corresponds to variant rs34434221 [ dbSNP | Ensembl ].
VAR_051986
Natural variant5741R → C. Ref.1 Ref.3
Corresponds to variant rs2061824 [ dbSNP | Ensembl ].
VAR_030927
Natural variant6241G → V. Ref.2
Corresponds to variant rs745191 [ dbSNP | Ensembl ].
VAR_030928
Natural variant6891E → K. Ref.3
Corresponds to variant rs7177107 [ dbSNP | Ensembl ].
VAR_030929
Natural variant8451V → A. Ref.3
Corresponds to variant rs4075256 [ dbSNP | Ensembl ].
VAR_030930
Natural variant8971V → M. Ref.2 Ref.3
Corresponds to variant rs4075254 [ dbSNP | Ensembl ].
VAR_030931
Natural variant10621P → A. Ref.3
Corresponds to variant rs4843074 [ dbSNP | Ensembl ].
VAR_030932
Natural variant10861D → N. Ref.3
Corresponds to variant rs4843075 [ dbSNP | Ensembl ].
VAR_030933
Natural variant12161M → T. Ref.3
Corresponds to variant rs7162168 [ dbSNP | Ensembl ].
VAR_030934
Natural variant15251S → G.
Corresponds to variant rs35079107 [ dbSNP | Ensembl ].
VAR_051987
Natural variant24571G → S. Ref.1 Ref.2 Ref.5 Ref.10
Corresponds to variant rs2241268 [ dbSNP | Ensembl ].
VAR_030935
Natural variant28011A → T.
Corresponds to variant rs2614668 [ dbSNP | Ensembl ].
VAR_030936

Experimental info

Mutagenesis12511A → P: Loss of PKA anchoring; when associated with P-1260. Ref.2
Mutagenesis12601I → P: Loss of PKA anchoring; when associated with P-1251. Ref.2
Mutagenesis12651A → P: Abolishes RII-binding. Ref.9
Mutagenesis21531Y → F: Loss of interaction with RHOA. Ref.2
Sequence conflict1911G → R in AAL40923. Ref.1
Sequence conflict3541C → R in AAL40923. Ref.1
Sequence conflict6091A → V in AAL40923. Ref.1
Sequence conflict6141A → T in AAL40923. Ref.1
Sequence conflict6181S → P in AAL40923. Ref.1
Sequence conflict6191D → A in AAL11723. Ref.2
Sequence conflict7551M → S in AAA58670. Ref.9
Sequence conflict1385 – 13873TQA → MLY in AAD21311. Ref.5
Sequence conflict15471N → H in BAD92651. Ref.10
Sequence conflict1766 – 17683EKE → KKK in AAA58670. Ref.9
Sequence conflict18771A → G in AAD40799. Ref.6
Sequence conflict18971Q → E in AAD40799. Ref.6
Sequence conflict20351V → D in AAD21311. Ref.5
Sequence conflict24881D → G in AAD21311. Ref.5
Sequence conflict2667 – 26682QL → HV in BAB62913. Ref.3
Sequence conflict2667 – 26682QL → HV in AAD21311. Ref.5

Secondary structure

.................................... 2813
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

Last modified March 6, 2007. Version 2.
Checksum: 6A8FDAC9A3D3B1F2

FASTA2,813307,550
        10         20         30         40         50         60 
MKLNPQQAPL YGDCVVTVLL AEEDKAEDDV VFYLVFLGST LRHCTSTRKV SSDTLETIAP 

        70         80         90        100        110        120 
GHDCCETVKV QLCASKEGLP VFVVAEEDFH FVQDEAYDAA QFLATSAGNQ QALNFTRFLD 

       130        140        150        160        170        180 
QSGPPSGDVN SLDKKLVLAF RHLKLPTEWN VLGTDQSLHD AGPRETLMHF AVRLGLLRLT 

       190        200        210        220        230        240 
WFLLQKPGGR GALSIHNQEG ATPVSLALER GYHKLHQLLT EENAGEPDSW SSLSYEIPYG 

       250        260        270        280        290        300 
DCSVRHHREL DIYTLTSESD SHHEHPFPGD GCTGPIFKLM NIQQQLMKTN LKQMDSLMPL 

       310        320        330        340        350        360 
MMTAQDPSSA PETDGQFLPC APEPTDPQRL SSSEETESTQ CCPGSPVAQT ESPCDLSSIV 

       370        380        390        400        410        420 
EEENTDRSCR KKNKGVERKG EEVEPAPIVD SGTVSDQDSC LQSLPDCGVK GTEGLSSCGN 

       430        440        450        460        470        480 
RNEETGTKSS GMPTDQESLS SGDAVLQRDL VMEPGTAQYS SGGELGGIST TNVSTPDTAG 

       490        500        510        520        530        540 
EMEHGLMNPD ATVWKNVLQG GESTKERFEN SNIGTAGASD VHVTSKPVDK ISVPNCAPAA 

       550        560        570        580        590        600 
SSLDGNKPAE SSLAFSNEET STEKTAETET SRSREESADA PVDQNSVVIP AAAKDKISDG 

       610        620        630        640        650        660 
LEPYTLLAAG IGEAMSPSDL ALLGLEEDVM PHQNSETNSS HAQSQKGKSS PICSTTGDDK 

       670        680        690        700        710        720 
LCADSACQQN TVTSSGDLVA KLCDNIVSES ESTTARQPSS QDPPDASHCE DPQAHTVTSD 

       730        740        750        760        770        780 
PVRDTQERAD FCPFKVVDNK GQRKDVKLDK PLTNMLEVVS HPHPVVPKME KELVPDQAVI 

       790        800        810        820        830        840 
SDSTFSLANS PGSESVTKDD ALSFVPSQKE KGTATPELHT ATDYRDGPDG NSNEPDTRPL 

       850        860        870        880        890        900 
EDRAVGLSTS STAAELQHGM GNTSLTGLGG EHEGPAPPAI PEALNIKGNT DSSLQSVGKA 

       910        920        930        940        950        960 
TLALDSVLTE EGKLLVVSES SAAQEQDKDK AVTCSSIKEN ALSSGTLQEE QRTPPPGQDT 

       970        980        990       1000       1010       1020 
QQFHEKSISA DCAKDKALQL SNSPGASSAF LKAETEHNKE VAPQVSLLTQ GGAAQSLVPP 

      1030       1040       1050       1060       1070       1080 
GASLATESRQ EALGAEHNSS ALLPCLLPDG SDGSDALNCS QPSPLDVGVK NTQSQGKTSA 

      1090       1100       1110       1120       1130       1140 
CEVSGDVTVD VTGVNALQGM AEPRRENISH NTQDILIPNV LLSQEKNAVL GLPVALQDKA 

      1150       1160       1170       1180       1190       1200 
VTDPQGVGTP EMIPLDWEKG KLEGADHSCT MGDAEEAQID DEAHPVLLQP VAKELPTDME 

      1210       1220       1230       1240       1250       1260 
LSAHDDGAPA GVREVMRAPP SGRERSTPSL PCMVSAQDAP LPKGADLIEE AASRIVDAVI 

      1270       1280       1290       1300       1310       1320 
EQVKAAGALL TEGEACHMSL SSPELGPLTK GLESAFTEKV STFPPGESLP MGSTPEEATG 

      1330       1340       1350       1360       1370       1380 
SLAGCFAGRE EPEKIILPVQ GPEPAAEMPD VKAEDEVDFR ASSISEEVAV GSIAATLKMK 

      1390       1400       1410       1420       1430       1440 
QGPMTQAINR ENWCTIEPCP DAASLLASKQ SPECENFLDV GLGRECTSKQ GVLKRESGSD 

      1450       1460       1470       1480       1490       1500 
SDLFHSPSDD MDSIIFPKPE EEHLACDITG SSSSTDDTAS LDRHSSHGSD VSLSQILKPN 

      1510       1520       1530       1540       1550       1560 
RSRDRQSLDG FYSHGMGAEG RESESEPADP GDVEEEEMDS ITEVPANCSV LRSSMRSLSP 

      1570       1580       1590       1600       1610       1620 
FRRHSWGPGK NAASDAEMNH RSSMRVLGDV VRRPPIHRRS FSLEGLTGGA GVGNKPSSSL 

      1630       1640       1650       1660       1670       1680 
EVSSANAEEL RHPFSGEERV DSLVSLSEED LESDQREHRM FDQQICHRSK QQGFNYCTSA 

      1690       1700       1710       1720       1730       1740 
ISSPLTKSIS LMTISHPGLD NSRPFHSTFH NTSANLTESI TEENYNFLPH SPSKKDSEWK 

      1750       1760       1770       1780       1790       1800 
SGTKVSRTFS YIKNKMSSSK KSKEKEKEKD KIKEKEKDSK DKEKDKKTVN GHTFSSIPVV 

      1810       1820       1830       1840       1850       1860 
GPISCSQCMK PFTNKDAYTC ANCSAFVHKG CRESLASCAK VKMKQPKGSL QAHDTSSLPT 

      1870       1880       1890       1900       1910       1920 
VIMRNKPSQP KERPRSAVLL VDETATTPIF ANRRSQQSVS LSKSVSIQNI TGVGNDENMS 

      1930       1940       1950       1960       1970       1980 
NTWKFLSHST DSLNKISKVN ESTESLTDEG VGTDMNEGQL LGDFEIESKQ LEAESWSRII 

      1990       2000       2010       2020       2030       2040 
DSKFLKQQKK DVVKRQEVIY ELMQTEFHHV RTLKIMSGVY SQGMMADLLF EQQMVEKLFP 

      2050       2060       2070       2080       2090       2100 
CLDELISIHS QFFQRILERK KESLVDKSEK NFLIKRIGDV LVNQFSGENA ERLKKTYGKF 

      2110       2120       2130       2140       2150       2160 
CGQHNQSVNY FKDLYAKDKR FQAFVKKKMS SSVVRRLGIP ECILLVTQRI TKYPVLFQRI 

      2170       2180       2190       2200       2210       2220 
LQCTKDNEVE QEDLAQSLSL VKDVIGAVDS KVASYEKKVR LNEIYTKTDS KSIMRMKSGQ 

      2230       2240       2250       2260       2270       2280 
MFAKEDLKRK KLVRDGSVFL KNAAGRLKEV QAVLLTDILV FLQEKDQKYI FASLDQKSTV 

      2290       2300       2310       2320       2330       2340 
ISLKKLIVRE VAHEEKGLFL ISMGMTDPEM VEVHASSKEE RNSWIQIIQD TINTLNRDED 

      2350       2360       2370       2380       2390       2400 
EGIPSENEEE KKMLDTRARE LKEQLHQKDQ KILLLLEEKE MIFRDMAECS TPLPEDCSPT 

      2410       2420       2430       2440       2450       2460 
HSPRVLFRSN TEEALKGGPL MKSAINEVEI LQGLVSGNLG GTLGPTVSSP IEQDVVGPVS 

      2470       2480       2490       2500       2510       2520 
LPRRAETFGG FDSHQMNASK GGEKEEGDDG QDLRRTESDS GLKKGGNANL VFMLKRNSEQ 

      2530       2540       2550       2560       2570       2580 
VVQSVVHLYE LLSALQGVVL QQDSYIEDQK LVLSERALTR SLSRPSSLIE QEKQRSLEKQ 

      2590       2600       2610       2620       2630       2640 
RQDLANLQKQ QAQYLEEKRR REREWEARER ELREREALLA QREEEVQQGQ QDLEKEREEL 

      2650       2660       2670       2680       2690       2700 
QQKKGTYQYD LERLRAAQKQ LEREQEQLRR EAERLSQRQT ERDLCQVSHP HTKLMRIPSF 

      2710       2720       2730       2740       2750       2760 
FPSPEEPPSP SAPSIAKSGS LDSELSVSPK RNSISRTHKD KGPFHILSST SQTNKGPEGQ 

      2770       2780       2790       2800       2810 
SQAPASTSAS TRLFGLTKPK EKKEKKKKNK TSRSQPGDGP ASEVSAEGEE IFC 

« Hide

Isoform 2 [UniParc].

Checksum: 4EA29B253C76698E
Show »

FASTA2,817307,845
Isoform 3 [UniParc].

Checksum: 117C84737CE9A79B
Show »

FASTA2,793305,281
Isoform 4 [UniParc].

Checksum: D441A72053F1EBC5
Show »

FASTA17919,992

References

« Hide 'large scale' references
[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]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract]
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]"Initial characterization of the human central proteome."
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.
BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract]
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.
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
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.
PIRA42915.
I38434.
RefSeqNP_001257475.1. NM_001270546.1.
NP_006729.4. NM_006738.5.
NP_009131.2. NM_007200.4.
XP_005254905.1. XM_005254848.1.
UniGeneHs.459211.
Hs.710656.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
2DRNNMR-C1246-1268[»]
2LG1NMR-A2164-2346[»]
ProteinModelPortalQ12802.
SMRQ12802. Positions 1789-1838, 1990-2346.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid116383. 17 interactions.
DIPDIP-180N.
IntActQ12802. 22 interactions.
MINTMINT-3308570.

PTM databases

PhosphoSiteQ12802.

Polymorphism databases

DMDM134048676.

Proteomic databases

PaxDbQ12802.
PRIDEQ12802.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000361243; ENSP00000354718; ENSG00000170776. [Q12802-2]
ENST00000394518; ENSP00000378026; ENSG00000170776. [Q12802-1]
ENST00000560302; ENSP00000453634; ENSG00000170776. [Q12802-5]
GeneID11214.
KEGGhsa:11214.
UCSCuc002bls.4. human. [Q12802-5]
uc002blu.2. human. [Q12802-2]
uc002blv.2. human. [Q12802-1]

Organism-specific databases

CTD11214.
GeneCardsGC15P085925.
H-InvDBHIX0021561.
HIX0172808.
HGNCHGNC:371. AKAP13.
HPAHPA019773.
MIM604686. gene.
neXtProtNX_Q12802.
PharmGKBPA24665.
GenAtlasSearch...

Phylogenomic databases

eggNOGCOG5422.
HOVERGENHBG080828.
KOK16529.
OMAGNDENMS.
TreeFamTF325887.

Enzyme and pathway databases

ReactomeREACT_111102. Signal Transduction.
SignaLinkQ12802.

Gene expression databases

ArrayExpressQ12802.
BgeeQ12802.
GenevestigatorQ12802.

Family and domain databases

Gene3D1.20.900.10. 1 hit.
2.30.29.30. 1 hit.
InterProIPR028852. AKAP13.
IPR000219. DH-domain.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
[Graphical view]
PANTHERPTHR13944:SF4. PTHR13944:SF4. 1 hit.
PfamPF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]
SMARTSM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]
SUPFAMSSF48065. SSF48065. 1 hit.
PROSITEPS50010. 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]
ProtoNetSearch...

Other

ChiTaRSAKAP13. human.
EvolutionaryTraceQ12802.
GeneWikiAKAP13.
GenomeRNAi11214.
NextBio42679.
PROQ12802.
SOURCESearch...

Entry information

Entry nameAKP13_HUMAN
AccessionPrimary (citable) accession number: Q12802
Secondary accession number(s): Q14572 expand/collapse secondary AC list , Q59FP6, Q86W90, Q8WXQ6, Q96JP6, Q96P79, Q9Y5T0, Q9Y5T6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 15, 1999
Last sequence update: March 6, 2007
Last modified: March 19, 2014
This is version 125 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM