AHNK2_HUMAN
ID AHNK2_HUMAN Reviewed; 5795 AA.
AC Q8IVF2; Q5BKX7; Q7Z343; Q7Z358; Q7Z394; Q7Z3G0; Q86WQ6; Q8IYY1; Q8N3G4;
AC Q96EX9;
DT 26-FEB-2008, integrated into UniProtKB/Swiss-Prot.
DT 26-FEB-2008, sequence version 2.
DT 03-AUG-2022, entry version 139.
DE RecName: Full=Protein AHNAK2;
GN Name=AHNAK2; Synonyms=C14orf78, KIAA2019;
OS Homo sapiens (Human).
OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia;
OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae;
OC Homo.
OX NCBI_TaxID=9606;
RN [1]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=12508121; DOI=10.1038/nature01348;
RA Heilig R., Eckenberg R., Petit J.-L., Fonknechten N., Da Silva C.,
RA Cattolico L., Levy M., Barbe V., De Berardinis V., Ureta-Vidal A.,
RA Pelletier E., Vico V., Anthouard V., Rowen L., Madan A., Qin S., Sun H.,
RA Du H., Pepin K., Artiguenave F., Robert C., Cruaud C., Bruels T.,
RA Jaillon O., Friedlander L., Samson G., Brottier P., Cure S., Segurens B.,
RA Aniere F., Samain S., Crespeau H., Abbasi N., Aiach N., Boscus D.,
RA Dickhoff R., Dors M., Dubois I., Friedman C., Gouyvenoux M., James R.,
RA Madan A., Mairey-Estrada B., Mangenot S., Martins N., Menard M., Oztas S.,
RA Ratcliffe A., Shaffer T., Trask B., Vacherie B., Bellemere C., Belser C.,
RA Besnard-Gonnet M., Bartol-Mavel D., Boutard M., Briez-Silla S.,
RA Combette S., Dufosse-Laurent V., Ferron C., Lechaplais C., Louesse C.,
RA Muselet D., Magdelenat G., Pateau E., Petit E., Sirvain-Trukniewicz P.,
RA Trybou A., Vega-Czarny N., Bataille E., Bluet E., Bordelais I., Dubois M.,
RA Dumont C., Guerin T., Haffray S., Hammadi R., Muanga J., Pellouin V.,
RA Robert D., Wunderle E., Gauguet G., Roy A., Sainte-Marthe L., Verdier J.,
RA Verdier-Discala C., Hillier L.W., Fulton L., McPherson J., Matsuda F.,
RA Wilson R., Scarpelli C., Gyapay G., Wincker P., Saurin W., Quetier F.,
RA Waterston R., Hood L., Weissenbach J.;
RT "The DNA sequence and analysis of human chromosome 14.";
RL Nature 421:601-607(2003).
RN [2]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE
RP [LARGE SCALE MRNA] OF 1-77 (ISOFORM 1), NUCLEOTIDE SEQUENCE [LARGE SCALE
RP MRNA] OF 1-647 (ISOFORM 3), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF
RP 5281-5795 (ISOFORMS 1/2/3), AND VARIANT ALA-5397.
RC TISSUE=Eye, Kidney, Skin, Testis, and Uterine adenocarcinoma;
RX PubMed=15489334; DOI=10.1101/gr.2596504;
RG The MGC Project Team;
RT "The status, quality, and expansion of the NIH full-length cDNA project:
RT the Mammalian Gene Collection (MGC).";
RL Genome Res. 14:2121-2127(2004).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 1-631 (ISOFORM 3).
RC TISSUE=Astrocyte;
RX PubMed=14702039; DOI=10.1038/ng1285;
RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H.,
RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M.,
RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K.,
RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T.,
RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M.,
RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S.,
RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H.,
RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K.,
RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N.,
RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y.,
RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K.,
RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T.,
RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T.,
RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y.,
RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H.,
RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y.,
RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H.,
RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O.,
RA Isogai T., Sugano S.;
RT "Complete sequencing and characterization of 21,243 full-length human
RT cDNAs.";
RL Nat. Genet. 36:40-45(2004).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 2994-5795 (ISOFORMS 1/3).
RC TISSUE=Brain;
RA Nagase T., Kikuno R., Ohara O.;
RT "The nucleotide sequence of a long cDNA clone isolated from human.";
RL Submitted (NOV-2002) to the EMBL/GenBank/DDBJ databases.
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 4587-5795 (ISOFORMS 1/3), AND
RP VARIANTS ALA-4664; ASP-5184 AND ALA-5397.
RC TISSUE=Colon endothelium, Melanoma, and Uterus;
RX PubMed=17974005; DOI=10.1186/1471-2164-8-399;
RA Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
RA Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H., Heubner D.,
RA Hoerlein A., Michel G., Wedler H., Koehrer K., Ottenwaelder B., Poustka A.,
RA Wiemann S., Schupp I.;
RT "The full-ORF clone resource of the German cDNA consortium.";
RL BMC Genomics 8:399-399(2007).
RN [6]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=17081983; DOI=10.1016/j.cell.2006.09.026;
RA Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.;
RT "Global, in vivo, and site-specific phosphorylation dynamics in signaling
RT networks.";
RL Cell 127:635-648(2006).
RN [7]
RP INTERACTION WITH DYSF.
RX PubMed=17185750; DOI=10.1096/fj.06-6628com;
RA Huang Y., Laval S.H., van Remoortere A., Baudier J., Benaud C.,
RA Anderson L.V., Straub V., Deelder A., Frants R.R., den Dunnen J.T.,
RA Bushby K., van der Maarel S.M.;
RT "AHNAK, a novel component of the dysferlin protein complex, redistributes
RT to the cytoplasm with dysferlin during skeletal muscle regeneration.";
RL FASEB J. 21:732-742(2007).
RN [8]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280 AND SER-294, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=18669648; DOI=10.1073/pnas.0805139105;
RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
RA Elledge S.J., Gygi S.P.;
RT "A quantitative atlas of mitotic phosphorylation.";
RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
RN [9]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-1510; LYS-1840 AND LYS-2500, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=19608861; DOI=10.1126/science.1175371;
RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C.,
RA Olsen J.V., Mann M.;
RT "Lysine acetylation targets protein complexes and co-regulates major
RT cellular functions.";
RL Science 325:834-840(2009).
RN [10]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-593; SER-842;
RP SER-1007; SER-1112; SER-1337; SER-1502; SER-1667; SER-1832; SER-2162;
RP SER-2492; SER-2822; SER-2987; SER-3152; SER-3408; SER-3812; SER-3977;
RP SER-4142; SER-4307; SER-4472; SER-4477; SER-4894 AND SER-4897, AND
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=20068231; DOI=10.1126/scisignal.2000475;
RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L.,
RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.;
RT "Quantitative phosphoproteomics reveals widespread full phosphorylation
RT site occupancy during mitosis.";
RL Sci. Signal. 3:RA3-RA3(2010).
RN [11]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21269460; DOI=10.1186/1752-0509-5-17;
RA Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T.,
RA Bennett K.L., Superti-Furga G., Colinge J.;
RT "Initial characterization of the human central proteome.";
RL BMC Syst. Biol. 5:17-17(2011).
RN [12]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=21406692; DOI=10.1126/scisignal.2001570;
RA Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T.,
RA Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.;
RT "System-wide temporal characterization of the proteome and phosphoproteome
RT of human embryonic stem cell differentiation.";
RL Sci. Signal. 4:RS3-RS3(2011).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-280; SER-294; SER-593;
RP SER-1418; SER-2243; SER-2408; SER-2738; SER-3068; SER-3233; SER-3408;
RP SER-4388; SER-4477 AND SER-5707, AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RC TISSUE=Cervix carcinoma;
RX PubMed=23186163; DOI=10.1021/pr300630k;
RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
RA Mohammed S.;
RT "Toward a comprehensive characterization of a human cancer cell
RT phosphoproteome.";
RL J. Proteome Res. 12:260-271(2013).
RN [14]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
RA Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
RA Vertegaal A.C.;
RT "SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
RL Cell Rep. 10:1778-1791(2015).
RN [15]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25755297; DOI=10.1074/mcp.o114.044792;
RA Xiao Z., Chang J.G., Hendriks I.A., Sigurdsson J.O., Olsen J.V.,
RA Vertegaal A.C.;
RT "System-wide analysis of SUMOylation dynamics in response to replication
RT stress reveals novel small ubiquitin-like modified target proteins and
RT acceptor lysines relevant for genome stability.";
RL Mol. Cell. Proteomics 14:1419-1434(2015).
RN [16]
RP SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-116, AND IDENTIFICATION BY MASS
RP SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=28112733; DOI=10.1038/nsmb.3366;
RA Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
RA Nielsen M.L.;
RT "Site-specific mapping of the human SUMO proteome reveals co-modification
RT with phosphorylation.";
RL Nat. Struct. Mol. Biol. 24:325-336(2017).
RN [17] {ECO:0007744|PDB:4CN0}
RP X-RAY CRYSTALLOGRAPHY (1.75 ANGSTROMS) OF 108-203, AND SUBUNIT.
RX PubMed=24675079; DOI=10.1074/jbc.m114.554816;
RA Han H., Kursula P.;
RT "Periaxin and AHNAK nucleoprotein 2 form intertwined homodimers through
RT domain swapping.";
RL J. Biol. Chem. 289:14121-14131(2014).
CC -!- SUBUNIT: Homodimer (via PDZ domain) (PubMed:24675079). Interacts with
CC DYSF; the interaction is direct and Ca(2+)-independent
CC (PubMed:17185750). {ECO:0000269|PubMed:17185750,
CC ECO:0000269|PubMed:24675079}.
CC -!- INTERACTION:
CC Q8IVF2-2; Q9H0R8: GABARAPL1; NbExp=3; IntAct=EBI-10217765, EBI-746969;
CC Q8IVF2-2; P60520: GABARAPL2; NbExp=3; IntAct=EBI-10217765, EBI-720116;
CC Q8IVF2-3; P07306: ASGR1; NbExp=3; IntAct=EBI-12078468, EBI-1172335;
CC Q8IVF2-3; P23141-3: CES1; NbExp=3; IntAct=EBI-12078468, EBI-12360993;
CC Q8IVF2-3; O43169: CYB5B; NbExp=3; IntAct=EBI-12078468, EBI-1058710;
CC Q8IVF2-3; Q9BQA9: CYBC1; NbExp=3; IntAct=EBI-12078468, EBI-2680384;
CC Q8IVF2-3; Q92520: FAM3C; NbExp=3; IntAct=EBI-12078468, EBI-2876774;
CC Q8IVF2-3; Q9H0R8: GABARAPL1; NbExp=8; IntAct=EBI-12078468, EBI-746969;
CC Q8IVF2-3; P24593: IGFBP5; NbExp=3; IntAct=EBI-12078468, EBI-720480;
CC Q8IVF2-3; Q59EV6: PPGB; NbExp=3; IntAct=EBI-12078468, EBI-14210385;
CC Q8IVF2-3; Q96NZ9: PRAP1; NbExp=3; IntAct=EBI-12078468, EBI-2116102;
CC Q8IVF2-3; Q5TGU0: TSPO2; NbExp=3; IntAct=EBI-12078468, EBI-12195249;
CC Q8IVF2-3; Q5BVD1: TTMP; NbExp=3; IntAct=EBI-12078468, EBI-10243654;
CC Q8IVF2-3; Q9Y5Z9: UBIAD1; NbExp=3; IntAct=EBI-12078468, EBI-2819725;
CC Q8IVF2-3; Q15836: VAMP3; NbExp=3; IntAct=EBI-12078468, EBI-722343;
CC Q8IVF2-3; O95159: ZFPL1; NbExp=3; IntAct=EBI-12078468, EBI-718439;
CC -!- SUBCELLULAR LOCATION: Nucleus {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=3;
CC Name=1;
CC IsoId=Q8IVF2-1; Sequence=Displayed;
CC Name=2;
CC IsoId=Q8IVF2-2; Sequence=VSP_031550;
CC Name=3;
CC IsoId=Q8IVF2-3; Sequence=VSP_031551;
CC -!- SEQUENCE CAUTION:
CC Sequence=AAH49216.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=AAH90889.1; Type=Erroneous initiation; Evidence={ECO:0000305};
CC Sequence=BAC23115.1; Type=Frameshift; Evidence={ECO:0000305};
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DR EMBL; AL512802; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AI915159; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; BC011859; AAH11859.2; -; mRNA.
DR EMBL; BC033372; AAH33372.1; -; mRNA.
DR EMBL; BC049216; AAH49216.1; ALT_INIT; mRNA.
DR EMBL; BC090889; AAH90889.1; ALT_INIT; mRNA.
DR EMBL; AK094143; -; NOT_ANNOTATED_CDS; mRNA.
DR EMBL; AB095939; BAC23115.1; ALT_FRAME; mRNA.
DR EMBL; AL834367; CAD39030.1; -; mRNA.
DR EMBL; BX537923; CAD97904.1; -; mRNA.
DR EMBL; BX538040; CAD97981.1; -; mRNA.
DR EMBL; BX538106; CAD98019.1; -; mRNA.
DR EMBL; BX538133; CAD98034.1; -; mRNA.
DR CCDS; CCDS45177.1; -. [Q8IVF2-1]
DR RefSeq; NP_612429.2; NM_138420.2. [Q8IVF2-1]
DR RefSeq; XP_005267356.1; XM_005267299.1.
DR PDB; 4CN0; X-ray; 1.75 A; A/B=108-203.
DR PDBsum; 4CN0; -.
DR SMR; Q8IVF2; -.
DR BioGRID; 125226; 129.
DR IntAct; Q8IVF2; 41.
DR STRING; 9606.ENSP00000353114; -.
DR GlyGen; Q8IVF2; 6 sites, 1 O-linked glycan (6 sites).
DR iPTMnet; Q8IVF2; -.
DR MetOSite; Q8IVF2; -.
DR PhosphoSitePlus; Q8IVF2; -.
DR SwissPalm; Q8IVF2; -.
DR BioMuta; AHNAK2; -.
DR DMDM; 172045740; -.
DR EPD; Q8IVF2; -.
DR jPOST; Q8IVF2; -.
DR MassIVE; Q8IVF2; -.
DR MaxQB; Q8IVF2; -.
DR PaxDb; Q8IVF2; -.
DR PeptideAtlas; Q8IVF2; -.
DR PRIDE; Q8IVF2; -.
DR ProteomicsDB; 70688; -. [Q8IVF2-1]
DR ProteomicsDB; 70689; -. [Q8IVF2-2]
DR ProteomicsDB; 70690; -. [Q8IVF2-3]
DR Antibodypedia; 28280; 137 antibodies from 19 providers.
DR DNASU; 113146; -.
DR Ensembl; ENST00000333244.6; ENSP00000353114.4; ENSG00000185567.7. [Q8IVF2-1]
DR Ensembl; ENST00000557457.1; ENSP00000450998.1; ENSG00000185567.7. [Q8IVF2-2]
DR GeneID; 113146; -.
DR KEGG; hsa:113146; -.
DR MANE-Select; ENST00000333244.6; ENSP00000353114.4; NM_138420.4; NP_612429.2.
DR UCSC; uc010axc.2; human. [Q8IVF2-1]
DR CTD; 113146; -.
DR DisGeNET; 113146; -.
DR GeneCards; AHNAK2; -.
DR HGNC; HGNC:20125; AHNAK2.
DR HPA; ENSG00000185567; Tissue enhanced (skin).
DR MIM; 608570; gene.
DR neXtProt; NX_Q8IVF2; -.
DR OpenTargets; ENSG00000185567; -.
DR PharmGKB; PA162376085; -.
DR VEuPathDB; HostDB:ENSG00000185567; -.
DR eggNOG; ENOG502R1NR; Eukaryota.
DR GeneTree; ENSGT00940000163336; -.
DR HOGENOM; CLU_019457_0_0_1; -.
DR InParanoid; Q8IVF2; -.
DR OMA; KDTKFKM; -.
DR OrthoDB; 71329at2759; -.
DR PhylomeDB; Q8IVF2; -.
DR TreeFam; TF350595; -.
DR PathwayCommons; Q8IVF2; -.
DR SignaLink; Q8IVF2; -.
DR BioGRID-ORCS; 113146; 20 hits in 1080 CRISPR screens.
DR ChiTaRS; AHNAK2; human.
DR GenomeRNAi; 113146; -.
DR Pharos; Q8IVF2; Tbio.
DR PRO; PR:Q8IVF2; -.
DR Proteomes; UP000005640; Chromosome 14.
DR RNAct; Q8IVF2; protein.
DR Bgee; ENSG00000185567; Expressed in tendon of biceps brachii and 168 other tissues.
DR Genevisible; Q8IVF2; HS.
DR GO; GO:0005737; C:cytoplasm; IBA:GO_Central.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0005634; C:nucleus; IBA:GO_Central.
DR GO; GO:0005886; C:plasma membrane; IDA:HPA.
DR GO; GO:0042383; C:sarcolemma; NAS:UniProtKB.
DR GO; GO:0030315; C:T-tubule; NAS:UniProtKB.
DR GO; GO:0043484; P:regulation of RNA splicing; IBA:GO_Central.
DR Gene3D; 2.30.42.10; -; 1.
DR InterPro; IPR001478; PDZ.
DR InterPro; IPR036034; PDZ_sf.
DR SMART; SM00228; PDZ; 1.
DR SUPFAM; SSF50156; SSF50156; 1.
DR PROSITE; PS50106; PDZ; 1.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative splicing; Isopeptide bond; Nucleus;
KW Phosphoprotein; Reference proteome; Ubl conjugation.
FT CHAIN 1..5795
FT /note="Protein AHNAK2"
FT /id="PRO_0000319962"
FT DOMAIN 112..193
FT /note="PDZ"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU00143"
FT REGION 12..88
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 197..412
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 427..454
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 466..647
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 930..956
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3071..3101
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 3235..3259
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4815..4848
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4933..4958
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 4993..5167
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5324..5361
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5537..5574
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5596..5639
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5659..5757
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 5769..5795
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 29..44
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 210..257
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 330..345
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 371..386
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 483..513
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 546..581
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 597..642
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 935..951
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3075..3096
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 3240..3259
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 4832..4848
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5041..5064
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5537..5551
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5659..5677
FT /note="Polar residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5713..5750
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 5773..5789
FT /note="Basic and acidic residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 280
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:20068231, ECO:0007744|PubMed:23186163"
FT MOD_RES 294
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:18669648,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 593
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 842
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1007
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1112
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1337
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1418
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 1502
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1510
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 1667
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1832
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 1840
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2162
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2243
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2492
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2500
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 2738
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 2822
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 2987
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 3068
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 3152
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 3233
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 3408
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 3812
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 3977
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4142
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4307
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4388
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT MOD_RES 4472
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4477
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231,
FT ECO:0007744|PubMed:23186163"
FT MOD_RES 4894
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 4897
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:20068231"
FT MOD_RES 5707
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:23186163"
FT CROSSLNK 116
FT /note="Glycyl lysine isopeptide (Lys-Gly) (interchain with
FT G-Cter in SUMO2)"
FT /evidence="ECO:0007744|PubMed:25755297,
FT ECO:0007744|PubMed:25772364, ECO:0007744|PubMed:28112733"
FT VAR_SEQ 1..5002
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:15489334"
FT /id="VSP_031550"
FT VAR_SEQ 1..100
FT /note="Missing (in isoform 3)"
FT /evidence="ECO:0000303|PubMed:14702039,
FT ECO:0000303|PubMed:15489334"
FT /id="VSP_031551"
FT VARIANT 525
FT /note="T -> A (in dbSNP:rs2278607)"
FT /id="VAR_050635"
FT VARIANT 1266
FT /note="V -> M (in dbSNP:rs748458962)"
FT /id="VAR_039069"
FT VARIANT 1298
FT /note="M -> I (in dbSNP:rs2819440)"
FT /id="VAR_061548"
FT VARIANT 1470
FT /note="L -> V"
FT /id="VAR_039070"
FT VARIANT 1856
FT /note="E -> D (in dbSNP:rs2819435)"
FT /id="VAR_059560"
FT VARIANT 2107
FT /note="M -> V (in dbSNP:rs11846918)"
FT /id="VAR_050636"
FT VARIANT 2115
FT /note="S -> R (in dbSNP:rs2582514)"
FT /id="VAR_039071"
FT VARIANT 2146
FT /note="L -> V (in dbSNP:rs12890949)"
FT /id="VAR_059561"
FT VARIANT 2410
FT /note="K -> R (in dbSNP:rs11845746)"
FT /id="VAR_050637"
FT VARIANT 2429
FT /note="D -> E (in dbSNP:rs11160826)"
FT /id="VAR_039072"
FT VARIANT 2430
FT /note="L -> V (in dbSNP:rs2819426)"
FT /id="VAR_039073"
FT VARIANT 2503
FT /note="E -> A (in dbSNP:rs2819429)"
FT /id="VAR_059562"
FT VARIANT 2616
FT /note="V -> A (in dbSNP:rs4264326)"
FT /id="VAR_039074"
FT VARIANT 2862
FT /note="R -> S (in dbSNP:rs2582514)"
FT /id="VAR_059563"
FT VARIANT 3176
FT /note="D -> E (in dbSNP:rs11160826)"
FT /id="VAR_059564"
FT VARIANT 3177
FT /note="L -> V (in dbSNP:rs2819426)"
FT /id="VAR_059565"
FT VARIANT 3336
FT /note="P -> L (in dbSNP:rs10438247)"
FT /id="VAR_059566"
FT VARIANT 3363
FT /note="V -> A (in dbSNP:rs4264326)"
FT /id="VAR_059567"
FT VARIANT 3654
FT /note="G -> E (in dbSNP:rs28380382)"
FT /id="VAR_061549"
FT VARIANT 3793
FT /note="D -> N (in dbSNP:rs11160825)"
FT /id="VAR_059568"
FT VARIANT 3796
FT /note="V -> L"
FT /id="VAR_050638"
FT VARIANT 3869
FT /note="M -> V (in dbSNP:rs10438246)"
FT /id="VAR_059569"
FT VARIANT 3902
FT /note="K -> N (in dbSNP:rs2819423)"
FT /id="VAR_059570"
FT VARIANT 3961
FT /note="M -> V (in dbSNP:rs10141053)"
FT /id="VAR_050639"
FT VARIANT 4071
FT /note="I -> M (in dbSNP:rs2582511)"
FT /id="VAR_050640"
FT VARIANT 4085
FT /note="A -> V (in dbSNP:rs372676751)"
FT /id="VAR_059571"
FT VARIANT 4138
FT /note="F -> L (in dbSNP:rs2582505)"
FT /id="VAR_050641"
FT VARIANT 4198
FT /note="D -> N (in dbSNP:rs534942818)"
FT /id="VAR_059572"
FT VARIANT 4232
FT /note="K -> N (in dbSNP:rs2819423)"
FT /id="VAR_050642"
FT VARIANT 4278
FT /note="V -> A (in dbSNP:rs2819422)"
FT /id="VAR_050643"
FT VARIANT 4326
FT /note="L -> P (in dbSNP:rs2819421)"
FT /id="VAR_059573"
FT VARIANT 4478
FT /note="P -> L (in dbSNP:rs763391124)"
FT /id="VAR_059574"
FT VARIANT 4536
FT /note="M -> L (in dbSNP:rs9672139)"
FT /id="VAR_050644"
FT VARIANT 4664
FT /note="T -> A (in dbSNP:rs4465542)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_050645"
FT VARIANT 5028
FT /note="L -> M (in dbSNP:rs9672139)"
FT /id="VAR_039075"
FT VARIANT 5072
FT /note="G -> R (in dbSNP:rs2819420)"
FT /id="VAR_050646"
FT VARIANT 5139
FT /note="G -> E (in dbSNP:rs61421370)"
FT /id="VAR_061550"
FT VARIANT 5184
FT /note="Y -> D (in dbSNP:rs2819419)"
FT /evidence="ECO:0000269|PubMed:17974005"
FT /id="VAR_050647"
FT VARIANT 5397
FT /note="P -> A (in dbSNP:rs3742935)"
FT /evidence="ECO:0000269|PubMed:15489334,
FT ECO:0000269|PubMed:17974005"
FT /id="VAR_050648"
FT VARIANT 5564
FT /note="G -> R (in dbSNP:rs2819420)"
FT /id="VAR_039076"
FT VARIANT 5732
FT /note="T -> M (in dbSNP:rs748358)"
FT /id="VAR_050649"
FT CONFLICT 3195
FT /note="P -> L (in Ref. 4; BAC23115)"
FT /evidence="ECO:0000305"
FT CONFLICT 3198
FT /note="A -> V (in Ref. 4; BAC23115)"
FT /evidence="ECO:0000305"
FT CONFLICT 4740
FT /note="E -> G (in Ref. 5; CAD98019)"
FT /evidence="ECO:0000305"
FT CONFLICT 5269
FT /note="L -> P (in Ref. 5; CAD98019)"
FT /evidence="ECO:0000305"
FT CONFLICT 5560
FT /note="D -> G (in Ref. 5; CAD97904)"
FT /evidence="ECO:0000305"
FT CONFLICT 5577
FT /note="I -> V (in Ref. 5; CAD97904)"
FT /evidence="ECO:0000305"
FT CONFLICT 5590
FT /note="T -> A (in Ref. 5; CAD97981)"
FT /evidence="ECO:0000305"
FT CONFLICT 5601
FT /note="D -> G (in Ref. 5; CAD98034)"
FT /evidence="ECO:0000305"
FT STRAND 111..116
FT /evidence="ECO:0007829|PDB:4CN0"
FT STRAND 125..130
FT /evidence="ECO:0007829|PDB:4CN0"
FT STRAND 136..141
FT /evidence="ECO:0007829|PDB:4CN0"
FT HELIX 146..149
FT /evidence="ECO:0007829|PDB:4CN0"
FT STRAND 158..165
FT /evidence="ECO:0007829|PDB:4CN0"
FT HELIX 171..181
FT /evidence="ECO:0007829|PDB:4CN0"
FT STRAND 184..193
FT /evidence="ECO:0007829|PDB:4CN0"
SQ SEQUENCE 5795 AA; 616629 MW; BEC73677308C1FAB CRC64;
MCDCFHMVLP TWPGTPGSVS GRQLQPGEPG AETEDDHSVT EGPADEGIRP RPQGSSPVYE
YTTEAADFGL QEDAPGRQGS AGRRRSWWKR DSGDSRTFFR MSRPEAVQEA TEVTLKTEVE
AGASGYSVTG GGDQGIFVKQ VLKDSSAAKL FNLREGDQLL STTVFFENIK YEDALKILQY
SEPYKVQFKI RRQLPAPQDE EWASSDAQHG PQGKEKEDTD VADGCRETPT KTLEGDGDQE
RLISKPRVGR GRQSQRERLS WPKFQSIKSK RGPGPQRSHS SSEAYEPRDA HDVSPTSTDT
EAQLTVERQE QKAGPGSQRR RKFLNLRFRT GSGQGPSSTG QPGRGFQSGV GRAGVLEELG
PWGDSLEETG AATGSRREER AEQDREVMPA QSMPLPTELG DPRLCEGTPQ EGGLRAARLH
GKTLEGQAQE TAVAQRKPRA QPTPGMSREG EGEGLQSLEI GIARLSLRDT TEGGTQIGPP
EIRVRVHDLK TPKFAFSTEK EPERERRLST PQRGKRQDAS SKAGTGLKGE EVEGAGWMPG
REPTTHAEAQ GDEGDGEEGL QRTRITEEQD KGREDTEGQI RMPKFKIPSL GWSPSKHTKT
GREKATEDTE QGREGEATAT ADRREQRRTE EGLKDKEDSD SMTNTTKIQL IHDEKRLKKE
QILTEKEVAT KDSKFKMPKF KMPLFGASAP GKSMEASVDV SAPKVEADVS LLSMQGDLKT
TDLSVQTPSA DLEVQDGQVD VKLPEGPLPE GASLKGHLPK VQRPSLKMPK VDLKGPKLDL
KGPKAEVTAP DVKMSLSSME VDVQAPRAKL DGARLEGDLS LADKEVTAKD SKFKMPKFKM
PSFGVSAPGK SMEDSVDVSA PKVEADVSLS SMQGDLKATD LSIQPPSADL EVQAGQVDVK
LPEGPVPEGA GPKVHLPKVE MPSFKMPKVD LKGPQIDVKG PKLDLKGPKA EVTAPDGEVS
LPSMEVDVQA QKAKLDGAWL EGDLSLADKD VTAKDSKFKM PKFKMPSFGV SAPGKSIKAL
VDVSAPKVEA DLSLPSMQGD LKTTDLSIQP ASTDLKVQAD QVDVKLPEGH LPEGAGLKGH
LPKVEMPSFK MPKVALKGPQ VDVKGPKLDL KSPKAEVTAP DVEVSLPSVE VDVEAPGAKL
DSARLEGELS LADKDVTAKD SRFKMPKFKM PSFGASAPGK SIEASVDVSA PKVEADVSLP
SMQGDLKTTD LSIQPPSADL EVHAGQVDVK LLEGHVPEGA GFKGHLPKVQ MPSLKMPKVD
LKGPQVEVRG PKLDLKGHKA EVTAHEVAVS LPSVEVDMQA PGAKLDGAQL DGDLSLADKD
VTAKDSKFKM PKFKMPSFGV SAPGKSIEAS VDLSAPKVEA DMSLPSMQGD LKTTDLSIQP
PSTDLELQAG QLDVKLPEGP VPEGAGLKGH LPKLQMPSFK VPKVDLKGPE IDIKGPKLDL
KDPKVEVTAP DVEVSLPSVE VDVEAPGAKL DGGRLEEDMS LADKDLTTKD SKFKMPKFKM
PSFGVSAPGK SIEASVDVSA PKVEADVSLP SMQGDLKATD LSIQPPSADL EVQAGQVDVK
LPEGPVSEGA GLKGHLPKVQ MPSFKMPKVD LKGPQIDVKG PKLDLKGPKV EVTAPDVKMS
LSSMEVDVQA PRAKLDGAQL EGDLSLADKA VTAKDSKFKM PKFKMPSFGV SAPGKSIEAS
VDVSEPKVEA DVSLPSMQGD LKTTDLSIQS PSADLEVQAG QVNVKLPEGP LPEGAGFKGH
LPKVQMPSLK MPKVALKGPQ MDVKGPKLDL KGPKAEVMAP DVEVSLPSVE VDVEAPGAKL
DSVRLEGDLS LADKDVTAKD SKFKMPKFKM PSFGVSAPGK SIEASVDVSA PKVEAEVSLP
SMQGDLKTTD LCIPLPSADL VVQAGQVDMK LPEGQVPEGA GLKGHLPKVD MPSFKMPKVD
LKGPQTDVKG AKLDLKGPKA EVTAPDVEVS LPSMEVDVQA QKAKLDGARL EGDLSLADKD
MTAKDSKFKM PKFKMPSFGV SAPGRSIEAS VDVPAPKVEA DVSLPSMQGD LKTTDLSIQP
PSADLKVQTG QVDVKLPEGH VPEGAGLKGH LPKVEMPSLK MPKVDLKGPQ VDIKGPKLDL
KDPKVEMRVP DVEVSLPSME VDVQAPRAKL DSAHLQGDLT LANKDLTTKD SKFKMPKFKM
PSFGVSAPGK SIEASVDVSP PKVEADMSLP SMQGDLKTTD LSIQPLSADV KVQAGQVDVK
LLEGPVPEEV GLKGHLPKLQ MPSFKVPKVD LKGPEIDIKG PKLDLKDPKV EVTAPDVEVS
LPSVEVDVKA PGAKLDGARL EGDMSLADKD VTAKDSKFKM PKFKMLSFGV SALGKSIEAS
ADVSALKVEA DVSLPSMQGD LKTTDLSVQP PSADLEVQAG QVDVKLPEGP VPEGAGLKGH
LPKLQMPSFK MPKVDLKGPQ IDVKGPKLDL KGPKTDVMAP DVEVSQPSVE VDVEAPGAKL
DGAWLEGDLS VADKDVTTKD SRFKIPKFKM PSFGVSAPGK SIEASVDVSA PKVEADGSLS
SMQGDLKATD LSIQPPSADL EVQAGQVDVK LPEGPVPEGA GLKGHLPKVQ MPSFKMPEMD
LKGPQLDVKG PKLDLKGPKA EVTAPDVEMS LSSMEVDVQA PRAKLDGARL EGDLSLADKG
VTAKDSKFKM PKFKMPSFRV SAPGESIEAL VDVSELKVEA DMSLPSMQGD LKTTDISIQP
PSAQLEVQAG QVDVKLPEGH VPEGAGLKGH LPKLQMPSFK MPEVDLKGPQ IDVKGPNVDL
KGPKAEVTAP DVKMSLSSME VDVQAPRAKL DGARLEGDLS LADKGMTAKD SKFKMPKFKM
PSFGVSAPGK SIEASVDVSE LKVEADGSFP SMQGDLKTTD IRIQPPSAQL EVQAGQVDVK
LPEGHVPEGA GLKGHLPKVQ MPSFKMPKVD LKGPQIDVKG PKLDLKGPKA EVTAPDVEVS
LPSVEVDVEA PRAKLDGARL EGDLSLADKD VTAKDSKFKM PKFKMPSFGV SAPGKSIEVS
VDVSAPKVEA EVSLPSMQGD LKTTDISIEP PSAQLEVQAG QVDLKLPEGH VPEGAGLKGH
LPKLQMPSFK MPKVDRKGPQ IDVKGPKLDL KGPKTDVTAP DVEVSQPGME VDVEAPGAKL
DGARLEGDLS LADKDVTAKD SKFKMPKFKM PSFGVSAPGK SIEVLVDVSA PKVEADLSLP
SMQGDLKNTD ISIEPPSAQL EVQAGQVDVK LPEGHVLEGA GLKGHLPKLQ MPSFKMPKVD
RKGPQIDIKG PKLDLKGPKM DVTAPDVEVS QPSMEVDVEA PGAKLDGARL EGDLSLADKD
VTAKDSKFKM PKFKMPSYRA SAPGKSIQAS VDVSAPKAEA DVSLPSMQGD LKTTDLSIQL
PSVDLEVQAG QVDVKLPEGH VPEGAGLKGH LPKVEMPSFK MPKVDLKSPQ VDIKGPKLDL
KVPKAEVTVP DVEVSLPSVE VDVQAPRAKL DGARLEGDLS LAEKDVTAKD SKFKMPKFKM
PSFGVSAPGR SIEASLDVSA PKVEADVSLS SMQGDLKATD LSIQPPSADL EVQAVQVDVE
LLEGPVPEGA GLKGHLPKVE MPSLKTPKVD LKGPQIDVKG PKLDLKGPKA EVRVPDVEVS
LPSVEVDVQA PKAKLDAGRL EGDLSLADKD VTAKDSKFKM PKFKMPSFRV SAPGKSMEAS
VDVSAPKVEA DVSLPSMQGD LKTTDLSIQP PSADLKVQAG QMDVKLPEGQ VPEGAGLKEH
LPKVEMPSLK MPKVDLKGPQ VDIKGPKLDL KVSKAEVTAP DVEVSLPSVE VDVQAPRAKL
DSAQLEGDLS LADKDVTAKD SKFKMPKFKM PSFGVSAPGK SIEASVHVSA PKVEADVSLP
SMQGDLKTTD LSIQPHSADL TVQARQVDMK LLEGHVPEEA GLKGHLPKVQ MPSFKMPKVD
LKGPEIDIKG PKLDLKDPKV EVTAPDVEVS LPSVEVDVEA PGAKLDGARL EGDLSLADKD
MTAKDSKFKM PKFKMPSFGV SAPGKSMEAS VDVTAPKVEA DVSLPSMQGD LKATDLSVQP
PSADLEVQAG QVDVKLPEGP VPEGASLKGH LPKVQMPSFK MPKVDLKGPQ IDVKGPKLDL
KGPKAEVTAP DVKMSLSSME VDVQAPRAKL DGVQLEGDLS LADKDVTAKD SKFKMPKFKM
PSFGVSAPGK SMEASVDVSE LKAKADVSLP SMQGDLKTTD LSIQSPSADL EVQAGQVDVK
LPEGPLPKGA GLKGHLPKVQ MPCLKMPKVA LKGPQVDVKG PKLDLKGPKA DVMTPVVEVS
LPSMEVDVEA PGAKLDSVRL EGDLSLADKD MTAKDSKFKM PKFKMPSFGV SAPGKSIEAS
LDVSALKVEA DVSLPSMQGD LKTTHLSIQP PSADLEVQAG QEDVKLPEGP VHEGAGLKGH
LPKLQMPSFK VPKVDLKGPQ IDVNVPKLDL KGPKVEVTSP NLDVSLPSME VDIQAPGAKL
DSTRLEGDLS LADKDVTAKD SKFKMPKFKM PSFGMLSPGK SIEVSVDVSA PKMEADMSIP
SMQGDLKTTD LRIQAPSADL EVQAGQVDLK LPEGHMPEVA GLKGHLPKVE MPSFKMPKVD
LKGPQVDVKG PKLDLKGPKA EVMAPDVEVS LPSVETDVQA PGSMLDGARL EGDLSLAHED
VAGKDSKFQG PKLSTSGFEW SSKKVSMSSS EIEGNVTFHE KTSTFPIVES VVHEGDLHDP
SRDGNLGLAV GEVGMDSKFK KLHFKVPKVS FSSTKTPKDS LVPGAKSSIG LSTIPLSSSE
CSSFELQQVS ACSEPSMQMP KVGFAGFPSS RLDLTGPHFE SSILSPCEDV TLTKYQVTVP
RAALAPELAL EIPSGSQADI PLPKTECSTD LQPPEGVPTS QAESHSGPLN SMIPVSLGQV
SFPKFYKPKF VFSVPQMAVP EGDLHAAVGA PVMSPLSPGE RVQCPLPSTQ LPSPGTCVSQ
GPEELVASLQ TSVVAPGEAP SEDADHEGKG SPLKMPKIKL PSFRWSPKKE TGPKVDPECS
VEDSKLSLVL DKDEVAPQSA IHMDLPPERD GEKGRSTKPG FAMPKLALPK MKASKSGVSL
PQRDVDPSLS SATAGGSFQD TEKASSDGGR GGLGATASAT GSEGVNLHRP QVHIPSLGFA
KPDLRSSKAK VEVSQPEADL PLPKHDLSTE GDSRGCGLGD VPVSQPCGEG IAPTPEDPLQ
PSCRKPDAEV LTVESPEEEA MTKYSQESWF KMPKFRMPSL RRSFRDRGGA GKLEVAQTQA
PAATGGEAAA KVKEFLVSGS NVEAAMSLQL PEADAEVTAS ESKSSTDILR CDLDSTGLKL
HLSTAGMTGD ELSTSEVRIH PSKGPLPFQM PGMRLPETQV LPGEIDETPL SKPGHDLASM
EDKTEKWSSQ PEGPLKLKAS STDMPSQISV VNVDQLWEDS VLTVKFPKLM VPRFSFPAPS
SEDDVFIPTV REVQCPEANI DTALCKESPG LWGASILKAG AGVPGEQPVD LNLPLEAPPI
SKVRVHIQGA QVESQEVTIH SIVTPEFVDL SVPRTFSTQI VRESEIPTSE IQTPSYGFSL
LKVKIPEPHT QARVYTTMTQ HSRTQEGTEE APIQATPGVD SISGDLQPDT GEPFEMISSS
VNVLGQQTLT FEVPSGHQLA DSCSDEEPAE ILEFPPDDSQ EATTPLADEG RAPKDKPESK
KSGLLWFWLP NIGFSSSVDE TGVDSKNDVQ RSAPIQTQPE ARPEAELPKK QEKAGWFRFP
KLGFSSSPTK KSKSTEDGAE LEEQKLQEET ITFFDARESF SPEEKEEGEL IGPVGTGLDS
RVMVTSAART ELILPEQDRK ADDESKGSGL GPNEG
