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UniProtKB/Swiss-Prot entry Q12802


[Entry info] [Name and origin] [References] [Comments] [Cross-references] [Keywords] [Features] [Sequence] [Tools]

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Entry information
Entry name AKP13_HUMAN
Primary accession number Q12802
Secondary accession numbers Q14572 Q59FP6 Q86W90 Q8WXQ6 Q96JP6 Q96P79 Q9Y5T0 Q9Y5T6
Integrated into Swiss-Prot on July 15, 1999
Sequence was last modified on March 6, 2007 (Sequence version 2)
Annotations were last modified on    July 1, 2008 (Entry version 65)
Name and origin of the protein
Protein name A-kinase anchor protein 13
Synonyms AKAP 13
Protein kinase A-anchoring protein 13
Breast cancer nuclear receptor-binding auxiliary protein
Human thyroid-anchoring protein 31
Guanine nucleotide exchange factor Lbc
AKAP-Lbc
P47
Lymphoid blast crisis oncogene
LBC oncogene
Non-oncogenic Rho GTPase-specific GTP exchange factor
Gene name
Name: AKAP13
Synonyms: BRX, HT31, LBC
From
Homo sapiens (Human) [TaxID: 9606] 
Taxonomy Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; Homo.
Protein existence 1: Evidence at protein level;
References
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 6).
PubMed=8290273 [NCBI, ExPASy, EBI, Israel, Japan]
Toksoz D., Williams D.A.;
"Novel human oncogene lbc detected by transfection with distinct homology regions to signal transduction products.";
Oncogene 9:621-628(1994).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3), FUNCTION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH ESR1; THRA AND PPARA, AND VARIANT SER-2457.
TISSUE=Testis;
DOI=10.1038/sj.onc.1201783; PubMed=9627117 [NCBI, ExPASy, EBI, Israel, Japan]
Rubino D., Driggers P., Arbit D., Kemp L., Miller B., Coso O., Pagliai K., Gray K., Gutkind S., Segars J.;
"Characterization of Brx, a novel Dbl family member that modulates estrogen receptor action.";
Oncogene 16:2513-2526(1998).
[3]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 7), ALTERNATIVE SPLICING (ISOFORM 6), FUNCTION, SUBCELLULAR LOCATION, DOMAIN, AND TISSUE SPECIFICITY.
TISSUE=Skeletal muscle;
PubMed=9891067 [NCBI, ExPASy, EBI, Israel, Japan]
Sterpetti P., Hack A.A., Bashar M.P., Park B., Cheng S.-D., Knoll J.H.M., Urano T., Feig L.A., Toksoz D.;
"Activation of the Lbc Rho exchange factor proto-oncogene by truncation of an extended C terminus that regulates transformation and targeting.";
Mol. Cell. Biol. 19:1334-1345(1999).
[4]
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).
[5]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), INTERACTION WITH RHOA, AND VARIANTS CYS-574 AND SER-2457.
DOI=10.1016/S0014-5793(01)02995-7; PubMed=11696353 [NCBI, ExPASy, EBI, Israel, Japan]
Klussmann E., Edemir B., Pepperle B., Tamma G., Henn V., Klauschenz E., Hundsrucker C., Maric K., Rosenthal W.;
"Ht31: the first protein kinase A anchoring protein to integrate protein kinase A and Rho signaling.";
FEBS Lett. 507:264-268(2001).
[6]
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, AND VARIANTS VAL-624; MET-897 AND SER-2457.
DOI=10.1074/jbc.M106629200; PubMed=11546812 [NCBI, ExPASy, EBI, Israel, Japan]
Diviani D., Soderling J., Scott J.D.;
"AKAP-Lbc anchors protein kinase A and nucleates Galpha 12-selective Rho-mediated stress fiber formation.";
J. Biol. Chem. 276:44247-44257(2001).
[7]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), AND VARIANTS THR-452; ARG-494; CYS-574; LYS-689; ALA-845; MET-897; ALA-1062; ASN-1086 AND THR-1216.
TISSUE=Lung;
Miyamoto M., Ono Y.;
Submitted (FEB-2001) to the EMBL/GenBank/DDBJ databases.
[8]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 5).
TISSUE=Brain;
DOI=10.1101/gr.2596504; PubMed=15489334 [NCBI, ExPASy, EBI, Israel, Japan]
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[9]
NUCLEOTIDE SEQUENCE [MRNA] OF 754-1768, PKA AND RII BINDING, AND MUTAGENESIS OF ALA-1265.
TISSUE=Thyroid;
PubMed=1618839 [NCBI, ExPASy, EBI, Israel, Japan]
Carr D.W., Hausken Z.E., Fraser I.D.C., Stofko-Hahn R.E., Scott J.D.;
"Association of the type II cAMP-dependent protein kinase with a human thyroid RII-anchoring protein. Cloning and characterization of the RII-binding domain.";
J. Biol. Chem. 267:13376-13382(1992).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1486-2813 (ISOFORM 4), AND VARIANT SER-2457.
TISSUE=Brain;
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.
[11]
FUNCTION, AND INTERACTION WITH ESR2.
DOI=10.1074/jbc.M106927200; PubMed=11579095 [NCBI, ExPASy, EBI, Israel, Japan]
Driggers P.H., Segars J.H., Rubino D.M.;
"The proto-oncoprotein Brx activates estrogen receptor beta by a p38 mitogen-activated protein kinase pathway.";
J. Biol. Chem. 276:46792-46797(2001).
[12]
INTERACTION WITH NME2.
DOI=10.1016/j.bbrc.2004.06.067; PubMed=15249197 [NCBI, ExPASy, EBI, Israel, Japan]
Iwashita S., Fujii M., Mukai H., Ono Y., Miyamoto M.;
"Lbc proto-oncogene product binds to and could be negatively regulated by metastasis suppressor nm23-H2.";
Biochem. Biophys. Res. Commun. 320:1063-1068(2004).
[13]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-1929 AND SER-1932, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1016/j.cell.2006.09.026; PubMed=17081983 [NCBI, ExPASy, EBI, Israel, Japan]
Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.";
Cell 127:635-648(2006).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983 AND SER-2728, AND MASS SPECTROMETRY.
TISSUE=Epithelium;
DOI=10.1038/nbt1240; PubMed=16964243 [NCBI, ExPASy, EBI, Israel, Japan]
Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.;
"A probability-based approach for high-throughput protein phosphorylation analysis and site localization.";
Nat. Biotechnol. 24:1285-1292(2006).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-983, AND MASS SPECTROMETRY.
DOI=10.2116/analsci.24.161; PubMed=18187866 [NCBI, ExPASy, EBI, Israel, Japan]
Imami K., Sugiyama N., Kyono Y., Tomita M., Ishihama Y.;
"Automated phosphoproteome analysis for cultured cancer cells by two-dimensional nanoLC-MS using a calcined titania/C18 biphasic column.";
Anal. Sci. 24:161-166(2008).
[16]
STRUCTURE BY NMR OF 493-516.
DOI=10.1093/emboj/20.7.1651; PubMed=11285229 [NCBI, ExPASy, EBI, Israel, Japan]
Newlon M.G., Roy M., Morikis D., Carr D.W., Westphal R., Scott J.D., Jennings P.A.;
"A novel mechanism of PKA anchoring revealed by solution structures of anchoring complexes.";
EMBO J. 20:1651-1662(2001).
Comments
Copyright
Copyrighted by the UniProt Consortium, see http://www.uniprot.org/terms. Distributed under the Creative Commons Attribution-NoDerivs License.
Cross-references
Sequence databases
EMBL
U03634; AAC50065.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF126008; AAD21311.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF127481; AAD40799.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF387101; AAL40923.1; ALT_FRAME; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AF406992; AAL11723.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB055890; BAB62913.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
BC050312; AAH50312.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
M90360; AAA58670.1; ALT_TERM; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
AB209414; BAD92651.1; -; mRNA.[EMBL / GenBank / DDBJ] [CoDingSequence]
PIR A42915; A42915.
I38434; I38434.
RefSeq NP_006729.4; -.
NP_009131.2; -.
NP_658913.1; -.
UniGene Hs.459211
3D structure databases
PDB
2DRN; NMR; -; C=1246-1268.[ExPASy / RCSB / EBI]
PDBsum 2DRN; -.
ModBase Q12802.
Protein-protein interaction databases
IntAct Q12802; -.
PTM databases
PhosphoSite Q12802; -.
Enzyme and pathway databases
Reactome REACT_11044; Signaling by Rho GTPases.
Organism-specific databases
HGNC HGNC:371; AKAP13.
GeneLynx AKAP13; Homo sapiens.
GenAtlas AKAP13.
MIM 604686; gene. [NCBI / EBI]
PharmGKB PA24665; -.
GeneCards Q12802.
Gene expression databases
ArrayExpress Q12802; -.
Ontologies
GO
GO:0005624; Cellular component: membrane fraction (traceable author statement from ProtInc).
GO:0004691; Molecular function: cAMP-dependent protein kinase activity (non-traceable author statement from UniProtKB).
GO:0005515; Molecular function: protein binding (inferred from physical interaction from IntAct).
GO:0004871; Molecular function: signal transducer activity (traceable author statement from ProtInc).
QuickGo view.
Family and domain databases
InterPro IPR002219; DAG_PE_bd.
IPR000219; DH-domain.
IPR001331; GDS_CDC24_CS.
IPR001849; PH.
IPR011993; PH_type.
IPR015721; RhoGEF_like.
Graphical view of domain structure.
Gene3D G3DSA:2.30.29.30; PH_type; 1.
G3DSA:1.20.900.10; RhoGEF; 1.
PANTHER PTHR22825; RhoGEF_like; 1.
Pfam PF00130; C1_1; 1.
PF00169; PH; 1.
PF00621; RhoGEF; 1.
Pfam graphical view of domain structure.
SMART SM00109; C1; 1.
SM00233; PH; 1.
SM00325; RhoGEF; 1.
SMART graphical view of domain structure.
PROSITE PS00741; DH_1; FALSE_NEG.
PS50010; DH_2; 1.
PS50003; PH_DOMAIN; 1.
PS00479; ZF_DAG_PE_1; 1.
PS50081; ZF_DAG_PE_2; 1.
PROSITE graphical view of domain structure (profiles).
BLOCKS Q12802.
Genome annotation databases
Ensembl ENSG00000170776; Homo sapiens. [Contig view]
GeneID 11214; -.
KEGG hsa:11214; -.
Phylogenomic databases
HOVERGEN Q12802; -.
Other
SOURCE AKAP13; Homo sapiens.
ProtoNet Q12802.
UniRef View cluster of proteins with at least 50% / 90% / 100% identity.
Keywords
3D-structure; Alternative splicing; Coiled coil; Cytoplasm; Guanine-nucleotide releasing factor; Membrane; Metal-binding; Nucleus; Phorbol-ester binding; Phosphoprotein; Polymorphism; Proto-oncogene; Zinc; Zinc-finger.
Features
SEVIEWER logo Feature table viewer FT aligner logo Feature aligner
KeyFrom    To Length Description FTId
CHAIN   1   2813  2813     A-kinase anchor protein 13. PRO_0000080963
DOMAIN   1994   2191  198     DH. 
DOMAIN   2231   2333  103     PH. 
ZN_FING   1791   1838  48     Phorbol-ester/DAG-type. 
REGION   494    516  23     RII-binding. 
REGION   1919   2813  895     Interaction with ESR1. 
COILED   1758   1790  33     Potential. 
COILED   2345   2381  37     Potential. 
COILED   2568   2683  116     Potential. 
COMPBIAS   1471   1474  4     Poly-Ser. 
COMPBIAS   1534   1537  4     Poly-Glu. 
COMPBIAS   2778   2790  13     Poly-Lys. 
MOD_RES   983    983        Phosphoserine. 
MOD_RES   1929   1929        Phosphoserine. 
MOD_RES   1932   1932        Phosphoserine. 
MOD_RES   2728   2728        Phosphoserine. 
VAR_SEQ   1   1918        Missing (in isoform 6 and isoform 7). VSP_023484
VAR_SEQ   1   1384        Missing (in isoform 3). VSP_023485
VAR_SEQ   160    179        DAGPRETLMHFAVRLGLLRL -> GENLYDLQTHFKFVIFLLFF (in isoform 5). VSP_023486
VAR_SEQ   180   2813        Missing (in isoform 5). VSP_023487
VAR_SEQ   1385   1387        TQA -> MLY (in isoform 3). VSP_023488
VAR_SEQ   1581   1598        Missing (in isoform 4). VSP_023489
VAR_SEQ   1583   1598        SMRVLGDVVRRPPIHR -> MSWCPSGVQYSAGLSADFNY (in isoform 2). VSP_023490
VAR_SEQ   1950   1951        Missing (in isoform 4, isoform 6 and isoform 7). VSP_023491
VAR_SEQ   2336   2344        NRDEDEGIP -> SGNGWRCFN (in isoform 6). VSP_023492
VAR_SEQ   2345   2813        Missing (in isoform 6). VSP_023493
VARIANT   452    452  1     M -> T (in dbSNP:rs2061821 [NCBI]). VAR_030925 
VARIANT   494    494  1     W -> R (in dbSNP:rs2061822 [NCBI]). VAR_030926 
VARIANT   574    574  1     R -> C (in dbSNP:rs2061824 [NCBI]). VAR_030927 
VARIANT   624    624  1     G -> V (in dbSNP:rs745191 [NCBI]). VAR_030928 
VARIANT   689    689  1     E -> K (in dbSNP:rs7177107 [NCBI]). VAR_030929 
VARIANT   845    845  1     V -> A (in dbSNP:rs4075256 [NCBI]). VAR_030930 
VARIANT   897    897  1     V -> M (in dbSNP:rs4075254 [NCBI]). VAR_030931 
VARIANT   1062   1062  1     P -> A (in dbSNP:rs4843074 [NCBI]). VAR_030932 
VARIANT   1086   1086  1     D -> N (in dbSNP:rs4843075 [NCBI]). VAR_030933 
VARIANT   1216   1216  1     M -> T (in dbSNP:rs7162168 [NCBI]). VAR_030934 
VARIANT   2457   2457  1     G -> S (in dbSNP:rs2241268 [NCBI]). VAR_030935 
VARIANT   2801   2801  1     A -> T (in dbSNP:rs2614668 [NCBI]). VAR_030936 
MUTAGEN   1251   1251        A->P: Loss of PKA anchoring; when associated with P-1260. 
MUTAGEN   1260   1260        I->P: Loss of PKA anchoring; when associated with P-1251. 
MUTAGEN   1265   1265        A->P: Abolishes RII-binding. 
MUTAGEN   2153   2153        Y->F: Loss of interaction with RHOA. 
CONFLICT   191    191        G -> R (in Ref. 5; AAL40923). 
CONFLICT   354    354        C -> R (in Ref. 5; AAL40923). 
CONFLICT   609    609        A -> V (in Ref. 5; AAL40923). 
CONFLICT   614    614        A -> T (in Ref. 5; AAL40923). 
CONFLICT   618    618        S -> P (in Ref. 5; AAL40923). 
CONFLICT   619    619        D -> A (in Ref. 6; AAL11723). 
CONFLICT   755    755        M -> S (in Ref. 9; AAA58670). 
CONFLICT   1547   1547        N -> H (in Ref. 10; BAD92651). 
CONFLICT   2035   2035        V -> D (in Ref. 2; AAD21311). 
CONFLICT   2488   2488        D -> G (in Ref. 2; AAD21311). 
CONFLICT   2667   2668        QL -> HV (in Ref. 2; AAD21311 and 7; BAB62913). 
Sequence information
Length: 2813 AA [This is the length of the unprocessed precursor] Molecular weight: 307550 Da [This is the MW of the unprocessed precursor] CRC64: 6A8FDAC9A3D3B1F2 [This is a checksum on the sequence]
        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 

Q12802 in FASTA format

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BLAST logo BLAST submission on ExPASy/SIB
or at NCBI (USA)
Tools Sequence analysis tools: ProtParam, ProtScale, Compute pI/Mw, PeptideMass, PeptideCutter, Dotlet (Java)
PROSITE logo ScanProsite, MotifScan SWISS-MODEL Submit a homology modeling request to SWISS-MODEL
NPSA logo NPSA Sequence analysis tools

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