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Q2Q1M6 (ANXA2_CEREL) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 46. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | 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 A2
Alternative name(s):
Annexin-2
Gene names
Name:ANXA2
Synonyms:ANX2
OrganismCervus elaphus (Red deer)
Taxonomic identifier9860 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaLaurasiatheriaCetartiodactylaRuminantiaPecoraCervidaeCervinaeCervus

Protein attributes

Sequence length339 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is further processed into a mature form.
Protein existenceEvidence at transcript 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 By similarity.

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 COCH By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane. Note: In the lamina beneath the plasma membrane By similarity.

Tissue specificity

Expressed strongly in velvet antler reserve mesenchyme. Ref.1

Domain

A pair of annexin repeats may form one binding site for calcium and phospholipid.

Post-translational modification

ISGylated By similarity.

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 annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 339338Annexin A2
PRO_0000288685

Regions

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

Amino acid modifications

Modified residue21N-acetylserine By similarity
Modified residue241Phosphotyrosine; by SRC By similarity
Modified residue261Phosphoserine; by PKC By similarity
Modified residue491N6-acetyllysine By similarity
Modified residue1521N6-acetyllysine By similarity
Modified residue1991Phosphotyrosine By similarity
Modified residue2271N6-acetyllysine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q2Q1M6 [UniParc].

Last modified January 24, 2006. Version 1.
Checksum: A22C3DA3F6829FEF

FASTA33938,621
        10         20         30         40         50         60 
MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIL 

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

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

       190        200        210        220        230        240 
EDGSVIDYEL IDQDARDLYD AGVKXKXTDV PKWISIMTER SVCHLQKVFE RYKSYSPYDM 

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

       310        320        330 
LKIRSEFKKK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD 

« Hide

References

[1]"Identification of differentially expressed genes in the developing antler of red deer Cervus elaphus."
Molnar A., Gyurjan I., Korpos E., Borsy A., Steger V., Buzas Z., Kiss I., Zomborszky Z., Papp P., Deak F., Orosz L.
Mol. Genet. Genomics 277:237-248(2007) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], TISSUE SPECIFICITY.

Web resources

Protein Spotlight

Red velvet - Issue 86 of September 2007

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
DQ239920 mRNA. Translation: ABB77206.1.

3D structure databases

ModBaseSearch...
MobiDBSearch...

Proteomic databases

PRIDEQ2Q1M6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Phylogenomic databases

HOVERGENHBG061815.

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...

Entry information

Entry nameANXA2_CEREL
AccessionPrimary (citable) accession number: Q2Q1M6
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: January 24, 2006
Last modified: April 16, 2014
This is version 46 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Relevant documents

SIMILARITY comments

Index of protein domains and families

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries