Q12802 (AKP13_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

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 names

Name:	AKAP13
Synonyms:	BRX, HT31, LBC

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	2813 AA.
Sequence status	Complete.
Protein existence	Evidence 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 component	Cytoplasm Membrane Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Disease	Proto-oncogene
Domain	Coiled coil Zinc-finger
Ligand	Metal-binding Zinc
Molecular function	Guanine-nucleotide releasing factor
PTM	Phosphoprotein
Technical term	3D-structure Complete proteome Reference proteome
Gene Ontology (GO)
Biological_process	apoptotic process Traceable author statement. Source: Reactome nerve growth factor receptor signaling pathway Traceable author statement. Source: Reactome regulation of Rho protein signal transduction Inferred from electronic annotation. Source: InterPro regulation of glucocorticoid mediated signaling pathway Inferred from electronic annotation. Source: Compara regulation of small GTPase mediated signal transduction Traceable author statement. Source: Reactome small GTPase mediated signal transduction Traceable author statement. Source: Reactome
Cellular_component	cytosol Traceable author statement. Source: Reactome membrane Traceable author statement Ref.6. Source: ProtInc nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular_function	Rho 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 phospholipid binding Inferred from electronic annotation. Source: InterPro signal transducer activity Traceable author statement Ref.8. Source: ProtInc
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
ESR1	P03372	3	EBI-1373806,EBI-78473
TGM2	P21980	4	EBI-1373806,EBI-727668

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 key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 2813

2813

A-kinase anchor protein 13

PRO_0000080963

Regions

Domain

1994 – 2191

198

DH

Domain

2231 – 2333

103

PH

Zinc finger

1791 – 1838

48

Phorbol-ester/DAG-type

Region

494 – 516

23

RII-binding

Region

1919 – 2813

895

Interaction with ESR1

Coiled coil

1758 – 1790

33

Potential

Coiled coil

2345 – 2381

37

Potential

Coiled coil

2568 – 2683

116

Potential

Compositional bias

1471 – 1474

4

Poly-Ser

Compositional bias

1534 – 1537

4

Poly-Glu

Compositional bias

2778 – 2790

13

Poly-Lys

Amino acid modifications

Modified residue

790

1

Phosphoserine Ref.18

Modified residue

983

1

Phosphoserine Ref.14 Ref.16 Ref.17 Ref.18 Ref.20

Modified residue

1565

1

Phosphoserine Ref.13

Modified residue

1642

1

Phosphoserine Ref.17 Ref.20

Modified residue

1645

1

Phosphoserine Ref.16 Ref.17 Ref.20

Modified residue

1647

1

Phosphoserine Ref.16 Ref.17 Ref.20

Modified residue

1876

1

Phosphoserine Ref.16 Ref.17

Modified residue

1895

1

Phosphoserine Ref.20

Modified residue

1929

1

Phosphoserine Ref.16 Ref.18 Ref.20

Modified residue

1930

1

Phosphothreonine Ref.20

Modified residue

1932

1

Phosphoserine Ref.16 Ref.20

Modified residue

2398

1

Phosphoserine Ref.16

Modified residue

2563

1

Phosphoserine Ref.20

Modified residue

2703

1

Phosphoserine Ref.16

Modified residue

2709

1

Phosphoserine Ref.16

Modified residue

2728

1

Phosphoserine Ref.14 Ref.16 Ref.17 Ref.20

Natural variations

Alternative sequence

160 – 179

20

DAGPR…GLLRL → GENLYDLQTHFKFVIFLLFF in isoform 4.

VSP_023486

Alternative sequence

180 – 2813

2634

Missing in isoform 4.

VSP_023487

Alternative sequence

1581 – 1598

18

Missing in isoform 3.

VSP_023489

Alternative sequence

1583 – 1598

16

SMRVL…PPIHR → MSWCPSGVQYSAGLSADFNY in isoform 2.

VSP_023490

Alternative sequence

1950 – 1951

2

Missing in isoform 3.

VSP_023491

Natural variant

452

1

M → T. Ref.3
Corresponds to variant rs2061821 [ dbSNP | Ensembl ].

VAR_030925

Natural variant

494

1

W → R. Ref.3
Corresponds to variant rs2061822 [ dbSNP | Ensembl ].

VAR_030926

Natural variant

526

1

K → Q.
Corresponds to variant rs34434221 [ dbSNP | Ensembl ].

VAR_051986

Natural variant

574

1

R → C. Ref.1 Ref.3
Corresponds to variant rs2061824 [ dbSNP | Ensembl ].

VAR_030927

Natural variant

624

1

G → V. Ref.2
Corresponds to variant rs745191 [ dbSNP | Ensembl ].

VAR_030928

Natural variant

689

1

E → K. Ref.3
Corresponds to variant rs7177107 [ dbSNP | Ensembl ].

VAR_030929

Natural variant

845

1

V → A. Ref.3
Corresponds to variant rs4075256 [ dbSNP | Ensembl ].

VAR_030930

Natural variant

897

1

V → M. Ref.2 Ref.3
Corresponds to variant rs4075254 [ dbSNP | Ensembl ].

VAR_030931

Natural variant

1062

1

P → A. Ref.3
Corresponds to variant rs4843074 [ dbSNP | Ensembl ].

VAR_030932

Natural variant

1086

1

D → N. Ref.3
Corresponds to variant rs4843075 [ dbSNP | Ensembl ].

VAR_030933

Natural variant

1216

1

M → T. Ref.3
Corresponds to variant rs7162168 [ dbSNP | Ensembl ].

VAR_030934

Natural variant

1525

1

S → G.
Corresponds to variant rs35079107 [ dbSNP | Ensembl ].

VAR_051987

Natural variant

2457

1

G → S. Ref.1 Ref.2 Ref.5 Ref.10
Corresponds to variant rs2241268 [ dbSNP | Ensembl ].

VAR_030935

Natural variant

2801

1

A → T.
Corresponds to variant rs2614668 [ dbSNP | Ensembl ].

VAR_030936

Experimental info

Mutagenesis

1251

1

A → P: Loss of PKA anchoring; when associated with P-1260. Ref.2

Mutagenesis

1260

1

I → P: Loss of PKA anchoring; when associated with P-1251. Ref.2

Mutagenesis

1265

1

A → P: Abolishes RII-binding. Ref.9

Mutagenesis

2153

1

Y → F: Loss of interaction with RHOA. Ref.2

Sequence conflict

191

1

G → R in AAL40923. Ref.1

Sequence conflict

354

1

C → R in AAL40923. Ref.1

Sequence conflict

609

1

A → V in AAL40923. Ref.1

Sequence conflict

614

1

A → T in AAL40923. Ref.1

Sequence conflict

618

1

S → P in AAL40923. Ref.1

Sequence conflict

619

1

D → A in AAL11723. Ref.2

Sequence conflict

755

1

M → S in AAA58670. Ref.9

Sequence conflict

1385 – 1387

3

TQA → MLY in AAD21311. Ref.5

Sequence conflict

1547

1

N → H in BAD92651. Ref.10

Sequence conflict

1766 – 1768

3

EKE → KKK in AAA58670. Ref.9

Sequence conflict

1877

1

A → G in AAD40799. Ref.6

Sequence conflict

1897

1

Q → E in AAD40799. Ref.6

Sequence conflict

2035

1

V → D in AAD21311. Ref.5

Sequence conflict

2488

1

D → G in AAD21311. Ref.5

Sequence conflict

2667 – 2668

2

QL → HV in BAB62913. Ref.3

Sequence conflict

2667 – 2668

2

QL → HV in AAD21311. Ref.5

Secondary structure

1

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2813

Helix Strand Turn

Details...

Turn

2166 – 2168

3

Beta strand

2177 – 2181

5

Turn

2182 – 2184

3

Helix

2186 – 2191

6

Helix

2192 – 2206

15

Helix

2224 – 2227

4

Beta strand

2232 – 2241

10

Beta strand

2247 – 2260

14

Beta strand

2263 – 2265

3

Beta strand

2268 – 2270

3

Beta strand

2275 – 2277

3

Beta strand

2279 – 2285

7

Beta strand

2287 – 2289

3

Beta strand

2295 – 2301

7

Beta strand

2304 – 2306

3

Beta strand

2311 – 2314

4

Helix

2318 – 2338

21

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified March 6, 2007. Version 2. Checksum: 6A8FDAC9A3D3B1F2	FASTA	2,813	307,550
	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
	Isoform 2 [UniParc]. Checksum: 4EA29B253C76698E	FASTA	2,817	307,845
	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 RSMSWCPSGV QYSAGLSADF NYRSFSLEGL TGGAGVGNKP 1630 1640 1650 1660 1670 1680 SSSLEVSSAN AEELRHPFSG EERVDSLVSL SEEDLESDQR EHRMFDQQIC HRSKQQGFNY 1690 1700 1710 1720 1730 1740 CTSAISSPLT KSISLMTISH PGLDNSRPFH STFHNTSANL TESITEENYN FLPHSPSKKD 1750 1760 1770 1780 1790 1800 SEWKSGTKVS RTFSYIKNKM SSSKKSKEKE KEKDKIKEKE KDSKDKEKDK KTVNGHTFSS 1810 1820 1830 1840 1850 1860 IPVVGPISCS QCMKPFTNKD AYTCANCSAF VHKGCRESLA SCAKVKMKQP KGSLQAHDTS 1870 1880 1890 1900 1910 1920 SLPTVIMRNK PSQPKERPRS AVLLVDETAT TPIFANRRSQ QSVSLSKSVS IQNITGVGND 1930 1940 1950 1960 1970 1980 ENMSNTWKFL SHSTDSLNKI SKVNESTESL TDEGVGTDMN EGQLLGDFEI ESKQLEAESW 1990 2000 2010 2020 2030 2040 SRIIDSKFLK QQKKDVVKRQ EVIYELMQTE FHHVRTLKIM SGVYSQGMMA DLLFEQQMVE 2050 2060 2070 2080 2090 2100 KLFPCLDELI SIHSQFFQRI LERKKESLVD KSEKNFLIKR IGDVLVNQFS GENAERLKKT 2110 2120 2130 2140 2150 2160 YGKFCGQHNQ SVNYFKDLYA KDKRFQAFVK KKMSSSVVRR LGIPECILLV TQRITKYPVL 2170 2180 2190 2200 2210 2220 FQRILQCTKD NEVEQEDLAQ SLSLVKDVIG AVDSKVASYE KKVRLNEIYT KTDSKSIMRM 2230 2240 2250 2260 2270 2280 KSGQMFAKED LKRKKLVRDG SVFLKNAAGR LKEVQAVLLT DILVFLQEKD QKYIFASLDQ 2290 2300 2310 2320 2330 2340 KSTVISLKKL IVREVAHEEK GLFLISMGMT DPEMVEVHAS SKEERNSWIQ IIQDTINTLN 2350 2360 2370 2380 2390 2400 RDEDEGIPSE NEEEKKMLDT RARELKEQLH QKDQKILLLL EEKEMIFRDM AECSTPLPED 2410 2420 2430 2440 2450 2460 CSPTHSPRVL FRSNTEEALK GGPLMKSAIN EVEILQGLVS GNLGGTLGPT VSSPIEQDVV 2470 2480 2490 2500 2510 2520 GPVSLPRRAE TFGGFDSHQM NASKGGEKEE GDDGQDLRRT ESDSGLKKGG NANLVFMLKR 2530 2540 2550 2560 2570 2580 NSEQVVQSVV HLYELLSALQ GVVLQQDSYI EDQKLVLSER ALTRSLSRPS SLIEQEKQRS 2590 2600 2610 2620 2630 2640 LEKQRQDLAN LQKQQAQYLE EKRRREREWE ARERELRERE ALLAQREEEV QQGQQDLEKE 2650 2660 2670 2680 2690 2700 REELQQKKGT YQYDLERLRA AQKQLEREQE QLRREAERLS QRQTERDLCQ VSHPHTKLMR 2710 2720 2730 2740 2750 2760 IPSFFPSPEE PPSPSAPSIA KSGSLDSELS VSPKRNSISR THKDKGPFHI LSSTSQTNKG 2770 2780 2790 2800 2810 PEGQSQAPAS TSASTRLFGL TKPKEKKEKK KKNKTSRSQP GDGPASEVSA EGEEIFC
	Isoform 3 [UniParc]. Checksum: 117C84737CE9A79B	FASTA	2,793	305,281
	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 RSFSLEGLTG GAGVGNKPSS SLEVSSANAE ELRHPFSGEE 1630 1640 1650 1660 1670 1680 RVDSLVSLSE EDLESDQREH RMFDQQICHR SKQQGFNYCT SAISSPLTKS ISLMTISHPG 1690 1700 1710 1720 1730 1740 LDNSRPFHST FHNTSANLTE SITEENYNFL PHSPSKKDSE WKSGTKVSRT FSYIKNKMSS 1750 1760 1770 1780 1790 1800 SKKSKEKEKE KDKIKEKEKD SKDKEKDKKT VNGHTFSSIP VVGPISCSQC MKPFTNKDAY 1810 1820 1830 1840 1850 1860 TCANCSAFVH KGCRESLASC AKVKMKQPKG SLQAHDTSSL PTVIMRNKPS QPKERPRSAV 1870 1880 1890 1900 1910 1920 LLVDETATTP IFANRRSQQS VSLSKSVSIQ NITGVGNDEN MSNTWKFLSH STDSLNKISK 1930 1940 1950 1960 1970 1980 VNESTESLTD EGTDMNEGQL LGDFEIESKQ LEAESWSRII DSKFLKQQKK DVVKRQEVIY 1990 2000 2010 2020 2030 2040 ELMQTEFHHV RTLKIMSGVY SQGMMADLLF EQQMVEKLFP CLDELISIHS QFFQRILERK 2050 2060 2070 2080 2090 2100 KESLVDKSEK NFLIKRIGDV LVNQFSGENA ERLKKTYGKF CGQHNQSVNY FKDLYAKDKR 2110 2120 2130 2140 2150 2160 FQAFVKKKMS SSVVRRLGIP ECILLVTQRI TKYPVLFQRI LQCTKDNEVE QEDLAQSLSL 2170 2180 2190 2200 2210 2220 VKDVIGAVDS KVASYEKKVR LNEIYTKTDS KSIMRMKSGQ MFAKEDLKRK KLVRDGSVFL 2230 2240 2250 2260 2270 2280 KNAAGRLKEV QAVLLTDILV FLQEKDQKYI FASLDQKSTV ISLKKLIVRE VAHEEKGLFL 2290 2300 2310 2320 2330 2340 ISMGMTDPEM VEVHASSKEE RNSWIQIIQD TINTLNRDED EGIPSENEEE KKMLDTRARE 2350 2360 2370 2380 2390 2400 LKEQLHQKDQ KILLLLEEKE MIFRDMAECS TPLPEDCSPT HSPRVLFRSN TEEALKGGPL 2410 2420 2430 2440 2450 2460 MKSAINEVEI LQGLVSGNLG GTLGPTVSSP IEQDVVGPVS LPRRAETFGG FDSHQMNASK 2470 2480 2490 2500 2510 2520 GGEKEEGDDG QDLRRTESDS GLKKGGNANL VFMLKRNSEQ VVQSVVHLYE LLSALQGVVL 2530 2540 2550 2560 2570 2580 QQDSYIEDQK LVLSERALTR SLSRPSSLIE QEKQRSLEKQ RQDLANLQKQ QAQYLEEKRR 2590 2600 2610 2620 2630 2640 REREWEARER ELREREALLA QREEEVQQGQ QDLEKEREEL QQKKGTYQYD LERLRAAQKQ 2650 2660 2670 2680 2690 2700 LEREQEQLRR EAERLSQRQT ERDLCQVSHP HTKLMRIPSF FPSPEEPPSP SAPSIAKSGS 2710 2720 2730 2740 2750 2760 LDSELSVSPK RNSISRTHKD KGPFHILSST SQTNKGPEGQ SQAPASTSAS TRLFGLTKPK 2770 2780 2790 EKKEKKKKNK TSRSQPGDGP ASEVSAEGEE IFC
	Isoform 4 [UniParc]. Checksum: D441A72053F1EBC5	FASTA	179	19,992
	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 QSGPPSGDVN SLDKKLVLAF RHLKLPTEWN VLGTDQSLHG ENLYDLQTHF KFVIFLLFF

References

	« Hide 'large scale' referencesShow '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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[17]	"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, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[18]	"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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[19]	"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].
[20]	"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, MASS SPECTROMETRY.
[21]	"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.

IPI

IPI00065931.
IPI00329783.
IPI00375281.
IPI00384381.
IPI00829717.
IPI00829774.
IPI00829853.

PIR

A42915.
I38434.

RefSeq

NP_001257475.1. NM_001270546.1.
NP_006729.4. NM_006738.5.
NP_009131.2. NM_007200.4.

UniGene

Hs.459211.
Hs.710656.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
2DRN	NMR	-	C	1246-1268	[»]
2LG1	NMR	-	A	2164-2346	[»]

ProteinModelPortal

Q12802.

ModBase

Search...

Protein-protein interaction databases

DIP

DIP-180N.

IntAct

Q12802. 20 interactions.

MINT

MINT-3308570.

PTM databases

PhosphoSite

Q12802.

Polymorphism databases

DMDM

134048676.

Proteomic databases

PaxDb

Q12802.

PRIDE

Q12802.

Protocols and materials databases

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000361243; ENSP00000354718; ENSG00000170776.
ENST00000394518; ENSP00000378026; ENSG00000170776.
ENST00000560302; ENSP00000453634; ENSG00000170776.

GeneID

11214.

KEGG

hsa:11214.

UCSC

uc002bls.3. human.
uc002blt.1. human.
uc002blu.1. human.
uc002blv.1. human.
uc002blw.1. human.

Organism-specific databases

CTD

11214.

GeneCards

GC15P085777.

H-InvDB

HIX0021561.
HIX0172808.

HGNC

HGNC:371. AKAP13.

HPA

HPA019773.

MIM

604686. gene.

neXtProt

NX_Q12802.

PharmGKB

PA24665.

GenAtlas

Search...

Phylogenomic databases

eggNOG

COG5422.

HOVERGEN

HBG080828.

KO

K16529.

OMA

QQLMKTN.

OrthoDB

EOG4B8JC4.

Enzyme and pathway databases

Reactome

REACT_111102. Signal Transduction.

Gene expression databases

ArrayExpress

Q12802.

Bgee

Q12802.

Genevestigator

Q12802.

Family and domain databases

Gene3D

1.20.900.10. 1 hit.
2.30.29.30. 1 hit.

InterPro

IPR000219. DH-domain.
IPR011993. PH_like_dom.
IPR001849. Pleckstrin_homology.
IPR002219. Prot_Kinase_C-like_PE/DAG-bd.
IPR015721. RhoGEF-like.
[Graphical view]

PANTHER

PTHR22825. PTHR22825. 1 hit.

Pfam

PF00169. PH. 1 hit.
PF00621. RhoGEF. 1 hit.
[Graphical view]

SMART

SM00109. C1. 1 hit.
SM00233. PH. 1 hit.
SM00325. RhoGEF. 1 hit.
[Graphical view]

SUPFAM

SSF48065. DH-domain. 1 hit.

PROSITE

PS00741. DH_1. False negative.
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]

ProtoNet

Search...

Other

ChiTaRS

AKAP13. human.

EvolutionaryTrace

Q12802.

GenomeRNAi

11214.

NextBio

42679.

SOURCE

Search...

Entry information

Entry name

AKP13_HUMAN

Accession

Primary (citable) accession number: Q12802
Secondary accession number(s): Q14572 , 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:	May 1, 2013
This is version 117 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.