Annexin A2 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P07355 (ANXA2_HUMAN)

Last modified July 22, 2008. Version 112. History...

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Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

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Names and origin

Protein names

Recommended name:
    Annexin A2
      Short name(s)=Annexin-2
Alternative name(s):
    Annexin II
    Lipocortin II
    Calpactin I heavy chain
    Chromobindin-8
    p36
    Protein I
    Placental anticoagulant protein IV
      Short name(s)=PAP-IV

Gene names

Name:	ANXA2
Synonyms:	ANX2, ANX2L4, CAL1H, LPC2D

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

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Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

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.
Subunit structure	Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2/p36.
Subcellular location	Secreted › extracellular space › extracellular matrix › basement membrane. Melanosome. 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.
Domain	A pair of annexin repeats may form one binding site for calcium and phospholipid.
Post-translational modification	Phosphorylation of Tyr-24 enhances heat stress-induced translocation to the cell surface.
Miscellaneous	It may cross-link plasma membrane phospholipids with actin and the cytoskeleton and be involved with exocytosis.
Sequence similarities	Belongs to the annexin family. Contains 4 annexin repeats.

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Ontologies

Keywords
Cellular component	Basement membrane Extracellular matrix Secreted
Coding sequence diversity	Polymorphism
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation Phosphoprotein
Technical term	3D-structure Direct protein sequencing
Gene Ontology (GO)
Biological process	skeletal development Traceable author statement. Source: ProtInc
Cellular component	plasma membrane Traceable author statement. Source: ProtInc soluble fraction Traceable author statement. Source: ProtInc
Molecular function	phospholipase inhibitor activity Ref.1 Traceable author statement. Source: ProtInc protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
PPM1B	O75688	1	EBI-352622,EBI-1047039

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Molecule processing

Initiator methionine

Removed

Chain

2 – 339

338

Annexin A2

Regions

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 Potential

Amino acid modifications

Modified residue

N-acetylserine

Modified residue

Phosphoserine

Modified residue

Phosphothreonine

Modified residue

Phosphotyrosine; by SRC

Modified residue

Phosphoserine; by PKC

Modified residue

Phosphotyrosine

Modified residue

188

Phosphotyrosine By similarity

Natural variations

Natural variant

V → L

Experimental info

Mutagenesis

Y → A: Abolishes heat stress-induced cell surface localization

Sequence conflict

A → P AA sequence Ref.7

Secondary structure

339

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P07355-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 5126E1337A0CBEA1
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FASTA

339

38,604

        10         20         30         40         50         60 
MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL 

        70         80         90        100        110        120 
TNRSNAQRQD IAFAYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG 

       130        140        150        160        170        180 
LGTDEDSLIE IICSRTNQEL QEINRVYKEM YKTDLEKDII SDTSGDFRKL MVALAKGRRA 

       190        200        210        220        230        240 
EDGSVIDYEL IDQDARDLYD AGVKRKGTDV PKWISIMTER SVPHLQKVFD RYKSYSPYDM 

       250        260        270        280        290        300 
LESIRKEVKG DLENAFLNLV QCIQNKPLYF ADRLYDSMKG KGTRDKVLIR IMVSRSEVDM 

       310        320        330 
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Two human 35 kd inhibitors of phospholipase A2 are related to substrates of pp60v-src and of the epidermal growth factor receptor/kinase." 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. Cell 46:191-199(1986) [PubMed: 3013422] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA]. Tissue: Placenta.
[2]	"Characterization of the human lipocortin-2-encoding multigene family: its structure suggests the existence of a short amino acid unit undergoing duplication." Spano F., Raugei G., Palla E., Colella C., Melli M. Gene 95:243-251(1990) [PubMed: 2174397] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[3]	"Cloning of human full-length CDSs in BD Creator(TM) system donor vector." 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. Submitted (MAY-2003) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT LEU-98. Tissue: Brain, Colon, Pancreas, Prostate, Skin and Testis.
[5]	Bienvenut W.V., Murray L., Brunton V.G., Frame M.C., Bensaad K., Vousden K.H. Submitted (FEB-2008) to UniProtKB Cited for: 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, MASS SPECTROMETRY. Tissue: Colon adenocarcinoma and Osteosarcoma.
[6]	"The protein-tyrosine kinase substrate, calpactin I heavy chain (p36), is part of the primer recognition protein complex that interacts with DNA polymerase alpha." Jindal H.K., Chaney W.G., Anderson C.W., Davis R.G., Vishwanatha J.K. J. Biol. Chem. 266:5169-5176(1991) [PubMed: 1825830] [Abstract] Cited for: PROTEIN SEQUENCE OF 11-27; 49-62; 68-77; 120-135; 314-323 AND 329-339.
[7]	"Identification and characterization of alpha-protein kinase C binding proteins in normal and transformed REF52 cells." Hyatt S.L., Liao L., Chapline C., Jaken S. Biochemistry 33:1223-1228(1994) [PubMed: 8110754] [Abstract] Cited for: PROTEIN SEQUENCE OF 15-40 AND 50-63.
[8]	"An endothelial cell-surface form of annexin II binds human cytomegalovirus." Wright J.F., Kurosky A., Wasi S. Biochem. Biophys. Res. Commun. 198:983-989(1994) [PubMed: 8117306] [Abstract] Cited for: PROTEIN SEQUENCE OF 18-37; 119-126; 172-191 AND 301-307.
[9]	"Annexin II is a major component of fusogenic endosomal vesicles." Emans N., Gorvel J.P., Walter C., Gerke V., Kellner R., Griffiths G., Gruenberg J. J. Cell Biol. 120:1357-1369(1993) [PubMed: 8449982] [Abstract] Cited for: PROTEIN SEQUENCE OF 234-241 AND 252-261.
[10]	"The protein-tyrosine kinase substrate p36 is also a substrate for protein kinase C in vitro and in vivo." Gould K.L., Woodgett J.R., Isacke C.M., Hunter T. Mol. Cell. Biol. 6:2738-2744(1986) [PubMed: 2946940] [Abstract] Cited for: PHOSPHORYLATION AT SER-26.
[11]	"An annexin 2 phosphorylation switch mediates p11-dependent translocation of annexin 2 to the cell surface." Deora A.B., Kreitzer G., Jacovina A.T., Hajjar K.A. J. Biol. Chem. 279:43411-43418(2004) [PubMed: 15302870] [Abstract] Cited for: PHOSPHORYLATION AT TYR-24, MUTAGENESIS OF TYR-24.
[12]	"Time-resolved mass spectrometry of tyrosine phosphorylation sites in the epidermal growth factor receptor signaling network reveals dynamic modules." Zhang Y., Wolf-Yadlin A., Ross P.L., Pappin D.J., Rush J., Lauffenburger D.A., White F.M. Mol. Cell. Proteomics 4:1240-1250(2005) [PubMed: 15951569] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-30, MASS SPECTROMETRY. Tissue: Epithelium.
[13]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19, MASS SPECTROMETRY. Tissue: Epithelium.
[14]	"Proteomic and bioinformatic characterization of the biogenesis and function of melanosomes." 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. J. Proteome Res. 5:3135-3144(2006) [PubMed: 17081065] [Abstract] Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[15]	"Phosphoproteome analysis of the human mitotic spindle." Nousiainen M., Sillje H.H.W., Sauer G., Nigg E.A., Koerner R. Proc. Natl. Acad. Sci. U.S.A. 103:5391-5396(2006) [PubMed: 16565220] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-18, MASS SPECTROMETRY. Tissue: Epithelium.
[16]	"Improved titanium dioxide enrichment of phosphopeptides from HeLa cells and high confident phosphopeptide identification by cross-validation of MS/MS and MS/MS/MS spectra." Yu L.-R., Zhu Z., Chan K.C., Issaq H.J., Dimitrov D.S., Veenstra T.D. J. Proteome Res. 6:4150-4162(2007) [PubMed: 17924679] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19, MASS SPECTROMETRY. Tissue: Epithelium.
[17]	"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry." Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A. Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24, MASS SPECTROMETRY.
[18]	"The crystal structure and ion channel activity of human annexin II, a peripheral membrane protein." Burger A., Berendes R., Liemann S., Benz J., Hofmann A., Goettig P., Huber R., Gerke V., Tiel C., Roemisch J., Weber K. J. Mol. Biol. 257:839-847(1996) [PubMed: 8636985] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).

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Web resources

Protein Spotlight

Red velvet - Issue 86 of September 2007

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Cross-references

Sequence databases

D00017 mRNA. Translation: BAA00013.1.
BT007432 mRNA. Translation: AAP36100.1.
BC001388 mRNA. Translation: AAH01388.1.
BC009564 mRNA. Translation: AAH09564.1.
BC015834 mRNA. Translation: AAH15834.1.
BC016774 mRNA. Translation: AAH16774.1.
BC021114 mRNA. Translation: AAH21114.1.
BC052558 mRNA. Translation: AAH52558.1.
BC052567 mRNA. Translation: AAH52567.1.
BC066955 mRNA. Translation: AAH66955.2. Different initiation.
BC068065 mRNA. Translation: AAH68065.1.
BC093056 mRNA. Translation: AAH93056.1.

PIR

LUHU36. A23942.

RefSeq

NP_001002857.1.
NP_001002858.1.
NP_004030.1.

UniGene

Hs.511605

3D structure databases

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1W7B	X-ray	1.52	A	1-339	[»]
1XJL	X-ray	2.59	A/B	21-339	[»]
2HYU	X-ray	1.86	A	32-339	[»]
2HYV	X-ray	1.42	A	32-339	[»]
2HYW	X-ray	2.10	A/B	32-339	[»]