ID H0YN42_HUMAN Unreviewed; 256 AA. AC H0YN42; DT 22-FEB-2012, integrated into UniProtKB/TrEMBL. DT 22-FEB-2012, sequence version 1. DT 08-NOV-2023, entry version 73. DE RecName: Full=Annexin {ECO:0000256|RuleBase:RU003540}; DE Flags: Fragment; GN Name=ANXA2 {ECO:0000313|Ensembl:ENSP00000453859}; 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 {ECO:0000313|Ensembl:ENSP00000453859, ECO:0000313|Proteomes:UP000005640}; RN [1] {ECO:0000313|Ensembl:ENSP00000453859, ECO:0000313|Proteomes:UP000005640} RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=16572171; DOI=10.1038/nature04601; RA Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K., RA Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K., RA FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N., RA Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S., RA Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K., RA DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R., Fahey J., RA Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G., Johnson E., RA Jones C., Kamat A., Kaur A., Locke D.P., Madan A., Munson G., Jaffe D.B., RA Lui A., Macdonald P., Mauceli E., Naylor J.W., Nesbitt R., Nicol R., RA O'Leary S.B., Ratcliffe A., Rounsley S., She X., Sneddon K.M., Stewart S., RA Sougnez C., Stone S.M., Topham K., Vincent D., Wang S., Zimmer A.R., RA Birren B.W., Hood L., Lander E.S., Nusbaum C.; RT "Analysis of the DNA sequence and duplication history of human chromosome RT 15."; RL Nature 440:671-675(2006). RN [2] {ECO:0007829|PubMed:21269460} 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., Burckstummer 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 [3] {ECO:0000313|Ensembl:ENSP00000453859} RP IDENTIFICATION. RG Ensembl; RL Submitted (JAN-2012) to UniProtKB. RN [4] {ECO:0007829|PubMed:23186163} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=23186163; 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 [5] {ECO:0007829|PubMed:24275569} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 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 [6] {ECO:0007829|PubMed:25114211} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25114211; RA Impens F., Radoshevich L., Cossart P., Ribet D.; RT "Mapping of SUMO sites and analysis of SUMOylation changes induced by RT external stimuli."; RL Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014). RN [7] {ECO:0007829|PubMed:25944712} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=25944712; 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 [8] {ECO:0007829|PubMed:28112733} RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=28112733; 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). CC -!- SUBCELLULAR LOCATION: Membrane {ECO:0000256|ARBA:ARBA00004370}. CC Secreted, extracellular space, extracellular matrix, basement membrane CC {ECO:0000256|ARBA:ARBA00004302}. CC -!- DOMAIN: A pair of annexin repeats may form one binding site for calcium CC and phospholipid. {ECO:0000256|RuleBase:RU003540}. CC -!- SIMILARITY: Belongs to the annexin family. CC {ECO:0000256|ARBA:ARBA00007831, ECO:0000256|RuleBase:RU003540}. 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; AC087385; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR AlphaFoldDB; H0YN42; -. DR SMR; H0YN42; -. DR SwissPalm; H0YN42; -. DR MaxQB; H0YN42; -. DR PeptideAtlas; H0YN42; -. DR PRIDE; H0YN42; -. DR ProteomicsDB; 40450; -. DR Antibodypedia; 3808; 908 antibodies from 46 providers. DR Ensembl; ENST00000559818; ENSP00000453859; ENSG00000182718. DR UCSC; uc059jwn.1; human. DR HGNC; HGNC:537; ANXA2. DR OpenTargets; ENSG00000182718; -. DR VEuPathDB; HostDB:ENSG00000182718; -. DR ChiTaRS; ANXA2; human. DR Proteomes; UP000005640; Chromosome 15. DR Bgee; ENSG00000182718; Expressed in bronchial epithelial cell and 203 other tissues. DR ExpressionAtlas; H0YN42; baseline and differential. DR GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005576; C:extracellular region; IEA:UniProtKB-KW. DR GO; GO:0016020; C:membrane; IEA:UniProtKB-SubCell. DR GO; GO:0005509; F:calcium ion binding; IEA:InterPro. DR GO; GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW. DR GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro. DR GO; GO:0004859; F:phospholipase inhibitor activity; IEA:InterPro. DR Gene3D; 1.10.220.10; Annexin; 3. DR InterPro; IPR001464; Annexin. DR InterPro; IPR018502; Annexin_repeat. DR InterPro; IPR018252; Annexin_repeat_CS. DR InterPro; IPR037104; Annexin_sf. DR InterPro; IPR002389; ANX2. DR PANTHER; PTHR10502; ANNEXIN; 1. DR PANTHER; PTHR10502:SF18; ANNEXIN A2-RELATED; 1. DR Pfam; PF00191; Annexin; 3. DR PRINTS; PR00196; ANNEXIN. DR PRINTS; PR00198; ANNEXINII. DR SMART; SM00335; ANX; 3. DR SUPFAM; SSF47874; Annexin; 1. DR PROSITE; PS00223; ANNEXIN_1; 2. DR PROSITE; PS51897; ANNEXIN_2; 3. PE 1: Evidence at protein level; KW Annexin {ECO:0000256|ARBA:ARBA00023216, ECO:0000256|RuleBase:RU003540}; KW Basement membrane {ECO:0000256|ARBA:ARBA00022869}; KW Calcium {ECO:0000256|ARBA:ARBA00022837, ECO:0000256|RuleBase:RU003540}; KW Calcium/phospholipid-binding {ECO:0000256|ARBA:ARBA00023302, KW ECO:0000256|RuleBase:RU003540}; KW Extracellular matrix {ECO:0000256|ARBA:ARBA00022530}; KW Phosphoprotein {ECO:0000256|ARBA:ARBA00022553}; KW Proteomics identification {ECO:0007829|EPD:H0YN42, KW ECO:0007829|MaxQB:H0YN42}; KW Reference proteome {ECO:0000313|Proteomes:UP000005640}; KW Repeat {ECO:0000256|ARBA:ARBA00022737, ECO:0000256|RuleBase:RU003540}; KW Secreted {ECO:0000256|ARBA:ARBA00022525}. FT NON_TER 256 FT /evidence="ECO:0000313|Ensembl:ENSP00000453859" SQ SEQUENCE 256 AA; 28825 MW; 9AAF40EE90AD53AF CRC64; MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM LESIRKEVKG DLENAF //