ANX11_HUMAN
ID ANX11_HUMAN Reviewed; 505 AA.
AC P50995; B4DVE7;
DT 01-OCT-1996, integrated into UniProtKB/Swiss-Prot.
DT 01-OCT-1996, sequence version 1.
DT 03-AUG-2022, entry version 193.
DE RecName: Full=Annexin A11;
DE AltName: Full=56 kDa autoantigen;
DE AltName: Full=Annexin XI;
DE AltName: Full=Annexin-11;
DE AltName: Full=Calcyclin-associated annexin 50;
DE Short=CAP-50;
GN Name=ANXA11; Synonyms=ANX11;
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 1).
RC TISSUE=Teratocarcinoma;
RX PubMed=7508441; DOI=10.1016/s0021-9258(17)41769-8;
RA Misaki Y., Pruijn G.J.M., van der Kemp A.W., van Venrooij W.J.;
RT "The 56K autoantigen is identical to human annexin XI.";
RL J. Biol. Chem. 269:4240-4246(1994).
RN [2]
RP NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
RX PubMed=11013079; DOI=10.1006/geno.2000.6309;
RA Bances P., Fernandez M.R., Rodriguez-Garcia M.I., Morgan R.O.,
RA Fernandez M.-P.;
RT "Annexin A11 (ANXA11) gene structure as the progenitor of paralogous
RT annexins and source of orthologous cDNA isoforms.";
RL Genomics 69:95-103(2000).
RN [3]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
RC TISSUE=Spleen;
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 GENOMIC DNA].
RX PubMed=15164054; DOI=10.1038/nature02462;
RA Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L.,
RA Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K.,
RA Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L.,
RA Taylor A., Battles J., Bird C.P., Ainscough R., Almeida J.P.,
RA Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J.,
RA Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y.,
RA Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P.,
RA Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N.,
RA Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A.,
RA Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C.,
RA Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D.,
RA Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C.,
RA Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K.,
RA Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A.,
RA Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S.,
RA McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S.,
RA Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V.,
RA Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A.,
RA Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M.,
RA Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A.,
RA Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P.,
RA Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y.,
RA Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D.,
RA Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.;
RT "The DNA sequence and comparative analysis of human chromosome 10.";
RL Nature 429:375-381(2004).
RN [5]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
RC TISSUE=Lymph;
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 [6]
RP INTERACTION WITH PDCD6.
RX PubMed=11883939; DOI=10.1006/bbrc.2002.6600;
RA Satoh H., Shibata H., Nakano Y., Kitaura Y., Maki M.;
RT "ALG-2 interacts with the amino-terminal domain of annexin XI in a Ca(2+)-
RT dependent manner.";
RL Biochem. Biophys. Res. Commun. 291:1166-1172(2002).
RN [7]
RP SUBCELLULAR LOCATION.
RX PubMed=12601007; DOI=10.1074/jbc.m212669200;
RA Tomas A., Moss S.E.;
RT "Calcium- and cell cycle-dependent association of annexin 11 with the
RT nuclear envelope.";
RL J. Biol. Chem. 278:20210-20216(2003).
RN [8]
RP SUBCELLULAR LOCATION.
RX PubMed=12805373; DOI=10.1074/jbc.m210852200;
RA Farnaes L., Ditzel H.J.;
RT "Dissecting the cellular functions of annexin XI using recombinant human
RT annexin XI-specific autoantibodies cloned by phage display.";
RL J. Biol. Chem. 278:33120-33126(2003).
RN [9]
RP FUNCTION, SUBCELLULAR LOCATION, AND INTERACTION WITH KIF23.
RX PubMed=15197175; DOI=10.1083/jcb.200311054;
RA Tomas A., Futter C., Moss S.E.;
RT "Annexin 11 is required for midbody formation and completion of the
RT terminal phase of cytokinesis.";
RL J. Cell Biol. 165:813-822(2004).
RN [10]
RP SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
RC TISSUE=Melanoma;
RX PubMed=17081065; DOI=10.1021/pr060363j;
RA Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H., Mangini N.J.,
RA Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R., Yamagishi S.,
RA Shabanowitz J., Hearing V.J., Wu C., Appella E., Hunt D.F.;
RT "Proteomic and bioinformatic characterization of the biogenesis and
RT function of melanosomes.";
RL J. Proteome Res. 5:3135-3144(2006).
RN [11]
RP INTERACTION WITH PDCD6.
RX PubMed=18256029; DOI=10.1074/jbc.m800717200;
RA Shibata H., Suzuki H., Kakiuchi T., Inuzuka T., Yoshida H., Mizuno T.,
RA Maki M.;
RT "Identification of Alix-type and non-Alix-type ALG-2-binding sites in human
RT phospholipid scramblase 3: differential binding to an alternatively spliced
RT isoform and amino acid-substituted mutants.";
RL J. Biol. Chem. 283:9623-9632(2008).
RN [12]
RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-248; LYS-255 AND LYS-479, 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 [13]
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 [14]
RP IDENTIFICATION BY 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 [15]
RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
RX PubMed=25944712; DOI=10.1002/pmic.201400617;
RA Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M., Ayoub D.,
RA Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
RT "N-terminome analysis of the human mitochondrial proteome.";
RL Proteomics 15:2519-2524(2015).
RN [16]
RP INVOLVEMENT IN ALS23, VARIANTS ALS23 ARG-38; GLY-40; ARG-175; GLU-189;
RP GLN-235 AND CYS-346, CHARACTERIZATION OF VARIANTS ALS23 ARG-38; GLY-40;
RP GLU-189 AND GLN-235, INTERACTION WITH S100A6, AND SUBCELLULAR LOCATION.
RX PubMed=28469040; DOI=10.1126/scitranslmed.aad9157;
RA Smith B.N., Topp S.D., Fallini C., Shibata H., Chen H.J., Troakes C.,
RA King A., Ticozzi N., Kenna K.P., Soragia-Gkazi A., Miller J.W., Sato A.,
RA Dias D.M., Jeon M., Vance C., Wong C.H., de Majo M., Kattuah W.,
RA Mitchell J.C., Scotter E.L., Parkin N.W., Sapp P.C., Nolan M., Nestor P.J.,
RA Simpson M., Weale M., Lek M., Baas F., Vianney de Jong J.M.,
RA Ten Asbroek A.L.M.A., Redondo A.G., Esteban-Perez J., Tiloca C., Verde F.,
RA Duga S., Leigh N., Pall H., Morrison K.E., Al-Chalabi A., Shaw P.J.,
RA Kirby J., Turner M.R., Talbot K., Hardiman O., Glass J.D.,
RA De Belleroche J., Maki M., Moss S.E., Miller C., Gellera C., Ratti A.,
RA Al-Sarraj S., Brown R.H. Jr., Silani V., Landers J.E., Shaw C.E.;
RT "Mutations in the vesicular trafficking protein annexin A11 are associated
RT with amyotrophic lateral sclerosis.";
RL Sci. Transl. Med. 9:0-0(2017).
CC -!- FUNCTION: Binds specifically to calcyclin in a calcium-dependent manner
CC (By similarity). Required for midbody formation and completion of the
CC terminal phase of cytokinesis. {ECO:0000250,
CC ECO:0000269|PubMed:15197175}.
CC -!- SUBUNIT: Interacts with S100A6 (PubMed:28469040). Interacts with PDCD6
CC in a calcium-dependent manner. Interacts with KIF23 during cytokinesis.
CC {ECO:0000250, ECO:0000269|PubMed:11883939, ECO:0000269|PubMed:15197175,
CC ECO:0000269|PubMed:18256029, ECO:0000269|PubMed:28469040}.
CC -!- INTERACTION:
CC P50995; P15289: ARSA; NbExp=3; IntAct=EBI-715243, EBI-2117357;
CC P50995; Q53EZ4: CEP55; NbExp=8; IntAct=EBI-715243, EBI-747776;
CC P50995; Q96AE4-2: FUBP1; NbExp=3; IntAct=EBI-715243, EBI-12121668;
CC P50995; Q52LG2: KRTAP13-2; NbExp=3; IntAct=EBI-715243, EBI-11953846;
CC P50995; Q3LI66: KRTAP6-2; NbExp=3; IntAct=EBI-715243, EBI-11962084;
CC P50995; Q8NI38: NFKBID; NbExp=3; IntAct=EBI-715243, EBI-10271199;
CC P50995; O75340: PDCD6; NbExp=5; IntAct=EBI-715243, EBI-352915;
CC P50995; Q92734: TFG; NbExp=4; IntAct=EBI-715243, EBI-357061;
CC P50995; Q9NZC7-5: WWOX; NbExp=3; IntAct=EBI-715243, EBI-12040603;
CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:28469040}.
CC Melanosome. Nucleus envelope. Nucleus, nucleoplasm
CC {ECO:0000269|PubMed:28469040}. Cytoplasm, cytoskeleton, spindle.
CC Note=Found throughout the nucleoplasm at interphase and during mitosis
CC concentrates around the mitotic apparatus (By similarity). Elevation of
CC intracellular calcium causes relocalization from the nucleoplasm to the
CC nuclear envelope, with little effect on the cytoplasmic pool.
CC Localization to the nuclear envelope is cell-cycle dependent.
CC {ECO:0000250}.
CC -!- ALTERNATIVE PRODUCTS:
CC Event=Alternative splicing; Named isoforms=2;
CC Name=1;
CC IsoId=P50995-1; Sequence=Displayed;
CC Name=2;
CC IsoId=P50995-2; Sequence=VSP_054553;
CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium
CC and phospholipid.
CC -!- DISEASE: Amyotrophic lateral sclerosis 23 (ALS23) [MIM:617839]: A form
CC of amyotrophic lateral sclerosis, a neurodegenerative disorder
CC affecting upper motor neurons in the brain and lower motor neurons in
CC the brain stem and spinal cord, resulting in fatal paralysis. Sensory
CC abnormalities are absent. The pathologic hallmarks of the disease
CC include pallor of the corticospinal tract due to loss of motor neurons,
CC presence of ubiquitin-positive inclusions within surviving motor
CC neurons, and deposition of pathologic aggregates. The etiology of
CC amyotrophic lateral sclerosis is likely to be multifactorial, involving
CC both genetic and environmental factors. The disease is inherited in 5-
CC 10% of the cases. ALS23 is an autosomal dominant form with incomplete
CC penetrance. {ECO:0000269|PubMed:28469040}. Note=The disease is caused
CC by variants affecting the gene represented in this entry.
CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE-
CC ProRule:PRU01245, ECO:0000305}.
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DR EMBL; L19605; AAA19734.1; -; mRNA.
DR EMBL; AJ278463; CAB94995.1; -; mRNA.
DR EMBL; AJ278464; CAB94996.1; -; mRNA.
DR EMBL; AJ278465; CAB94997.1; -; mRNA.
DR EMBL; AK301047; BAG62659.1; -; mRNA.
DR EMBL; AL356095; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; AL513174; -; NOT_ANNOTATED_CDS; Genomic_DNA.
DR EMBL; BC007564; AAH07564.1; -; mRNA.
DR CCDS; CCDS60576.1; -. [P50995-2]
DR CCDS; CCDS7364.1; -. [P50995-1]
DR PIR; A53152; A53152.
DR RefSeq; NP_001148.1; NM_001157.2. [P50995-1]
DR RefSeq; NP_001265336.1; NM_001278407.1. [P50995-1]
DR RefSeq; NP_001265337.1; NM_001278408.1. [P50995-1]
DR RefSeq; NP_001265338.1; NM_001278409.1. [P50995-2]
DR RefSeq; NP_665875.1; NM_145868.1. [P50995-1]
DR RefSeq; NP_665876.1; NM_145869.1. [P50995-1]
DR RefSeq; XP_011538038.1; XM_011539736.2. [P50995-1]
DR AlphaFoldDB; P50995; -.
DR SMR; P50995; -.
DR BioGRID; 106808; 74.
DR ELM; P50995; -.
DR IntAct; P50995; 30.
DR MINT; P50995; -.
DR STRING; 9606.ENSP00000398610; -.
DR TCDB; 3.A.5.9.1; the general secretory pathway (sec) family.
DR GlyGen; P50995; 1 site, 1 O-linked glycan (1 site).
DR iPTMnet; P50995; -.
DR MetOSite; P50995; -.
DR PhosphoSitePlus; P50995; -.
DR SwissPalm; P50995; -.
DR BioMuta; ANXA11; -.
DR DMDM; 1703322; -.
DR REPRODUCTION-2DPAGE; P50995; -.
DR CPTAC; CPTAC-1217; -.
DR CPTAC; CPTAC-1218; -.
DR EPD; P50995; -.
DR jPOST; P50995; -.
DR MassIVE; P50995; -.
DR MaxQB; P50995; -.
DR PaxDb; P50995; -.
DR PeptideAtlas; P50995; -.
DR PRIDE; P50995; -.
DR ProteomicsDB; 5263; -.
DR ProteomicsDB; 56275; -. [P50995-1]
DR Antibodypedia; 3904; 320 antibodies from 40 providers.
DR DNASU; 311; -.
DR Ensembl; ENST00000265447.8; ENSP00000265447.5; ENSG00000122359.18. [P50995-2]
DR Ensembl; ENST00000372231.7; ENSP00000361305.3; ENSG00000122359.18. [P50995-1]
DR Ensembl; ENST00000422982.8; ENSP00000404412.2; ENSG00000122359.18. [P50995-1]
DR Ensembl; ENST00000438331.5; ENSP00000398610.1; ENSG00000122359.18. [P50995-1]
DR GeneID; 311; -.
DR KEGG; hsa:311; -.
DR MANE-Select; ENST00000422982.8; ENSP00000404412.2; NM_145868.2; NP_665875.1.
DR UCSC; uc057umu.1; human. [P50995-1]
DR CTD; 311; -.
DR DisGeNET; 311; -.
DR GeneCards; ANXA11; -.
DR HGNC; HGNC:535; ANXA11.
DR HPA; ENSG00000122359; Low tissue specificity.
DR MalaCards; ANXA11; -.
DR MIM; 602572; gene.
DR MIM; 617839; phenotype.
DR neXtProt; NX_P50995; -.
DR OpenTargets; ENSG00000122359; -.
DR Orphanet; 803; Amyotrophic lateral sclerosis.
DR PharmGKB; PA24825; -.
DR VEuPathDB; HostDB:ENSG00000122359; -.
DR eggNOG; KOG0819; Eukaryota.
DR GeneTree; ENSGT00940000156914; -.
DR HOGENOM; CLU_025300_6_0_1; -.
DR InParanoid; P50995; -.
DR OMA; MTYPGQQ; -.
DR OrthoDB; 856254at2759; -.
DR PhylomeDB; P50995; -.
DR TreeFam; TF105452; -.
DR PathwayCommons; P50995; -.
DR SignaLink; P50995; -.
DR BioGRID-ORCS; 311; 9 hits in 1085 CRISPR screens.
DR ChiTaRS; ANXA11; human.
DR GeneWiki; ANXA11; -.
DR GenomeRNAi; 311; -.
DR Pharos; P50995; Tbio.
DR PRO; PR:P50995; -.
DR Proteomes; UP000005640; Chromosome 10.
DR RNAct; P50995; protein.
DR Bgee; ENSG00000122359; Expressed in lower esophagus mucosa and 206 other tissues.
DR ExpressionAtlas; P50995; baseline and differential.
DR Genevisible; P50995; HS.
DR GO; GO:0042582; C:azurophil granule; IDA:UniProtKB.
DR GO; GO:0062023; C:collagen-containing extracellular matrix; HDA:BHF-UCL.
DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB.
DR GO; GO:0005829; C:cytosol; IDA:HPA.
DR GO; GO:0070062; C:extracellular exosome; HDA:UniProtKB.
DR GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
DR GO; GO:0016020; C:membrane; HDA:UniProtKB.
DR GO; GO:0030496; C:midbody; IDA:UniProtKB.
DR GO; GO:0005635; C:nuclear envelope; IDA:UniProtKB.
DR GO; GO:0005654; C:nucleoplasm; IDA:UniProtKB.
DR GO; GO:0045335; C:phagocytic vesicle; IDA:UniProtKB.
DR GO; GO:0042581; C:specific granule; IDA:UniProtKB.
DR GO; GO:0005819; C:spindle; IDA:UniProtKB.
DR GO; GO:0005509; F:calcium ion binding; IBA:GO_Central.
DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
DR GO; GO:0048306; F:calcium-dependent protein binding; IPI:UniProtKB.
DR GO; GO:0023026; F:MHC class II protein complex binding; HDA:UniProtKB.
DR GO; GO:0008429; F:phosphatidylethanolamine binding; IEA:Ensembl.
DR GO; GO:0003723; F:RNA binding; HDA:UniProtKB.
DR GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
DR GO; GO:0032506; P:cytokinetic process; IMP:UniProtKB.
DR GO; GO:0006909; P:phagocytosis; IEP:UniProtKB.
DR GO; GO:0051592; P:response to calcium ion; IDA: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; IPR008157; ANX11.
DR PANTHER; PTHR10502:SF29; PTHR10502:SF29; 1.
DR Pfam; PF00191; Annexin; 4.
DR PRINTS; PR00196; ANNEXIN.
DR PRINTS; PR01810; ANNEXINXI.
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 Acetylation; Alternative splicing; Amyotrophic lateral sclerosis; Annexin;
KW Calcium; Calcium/phospholipid-binding; Cell cycle; Cell division;
KW Cytoplasm; Cytoskeleton; Disease variant; Neurodegeneration; Nucleus;
KW Reference proteome; Repeat.
FT CHAIN 1..505
FT /note="Annexin A11"
FT /id="PRO_0000067510"
FT REPEAT 200..271
FT /note="Annexin 1"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 272..343
FT /note="Annexin 2"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 355..427
FT /note="Annexin 3"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REPEAT 431..502
FT /note="Annexin 4"
FT /evidence="ECO:0000255|PROSITE-ProRule:PRU01245"
FT REGION 1..38
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT REGION 84..199
FT /note="Disordered"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 1..17
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT COMPBIAS 84..168
FT /note="Pro residues"
FT /evidence="ECO:0000256|SAM:MobiDB-lite"
FT MOD_RES 248
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 255
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT MOD_RES 479
FT /note="N6-acetyllysine"
FT /evidence="ECO:0007744|PubMed:19608861"
FT VAR_SEQ 1..33
FT /note="Missing (in isoform 2)"
FT /evidence="ECO:0000303|PubMed:14702039"
FT /id="VSP_054553"
FT VARIANT 38
FT /note="G -> R (in ALS23; unknown pathological significance;
FT changed cytoplasmic localization with decreased association
FT with vesicle-like structures; increased interaction with
FT S100A6; dbSNP:rs142083484)"
FT /evidence="ECO:0000269|PubMed:28469040"
FT /id="VAR_080653"
FT VARIANT 40
FT /note="D -> G (in ALS23; forms cytoplasmic aggregates in
FT patient tissues; no effect on nuclear and cytoplasmic
FT localization; loss of interaction with S100A6;
FT dbSNP:rs1247392012)"
FT /evidence="ECO:0000269|PubMed:28469040"
FT /id="VAR_080654"
FT VARIANT 175
FT /note="G -> R (in ALS23; unknown pathological significance;
FT dbSNP:rs754594235)"
FT /evidence="ECO:0000269|PubMed:28469040"
FT /id="VAR_080655"
FT VARIANT 189
FT /note="G -> E (in ALS23; unknown pathological significance;
FT no effect on aggregation; loss of interaction with S100A6;
FT dbSNP:rs569546089)"
FT /evidence="ECO:0000269|PubMed:28469040"
FT /id="VAR_080656"
FT VARIANT 191
FT /note="R -> Q (in dbSNP:rs2229554)"
FT /id="VAR_048259"
FT VARIANT 230
FT /note="R -> C (in dbSNP:rs1049550)"
FT /id="VAR_012006"
FT VARIANT 235
FT /note="R -> Q (in ALS23; unknown pathological significance;
FT increased aggregation in the cytoplasm sequestering the
FT wild-type protein in these aggregates; loss of interaction
FT with S100A6; dbSNP:rs765489119)"
FT /evidence="ECO:0000269|PubMed:28469040"
FT /id="VAR_080657"
FT VARIANT 346
FT /note="R -> C (in ALS23; unknown pathological significance;
FT dbSNP:rs770574196)"
FT /evidence="ECO:0000269|PubMed:28469040"
FT /id="VAR_080658"
FT VARIANT 457
FT /note="I -> V (in dbSNP:rs1802932)"
FT /id="VAR_012007"
SQ SEQUENCE 505 AA; 54390 MW; 4ADCAC8F270BFEE4 CRC64;
MSYPGYPPPP GGYPPAAPGG GPWGGAAYPP PPSMPPIGLD NVATYAGQFN QDYLSGMAAN
MSGTFGGANM PNLYPGAPGA GYPPVPPGGF GQPPSAQQPV PPYGMYPPPG GNPPSRMPSY
PPYPGAPVPG QPMPPPGQQP PGAYPGQPPV TYPGQPPVPL PGQQQPVPSY PGYPGSGTVT
PAVPPTQFGS RGTITDAPGF DPLRDAEVLR KAMKGFGTDE QAIIDCLGSR SNKQRQQILL
SFKTAYGKDL IKDLKSELSG NFEKTILALM KTPVLFDIYE IKEAIKGVGT DEACLIEILA
SRSNEHIREL NRAYKAEFKK TLEEAIRSDT SGHFQRLLIS LSQGNRDEST NVDMSLAQRD
AQELYAAGEN RLGTDESKFN AVLCSRSRAH LVAVFNEYQR MTGRDIEKSI CREMSGDLEE
GMLAVVKCLK NTPAFFAERL NKAMRGAGTK DRTLIRIMVS RSETDLLDIR SEYKRMYGKS
LYHDISGDTS GDYRKILLKI CGGND
