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 24-JAN-2024, entry version 201. 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). RN [17] RP INVOLVEMENT IN IBMWMA, AND VARIANT IBMWMA TYR-40. RX PubMed=34048612; DOI=10.1002/ana.26136; RA Leoni T.B., Gonzalez-Salazar C., Rezende T.J.R., Hernandez A.L.C., RA Mattos A.H.B., Coimbra Neto A.R., da Graca F.F., Goncalves J.P.N., RA Martinez A.R.M., Taniguti L., Kitajima J.P., Kok F., Rogerio F., RA da Silva A.M.S., de Oliveira A.L.R., Zanoteli E., Nucci A., RA Franca M.C. Jr.; RT "A Novel Multisystem Proteinopathy Caused by a Missense ANXA11 Variant."; RL Ann. Neurol. 90:239-252(2021). 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 -!- DISEASE: Inclusion body myopathy and brain white matter abnormalities CC (IBMWMA) [MIM:619733]: An autosomal dominant, adult-onset disorder CC characterized predominantly by proximal limb girdle muscle weakness CC affecting the lower and upper limbs and resulting in gait difficulties CC and scapular winging. Additional features may include dysarthria, CC dysphagia, low back pain, and hyporeflexia. Muscle biopsy shows fiber CC type variation, internal nuclei, rimmed vacuoles, and cytoplasmic CC protein aggregates or inclusions. Cognitive impairment or CC frontotemporal dementia occurs in some patients. CC {ECO:0000269|PubMed:34048612}. Note=The gene represented in this entry CC is involved in disease pathogenesis. CC -!- SIMILARITY: Belongs to the annexin family. {ECO:0000255|PROSITE- CC ProRule:PRU01245, ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- 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. DR AlphaFoldDB; P50995; -. DR SMR; P50995; -. DR BioGRID; 106808; 98. DR ELM; P50995; -. DR IntAct; P50995; 33. 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; 9606-ENSP00000398610; -. DR PeptideAtlas; P50995; -. DR PRIDE; P50995; -. DR ProteomicsDB; 5263; -. DR ProteomicsDB; 56275; -. [P50995-1] DR Antibodypedia; 3904; 346 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 AGR; HGNC:535; -. 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 MIM; 619733; 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; GQQPMTY; -. DR OrthoDB; 1500773at2759; -. DR PhylomeDB; P50995; -. DR TreeFam; TF105452; -. DR PathwayCommons; P50995; -. DR SignaLink; P50995; -. DR BioGRID-ORCS; 311; 10 hits in 1163 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 208 other cell types or tissues. DR ExpressionAtlas; P50995; baseline and differential. 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:HPA. 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; Annexin; 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; ANNEXIN; 1. DR PANTHER; PTHR10502:SF29; ANNEXIN A11; 1. DR Pfam; PF00191; Annexin; 4. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR01810; ANNEXINXI. DR SMART; SM00335; ANX; 4. DR SUPFAM; SSF47874; Annexin; 1. DR PROSITE; PS00223; ANNEXIN_1; 4. DR PROSITE; PS51897; ANNEXIN_2; 4. DR Genevisible; P50995; HS. 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; uncertain significance; changed FT cytoplasmic localization with decreased association with FT vesicle-like structures; increased interaction with S100A6; FT 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 40 FT /note="D -> Y (in IBMWMA)" FT /evidence="ECO:0000269|PubMed:34048612" FT /id="VAR_087101" FT VARIANT 175 FT /note="G -> R (in ALS23; uncertain significance; FT dbSNP:rs754594235)" FT /evidence="ECO:0000269|PubMed:28469040" FT /id="VAR_080655" FT VARIANT 189 FT /note="G -> E (in ALS23; uncertain significance; no effect FT 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; uncertain significance; increased FT aggregation in the cytoplasm sequestering the wild-type FT protein in these aggregates; loss of interaction with FT S100A6; dbSNP:rs765489119)" FT /evidence="ECO:0000269|PubMed:28469040" FT /id="VAR_080657" FT VARIANT 346 FT /note="R -> C (in ALS23; uncertain 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 //