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Annexin A2 (Annexin II) (Annexin-2) (Calpactin I heavy chain) (Calpactin-1 heavy chain) (Chromobindin-8) (Lipocortin II) (Placental anticoagulant protein IV) (PAP-IV) (Protein I) (p36)

 ANXA2_HUMAN             Reviewed;         339 AA.
P07355; Q567R4; Q6N0B3; Q8TBV2; Q96DD5; Q9UDH8;
01-APR-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 215.
RecName: Full=Annexin A2;
AltName: Full=Annexin II;
AltName: Full=Annexin-2;
AltName: Full=Calpactin I heavy chain;
AltName: Full=Calpactin-1 heavy chain;
AltName: Full=Chromobindin-8;
AltName: Full=Lipocortin II;
AltName: Full=Placental anticoagulant protein IV;
Short=PAP-IV;
AltName: Full=Protein I;
AltName: Full=p36;
Name=ANXA2; Synonyms=ANX2, ANX2L4, CAL1H, LPC2D;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
TISSUE=Placenta;
PubMed=3013422; DOI=10.1016/0092-8674(86)90736-1;
Huang K.-S., Wallner B.P., Mattaliano R.J., Tizard R., Burne C.,
Frey A., Hession C., McGray P., Sinclair L.K., Chow E.P.,
Browning J.L., Ramachandran K.L., Tang J., Smart J.E., Pepinsky R.B.;
"Two human 35 kd inhibitors of phospholipase A2 are related to
substrates of pp60v-src and of the epidermal growth factor
receptor/kinase.";
Cell 46:191-199(1986).
[2]
NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
PubMed=2174397; DOI=10.1016/0378-1119(90)90367-Z;
Spano F., Raugei G., Palla E., Colella C., Melli M.;
"Characterization of the human lipocortin-2-encoding multigene family:
its structure suggests the existence of a short amino acid unit
undergoing duplication.";
Gene 95:243-251(1990).
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
Kalnine N., Chen X., Rolfs A., Halleck A., Hines L., Eisenstein S.,
Koundinya M., Raphael J., Moreira D., Kelley T., LaBaer J., Lin Y.,
Phelan M., Farmer A.;
"Cloning of human full-length CDSs in BD Creator(TM) system donor
vector.";
Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases.
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
TISSUE=Colon endothelium;
PubMed=17974005; DOI=10.1186/1471-2164-8-399;
Bechtel S., Rosenfelder H., Duda A., Schmidt C.P., Ernst U.,
Wellenreuther R., Mehrle A., Schuster C., Bahr A., Bloecker H.,
Heubner D., Hoerlein A., Michel G., Wedler H., Koehrer K.,
Ottenwaelder B., Poustka A., Wiemann S., Schupp I.;
"The full-ORF clone resource of the German cDNA consortium.";
BMC Genomics 8:399-399(2007).
[5]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=16572171; DOI=10.1038/nature04601;
Zody M.C., Garber M., Sharpe T., Young S.K., Rowen L., O'Neill K.,
Whittaker C.A., Kamal M., Chang J.L., Cuomo C.A., Dewar K.,
FitzGerald M.G., Kodira C.D., Madan A., Qin S., Yang X., Abbasi N.,
Abouelleil A., Arachchi H.M., Baradarani L., Birditt B., Bloom S.,
Bloom T., Borowsky M.L., Burke J., Butler J., Cook A., DeArellano K.,
DeCaprio D., Dorris L. III, Dors M., Eichler E.E., Engels R.,
Fahey J., Fleetwood P., Friedman C., Gearin G., Hall J.L., Hensley G.,
Johnson E., Jones C., Kamat A., Kaur A., Locke D.P., Madan A.,
Munson G., Jaffe D.B., Lui A., Macdonald P., Mauceli E., Naylor J.W.,
Nesbitt R., Nicol R., O'Leary S.B., Ratcliffe A., Rounsley S., She X.,
Sneddon K.M.B., Stewart S., Sougnez C., Stone S.M., Topham K.,
Vincent D., Wang S., Zimmer A.R., Birren B.W., Hood L., Lander E.S.,
Nusbaum C.;
"Analysis of the DNA sequence and duplication history of human
chromosome 15.";
Nature 440:671-675(2006).
[6]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1), AND VARIANT
LEU-98.
TISSUE=Brain, Colon, Pancreas, Prostate, Skin, Testis, and
Urinary bladder;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[7]
PROTEIN SEQUENCE OF 2-10; 38-47; 50-63; 69-77; 89-115; 153-169 AND
213-220, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT SER-2, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Colon adenocarcinoma, and Osteosarcoma;
Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Bensaad K.,
Vousden K.H.;
Submitted (FEB-2008) to UniProtKB.
[8]
PROTEIN SEQUENCE OF 11-27; 49-62; 68-77; 120-135; 314-323 AND 329-339.
PubMed=1825830;
Jindal H.K., Chaney W.G., Anderson C.W., Davis R.G., Vishwanatha J.K.;
"The protein-tyrosine kinase substrate, calpactin I heavy chain (p36),
is part of the primer recognition protein complex that interacts with
DNA polymerase alpha.";
J. Biol. Chem. 266:5169-5176(1991).
[9]
PROTEIN SEQUENCE OF 15-40 AND 50-63.
PubMed=8110754; DOI=10.1021/bi00171a023;
Hyatt S.L., Liao L., Chapline C., Jaken S.;
"Identification and characterization of alpha-protein kinase C binding
proteins in normal and transformed REF52 cells.";
Biochemistry 33:1223-1228(1994).
[10]
PROTEIN SEQUENCE OF 18-37; 119-126; 172-191 AND 301-307, AND
INTERACTION WITH HCMV (MICROBIAL INFECTION).
TISSUE=Umbilical vein endothelial cell;
PubMed=8117306; DOI=10.1006/bbrc.1994.1140;
Wright J.F., Kurosky A., Wasi S.;
"An endothelial cell-surface form of annexin II binds human
cytomegalovirus.";
Biochem. Biophys. Res. Commun. 198:983-989(1994).
[11]
PROTEIN SEQUENCE OF 234-241 AND 252-261.
PubMed=8449982; DOI=10.1083/jcb.120.6.1357;
Emans N., Gorvel J.P., Walter C., Gerke V., Kellner R., Griffiths G.,
Gruenberg J.;
"Annexin II is a major component of fusogenic endosomal vesicles.";
J. Cell Biol. 120:1357-1369(1993).
[12]
PHOSPHORYLATION AT SER-26.
PubMed=2946940; DOI=10.1128/MCB.6.7.2738;
Gould K.L., Woodgett J.R., Isacke C.M., Hunter T.;
"The protein-tyrosine kinase substrate p36 is also a substrate for
protein kinase C in vitro and in vivo.";
Mol. Cell. Biol. 6:2738-2744(1986).
[13]
INTERACTION WITH CEACAM1.
PubMed=14522961; DOI=10.1074/jbc.M309115200;
Kirshner J., Schumann D., Shively J.E.;
"CEACAM1, a cell-cell adhesion molecule, directly associates with
annexin II in a three-dimensional model of mammary morphogenesis.";
J. Biol. Chem. 278:50338-50345(2003).
[14]
PHOSPHORYLATION AT TYR-24, AND MUTAGENESIS OF TYR-24.
PubMed=15302870; DOI=10.1074/jbc.M408078200;
Deora A.B., Kreitzer G., Jacovina A.T., Hajjar K.A.;
"An annexin 2 phosphorylation switch mediates p11-dependent
translocation of annexin 2 to the cell surface.";
J. Biol. Chem. 279:43411-43418(2004).
[15]
ISGYLATION.
PubMed=16139798; DOI=10.1016/j.bbrc.2005.08.132;
Giannakopoulos N.V., Luo J.K., Papov V., Zou W., Lenschow D.J.,
Jacobs B.S., Borden E.C., Li J., Virgin H.W., Zhang D.E.;
"Proteomic identification of proteins conjugated to ISG15 in mouse and
human cells.";
Biochem. Biophys. Res. Commun. 336:496-506(2005).
[16]
SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
TISSUE=Melanoma;
PubMed=17081065; DOI=10.1021/pr060363j;
Chi A., Valencia J.C., Hu Z.-Z., Watabe H., Yamaguchi H.,
Mangini N.J., Huang H., Canfield V.A., Cheng K.C., Yang F., Abe R.,
Yamagishi S., Shabanowitz J., Hearing V.J., Wu C., Appella E.,
Hunt D.F.;
"Proteomic and bioinformatic characterization of the biogenesis and
function of melanosomes.";
J. Proteome Res. 5:3135-3144(2006).
[17]
FUNCTION, INTERACTION WITH PCSK9, AND MUTAGENESIS OF 77-ARG--LYS-81;
80-LYS--ALA-84 AND LYS-88.
PubMed=18799458; DOI=10.1074/jbc.M805971200;
Mayer G., Poirier S., Seidah N.G.;
"Annexin A2 is a C-terminal PCSK9-binding protein that regulates
endogenous low density lipoprotein receptor levels.";
J. Biol. Chem. 283:31791-31801(2008).
[18]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[19]
INTERACTION WITH COCH.
PubMed=21886777; DOI=10.1371/journal.pone.0023070;
Goel M., Sienkiewicz A.E., Picciani R., Lee R.K., Bhattacharya S.K.;
"Cochlin induced TREK-1 co-expression and annexin A2 secretion: role
in trabecular meshwork cell elongation and motility.";
PLoS ONE 6:E23070-E23070(2011).
[20]
FUNCTION, VARIANT LEU-98, CHARACTERIZATION OF VARIANT LEU-98, AND
MUTAGENESIS OF 28-LYS--GLU-36; 37-ARG--LYS-47; 77-ARG--LYS-80 AND
77-ARG--LYS-81.
PubMed=22848640; DOI=10.1371/journal.pone.0041865;
Seidah N.G., Poirier S., Denis M., Parker R., Miao B., Mapelli C.,
Prat A., Wassef H., Davignon J., Hajjar K.A., Mayer G.;
"Annexin A2 is a natural extrahepatic inhibitor of the PCSK9-induced
LDL receptor degradation.";
PLoS ONE 7:E41865-E41865(2012).
[21]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-184, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[22]
FUNCTION, INTERACTION WITH PCSK9, AND RNA-BINDING.
PubMed=24808179; DOI=10.1074/jbc.M113.541094;
Ly K., Saavedra Y.G., Canuel M., Routhier S., Desjardins R.,
Hamelin J., Mayne J., Lazure C., Seidah N.G., Day R.;
"Annexin A2 reduces PCSK9 protein levels via a translational mechanism
and interacts with the M1 and M2 domains of PCSK9.";
J. Biol. Chem. 289:17732-17746(2014).
[23]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
[24]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25114211; DOI=10.1073/pnas.1413825111;
Impens F., Radoshevich L., Cossart P., Ribet D.;
"Mapping of SUMO sites and analysis of SUMOylation changes induced by
external stimuli.";
Proc. Natl. Acad. Sci. U.S.A. 111:12432-12437(2014).
[25]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25944712; DOI=10.1002/pmic.201400617;
Vaca Jacome A.S., Rabilloud T., Schaeffer-Reiss C., Rompais M.,
Ayoub D., Lane L., Bairoch A., Van Dorsselaer A., Carapito C.;
"N-terminome analysis of the human mitochondrial proteome.";
Proteomics 15:2519-2524(2015).
[26]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-49, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=28112733; DOI=10.1038/nsmb.3366;
Hendriks I.A., Lyon D., Young C., Jensen L.J., Vertegaal A.C.,
Nielsen M.L.;
"Site-specific mapping of the human SUMO proteome reveals co-
modification with phosphorylation.";
Nat. Struct. Mol. Biol. 24:325-336(2017).
[27]
X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
PubMed=8636985; DOI=10.1006/jmbi.1996.0205;
Burger A., Berendes R., Liemann S., Benz J., Hofmann A., Goettig P.,
Huber R., Gerke V., Tiel C., Roemisch J., Weber K.;
"The crystal structure and ion channel activity of human annexin II, a
peripheral membrane protein.";
J. Mol. Biol. 257:839-847(1996).
-!- FUNCTION: Calcium-regulated membrane-binding protein whose
affinity for calcium is greatly enhanced by anionic phospholipids.
It binds two calcium ions with high affinity. May be involved in
heat-stress response. Inhibits PCSK9-enhanced LDLR degradation,
probably reduces PCSK9 protein levels via a translational
mechanism but also competes with LDLR for binding with PCSK9
(PubMed:18799458, PubMed:24808179, PubMed:22848640).
{ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:22848640,
ECO:0000269|PubMed:24808179}.
-!- SUBUNIT: Heterotetramer containing 2 light chains of S100A10/p11
and 2 heavy chains of ANXA2/p36 (By similarity). Interacts with
ATP1B1 (By similarity). Interacts with DYSF (By similarity).
Interacts with COCH (PubMed:21886777). Interacts (via repeat
Annexin 1) with PCSK9 (via the C-terminal domain); the interaction
inhibits the degradation of LDLR (PubMed:18799458). Interacts with
CEACAM1 (via the cytoplasmic domain); this interaction is
regulated by phosphorylation of CEACAM1 (PubMed:14522961).
{ECO:0000250|UniProtKB:A2SW69, ECO:0000250|UniProtKB:P07356,
ECO:0000250|UniProtKB:Q6TEQ7, ECO:0000269|PubMed:14522961,
ECO:0000269|PubMed:18799458, ECO:0000269|PubMed:21886777}.
-!- SUBUNIT: (Microbial infection) Interacts with human
cytomegalovirus (HCMV). {ECO:0000269|PubMed:8117306}.
-!- INTERACTION:
Self; NbExp=5; IntAct=EBI-352622, EBI-352622;
Q99IB8:- (xeno); NbExp=5; IntAct=EBI-352622, EBI-6927873;
P03950:ANG; NbExp=6; IntAct=EBI-352622, EBI-525291;
P46092:CCR10; NbExp=2; IntAct=EBI-352622, EBI-348022;
P40692:MLH1; NbExp=7; IntAct=EBI-352622, EBI-744248;
P75409:MPN_372 (xeno); NbExp=6; IntAct=EBI-352622, EBI-2259548;
P15363:p37 (xeno); NbExp=10; IntAct=EBI-352622, EBI-12740262;
Q8NBP7:PCSK9; NbExp=7; IntAct=EBI-352622, EBI-7539251;
Q9NUX5:POT1; NbExp=2; IntAct=EBI-352622, EBI-752420;
-!- SUBCELLULAR LOCATION: Secreted, extracellular space, extracellular
matrix, basement membrane {ECO:0000269|PubMed:17081065}.
Melanosome {ECO:0000269|PubMed:17081065}. Note=In the lamina
beneath the plasma membrane. Identified by mass spectrometry in
melanosome fractions from stage I to stage IV. Translocated from
the cytoplasm to the cell surface through a Golgi-independent
mechanism.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=2;
Name=1;
IsoId=P07355-1; Sequence=Displayed;
Name=2;
IsoId=P07355-2; Sequence=VSP_038091;
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- PTM: Phosphorylation of Tyr-24 enhances heat stress-induced
translocation to the cell surface. {ECO:0000269|PubMed:15302870,
ECO:0000269|PubMed:2946940}.
-!- PTM: ISGylated. {ECO:0000269|PubMed:16139798}.
-!- MISCELLANEOUS: It may cross-link plasma membrane phospholipids
with actin and the cytoskeleton and be involved with exocytosis.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
-!- SEQUENCE CAUTION:
Sequence=AAH66955.2; Type=Erroneous initiation; Note=Translation N-terminally shortened.; Evidence={ECO:0000305};
-!- WEB RESOURCE: Name=Protein Spotlight; Note=Red velvet - Issue 86
of September 2007;
URL="http://web.expasy.org/spotlight/back_issues/086";
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EMBL; D00017; BAA00013.1; -; mRNA.
EMBL; BT007432; AAP36100.1; -; mRNA.
EMBL; BX640598; CAE45704.1; -; mRNA.
EMBL; AC087385; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC001388; AAH01388.1; -; mRNA.
EMBL; BC009564; AAH09564.1; -; mRNA.
EMBL; BC015834; AAH15834.1; -; mRNA.
EMBL; BC016774; AAH16774.1; -; mRNA.
EMBL; BC021114; AAH21114.1; -; mRNA.
EMBL; BC023990; AAH23990.1; -; mRNA.
EMBL; BC052558; AAH52558.1; -; mRNA.
EMBL; BC052567; AAH52567.1; -; mRNA.
EMBL; BC066955; AAH66955.2; ALT_INIT; mRNA.
EMBL; BC068065; AAH68065.1; -; mRNA.
EMBL; BC093056; AAH93056.1; -; mRNA.
CCDS; CCDS10175.1; -. [P07355-1]
CCDS; CCDS32256.1; -. [P07355-2]
PIR; A23942; LUHU36.
RefSeq; NP_001002857.1; NM_001002857.1. [P07355-1]
RefSeq; NP_001002858.1; NM_001002858.2. [P07355-2]
RefSeq; NP_001129487.1; NM_001136015.2. [P07355-1]
RefSeq; NP_004030.1; NM_004039.2. [P07355-1]
RefSeq; XP_016877579.1; XM_017022090.1. [P07355-1]
RefSeq; XP_016877580.1; XM_017022091.1. [P07355-1]
UniGene; Hs.511605; -.
PDB; 1W7B; X-ray; 1.52 A; A=1-339.
PDB; 1XJL; X-ray; 2.59 A; A/B=21-339.
PDB; 2HYU; X-ray; 1.86 A; A=32-339.
PDB; 2HYV; X-ray; 1.42 A; A=32-339.
PDB; 2HYW; X-ray; 2.10 A; A/B=32-339.
PDB; 4DRW; X-ray; 3.50 A; A/B/C/D=2-16.
PDB; 4FTG; X-ray; 2.51 A; C/D=2-16.
PDB; 4HRH; X-ray; 3.00 A; A/B=2-16.
PDBsum; 1W7B; -.
PDBsum; 1XJL; -.
PDBsum; 2HYU; -.
PDBsum; 2HYV; -.
PDBsum; 2HYW; -.
PDBsum; 4DRW; -.
PDBsum; 4FTG; -.
PDBsum; 4HRH; -.
ProteinModelPortal; P07355; -.
SMR; P07355; -.
BioGrid; 106799; 112.
CORUM; P07355; -.
IntAct; P07355; 71.
MINT; MINT-1213203; -.
STRING; 9606.ENSP00000346032; -.
ChEMBL; CHEMBL1764938; -.
DrugBank; DB00031; Tenecteplase.
TCDB; 1.A.31.1.4; the annexin (annexin) family.
iPTMnet; P07355; -.
PhosphoSitePlus; P07355; -.
SwissPalm; P07355; -.
BioMuta; ANXA2; -.
DMDM; 113950; -.
DOSAC-COBS-2DPAGE; P07355; -.
REPRODUCTION-2DPAGE; IPI00455315; -.
REPRODUCTION-2DPAGE; P07355; -.
UCD-2DPAGE; P07355; -.
EPD; P07355; -.
MaxQB; P07355; -.
PaxDb; P07355; -.
PeptideAtlas; P07355; -.
PRIDE; P07355; -.
TopDownProteomics; P07355-1; -. [P07355-1]
DNASU; 302; -.
Ensembl; ENST00000332680; ENSP00000346032; ENSG00000182718. [P07355-2]
Ensembl; ENST00000396024; ENSP00000379342; ENSG00000182718. [P07355-1]
Ensembl; ENST00000421017; ENSP00000411352; ENSG00000182718. [P07355-1]
Ensembl; ENST00000451270; ENSP00000387545; ENSG00000182718. [P07355-1]
GeneID; 302; -.
KEGG; hsa:302; -.
UCSC; uc002agk.4; human. [P07355-1]
CTD; 302; -.
DisGeNET; 302; -.
EuPathDB; HostDB:ENSG00000182718.16; -.
GeneCards; ANXA2; -.
HGNC; HGNC:537; ANXA2.
HPA; CAB004311; -.
MIM; 151740; gene.
neXtProt; NX_P07355; -.
OpenTargets; ENSG00000182718; -.
PharmGKB; PA24827; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P07355; -.
KO; K17092; -.
OMA; FIQQDTK; -.
OrthoDB; EOG091G0H6H; -.
TreeFam; TF105452; -.
Reactome; R-HSA-445355; Smooth Muscle Contraction.
Reactome; R-HSA-6798695; Neutrophil degranulation.
Reactome; R-HSA-75205; Dissolution of Fibrin Clot.
Reactome; R-HSA-8950505; Gene and protein expression by JAK-STAT signaling after Interleukin-12 stimulation.
SIGNOR; P07355; -.
ChiTaRS; ANXA2; human.
EvolutionaryTrace; P07355; -.
GeneWiki; Annexin_A2; -.
GenomeRNAi; 302; -.
PRO; PR:P07355; -.
Proteomes; UP000005640; Chromosome 15.
Bgee; ENSG00000182718; -.
CleanEx; HS_ANXA2; -.
ExpressionAtlas; P07355; baseline and differential.
Genevisible; P07355; HS.
GO; GO:0035578; C:azurophil granule lumen; TAS:Reactome.
GO; GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
GO; GO:0016323; C:basolateral plasma membrane; ISS:BHF-UCL.
GO; GO:0005938; C:cell cortex; IEA:Ensembl.
GO; GO:0009986; C:cell surface; IDA:UniProtKB.
GO; GO:0005913; C:cell-cell adherens junction; IDA:BHF-UCL.
GO; GO:0005737; C:cytoplasm; IDA:AgBase.
GO; GO:0005829; C:cytosol; IEA:Ensembl.
GO; GO:0005769; C:early endosome; IEA:Ensembl.
GO; GO:0005768; C:endosome; IDA:UniProtKB.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005615; C:extracellular space; IDA:UniProtKB.
GO; GO:0019897; C:extrinsic component of plasma membrane; IEA:Ensembl.
GO; GO:0031902; C:late endosome membrane; IDA:UniProtKB.
GO; GO:0005811; C:lipid droplet; IDA:UniProtKB.
GO; GO:0005765; C:lysosomal membrane; IDA:UniProtKB.
GO; GO:0044354; C:macropinosome; IEA:Ensembl.
GO; GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0045121; C:membrane raft; IEA:Ensembl.
GO; GO:0030496; C:midbody; IDA:UniProtKB.
GO; GO:0035749; C:myelin sheath adaxonal region; IEA:Ensembl.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:1990667; C:PCSK9-AnxA2 complex; IDA:BHF-UCL.
GO; GO:0048471; C:perinuclear region of cytoplasm; IEA:Ensembl.
GO; GO:0005886; C:plasma membrane; IDA:BHF-UCL.
GO; GO:0001726; C:ruffle; IEA:Ensembl.
GO; GO:0042383; C:sarcolemma; IEA:Ensembl.
GO; GO:0043220; C:Schmidt-Lanterman incisure; IEA:Ensembl.
GO; GO:0031982; C:vesicle; IDA:UniProtKB.
GO; GO:0098641; F:cadherin binding involved in cell-cell adhesion; IDA:BHF-UCL.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0048306; F:calcium-dependent protein binding; IPI:AgBase.
GO; GO:0008092; F:cytoskeletal protein binding; IEA:InterPro.
GO; GO:0042802; F:identical protein binding; IPI:IntAct.
GO; GO:0005546; F:phosphatidylinositol-4,5-bisphosphate binding; IMP:UniProtKB.
GO; GO:0019834; F:phospholipase A2 inhibitor activity; IDA:UniProtKB.
GO; GO:0002020; F:protease binding; IPI:BHF-UCL.
GO; GO:0017137; F:Rab GTPase binding; IEA:Ensembl.
GO; GO:0003723; F:RNA binding; IDA:UniProtKB.
GO; GO:0044548; F:S100 protein binding; IPI:UniProtKB.
GO; GO:0001525; P:angiogenesis; IEP:UniProtKB.
GO; GO:0007589; P:body fluid secretion; IEA:Ensembl.
GO; GO:0052362; P:catabolism by host of symbiont protein; IMP:AgBase.
GO; GO:0030199; P:collagen fibril organization; IEA:Ensembl.
GO; GO:0042730; P:fibrinolysis; IEA:Ensembl.
GO; GO:0035722; P:interleukin-12-mediated signaling pathway; TAS:Reactome.
GO; GO:0006900; P:membrane budding; IMP:UniProtKB.
GO; GO:0001765; P:membrane raft assembly; IMP:UniProtKB.
GO; GO:0052405; P:negative regulation by host of symbiont molecular function; IMP:AgBase.
GO; GO:0044147; P:negative regulation of development of symbiont involved in interaction with host; IMP:AgBase.
GO; GO:0032804; P:negative regulation of low-density lipoprotein particle receptor catabolic process; IDA:BHF-UCL.
GO; GO:0043312; P:neutrophil degranulation; TAS:Reactome.
GO; GO:0036035; P:osteoclast development; IDA:UniProtKB.
GO; GO:0048146; P:positive regulation of fibroblast proliferation; IEA:Ensembl.
GO; GO:1905581; P:positive regulation of low-density lipoprotein particle clearance; IDA:BHF-UCL.
GO; GO:1905597; P:positive regulation of low-density lipoprotein particle receptor binding; IDA:BHF-UCL.
GO; GO:1905599; P:positive regulation of low-density lipoprotein receptor activity; IMP:BHF-UCL.
GO; GO:0001934; P:positive regulation of protein phosphorylation; IEA:Ensembl.
GO; GO:0001921; P:positive regulation of receptor recycling; IDA:BHF-UCL.
GO; GO:1905602; P:positive regulation of receptor-mediated endocytosis involved in cholesterol transport; IDA:BHF-UCL.
GO; GO:0044090; P:positive regulation of vacuole organization; IMP:AgBase.
GO; GO:0031340; P:positive regulation of vesicle fusion; IDA:UniProtKB.
GO; GO:0051290; P:protein heterotetramerization; IDA:UniProtKB.
GO; GO:0072661; P:protein targeting to plasma membrane; IEA:Ensembl.
GO; GO:0097066; P:response to thyroid hormone; IEA:Ensembl.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR002389; ANX2.
PANTHER; PTHR10502:SF151; PTHR10502:SF151; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00198; ANNEXINII.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Alternative splicing; Annexin;
Basement membrane; Calcium; Calcium/phospholipid-binding;
Complete proteome; Direct protein sequencing; Extracellular matrix;
Isopeptide bond; Phosphoprotein; Polymorphism; Reference proteome;
Repeat; RNA-binding; Secreted; Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000269|Ref.7}.
CHAIN 2 339 Annexin A2.
/FTId=PRO_0000067470.
REPEAT 42 102 Annexin 1.
REPEAT 114 174 Annexin 2.
REPEAT 199 259 Annexin 3.
REPEAT 274 334 Annexin 4.
REGION 2 24 S100A10-binding site. {ECO:0000255}.
MOD_RES 2 2 N-acetylserine. {ECO:0000269|Ref.7}.
MOD_RES 24 24 Phosphotyrosine; by SRC.
{ECO:0000269|PubMed:15302870}.
MOD_RES 26 26 Phosphoserine; by PKC.
{ECO:0000269|PubMed:2946940}.
MOD_RES 49 49 N6-acetyllysine; alternate.
{ECO:0000250|UniProtKB:P07356}.
MOD_RES 152 152 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07356}.
MOD_RES 184 184 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 199 199 Phosphotyrosine.
{ECO:0000250|UniProtKB:P07356}.
MOD_RES 227 227 N6-acetyllysine.
{ECO:0000250|UniProtKB:P07356}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1);
alternate. {ECO:0000244|PubMed:25114211}.
CROSSLNK 49 49 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2);
alternate. {ECO:0000244|PubMed:28112733}.
VAR_SEQ 1 1 M -> MGRQLAGCGDAGKKASFKM (in isoform 2).
{ECO:0000303|PubMed:17974005}.
/FTId=VSP_038091.
VARIANT 98 98 V -> L (polymorphism; does not affect
interaction with PCSK9;
dbSNP:rs17845226).
{ECO:0000269|PubMed:15489334,
ECO:0000269|PubMed:22848640}.
/FTId=VAR_012982.
MUTAGEN 24 24 Y->A: Abolishes heat stress-induced cell
surface localization.
{ECO:0000269|PubMed:15302870}.
MUTAGEN 28 36 KAYTNFDAE->SAYTNFNAS: No effect on
interaction with PCSK9.
{ECO:0000269|PubMed:22848640}.
MUTAGEN 37 47 RDALNIETAIK->SDALNIHTAIM: Slightly
decreases interaction with PCSK9.
{ECO:0000269|PubMed:22848640}.
MUTAGEN 77 81 RRTKK->AATAA: Strongly decreases
interaction with PCSK9.
{ECO:0000269|PubMed:18799458,
ECO:0000269|PubMed:22848640}.
MUTAGEN 77 80 RRTK->AATA: Decreases interaction with
PCSK9. Strongly decreases interaction
with PCSK9; when associated with K-88.
{ECO:0000269|PubMed:18799458}.
MUTAGEN 80 84 KKELA->GKPLD: No effect on interaction
with PCSK9.
{ECO:0000269|PubMed:18799458}.
MUTAGEN 88 88 K->A: Strongly decreases interaction with
PCSK9; when associated with 77-A--A-80.
{ECO:0000269|PubMed:18799458}.
CONFLICT 29 29 A -> P (in Ref. 9; AA sequence).
{ECO:0000305}.
CONFLICT 166 166 D -> G (in Ref. 4; CAE45704).
{ECO:0000305}.
CONFLICT 293 293 V -> A (in Ref. 6; AAH23990).
{ECO:0000305}.
HELIX 3 8 {ECO:0000244|PDB:4FTG}.
HELIX 35 47 {ECO:0000244|PDB:2HYV}.
HELIX 53 60 {ECO:0000244|PDB:2HYV}.
HELIX 65 79 {ECO:0000244|PDB:2HYV}.
HELIX 83 90 {ECO:0000244|PDB:2HYV}.
HELIX 93 103 {ECO:0000244|PDB:2HYV}.
HELIX 106 117 {ECO:0000244|PDB:2HYV}.
STRAND 120 122 {ECO:0000244|PDB:1W7B}.
HELIX 125 134 {ECO:0000244|PDB:2HYV}.
HELIX 137 151 {ECO:0000244|PDB:2HYV}.
HELIX 155 161 {ECO:0000244|PDB:2HYV}.
HELIX 165 175 {ECO:0000244|PDB:2HYV}.
HELIX 188 200 {ECO:0000244|PDB:2HYV}.
TURN 201 204 {ECO:0000244|PDB:2HYV}.
STRAND 205 207 {ECO:0000244|PDB:2HYV}.
HELIX 210 219 {ECO:0000244|PDB:2HYV}.
HELIX 222 232 {ECO:0000244|PDB:2HYV}.
TURN 233 235 {ECO:0000244|PDB:2HYV}.
HELIX 240 247 {ECO:0000244|PDB:2HYV}.
HELIX 250 264 {ECO:0000244|PDB:2HYV}.
HELIX 266 278 {ECO:0000244|PDB:2HYV}.
STRAND 279 282 {ECO:0000244|PDB:2HYV}.
HELIX 285 295 {ECO:0000244|PDB:2HYV}.
TURN 296 298 {ECO:0000244|PDB:2HYV}.
HELIX 300 311 {ECO:0000244|PDB:2HYV}.
HELIX 315 322 {ECO:0000244|PDB:2HYV}.
HELIX 325 335 {ECO:0000244|PDB:2HYV}.
SEQUENCE 339 AA; 38604 MW; 5126E1337A0CBEA1 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 DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD


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