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P08758 (ANXA5_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 169. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (4) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended 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
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length320 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence 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 processBlood coagulation
Hemostasis
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
   PTMAcetylation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processblood coagulation

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of apoptotic process

Traceable author statement PubMed 16130169. Source: UniProtKB

negative regulation of catalytic activity

Traceable author statement Ref.6. Source: GOC

negative regulation of coagulation

Inferred from electronic annotation. Source: InterPro

response to organic substance

Inferred from electronic annotation. Source: Ensembl

signal transduction

Traceable author statement PubMed 16130169. Source: UniProtKB

   Cellular_componentcytoplasm

Traceable author statement PubMed 16130169. Source: UniProtKB

endothelial microparticle

Inferred from electronic annotation. Source: Ensembl

external side of plasma membrane

Inferred from electronic annotation. Source: Ensembl

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

intracellular

Inferred from direct assay. Source: LIFEdb

   Molecular_functioncalcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipid binding

Inferred from direct assay PubMed 2138016. Source: UniProtKB

phospholipase inhibitor activity

Traceable author statement Ref.6. Source: ProtInc

phospholipid binding

Traceable author statement Ref.4. Source: ProtInc

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.2 Ref.22
Chain2 – 320319Annexin A5
PRO_0000067487

Regions

Repeat24 – 8461Annexin 1
Repeat96 – 15661Annexin 2
Repeat180 – 24061Annexin 3
Repeat255 – 31561Annexin 4

Amino acid modifications

Modified residue21N-acetylalanine Ref.1 Ref.22
Modified residue701N6-acetyllysine Ref.23
Modified residue761N6-acetyllysine Ref.23
Modified residue791N6-acetyllysine Ref.23
Modified residue971N6-acetyllysine Ref.23
Modified residue1011N6-acetyllysine Ref.20
Modified residue2901N6-succinyllysine By similarity

Experimental info

Sequence conflict1351S → L in CAG38759. Ref.10
Sequence conflict2791I → T in AAH18671. Ref.13

Secondary structure

.................................................. 320
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
P08758 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 45E14E3964BA4D1A

FASTA32035,937
        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 

« Hide

References

« Hide '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. expand/collapse author list , 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. expand/collapse author list , 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. expand/collapse author list , 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, IDENTIFICATION BY 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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
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]"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
[23]"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, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[24]"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].
[25]"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).
[26]"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).
[27]"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).
[28]"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).
[29]"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.

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 expand/collapse EMBL AC list , U01681, U01682, U01683, U01685, U01686, U01687, U01689, U01690 Genomic DNA. Translation: AAB40047.1.
U05770 expand/collapse EMBL AC list , 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.
PIRAQHUP. D29250.
RefSeqNP_001145.1. NM_001154.3.
UniGeneHs.480653.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1ANWX-ray2.40A/B2-319[»]
1ANXX-ray1.90A/B/C2-319[»]
1AVHX-ray2.30A/B1-320[»]
1AVRX-ray2.30A1-320[»]
1HAKX-ray3.00A/B1-320[»]
1HVDX-ray2.00A2-319[»]
1HVEX-ray2.30A2-319[»]
1HVFX-ray2.00A2-319[»]
1HVGX-ray3.00A2-319[»]
1SAVX-ray2.50A1-320[»]
2XO2X-ray2.80A2-320[»]
2XO3X-ray2.30A1-320[»]
ProteinModelPortalP08758.
SMRP08758. Positions 3-318.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106805. 30 interactions.
IntActP08758. 16 interactions.
MINTMINT-1382250.
STRING9606.ENSP00000296511.

PTM databases

PhosphoSiteP08758.

Polymorphism databases

DMDM113960.

2D gel databases

OGPP08758.
REPRODUCTION-2DPAGEIPI00329801.
P08758.

Proteomic databases

PaxDbP08758.
PeptideAtlasP08758.
PRIDEP08758.

Protocols and materials databases

DNASU308.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000296511; ENSP00000296511; ENSG00000164111.
GeneID308.
KEGGhsa:308.
UCSCuc003idu.4. human.

Organism-specific databases

CTD308.
GeneCardsGC04M122589.
HGNCHGNC:543. ANXA5.
HPACAB003677.
HPA035330.
MIM131230. gene.
614391. phenotype.
neXtProtNX_P08758.
PharmGKBPA24833.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG281174.
HOGENOMHOG000158803.
HOVERGENHBG061815.
InParanoidP08758.
KOK16646.
OMAKVFDAYM.
OrthoDBEOG74XS72.
PhylomeDBP08758.
TreeFamTF105452.

Enzyme and pathway databases

SignaLinkP08758.

Gene expression databases

ArrayExpressP08758.
BgeeP08758.
CleanExHS_ANXA5.
GenevestigatorP08758.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR015473. Annexins_V.
IPR002392. AnnexinV.
[Graphical view]
PANTHERPTHR10502:SF26. PTHR10502:SF26. 1 hit.
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00201. ANNEXINV.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
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ChiTaRSANXA5. human.
EvolutionaryTraceP08758.
GeneWikiAnnexin_A5.
GenomeRNAi308.
NextBio1243.
PROP08758.
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Entry information

Entry nameANXA5_HUMAN
AccessionPrimary (citable) accession number: P08758
Secondary accession number(s): D3DNW7 expand/collapse secondary AC list , Q6FHB3, Q6FI16, Q8WV69, Q9UDH9
Entry history
Integrated into UniProtKB/Swiss-Prot: November 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 169 of the entry and version 2 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny 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.

Relevant documents

SIMILARITY comments

Index of protein domains and families

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

Human chromosome 4

Human chromosome 4: entries, gene names and cross-references to MIM