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Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CBP-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (PP4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha)

 ANXA5_HUMAN             Reviewed;         320 AA.
P08758; D3DNW7; Q6FHB3; Q6FI16; Q8WV69; Q9UDH9;
01-NOV-1988, integrated into UniProtKB/Swiss-Prot.
23-JAN-2007, sequence version 2.
27-SEP-2017, entry version 200.
RecName: Full=Annexin A5;
AltName: Full=Anchorin CII;
AltName: Full=Annexin V;
AltName: Full=Annexin-5;
AltName: Full=Calphobindin I;
Short=CBP-I;
AltName: Full=Endonexin II;
AltName: Full=Lipocortin V;
AltName: Full=Placental anticoagulant protein 4;
Short=PP4;
AltName: Full=Placental anticoagulant protein I;
Short=PAP-I;
AltName: Full=Thromboplastin inhibitor;
AltName: Full=Vascular anticoagulant-alpha;
Short=VAC-alpha;
Name=ANXA5; Synonyms=ANX5, ENX2, PP4;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2964863; DOI=10.1021/bi00399a011;
Funakoshi T., Hendrickson L.E., McMullen B.A., Fujikawa K.;
"Primary structure of human placental anticoagulant protein.";
Biochemistry 26:8087-8092(1987).
[2]
NUCLEOTIDE SEQUENCE [MRNA], AND PROTEIN SEQUENCE OF 2-320.
PubMed=2963810;
Iwasaki A., Suda M., Nakao H., Nagoya T., Saino Y., Arai K.,
Mizoguchi T., Sato F., Yoshizaki H., Hirata M., Miyata T., Shidara Y.,
Murata M., Maki M.;
"Structure and expression of cDNA for an inhibitor of blood
coagulation isolated from human placenta: a new lipocortin-like
protein.";
J. Biochem. 102:1261-1273(1987).
[3]
NUCLEOTIDE SEQUENCE [MRNA], AND PARTIAL PROTEIN SEQUENCE.
PubMed=2455636; DOI=10.1111/j.1432-1033.1988.tb14139.x;
Maurer-Fogy I., Reutelingsperger C.P.M., Pieters J., Bodo G.,
Stratowa C., Hauptmann R.;
"Cloning and expression of cDNA for human vascular anticoagulant, a
Ca2+-dependent phospholipid-binding protein.";
Eur. J. Biochem. 174:585-592(1988).
[4]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2967291;
Kaplan R., Jaye M., Burgess W.H., Schlaepfer D.D., Haigler H.T.;
"Cloning and expression of cDNA for human endonexin II, a Ca2+ and
phospholipid binding protein.";
J. Biol. Chem. 263:8037-8043(1988).
[5]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2968983;
Pepinsky R.B., Tizard R., Mattaliano R.J., Sinclair L.K., Miller G.T.,
Browning J.L., Chow E.P., Burne C., Huang K.-S., Pratt D., Wachter L.,
Hession C., Frey A.Z., Wallner B.P.;
"Five distinct calcium and phospholipid binding proteins share
homology with lipocortin I.";
J. Biol. Chem. 263:10799-10811(1988).
[6]
NUCLEOTIDE SEQUENCE [MRNA].
PubMed=2967495; DOI=10.1073/pnas.85.11.3708;
Grundmann U., Abel K.-J., Bohn H., Loebermann H., Lottspeich F.,
Kuepper H.;
"Characterization of cDNA encoding human placental anticoagulant
protein (PP4): homology with the lipocortin family.";
Proc. Natl. Acad. Sci. U.S.A. 85:3708-3712(1988).
[7]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
TISSUE=Lung;
PubMed=7958998; DOI=10.1016/0378-1119(94)90157-0;
Fernandez M.-P., Morgan R.O., Fernandez M.R., Carcedo M.-T.;
"The gene encoding human annexin V has a TATA-less promoter with a
high G+C content.";
Gene 149:253-260(1994).
[8]
NUCLEOTIDE SEQUENCE [GENOMIC DNA].
PubMed=8034319; DOI=10.1006/geno.1994.1201;
Cookson B.T., Engelhardt S., Smith C., Bamford H.A., Prochazka M.,
Tait J.F.;
"Organization of the human annexin V (ANX5) gene.";
Genomics 20:463-467(1994).
[9]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Neuroblastoma;
PubMed=14702039; DOI=10.1038/ng1285;
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R.,
Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H.,
Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S.,
Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K.,
Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A.,
Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M.,
Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y.,
Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M.,
Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K.,
Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S.,
Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J.,
Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y.,
Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N.,
Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S.,
Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S.,
Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O.,
Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H.,
Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B.,
Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y.,
Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T.,
Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y.,
Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S.,
Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T.,
Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M.,
Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T.,
Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K.,
Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R.,
Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[10]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Halleck A., Ebert L., Mkoundinya M., Schick M., Eisenstein S.,
Neubert P., Kstrang K., Schatten R., Shen B., Henze S., Mar W.,
Korn B., Zuo D., Hu Y., LaBaer J.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[11]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15815621; DOI=10.1038/nature03466;
Hillier L.W., Graves T.A., Fulton R.S., Fulton L.A., Pepin K.H.,
Minx P., Wagner-McPherson C., Layman D., Wylie K., Sekhon M.,
Becker M.C., Fewell G.A., Delehaunty K.D., Miner T.L., Nash W.E.,
Kremitzki C., Oddy L., Du H., Sun H., Bradshaw-Cordum H., Ali J.,
Carter J., Cordes M., Harris A., Isak A., van Brunt A., Nguyen C.,
Du F., Courtney L., Kalicki J., Ozersky P., Abbott S., Armstrong J.,
Belter E.A., Caruso L., Cedroni M., Cotton M., Davidson T., Desai A.,
Elliott G., Erb T., Fronick C., Gaige T., Haakenson W., Haglund K.,
Holmes A., Harkins R., Kim K., Kruchowski S.S., Strong C.M.,
Grewal N., Goyea E., Hou S., Levy A., Martinka S., Mead K.,
McLellan M.D., Meyer R., Randall-Maher J., Tomlinson C.,
Dauphin-Kohlberg S., Kozlowicz-Reilly A., Shah N.,
Swearengen-Shahid S., Snider J., Strong J.T., Thompson J., Yoakum M.,
Leonard S., Pearman C., Trani L., Radionenko M., Waligorski J.E.,
Wang C., Rock S.M., Tin-Wollam A.-M., Maupin R., Latreille P.,
Wendl M.C., Yang S.-P., Pohl C., Wallis J.W., Spieth J., Bieri T.A.,
Berkowicz N., Nelson J.O., Osborne J., Ding L., Meyer R., Sabo A.,
Shotland Y., Sinha P., Wohldmann P.E., Cook L.L., Hickenbotham M.T.,
Eldred J., Williams D., Jones T.A., She X., Ciccarelli F.D.,
Izaurralde E., Taylor J., Schmutz J., Myers R.M., Cox D.R., Huang X.,
McPherson J.D., Mardis E.R., Clifton S.W., Warren W.C.,
Chinwalla A.T., Eddy S.R., Marra M.A., Ovcharenko I., Furey T.S.,
Miller W., Eichler E.E., Bork P., Suyama M., Torrents D.,
Waterston R.H., Wilson R.K.;
"Generation and annotation of the DNA sequences of human chromosomes 2
and 4.";
Nature 434:724-731(2005).
[12]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L.,
Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R.,
Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V.,
Hannenhalli S., Turner R., Yooseph S., Lu F., Nusskern D.R.,
Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H.,
Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G.,
Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W.,
Venter J.C.;
Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases.
[13]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
TISSUE=Muscle, Ovary, and Skin;
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).
[14]
PARTIAL PROTEIN SEQUENCE.
PubMed=2532007; DOI=10.1042/bj2630929;
Rothhut R., Comera C., Cortial S., Haumont P.-Y., Diep Le K.H.,
Cavadore J.-C., Conard J., Russo-Marie F., Lederer F.;
"A 32 kDa lipocortin from human mononuclear cells appears to be
identical with the placental inhibitor of blood coagulation.";
Biochem. J. 263:929-935(1989).
[15]
PROTEIN SEQUENCE OF 7-18; 30-45; 187-201 AND 277-286, AND
IDENTIFICATION BY MASS SPECTROMETRY.
TISSUE=Melanoma;
Quadroni M., Potts A., Barblan J., Bienvenut W.V.;
Submitted (JAN-2005) to UniProtKB.
[16]
PROTEIN SEQUENCE OF 21-31; 93-108; 176-188 AND 304-319, AND
INTERACTION WITH HBV.
PubMed=8249278; DOI=10.1006/viro.1993.1628;
Hertogs K., Leenders W.P., Depla E., De Bruin W.C., Meheus L.,
Raymackers J., Moshage H., Yap S.H.;
"Endonexin II, present on human liver plasma membranes, is a specific
binding protein of small hepatitis B virus (HBV) envelope protein.";
Virology 197:549-557(1993).
[17]
PROTEIN SEQUENCE OF 86-131; 259-297 AND 300-320.
PubMed=2957692; DOI=10.1073/pnas.84.17.6078;
Schlaepfer D.D., Mehlman T., Burgess W.H., Haigler H.T.;
"Structural and functional characterization of endonexin II, a
calcium- and phospholipid-binding protein.";
Proc. Natl. Acad. Sci. U.S.A. 84:6078-6082(1987).
[18]
PROTEIN SEQUENCE OF 85-93.
TISSUE=Placenta;
PubMed=2974032;
Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W.,
de Haen C.;
"Sedimentation equilibrium analysis of five lipocortin-related
phospholipase A2 inhibitors from human placenta. Evidence against a
mechanistically relevant association between enzyme and inhibitor.";
J. Biol. Chem. 263:18657-18663(1988).
[19]
PROTEIN SEQUENCE OF 152-161 AND 246-260.
TISSUE=Adipocyte;
PubMed=15242332; DOI=10.1042/BJ20040647;
Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V.;
"Vectorial proteomics reveal targeting, phosphorylation and specific
fragmentation of polymerase I and transcript release factor (PTRF) at
the surface of caveolae in human adipocytes.";
Biochem. J. 383:237-248(2004).
[20]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=16916647; DOI=10.1016/j.molcel.2006.06.026;
Kim S.C., Sprung R., Chen Y., Xu Y., Ball H., Pei J., Cheng T.,
Kho Y., Xiao H., Xiao L., Grishin N.V., White M., Yang X.-J., Zhao Y.;
"Substrate and functional diversity of lysine acetylation revealed by
a proteomics survey.";
Mol. Cell 23:607-618(2006).
[21]
INVOLVEMENT IN RPRGL3.
PubMed=17339269; DOI=10.1093/hmg/ddm017;
Bogdanova N., Horst J., Chlystun M., Croucher P.J., Nebel A.,
Bohring A., Todorova A., Schreiber S., Gerke V., Krawczak M.,
Markoff A.;
"A common haplotype of the annexin A5 (ANXA5) gene promoter is
associated with recurrent pregnancy loss.";
Hum. Mol. Genet. 16:573-578(2007).
[22]
ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, CLEAVAGE OF INITIATOR
METHIONINE [LARGE SCALE ANALYSIS], AND IDENTIFICATION BY MASS
SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[23]
ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-76; LYS-79 AND
LYS-97, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[24]
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).
[25]
S-NITROSYLATION, AND DOMAIN.
PubMed=25417112; DOI=10.1016/j.cell.2014.09.032;
Jia J., Arif A., Terenzi F., Willard B., Plow E.F., Hazen S.L.,
Fox P.L.;
"Target-selective protein S-nitrosylation by sequence motif
recognition.";
Cell 159:623-634(2014).
[26]
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).
[27]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29, 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).
[28]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29, AND IDENTIFICATION BY
MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=25772364; DOI=10.1016/j.celrep.2015.02.033;
Hendriks I.A., Treffers L.W., Verlaan-de Vries M., Olsen J.V.,
Vertegaal A.C.;
"SUMO-2 orchestrates chromatin modifiers in response to DNA damage.";
Cell Rep. 10:1778-1791(2015).
[29]
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).
[30]
SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-29, 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).
[31]
X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
PubMed=2147412;
Huber R., Roemisch J., Paques E.-P.;
"The crystal and molecular structure of human annexin V, an
anticoagulant protein that binds to calcium and membranes.";
EMBO J. 9:3867-3874(1990).
[32]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=2148156; DOI=10.1016/0014-5793(90)81428-Q;
Huber R., Schneider M., Mayr I., Roemisch J., Paques E.-P.;
"The calcium binding sites in human annexin V by crystal structure
analysis at 2.0-A resolution. Implications for membrane binding and
calcium channel activity.";
FEBS Lett. 275:15-21(1990).
[33]
X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
PubMed=1311770; DOI=10.1016/0022-2836(92)90984-R;
Huber R., Berendes R., Burger A., Schneider M., Karshikov A.,
Luecke H., Roemisch J., Paques E.-P.;
"Crystal and molecular structure of human annexin V after refinement.
Implications for structure, membrane binding and ion channel formation
of the annexin family of proteins.";
J. Mol. Biol. 223:683-704(1992).
[34]
X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
PubMed=9398511; DOI=10.1006/jmbi.1997.1375;
Kaneko N., Ago H., Matsuda R., Inagaki E., Miyano M.;
"Crystal structure of annexin V with its ligand K-201 as a calcium
channel activity inhibitor.";
J. Mol. Biol. 274:16-20(1997).
[35]
X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
PubMed=9435213; DOI=10.1073/pnas.95.2.455;
Budisa N., Minks C., Medrano F.J., Lutz J., Huber R., Moroder L.;
"Residue-specific bioincorporation of non-natural, biologically active
amino acids into proteins as possible drug carriers: structure and
stability of the per-thiaproline mutant of annexin V.";
Proc. Natl. Acad. Sci. U.S.A. 95:455-459(1998).
-!- FUNCTION: This protein is an anticoagulant protein that acts as an
indirect inhibitor of the thromboplastin-specific complex, which
is involved in the blood coagulation cascade.
-!- SUBUNIT: Monomer. Binds ATRX and EIF5B (By similarity). Interacts
with hepatitis B virus (HBV). {ECO:0000250,
ECO:0000269|PubMed:8249278}.
-!- INTERACTION:
Q9BSI4:TINF2; NbExp=2; IntAct=EBI-296601, EBI-717399;
-!- DOMAIN: The [IL]-x-C-x-x-[DE] motif is a proposed target motif for
cysteine S-nitrosylation mediated by the iNOS-S100A8/A9
transnitrosylase complex. {ECO:0000305|PubMed:25417112}.
-!- DOMAIN: A pair of annexin repeats may form one binding site for
calcium and phospholipid.
-!- PTM: S-nitrosylation is induced by interferon-gamma and
oxidatively-modified low-densitity lipoprotein (LDL(ox)) possibly
implicating the iNOS-S100A8/9 transnitrosylase complex.
{ECO:0000305|PubMed:25417112}.
-!- DISEASE: Pregnancy loss, recurrent, 3 (RPRGL3) [MIM:614391]: A
common complication of pregnancy, resulting in spontaneous
abortion before the fetus has reached viability. The term includes
all miscarriages from the time of conception until 24 weeks of
gestation. Recurrent pregnancy loss is defined as 3 or more
consecutive spontaneous abortions. {ECO:0000269|PubMed:17339269}.
Note=Disease susceptibility is associated with variations
affecting the gene represented in this entry.
-!- SIMILARITY: Belongs to the annexin family. {ECO:0000305}.
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EMBL; M18366; AAA35570.1; -; mRNA.
EMBL; D00172; BAA00122.1; -; mRNA.
EMBL; X12454; CAA30985.1; -; mRNA.
EMBL; J03745; AAA52386.1; -; mRNA.
EMBL; M21731; AAA36166.1; -; mRNA.
EMBL; M19384; AAB59545.1; -; mRNA.
EMBL; U01691; AAB40047.1; -; Genomic_DNA.
EMBL; U01681; AAB40047.1; JOINED; Genomic_DNA.
EMBL; U01682; AAB40047.1; JOINED; Genomic_DNA.
EMBL; U01683; AAB40047.1; JOINED; Genomic_DNA.
EMBL; U01685; AAB40047.1; JOINED; Genomic_DNA.
EMBL; U01686; AAB40047.1; JOINED; Genomic_DNA.
EMBL; U01687; AAB40047.1; JOINED; Genomic_DNA.
EMBL; U01689; AAB40047.1; JOINED; Genomic_DNA.
EMBL; U01690; AAB40047.1; JOINED; Genomic_DNA.
EMBL; U05770; AAB60648.1; -; Genomic_DNA.
EMBL; U05760; AAB60648.1; JOINED; Genomic_DNA.
EMBL; U05761; AAB60648.1; JOINED; Genomic_DNA.
EMBL; U05762; AAB60648.1; JOINED; Genomic_DNA.
EMBL; U05764; AAB60648.1; JOINED; Genomic_DNA.
EMBL; U05765; AAB60648.1; JOINED; Genomic_DNA.
EMBL; U05766; AAB60648.1; JOINED; Genomic_DNA.
EMBL; U05767; AAB60648.1; JOINED; Genomic_DNA.
EMBL; U05768; AAB60648.1; JOINED; Genomic_DNA.
EMBL; U05769; AAB60648.1; JOINED; Genomic_DNA.
EMBL; AK312644; BAG35528.1; -; mRNA.
EMBL; CR536522; CAG38759.1; -; mRNA.
EMBL; CR541842; CAG46640.1; -; mRNA.
EMBL; AC096730; AAY40954.1; -; Genomic_DNA.
EMBL; CH471056; EAX05257.1; -; Genomic_DNA.
EMBL; CH471056; EAX05258.1; -; Genomic_DNA.
EMBL; BC001429; AAH01429.1; -; mRNA.
EMBL; BC004993; AAH04993.1; -; mRNA.
EMBL; BC012804; AAH12804.1; -; mRNA.
EMBL; BC012822; AAH12822.1; -; mRNA.
EMBL; BC018671; AAH18671.1; -; mRNA.
CCDS; CCDS3720.1; -.
PIR; D29250; AQHUP.
RefSeq; NP_001145.1; NM_001154.3.
UniGene; Hs.480653; -.
PDB; 1ANW; X-ray; 2.40 A; A/B=2-320.
PDB; 1ANX; X-ray; 1.90 A; A/B/C=2-320.
PDB; 1AVH; X-ray; 2.30 A; A/B=1-320.
PDB; 1AVR; X-ray; 2.30 A; A=1-320.
PDB; 1HAK; X-ray; 3.00 A; A/B=1-320.
PDB; 1HVD; X-ray; 2.00 A; A=2-320.
PDB; 1HVE; X-ray; 2.30 A; A=2-320.
PDB; 1HVF; X-ray; 2.00 A; A=2-320.
PDB; 1HVG; X-ray; 3.00 A; A=2-320.
PDB; 1SAV; X-ray; 2.50 A; A=1-320.
PDB; 2XO2; X-ray; 2.80 A; A=1-320.
PDB; 2XO3; X-ray; 2.30 A; A=1-320.
PDBsum; 1ANW; -.
PDBsum; 1ANX; -.
PDBsum; 1AVH; -.
PDBsum; 1AVR; -.
PDBsum; 1HAK; -.
PDBsum; 1HVD; -.
PDBsum; 1HVE; -.
PDBsum; 1HVF; -.
PDBsum; 1HVG; -.
PDBsum; 1SAV; -.
PDBsum; 2XO2; -.
PDBsum; 2XO3; -.
ProteinModelPortal; P08758; -.
SMR; P08758; -.
BioGrid; 106805; 42.
IntAct; P08758; 44.
MINT; MINT-1382250; -.
STRING; 9606.ENSP00000296511; -.
DrugBank; DB02929; K201.
DrugBank; DB03484; L-Alpha-Glycerophosphorylethanolamine.
DrugBank; DB02497; L-Alpha-Glycerophosphorylserine.
DrugBank; DB02846; L-thioproline.
TCDB; 1.A.31.1.7; the annexin (annexin) family.
iPTMnet; P08758; -.
PhosphoSitePlus; P08758; -.
SwissPalm; P08758; -.
BioMuta; ANXA5; -.
DMDM; 113960; -.
OGP; P08758; -.
REPRODUCTION-2DPAGE; IPI00329801; -.
REPRODUCTION-2DPAGE; P08758; -.
EPD; P08758; -.
PaxDb; P08758; -.
PeptideAtlas; P08758; -.
PRIDE; P08758; -.
TopDownProteomics; P08758; -.
DNASU; 308; -.
Ensembl; ENST00000296511; ENSP00000296511; ENSG00000164111.
GeneID; 308; -.
KEGG; hsa:308; -.
CTD; 308; -.
DisGeNET; 308; -.
EuPathDB; HostDB:ENSG00000164111.14; -.
GeneCards; ANXA5; -.
HGNC; HGNC:543; ANXA5.
HPA; CAB003677; -.
HPA; HPA035330; -.
MalaCards; ANXA5; -.
MIM; 131230; gene.
MIM; 614391; phenotype.
neXtProt; NX_P08758; -.
OpenTargets; ENSG00000164111; -.
PharmGKB; PA24833; -.
eggNOG; KOG0819; Eukaryota.
eggNOG; ENOG410XPUN; LUCA.
GeneTree; ENSGT00760000118972; -.
HOGENOM; HOG000158803; -.
HOVERGEN; HBG061815; -.
InParanoid; P08758; -.
KO; K16646; -.
OMA; FAETLYY; -.
OrthoDB; EOG091G0H6H; -.
PhylomeDB; P08758; -.
TreeFam; TF105452; -.
Reactome; R-HSA-114608; Platelet degranulation.
SignaLink; P08758; -.
ChiTaRS; ANXA5; human.
EvolutionaryTrace; P08758; -.
GeneWiki; Annexin_A5; -.
GenomeRNAi; 308; -.
PRO; PR:P08758; -.
Proteomes; UP000005640; Chromosome 4.
Bgee; ENSG00000164111; -.
CleanEx; HS_ANXA5; -.
ExpressionAtlas; P08758; baseline and differential.
Genevisible; P08758; HS.
GO; GO:0005737; C:cytoplasm; TAS:UniProtKB.
GO; GO:0005829; C:cytosol; TAS:Reactome.
GO; GO:0072563; C:endothelial microparticle; IEA:Ensembl.
GO; GO:0009897; C:external side of plasma membrane; IEA:Ensembl.
GO; GO:0070062; C:extracellular exosome; IDA:UniProtKB.
GO; GO:0005576; C:extracellular region; TAS:Reactome.
GO; GO:0005925; C:focal adhesion; IDA:UniProtKB.
GO; GO:0005622; C:intracellular; IDA:LIFEdb.
GO; GO:0016020; C:membrane; IDA:UniProtKB.
GO; GO:0005509; F:calcium ion binding; IEA:InterPro.
GO; GO:0005544; F:calcium-dependent phospholipid binding; IDA:UniProtKB.
GO; GO:0004859; F:phospholipase inhibitor activity; TAS:ProtInc.
GO; GO:0005543; F:phospholipid binding; TAS:ProtInc.
GO; GO:0007596; P:blood coagulation; IEA:UniProtKB-KW.
GO; GO:0043066; P:negative regulation of apoptotic process; TAS:UniProtKB.
GO; GO:0050819; P:negative regulation of coagulation; IEA:InterPro.
GO; GO:0002576; P:platelet degranulation; TAS:Reactome.
GO; GO:0010033; P:response to organic substance; IEA:Ensembl.
GO; GO:0007165; P:signal transduction; TAS:UniProtKB.
Gene3D; 1.10.220.10; -; 4.
InterPro; IPR001464; Annexin.
InterPro; IPR018502; Annexin_repeat.
InterPro; IPR018252; Annexin_repeat_CS.
InterPro; IPR002392; ANX5.
PANTHER; PTHR10502:SF140; PTHR10502:SF140; 1.
Pfam; PF00191; Annexin; 4.
PRINTS; PR00196; ANNEXIN.
PRINTS; PR00201; ANNEXINV.
SMART; SM00335; ANX; 4.
PROSITE; PS00223; ANNEXIN; 4.
1: Evidence at protein level;
3D-structure; Acetylation; Annexin; Blood coagulation; Calcium;
Calcium/phospholipid-binding; Complete proteome;
Direct protein sequencing; Hemostasis; Isopeptide bond;
Phosphoprotein; Reference proteome; Repeat; S-nitrosylation;
Ubl conjugation.
INIT_MET 1 1 Removed. {ECO:0000244|PubMed:19413330,
ECO:0000269|PubMed:2963810}.
CHAIN 2 320 Annexin A5.
/FTId=PRO_0000067487.
REPEAT 24 84 Annexin 1.
REPEAT 96 156 Annexin 2.
REPEAT 180 240 Annexin 3.
REPEAT 255 315 Annexin 4.
MOTIF 314 319 [IL]-x-C-x-x-[DE] motif.
{ECO:0000305|PubMed:25417112}.
MOD_RES 2 2 N-acetylalanine.
{ECO:0000244|PubMed:19413330}.
MOD_RES 37 37 Phosphoserine.
{ECO:0000250|UniProtKB:P48036}.
MOD_RES 70 70 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 76 76 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 79 79 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 97 97 N6-acetyllysine.
{ECO:0000244|PubMed:19608861}.
MOD_RES 101 101 N6-acetyllysine.
{ECO:0000244|PubMed:16916647}.
MOD_RES 290 290 N6-succinyllysine.
{ECO:0000250|UniProtKB:P48036}.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO1).
{ECO:0000244|PubMed:25114211}.
CROSSLNK 29 29 Glycyl lysine isopeptide (Lys-Gly)
(interchain with G-Cter in SUMO2).
{ECO:0000244|PubMed:25772364,
ECO:0000244|PubMed:28112733}.
CONFLICT 135 135 S -> L (in Ref. 10; CAG38759).
{ECO:0000305}.
CONFLICT 279 279 I -> T (in Ref. 13; AAH18671).
{ECO:0000305}.
HELIX 17 28 {ECO:0000244|PDB:1ANX}.
STRAND 29 32 {ECO:0000244|PDB:1ANX}.
HELIX 35 43 {ECO:0000244|PDB:1ANX}.
HELIX 47 61 {ECO:0000244|PDB:1ANX}.
HELIX 65 72 {ECO:0000244|PDB:1ANX}.
HELIX 75 85 {ECO:0000244|PDB:1ANX}.
HELIX 88 100 {ECO:0000244|PDB:1ANX}.
STRAND 102 104 {ECO:0000244|PDB:1ANX}.
HELIX 107 116 {ECO:0000244|PDB:1ANX}.
HELIX 119 133 {ECO:0000244|PDB:1ANX}.
HELIX 137 144 {ECO:0000244|PDB:1ANX}.
HELIX 147 157 {ECO:0000244|PDB:1ANX}.
HELIX 169 182 {ECO:0000244|PDB:1ANX}.
TURN 183 185 {ECO:0000244|PDB:1ANX}.
STRAND 186 188 {ECO:0000244|PDB:1ANX}.
HELIX 191 200 {ECO:0000244|PDB:1ANX}.
HELIX 203 217 {ECO:0000244|PDB:1ANX}.
HELIX 221 228 {ECO:0000244|PDB:1ANX}.
HELIX 231 245 {ECO:0000244|PDB:1ANX}.
HELIX 247 256 {ECO:0000244|PDB:1ANX}.
HELIX 257 259 {ECO:0000244|PDB:1ANX}.
STRAND 260 263 {ECO:0000244|PDB:1ANX}.
HELIX 266 276 {ECO:0000244|PDB:1ANX}.
TURN 277 280 {ECO:0000244|PDB:1ANX}.
HELIX 281 290 {ECO:0000244|PDB:1ANX}.
STRAND 292 294 {ECO:0000244|PDB:1HVG}.
HELIX 296 303 {ECO:0000244|PDB:1ANX}.
HELIX 306 316 {ECO:0000244|PDB:1ANX}.
SEQUENCE 320 AA; 35937 MW; 45E14E3964BA4D1A CRC64;
MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL
FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE
ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF
QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV
VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI
KGDTSGDYKK ALLLLCGEDD


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