P08758 (ANXA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Annexin A5

Alternative name(s):
Anchorin CII
Annexin V
Annexin-5
Calphobindin I
Short name=CBP-I
Endonexin II
Lipocortin V
Placental anticoagulant protein 4
Short name=PP4
Placental anticoagulant protein I
Short name=PAP-I
Thromboplastin inhibitor
Vascular anticoagulant-alpha
Short name=VAC-alpha

Gene names

Name:	ANXA5
Synonyms:	ANX5, ENX2, PP4

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo

Protein attributes

Sequence length	320 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

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 structure	Monomer. Binds ATRX and EIF5B By similarity. Interacts with hepatitis B virus (HBV). Ref.16
Domain	A pair of annexin repeats may form one binding site for calcium and phospholipid.
Involvement in 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. Note: Disease susceptibility is associated with variations affecting the gene represented in this entry. Ref.21
Sequence similarities	Belongs to the annexin family. Contains 4 annexin repeats.

Ontologies

Keywords
Biological process	Blood coagulation Hemostasis
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation
Technical term	3D-structure Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	blood coagulation Inferred from electronic annotation. Source: UniProtKB-KW negative regulation of apoptotic process Traceable author statement PubMed 16130169. Source: UniProtKB negative regulation of coagulation Inferred from electronic annotation. Source: InterPro response to organic substance Inferred from electronic annotation. Source: Compara signal transduction Traceable author statement PubMed 16130169. Source: UniProtKB
Cellular_component	cytoplasm Traceable author statement PubMed 16130169. Source: UniProtKB endothelial microparticle Inferred from electronic annotation. Source: Compara external side of plasma membrane Inferred from electronic annotation. Source: Compara extracellular vesicular exosome Inferred from direct assay PubMed 21362503. Source: UniProtKB
Molecular_function	calcium ion binding Inferred from electronic annotation. Source: InterPro calcium-dependent phospholipid binding Inferred from direct assay PubMed 2138016. Source: UniProtKB eukaryotic cell surface binding Inferred from electronic annotation. Source: Compara phospholipase inhibitor activity Traceable author statement Ref.6. Source: ProtInc
Complete GO annotation...

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

1

1

Removed Ref.2

Chain

2 – 320

319

Annexin A5

PRO_0000067487

Regions

Repeat

24 – 84

61

Annexin 1

Repeat

96 – 156

61

Annexin 2

Repeat

180 – 240

61

Annexin 3

Repeat

255 – 315

61

Annexin 4

Amino acid modifications

Modified residue

2

1

N-acetylalanine By similarity

Modified residue

70

1

N6-acetyllysine Ref.22

Modified residue

76

1

N6-acetyllysine Ref.22

Modified residue

79

1

N6-acetyllysine Ref.22

Modified residue

97

1

N6-acetyllysine Ref.22

Modified residue

101

1

N6-acetyllysine Ref.20

Experimental info

Sequence conflict

135

1

S → L in CAG38759. Ref.10

Sequence conflict

279

1

I → T in AAH18671. Ref.13

Secondary structure

1

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

.

320

Helix Strand Turn

Details...

Helix

17 – 28

12

Beta strand

29 – 32

4

Helix

35 – 43

9

Helix

47 – 61

15

Helix

65 – 72

8

Helix

75 – 85

11

Helix

88 – 100

13

Beta strand

102 – 104

3

Helix

107 – 116

10

Helix

119 – 133

15

Helix

137 – 144

8

Helix

147 – 157

11

Helix

169 – 182

14

Turn

183 – 185

3

Beta strand

186 – 188

3

Helix

191 – 200

10

Helix

203 – 217

15

Helix

221 – 228

8

Helix

231 – 245

15

Helix

247 – 256

10

Helix

257 – 259

3

Beta strand

260 – 263

4

Helix

266 – 276

11

Turn

277 – 280

4

Helix

281 – 290

10

Beta strand

292 – 294

3

Helix

296 – 303

8

Helix

306 – 316

11

Sequences

	Sequence		Length	Mass (Da)
	P08758 [UniParc]. Last modified January 23, 2007. Version 2. Checksum: 45E14E3964BA4D1A	FASTA	320	35,937
	10 20 30 40 50 60 MAQVLRGTVT DFPGFDERAD AETLRKAMKG LGTDEESILT LLTSRSNAQR QEISAAFKTL 70 80 90 100 110 120 FGRDLLDDLK SELTGKFEKL IVALMKPSRL YDAYELKHAL KGAGTNEKVL TEIIASRTPE 130 140 150 160 170 180 ELRAIKQVYE EEYGSSLEDD VVGDTSGYYQ RMLVVLLQAN RDPDAGIDEA QVEQDAQALF 190 200 210 220 230 240 QAGELKWGTD EEKFITIFGT RSVSHLRKVF DKYMTISGFQ IEETIDRETS GNLEQLLLAV 250 260 270 280 290 300 VKSIRSIPAY LAETLYYAMK GAGTDDHTLI RVMVSRSEID LFNIRKEFRK NFATSLYSMI 310 320 KGDTSGDYKK ALLLLCGEDD

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Primary structure of human placental anticoagulant protein." Funakoshi T., Hendrickson L.E., McMullen B.A., Fujikawa K. Biochemistry 26:8087-8092(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Structure and expression of cDNA for an inhibitor of blood coagulation isolated from human placenta: a new lipocortin-like protein." 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. J. Biochem. 102:1261-1273(1987) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-320.
[3]	"Cloning and expression of cDNA for human vascular anticoagulant, a Ca2+-dependent phospholipid-binding protein." Maurer-Fogy I., Reutelingsperger C.P.M., Pieters J., Bodo G., Stratowa C., Hauptmann R. Eur. J. Biochem. 174:585-592(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCE.
[4]	"Cloning and expression of cDNA for human endonexin II, a Ca2+ and phospholipid binding protein." Kaplan R., Jaye M., Burgess W.H., Schlaepfer D.D., Haigler H.T. J. Biol. Chem. 263:8037-8043(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[5]	"Five distinct calcium and phospholipid binding proteins share homology with lipocortin I." 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. J. Biol. Chem. 263:10799-10811(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[6]	"Characterization of cDNA encoding human placental anticoagulant protein (PP4): homology with the lipocortin family." Grundmann U., Abel K.-J., Bohn H., Loebermann H., Lottspeich F., Kuepper H. Proc. Natl. Acad. Sci. U.S.A. 85:3708-3712(1988) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[7]	"The gene encoding human annexin V has a TATA-less promoter with a high G+C content." Fernandez M.-P., Morgan R.O., Fernandez M.R., Carcedo M.-T. Gene 149:253-260(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA]. Tissue: Lung.
[8]	"Organization of the human annexin V (ANX5) gene." Cookson B.T., Engelhardt S., Smith C., Bamford H.A., Prochazka M., Tait J.F. Genomics 20:463-467(1994) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[9]	"Complete sequencing and characterization of 21,243 full-length human cDNAs." 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. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Neuroblastoma.
[10]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." 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. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[11]	"Generation and annotation of the DNA sequences of human chromosomes 2 and 4." 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. Nature 434:724-731(2005) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[12]	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 Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[13]	"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)." The MGC Project Team Genome Res. 14:2121-2127(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Muscle, Ovary and Skin.
[14]	"A 32 kDa lipocortin from human mononuclear cells appears to be identical with the placental inhibitor of blood coagulation." Rothhut R., Comera C., Cortial S., Haumont P.-Y., Diep Le K.H., Cavadore J.-C., Conard J., Russo-Marie F., Lederer F. Biochem. J. 263:929-935(1989) [PubMed] [Europe PMC] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE.
[15]	Quadroni M., Potts A., Barblan J., Bienvenut W.V. Submitted (JAN-2005) to UniProtKB Cited for: PROTEIN SEQUENCE OF 7-18; 30-45; 187-201 AND 277-286, MASS SPECTROMETRY. Tissue: Melanoma.
[16]	"Endonexin II, present on human liver plasma membranes, is a specific binding protein of small hepatitis B virus (HBV) envelope protein." Hertogs K., Leenders W.P., Depla E., De Bruin W.C., Meheus L., Raymackers J., Moshage H., Yap S.H. Virology 197:549-557(1993) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 21-31; 93-108; 176-188 AND 304-319, INTERACTION WITH HBV.
[17]	"Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein." Schlaepfer D.D., Mehlman T., Burgess W.H., Haigler H.T. Proc. Natl. Acad. Sci. U.S.A. 84:6078-6082(1987) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 86-131; 259-297 AND 300-320.
[18]	"Sedimentation equilibrium analysis of five lipocortin-related phospholipase A2 inhibitors from human placenta. Evidence against a mechanistically relevant association between enzyme and inhibitor." Ahn N.G., Teller D.C., Bienkowski M.J., McMullen B.A., Lipkin E.W., de Haen C. J. Biol. Chem. 263:18657-18663(1988) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 85-93. Tissue: Placenta.
[19]	"Vectorial proteomics reveal targeting, phosphorylation and specific fragmentation of polymerase I and transcript release factor (PTRF) at the surface of caveolae in human adipocytes." Aboulaich N., Vainonen J.P., Stralfors P., Vener A.V. Biochem. J. 383:237-248(2004) [PubMed] [Europe PMC] [Abstract] Cited for: PROTEIN SEQUENCE OF 152-161 AND 246-260. Tissue: Adipocyte.
[20]	"Substrate and functional diversity of lysine acetylation revealed by a proteomics survey." 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. Mol. Cell 23:607-618(2006) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-101, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"A common haplotype of the annexin A5 (ANXA5) gene promoter is associated with recurrent pregnancy loss." Bogdanova N., Horst J., Chlystun M., Croucher P.J., Nebel A., Bohring A., Todorova A., Schreiber S., Gerke V., Krawczak M., Markoff A. Hum. Mol. Genet. 16:573-578(2007) [PubMed] [Europe PMC] [Abstract] Cited for: INVOLVEMENT IN RPRGL3.
[22]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-70; LYS-76; LYS-79 AND LYS-97, MASS SPECTROMETRY.
[23]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]	"The crystal and molecular structure of human annexin V, an anticoagulant protein that binds to calcium and membranes." Huber R., Roemisch J., Paques E.-P. EMBO J. 9:3867-3874(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[25]	"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." Huber R., Schneider M., Mayr I., Roemisch J., Paques E.-P. FEBS Lett. 275:15-21(1990) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[26]	"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." Huber R., Berendes R., Burger A., Schneider M., Karshikov A., Luecke H., Roemisch J., Paques E.-P. J. Mol. Biol. 223:683-704(1992) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS).
[27]	"Crystal structure of annexin V with its ligand K-201 as a calcium channel activity inhibitor." Kaneko N., Ago H., Matsuda R., Inagaki E., Miyano M. J. Mol. Biol. 274:16-20(1997) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (3.0 ANGSTROMS).
[28]	"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." Budisa N., Minks C., Medrano F.J., Lutz J., Huber R., Moroder L. Proc. Natl. Acad. Sci. U.S.A. 95:455-459(1998) [PubMed] [Europe PMC] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.3 ANGSTROMS).
+	Additional computationally mapped references.

Web resources

R&D Systems' cytokine source book: Annexin V

Cross-references

Sequence databases

EMBL
GenBank
DDBJ

M18366 mRNA. Translation: AAA35570.1.
D00172 mRNA. Translation: BAA00122.1.
X12454 mRNA. Translation: CAA30985.1.
J03745 mRNA. Translation: AAA52386.1.
M21731 mRNA. Translation: AAA36166.1.
M19384 mRNA. Translation: AAB59545.1.
U01691 , U01681, U01682, U01683, U01685, U01686, U01687, U01689, U01690 Genomic DNA. Translation: AAB40047.1.
U05770 , U05760, U05761, U05762, U05764, U05765, U05766, U05767, U05768, U05769 Genomic DNA. Translation: AAB60648.1.
AK312644 mRNA. Translation: BAG35528.1.
CR536522 mRNA. Translation: CAG38759.1.
CR541842 mRNA. Translation: CAG46640.1.
AC096730 Genomic DNA. Translation: AAY40954.1.
CH471056 Genomic DNA. Translation: EAX05257.1.
CH471056 Genomic DNA. Translation: EAX05258.1.
BC001429 mRNA. Translation: AAH01429.1.
BC004993 mRNA. Translation: AAH04993.1.
BC012804 mRNA. Translation: AAH12804.1.
BC012822 mRNA. Translation: AAH12822.1.
BC018671 mRNA. Translation: AAH18671.1.

IPI

IPI00329801.

PIR

AQHUP. D29250.

RefSeq

NP_001145.1. NM_001154.3.

UniGene

Hs.480653.

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1ANW	X-ray	2.40	A/B	2-319	[»]
1ANX	X-ray	1.90	A/B/C	2-319	[»]
1AVH	X-ray	2.30	A/B	1-320	[»]
1AVR	X-ray	2.30	A	1-320	[»]
1HAK	X-ray	3.00	A/B	1-320	[»]
1HVD	X-ray	2.00	A	2-319	[»]
1HVE	X-ray	2.30	A	2-319	[»]
1HVF	X-ray	2.00	A	2-319	[»]
1HVG	X-ray	3.00	A	2-319	[»]
1SAV	X-ray	2.50	A	1-320	[»]
2XO2	X-ray	2.80	A	2-320	[»]
2XO3	X-ray	2.30	A	1-320	[»]

ProteinModelPortal

P08758.

ModBase

Search...

Protein-protein interaction databases

IntAct

P08758. 16 interactions.

MINT

MINT-1382250.

STRING

9606.ENSP00000296511.

PTM databases

PhosphoSite

P08758.

Polymorphism databases

DMDM

113960.

2D gel databases

OGP

P08758.

REPRODUCTION-2DPAGE

IPI00329801.
P08758.

Proteomic databases

PaxDb

P08758.

PeptideAtlas

P08758.

PRIDE

P08758.

Protocols and materials databases

DNASU

308.

StructuralBiologyKnowledgebase

Search...

Genome annotation databases

Ensembl

ENST00000296511; ENSP00000296511; ENSG00000164111.

GeneID

308.

KEGG

hsa:308.

UCSC

uc003idu.4. human.

Organism-specific databases

CTD

308.

GeneCards

GC04M122589.

HGNC

HGNC:543. ANXA5.

HPA

CAB003677.

MIM

131230. gene.
614391. phenotype.

neXtProt

NX_P08758.

PharmGKB

PA24833.

GenAtlas

Search...

Phylogenomic databases

eggNOG

NOG281174.

HOGENOM

HOG000158803.

HOVERGEN

HBG061815.

InParanoid

P08758.

KO

K16646.

OMA

RGTVTAF.

OrthoDB

EOG4W9J4D.

PhylomeDB

P08758.

Gene expression databases

ArrayExpress

P08758.

Bgee

P08758.

CleanEx

HS_ANXA5.

Genevestigator

P08758.

GermOnline

ENSG00000164111. Homo sapiens.

Family and domain databases

Gene3D

1.10.220.10. 4 hits.

InterPro

IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR015473. Annexins_V.
IPR002392. AnnexinV.
[Graphical view]

PANTHER

PTHR10502. PTHR10502. 1 hit.
PTHR10502:SF26. PTHR10502:SF26. 1 hit.

Pfam

PF00191. Annexin. 4 hits.
[Graphical view]

PRINTS

PR00196. ANNEXIN.
PR00201. ANNEXINV.

SMART

SM00335. ANX. 4 hits.
[Graphical view]

SUPFAM

SSF47874. Annexin. 1 hit.

PROSITE

PS00223. ANNEXIN. 4 hits.
[Graphical view]

ProtoNet

Search...

Other

ChiTaRS

ANXA5. human.

EvolutionaryTrace

P08758.

GenomeRNAi

308.

NextBio

1243.

SOURCE

Search...

Entry information

Entry name

ANXA5_HUMAN

Accession

Primary (citable) accession number: P08758
Secondary accession number(s): D3DNW7 , Q6FHB3, Q6FI16, Q8WV69, Q9UDH9

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1988
Last sequence update:	January 23, 2007
Last modified:	May 1, 2013
This is version 160 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.