ANXA4_HUMAN
ID ANXA4_HUMAN Reviewed; 319 AA.
AC P09525; B4DDF9; Q6LES2; Q96F33; Q9BWK1;
DT 01-JUL-1989, integrated into UniProtKB/Swiss-Prot.
DT 23-JAN-2007, sequence version 4.
DT 03-AUG-2022, entry version 217.
DE RecName: Full=Annexin A4 {ECO:0000305};
DE AltName: Full=35-beta calcimedin;
DE AltName: Full=Annexin IV;
DE AltName: Full=Annexin-4;
DE AltName: Full=Carbohydrate-binding protein p33/p41;
DE AltName: Full=Chromobindin-4;
DE AltName: Full=Endonexin I;
DE AltName: Full=Lipocortin IV;
DE AltName: Full=P32.5;
DE AltName: Full=PP4-X;
DE AltName: Full=Placental anticoagulant protein II;
DE Short=PAP-II;
DE AltName: Full=Protein II;
GN Name=ANXA4 {ECO:0000312|HGNC:HGNC:542}; Synonyms=ANX4;
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 [MRNA] (ISOFORM 3).
RX PubMed=2970257;
RA Grundmann U., Amann E., Abel K.-J., Kuepper H.A.;
RT "Isolation and expression of cDNA coding for a new member of the
RT phospholipase A2 inhibitor family.";
RL Behring Inst. Mitt. 82:59-67(1988).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=1346776; DOI=10.1016/0888-7543(92)90379-7;
RA Tait J.F., Smith C., Frankenberry D.A., Miao C.H., Adler D.A.,
RA Disteche C.M.;
RT "Chromosomal mapping of the human annexin IV (ANX4) gene.";
RL Genomics 12:313-318(1992).
RN [3]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 3).
RX PubMed=9084877; DOI=10.1248/bpb.20.224;
RA Satoh A., Takayama E., Kojima K., Ogawa H., Katsura Y., Kina T.,
RA Matsumoto I.;
RT "Characterization of human p33/41 (annexin IV), a Ca2+ dependent
RT carbohydrate-binding protein with monoclonal anti-annexin IV antibodies,
RT AS11 and AS17.";
RL Biol. Pharm. Bull. 20:224-229(1997).
RN [4]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Adrenal gland;
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 [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RX PubMed=15815621; DOI=10.1038/nature03466;
RA Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H., Minx P.,
RA Wagner-McPherson C., Layman D., Wylie K., Sekhon M., Becker M.C.,
RA Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E., Kremitzki C., Oddy L.,
RA Du H., Sun H., Bradshaw-Cordum H., Ali J., Carter J., Cordes M., Harris A.,
RA Isak A., van Brunt A., Nguyen C., Du F., Courtney L., Kalicki J.,
RA Ozersky P., Abbott S., Armstrong J., Belter E.A., Caruso L., Cedroni M.,
RA Cotton M., Davidson T., Desai A., Elliott G., Erb T., Fronick C., Gaige T.,
RA Haakenson W., Haglund K., Holmes A., Harkins R., Kim K., Kruchowski S.S.,
RA Strong C.M., Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
RA McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
RA Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N., Swearengen-Shahid S.,
RA Snider J., Strong J.T., Thompson J., Yoakum M., Leonard S., Pearman C.,
RA Trani L., Radionenko M., Waligorski J.E., Wang C., Rock S.M.,
RA Tin-Wollam A.-M., Maupin R., Latreille P., Wendl M.C., Yang S.-P., Pohl C.,
RA Wallis J.W., Spieth J., Bieri T.A., Berkowicz N., Nelson J.O., Osborne J.,
RA Ding L., Meyer R., Sabo A., Shotland Y., Sinha P., Wohldmann P.E.,
RA Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Jones T.A., She X.,
RA Ciccarelli F.D., Izaurralde E., Taylor J., Schmutz J., Myers R.M.,
RA Cox D.R., Huang X., McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
RA Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
RA Miller W., Eichler E.E., Bork P., Suyama M., Torrents D., Waterston R.H.,
RA Wilson R.K.;
RT "Generation and annotation of the DNA sequences of human chromosomes 2 and
RT 4.";
RL Nature 434:724-731(2005).
RN [6]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RA Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M.,
RA Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J.,
RA Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S.,
RA Turner R., Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H.,
RA Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K.,
RA Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D.,
RA Hunkapiller M.W., Myers E.W., Venter J.C.;
RL Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).
RC TISSUE=Eye, and Uterus;
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 [8]
RP PROTEIN SEQUENCE OF 2-15; 28-72; 100-144 AND 281-319.
RX PubMed=2975506; DOI=10.1021/bi00417a011;
RA Tait J.F., Sakata M., McMullen B.A., Miao C.H., Funakoshi T.,
RA Hendrickson L.E., Fujikawa K.;
RT "Placental anticoagulant proteins: isolation and comparative
RT characterization four members of the lipocortin family.";
RL Biochemistry 27:6268-6276(1988).
RN [9]
RP PROTEIN SEQUENCE OF 27-56; 99-124 AND 280-308.
RC TISSUE=Placenta;
RX PubMed=2974032; DOI=10.1016/s0021-9258(18)37335-6;
RA Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W.,
RA de Haen C.;
RT "Sedimentation equilibrium analysis of five lipocortin-related
RT phospholipase A2 inhibitors from human placenta. Evidence against a
RT mechanistically relevant association between enzyme and inhibitor.";
RL J. Biol. Chem. 263:18657-18663(1988).
RN [10]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-213; LYS-293 AND LYS-300, 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 [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 ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
RP METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS SPECTROMETRY
RP [LARGE SCALE ANALYSIS].
RX PubMed=22814378; DOI=10.1073/pnas.1210303109;
RA Van Damme P., Lasa M., Polevoda B., Gazquez C., Elosegui-Artola A.,
RA Kim D.S., De Juan-Pardo E., Demeyer K., Hole K., Larrea E., Timmerman E.,
RA Prieto J., Arnesen T., Sherman F., Gevaert K., Aldabe R.;
RT "N-terminal acetylome analyses and functional insights of the N-terminal
RT acetyltransferase NatB.";
RL Proc. Natl. Acad. Sci. U.S.A. 109:12449-12454(2012).
RN [13]
RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12, AND IDENTIFICATION BY
RP MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RC TISSUE=Liver;
RX PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
RA Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D., Wang L.,
RA Ye M., Zou H.;
RT "An enzyme assisted RP-RPLC approach for in-depth analysis of human liver
RT phosphoproteome.";
RL J. Proteomics 96:253-262(2014).
RN [14]
RP X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
RX PubMed=2254922; DOI=10.1016/s0022-2836(05)80310-9;
RA Freemont P.S., Driessen H.P.C., Verbi W., Crumpton M.J.;
RT "Crystallization and preliminary X-ray crystallographic studies of human
RT placental annexin IV.";
RL J. Mol. Biol. 216:219-221(1990).
CC -!- FUNCTION: Calcium/phospholipid-binding protein which promotes membrane
CC fusion and is involved in exocytosis. {ECO:0000250}.
CC -!- INTERACTION:
CC P09525; Q9BSI4: TINF2; NbExp=2; IntAct=EBI-2556852, EBI-717399;
CC -!- SUBCELLULAR LOCATION: Zymogen granule membrane
CC {ECO:0000250|UniProtKB:P50994}; Peripheral membrane protein
CC {ECO:0000250|UniProtKB:P50994}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing, Alternative initiation; Named isoforms=3;
CC Name=1;
CC IsoId=P09525-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P09525-2; Sequence=VSP_056396;
CC Name=3;
CC IsoId=P09525-3; Sequence=VSP_061413;
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- MISCELLANEOUS: Seems to bind one calcium ion with high affinity.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; M19383; AAC41689.1; -; mRNA.
DR EMBL; M82809; AAA51740.1; -; mRNA.
DR EMBL; D78152; BAA11227.1; -; mRNA.
DR EMBL; AK293177; BAG56720.1; -; mRNA.
DR EMBL; AY453398; AAS47515.1; -; mRNA.
DR EMBL; AK315511; BAG37892.1; -; mRNA.
DR EMBL; CR407681; CAG28609.1; -; mRNA.
DR EMBL; AC019206; AAY14864.1; -; Genomic_DNA.
DR EMBL; AC092431; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AC112787; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; CH471053; EAW99844.1; -; Genomic_DNA.
DR EMBL; BC000182; AAH00182.1; -; mRNA.
DR EMBL; BC011659; AAH11659.1; -; mRNA.
DR CCDS; CCDS1894.1; -. [P09525-3]
DR PIR; A42077; A42077.
DR RefSeq; NP_001144.1; NM_001153.4.
DR RefSeq; NP_001307627.1; NM_001320698.1.
DR RefSeq; NP_001307629.1; NM_001320700.1.
DR RefSeq; NP_001307631.1; NM_001320702.1. [P09525-2]
DR RefSeq; XP_016859432.1; XM_017003943.1.
DR RefSeq; XP_016859433.1; XM_017003944.1. [P09525-2]
DR PDB; 2ZOC; X-ray; 2.00 A; A/B=1-319.
DR PDBsum; 2ZOC; -.
DR AlphaFoldDB; P09525; -.
DR SMR; P09525; -.
DR BioGRID; 106804; 32.
DR IntAct; P09525; 15.
DR MINT; P09525; -.
DR STRING; 9606.ENSP00000377833; -.
DR DrugBank; DB09130; Copper.
DR DrugBank; DB00591; Fluocinolone acetonide.
DR GlyGen; P09525; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P09525; -.
DR MetOSite; P09525; -.
DR PhosphoSitePlus; P09525; -.
DR SwissPalm; P09525; -.
DR BioMuta; ANXA4; -.
DR DMDM; 1703319; -.
DR DOSAC-COBS-2DPAGE; P09525; -.
DR OGP; P09525; -.
DR REPRODUCTION-2DPAGE; IPI00793199; -.
DR REPRODUCTION-2DPAGE; P09525; -.
DR SWISS-2DPAGE; P09525; -.
DR CPTAC; CPTAC-1381; -.
DR CPTAC; CPTAC-1382; -.
DR CPTAC; CPTAC-1383; -.
DR CPTAC; CPTAC-1384; -.
DR CPTAC; CPTAC-19; -.
DR CPTAC; CPTAC-20; -.
DR EPD; P09525; -.
DR jPOST; P09525; -.
DR MassIVE; P09525; -.
DR MaxQB; P09525; -.
DR PaxDb; P09525; -.
DR PeptideAtlas; P09525; -.
DR PRIDE; P09525; -.
DR ProteomicsDB; 3854; -.
DR ProteomicsDB; 52242; -. [P09525-1]
DR ABCD; P09525; 1 sequenced antibody.
DR Antibodypedia; 1552; 502 antibodies from 42 providers.
DR CPTC; P09525; 1 antibody.
DR DNASU; 307; -.
DR Ensembl; ENST00000394295.6; ENSP00000377833.4; ENSG00000196975.16. [P09525-3]
DR GeneID; 307; -.
DR KEGG; hsa:307; -.
DR MANE-Select; ENST00000394295.6; ENSP00000377833.4; NM_001153.5; NP_001144.1. [P09525-3]
DR UCSC; uc002sfr.5; human.
DR CTD; 307; -.
DR DisGeNET; 307; -.
DR GeneCards; ANXA4; -.
DR HGNC; HGNC:542; ANXA4.
DR HPA; ENSG00000196975; Tissue enhanced (gallbladder, pancreas).
DR MIM; 106491; gene.
DR neXtProt; NX_P09525; -.
DR OpenTargets; ENSG00000196975; -.
DR PharmGKB; PA24832; -.
DR VEuPathDB; HostDB:ENSG00000196975; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000156575; -.
DR InParanoid; P09525; -.
DR OMA; RHFMIVL; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P09525; -.
DR TreeFam; TF105452; -.
DR PathwayCommons; P09525; -.
DR SignaLink; P09525; -.
DR BioGRID-ORCS; 307; 4 hits in 1078 CRISPR screens.
DR ChiTaRS; ANXA4; human.
DR EvolutionaryTrace; P09525; -.
DR GeneWiki; ANXA4; -.
DR GenomeRNAi; 307; -.
DR Pharos; P09525; Tbio.
DR PRO; PR:P09525; -.
DR Proteomes; UP000005640; Chromosome 2.
DR RNAct; P09525; protein.
DR Bgee; ENSG00000196975; Expressed in pancreatic ductal cell and 205 other tissues.
DR ExpressionAtlas; P09525; baseline and differential.
DR Genevisible; P09525; HS.
DR GO; GO:0009986; C:cell surface; IDA:BHF-UCL.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:BHF-UCL.
DR GO; GO:0031410; C:cytoplasmic vesicle; IEA:UniProtKB-KW.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0031965; C:nuclear membrane; IDA:BHF-UCL.
DR GO; GO:0005634; C:nucleus; IDA:BHF-UCL.
DR GO; GO:0048471; C:perinuclear region of cytoplasm; IDA:BHF-UCL.
DR GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
DR GO; GO:0012506; C:vesicle membrane; IDA:BHF-UCL.
DR GO; GO:0005509; F:calcium ion binding; IDA:BHF-UCL.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:GO_Central.
DR GO; GO:0042802; F:identical protein binding; IPI:BHF-UCL.
DR GO; GO:0051059; F:NF-kappaB binding; IPI:BHF-UCL.
DR GO; GO:0004859; F:phospholipase inhibitor activity; NAS:UniProtKB.
DR GO; GO:0030855; P:epithelial cell differentiation; IEP:UniProtKB.
DR GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
DR GO; GO:0032717; P:negative regulation of interleukin-8 production; IMP:BHF-UCL.
DR GO; GO:0032088; P:negative regulation of NF-kappaB transcription factor activity; IDA:BHF-UCL.
DR GO; GO:0007219; P:Notch signaling pathway; IEA:Ensembl.
DR GO; GO:0006357; P:regulation of transcription by RNA polymerase II; IDA:BHF-UCL.
DR GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
DR Gene3D; 1.10.220.10; -; 4.
DR InterPro; IPR001464; Annexin.
DR InterPro; IPR018502; Annexin_repeat.
DR InterPro; IPR018252; Annexin_repeat_CS.
DR InterPro; IPR037104; Annexin_sf.
DR InterPro; IPR002391; ANX4.
DR PANTHER; PTHR10502:SF28; PTHR10502:SF28; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR SMART; SM00335; ANX; 4.
DR SUPFAM; SSF47874; SSF47874; 1.
DR PROSITE; PS00223; ANNEXIN_1; 4.
DR PROSITE; PS51897; ANNEXIN_2; 4.
PE 1: Evidence at protein level;
KW 3D-structure; Acetylation; Alternative initiation; Alternative splicing;
KW Annexin; Calcium; Calcium/phospholipid-binding; Cytoplasmic vesicle;
KW Direct protein sequencing; Membrane; Phosphoprotein; Reference proteome;
KW Repeat.
FT INIT_MET 1
FT /note="Removed"
FT /evidence="ECO:0000269|PubMed:2975506,
FT ECO:0007744|PubMed:22814378"
FT CHAIN 2..319
FT /note="Annexin A4"
FT /id="PRO_0000067482"
FT REPEAT 14..85
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 86..157
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 169..241
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 245..316
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT MOD_RES 2
FT /note="N-acetylalanine"
FT /evidence="ECO:0007744|PubMed:22814378"
FT MOD_RES 7
FT /note="Phosphothreonine"
FT /evidence="ECO:0000250|UniProtKB:P08132"
FT MOD_RES 12
FT /note="Phosphoserine"
FT /evidence="ECO:0007744|PubMed:24275569"
FT MOD_RES 213
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 293
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 300
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..82
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_056396"
FT VAR_SEQ 1
FT /note="M -> MAM (in isoform 3)"
FT /id="VSP_061413"
FT VARIANT 85
FT /note="T -> M (in dbSNP:rs2228203)"
FT /id="VAR_055500"
FT CONFLICT 96
FT /note="R -> Q (in Ref. 1; AAC41689)"
FT /evidence="ECO:0000305"
FT HELIX 16..26
FT /evidence="ECO:0007829|PDB:2ZOC"
FT STRAND 28..31
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 34..41
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 46..59
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 64..71
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 74..84
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 87..99
FT /evidence="ECO:0007829|PDB:2ZOC"
FT STRAND 100..103
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 106..115
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 118..132
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 136..143
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 146..155
FT /evidence="ECO:0007829|PDB:2ZOC"
FT TURN 156..158
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 168..181
FT /evidence="ECO:0007829|PDB:2ZOC"
FT TURN 182..184
FT /evidence="ECO:0007829|PDB:2ZOC"
FT STRAND 185..187
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 190..199
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 202..216
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 220..227
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 230..244
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 246..258
FT /evidence="ECO:0007829|PDB:2ZOC"
FT STRAND 259..262
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 265..275
FT /evidence="ECO:0007829|PDB:2ZOC"
FT TURN 276..279
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 280..291
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 295..302
FT /evidence="ECO:0007829|PDB:2ZOC"
FT HELIX 305..315
FT /evidence="ECO:0007829|PDB:2ZOC"
SQ SEQUENCE 319 AA; 35883 MW; 3799FE80A93AB215 CRC64;
MATKGGTVKA ASGFNAMEDA QTLRKAMKGL GTDEDAIISV LAYRNTAQRQ EIRTAYKSTI
GRDLIDDLKS ELSGNFEQVI VGMMTPTVLY DVQELRRAMK GAGTDEGCLI EILASRTPEE
IRRISQTYQQ QYGRSLEDDI RSDTSFMFQR VLVSLSAGGR DEGNYLDDAL VRQDAQDLYE
AGEKKWGTDE VKFLTVLCSR NRNHLLHVFD EYKRISQKDI EQSIKSETSG SFEDALLAIV
KCMRNKSAYF AEKLYKSMKG LGTDDNTLIR VMVSRAEIDM LDIRAHFKRL YGKSLYSFIK
GDTSGDYRKV LLVLCGGDD
