SubmitCancel

Skip Header

You are using a version of browser that may not display all the features of this website. Please consider upgrading your browser.

Q12802

- AKP13_HUMAN

UniProt

Q12802 - AKP13_HUMAN

(max 400 entries)x

Your basket is currently empty.

Select item(s) and click on "Add to basket" to create your own collection here
(400 entries max)

Protein
A-kinase anchor protein 13
Gene
AKAP13, BRX, HT31, LBC
Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5 - Experimental evidence at protein leveli

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-type
Add
BLAST

GO - Molecular functioni

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

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
Complete GO annotation...

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

Cytoplasm. Nucleus. Membrane 3 Publications

GO - Cellular componenti

  1. cytoplasm Source: HPA
  2. cytosol Source: Reactome
  3. membrane Source: ProtInc
  4. nucleus Source: UniProtKB-SubCell
  5. 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: 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 13
PRO_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

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.

Miscellaneous databases

EvolutionaryTraceiQ12802.

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini1994 – 2191198DH
Add
BLAST
Domaini2231 – 2333103PH
Add
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni494 – 51623RII-binding
Add
BLAST
Regioni1919 – 2813895Interaction with ESR1
Add
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili1758 – 179033 Reviewed prediction
Add
BLAST
Coiled coili2345 – 238137 Reviewed prediction
Add
BLAST
Coiled coili2568 – 2683116 Reviewed prediction
Add
BLAST

Compositional bias

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

Domaini

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

Sequence similaritiesi

Contains 1 PH domain.

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.

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.
VSP_023486Add
BLAST
Alternative sequencei180 – 28132634Missing in isoform 4.
VSP_023487Add
BLAST
Alternative sequencei1581 – 159818Missing in isoform 3.
VSP_023489Add
BLAST
Alternative sequencei1583 – 159816SMRVL…PPIHR → MSWCPSGVQYSAGLSADFNY in isoform 2.
VSP_023490Add
BLAST
Alternative sequencei1950 – 19512Missing in isoform 3.
VSP_023491

Sequence conflict

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

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...

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

« 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), 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: September 3, 2014
This is version 130 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

Similar proteinsi