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P07355 (ANXA2_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 178. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (7) | Third-party data text xml rdf/xml gff fasta
to top of pageNames·Attributes·General annotation·Ontologies·Interactions·Alt products·Sequence annotation·Sequences·References·Web links·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Annexin A2
Alternative name(s):
Annexin II
Annexin-2
Calpactin I heavy chain
Calpactin-1 heavy chain
Chromobindin-8
Lipocortin II
Placental anticoagulant protein IV
Short name=PAP-IV
Protein I
p36
Gene names
Name:ANXA2
Synonyms:ANX2, ANX2L4, CAL1H, LPC2D
OrganismHomo sapiens (Human) [Reference proteome]
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at protein level

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. Interacts with ATP1B1 and DYSF By similarity. Interacts with human cytomegalovirus (HCMV). Interacts with COCH. Ref.10 Ref.17

Subcellular location

Secretedextracellular spaceextracellular matrixbasement 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. Ref.15

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.

ISGylated. Ref.14

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.

Sequence caution

The sequence AAH66955.2 differs from that shown. Reason: Erroneous initiation.

Ontologies

Keywords
   Cellular componentBasement membrane
Extracellular matrix
Secreted
   Coding sequence diversityAlternative splicing
Polymorphism
   DomainAnnexin
Repeat
   LigandCalcium
Calcium/phospholipid-binding
   PTMAcetylation
Phosphoprotein
Ubl conjugation
   Technical term3D-structure
Complete proteome
Direct protein sequencing
Reference proteome
Gene Ontology (GO)
   Biological_processangiogenesis

Inferred from expression pattern PubMed 11866539. Source: UniProtKB

body fluid secretion

Inferred from electronic annotation. Source: Ensembl

cellular response to acid

Inferred from electronic annotation. Source: Ensembl

collagen fibril organization

Inferred from electronic annotation. Source: Ensembl

fibrinolysis

Inferred from electronic annotation. Source: Ensembl

membrane budding

Inferred from mutant phenotype PubMed 23861394. Source: UniProt

membrane raft assembly

Inferred from mutant phenotype PubMed 23861394. Source: UniProt

negative regulation of catalytic activity

Inferred from direct assay Ref.1. Source: GOC

osteoclast development

Inferred from direct assay PubMed 7961821. Source: UniProt

positive regulation of binding

Inferred from electronic annotation. Source: Ensembl

positive regulation of fibroblast proliferation

Inferred from electronic annotation. Source: Ensembl

positive regulation of protein phosphorylation

Inferred from electronic annotation. Source: Ensembl

positive regulation of vesicle fusion

Inferred from direct assay PubMed 2138016. Source: UniProtKB

protein heterotetramerization

Inferred from direct assay PubMed 23091277PubMed 23861394. Source: UniProt

protein targeting to plasma membrane

Inferred from electronic annotation. Source: Ensembl

   Cellular_componentSchmidt-Lanterman incisure

Inferred from electronic annotation. Source: Ensembl

basement membrane

Inferred from electronic annotation. Source: UniProtKB-SubCell

cell cortex

Inferred from electronic annotation. Source: Ensembl

cell surface

Inferred from direct assay PubMed 10809787. Source: UniProt

early endosome

Inferred from electronic annotation. Source: Ensembl

extracellular space

Inferred from direct assay PubMed 22664934. Source: UniProt

extracellular vesicular exosome

Inferred from direct assay PubMed 21362503. Source: UniProtKB

extrinsic component of plasma membrane

Inferred from electronic annotation. Source: Ensembl

lipid particle

Inferred from direct assay PubMed 14741744. Source: UniProtKB

macropinosome

Inferred from electronic annotation. Source: Ensembl

melanosome

Inferred from electronic annotation. Source: UniProtKB-SubCell

midbody

Inferred from direct assay PubMed 15166316. Source: UniProtKB

myelin sheath adaxonal region

Inferred from electronic annotation. Source: Ensembl

perinuclear region of cytoplasm

Inferred from electronic annotation. Source: Ensembl

protein complex

Inferred from electronic annotation. Source: Ensembl

ruffle

Inferred from electronic annotation. Source: Ensembl

sarcolemma

Inferred from electronic annotation. Source: Ensembl

   Molecular_functionS100 protein binding

Inferred from physical interaction PubMed 14699089PubMed 23091277. Source: UniProt

calcium ion binding

Inferred from electronic annotation. Source: InterPro

calcium-dependent phospholipid binding

Inferred from direct assay PubMed 2138016. Source: UniProtKB

phosphatidylinositol-4,5-bisphosphate binding

Inferred from mutant phenotype PubMed 23861394. Source: UniProt

phospholipase A2 inhibitor activity

Inferred from direct assay Ref.1. Source: UniProt

poly(A) RNA binding

Inferred from direct assay PubMed 22658674. Source: UniProtKB

Complete GO annotation...

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Q99IB85EBI-352622,EBI-6931023From a different organism.
MLH1P406927EBI-352622,EBI-744248

Alternative products

This entry describes 2 isoforms produced by alternative splicing. [Align] [Select]
Isoform 1 (identifier: P07355-1)

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.
Isoform 2 (identifier: P07355-2)

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MGRQLAGCGDAGKKASFKM

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed Ref.7
Chain2 – 339338Annexin A2
PRO_0000067470

Regions

Repeat42 – 10261Annexin 1
Repeat114 – 17461Annexin 2
Repeat199 – 25961Annexin 3
Repeat274 – 33461Annexin 4
Region2 – 2423S100A10-binding site Potential

Amino acid modifications

Modified residue21N-acetylserine Ref.7
Modified residue241Phosphotyrosine; by SRC Ref.13
Modified residue261Phosphoserine; by PKC Ref.12
Modified residue491N6-acetyllysine By similarity
Modified residue1521N6-acetyllysine By similarity
Modified residue1991Phosphotyrosine By similarity
Modified residue2271N6-acetyllysine By similarity

Natural variations

Alternative sequence11M → MGRQLAGCGDAGKKASFKM in isoform 2.
VSP_038091
Natural variant981V → L. Ref.6
Corresponds to variant rs17845226 [ dbSNP | Ensembl ].
VAR_012982

Experimental info

Mutagenesis241Y → A: Abolishes heat stress-induced cell surface localization. Ref.13
Sequence conflict291A → P AA sequence Ref.9
Sequence conflict1661D → G in CAE45704. Ref.4
Sequence conflict2931V → A in AAH23990. Ref.6

Secondary structure

.................................................. 339
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
Isoform 1 [UniParc].

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

FASTA33938,604
        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 

« Hide

Isoform 2 [UniParc].

Checksum: 2AA081CB4E7AC75C
Show »

FASTA35740,411

References

« Hide '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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
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] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
[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] (ISOFORM 1).
[4]"The full-ORF clone resource of the German cDNA consortium."
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.
BMC Genomics 8:399-399(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Tissue: Colon endothelium.
[5]"Analysis of the DNA sequence and duplication history of human chromosome 15."
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. expand/collapse author list , 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.
Nature 440:671-675(2006) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[6]"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] (ISOFORM 1), VARIANT LEU-98.
Tissue: Brain, Colon, Pancreas, Prostate, Skin, Testis and Urinary bladder.
[7]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, IDENTIFICATION BY MASS SPECTROMETRY.
Tissue: Colon adenocarcinoma and Osteosarcoma.
[8]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 11-27; 49-62; 68-77; 120-135; 314-323 AND 329-339.
[9]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 15-40 AND 50-63.
[10]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 18-37; 119-126; 172-191 AND 301-307, INTERACTION WITH HCMV.
Tissue: Umbilical vein endothelial cell.
[11]"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] [Europe PMC] [Abstract]
Cited for: PROTEIN SEQUENCE OF 234-241 AND 252-261.
[12]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT SER-26.
[13]"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] [Europe PMC] [Abstract]
Cited for: PHOSPHORYLATION AT TYR-24, MUTAGENESIS OF TYR-24.
[14]"Proteomic identification of proteins conjugated to ISG15 in mouse and human cells."
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.
Biochem. Biophys. Res. Commun. 336:496-506(2005) [PubMed] [Europe PMC] [Abstract]
Cited for: ISGYLATION.
[15]"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] [Europe PMC] [Abstract]
Cited for: SUBCELLULAR LOCATION [LARGE SCALE ANALYSIS].
Tissue: Melanoma.
[16]"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].
[17]"Cochlin induced TREK-1 co-expression and annexin A2 secretion: role in trabecular meshwork cell elongation and motility."
Goel M., Sienkiewicz A.E., Picciani R., Lee R.K., Bhattacharya S.K.
PLoS ONE 6:E23070-E23070(2011) [PubMed] [Europe PMC] [Abstract]
Cited for: INTERACTION WITH COCH.
[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] [Europe PMC] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.2 ANGSTROMS).
+Additional computationally mapped references.

Web resources

Protein Spotlight

Red velvet - Issue 86 of September 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
D00017 mRNA. Translation: BAA00013.1.
BT007432 mRNA. Translation: AAP36100.1.
BX640598 mRNA. Translation: CAE45704.1.
AC087385 Genomic DNA. No translation available.
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.
BC023990 mRNA. Translation: AAH23990.1.
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.
PIRLUHU36. A23942.
RefSeqNP_001002857.1. NM_001002857.1.
NP_001002858.1. NM_001002858.2.
NP_001129487.1. NM_001136015.2.
NP_004030.1. NM_004039.2.
UniGeneHs.511605.

3D structure databases

PDBe
RCSB PDB
PDBj
EntryMethodResolution (Å)ChainPositionsPDBsum
1W7BX-ray1.52A1-339[»]
1XJLX-ray2.59A/B21-338[»]
2HYUX-ray1.86A32-338[»]
2HYVX-ray1.42A32-338[»]
2HYWX-ray2.10A/B32-338[»]
4DRWX-ray3.50A/B/C/D2-16[»]
4HRHX-ray3.00A/B2-16[»]
ProteinModelPortalP07355.
SMRP07355. Positions 32-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

BioGrid106799. 63 interactions.
IntActP07355. 30 interactions.
MINTMINT-1213203.
STRING9606.ENSP00000346032.

Chemistry

BindingDBP07355.
ChEMBLCHEMBL2111435.
DrugBankDB00009. Alteplase.
DB00029. Anistreplase.
DB00031. Tenecteplase.

PTM databases

PhosphoSiteP07355.

Polymorphism databases

DMDM113950.

2D gel databases

DOSAC-COBS-2DPAGEP07355.
REPRODUCTION-2DPAGEIPI00455315.
P07355.
UCD-2DPAGEP07355.

Proteomic databases

PaxDbP07355.
PRIDEP07355.

Protocols and materials databases

DNASU302.
StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

EnsemblENST00000332680; ENSP00000346032; ENSG00000182718. [P07355-2]
ENST00000396024; ENSP00000379342; ENSG00000182718. [P07355-1]
ENST00000421017; ENSP00000411352; ENSG00000182718. [P07355-1]
ENST00000451270; ENSP00000387545; ENSG00000182718. [P07355-1]
GeneID302.
KEGGhsa:302.
UCSCuc002agk.3. human. [P07355-1]
uc002agm.3. human. [P07355-2]

Organism-specific databases

CTD302.
GeneCardsGC15M060639.
HGNCHGNC:537. ANXA2.
HPACAB004311.
HPA046964.
MIM151740. gene.
neXtProtNX_P07355.
PharmGKBPA24827.
GenAtlasSearch...

Phylogenomic databases

eggNOGNOG259189.
HOGENOMHOG000158803.
HOVERGENHBG061815.
InParanoidP07355.
KOK17092.
OMAFIQQDTK.
OrthoDBEOG74XS72.
TreeFamTF105452.

Gene expression databases

ArrayExpressP07355.
BgeeP07355.
CleanExHS_ANXA2.
GenevestigatorP07355.

Family and domain databases

Gene3D1.10.220.10. 4 hits.
InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002389. AnnexinII.
[Graphical view]
PANTHERPTHR10502:SF18. PTHR10502:SF18. 1 hit.
PfamPF00191. Annexin. 4 hits.
[Graphical view]
PRINTSPR00196. ANNEXIN.
PR00198. ANNEXINII.
SMARTSM00335. ANX. 4 hits.
[Graphical view]
PROSITEPS00223. ANNEXIN. 4 hits.
[Graphical view]
ProtoNetSearch...

Other

ChiTaRSANXA2. human.
EvolutionaryTraceP07355.
GeneWikiAnnexin_A2.
GenomeRNAi302.
NextBio1217.
PROP07355.
SOURCESearch...

Entry information

Entry nameANXA2_HUMAN
AccessionPrimary (citable) accession number: P07355
Secondary accession number(s): Q567R4 expand/collapse secondary AC list , Q6N0B3, Q8TBV2, Q96DD5, Q9UDH8
Entry history
Integrated into UniProtKB/Swiss-Prot: April 1, 1988
Last sequence update: January 23, 2007
Last modified: April 16, 2014
This is version 178 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

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

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 polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human chromosome 15

Human chromosome 15: entries, gene names and cross-references to MIM