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Reviewed, UniProtKB/Swiss-Prot Q5R5A0 (ANXA2_PONAB)

Last modified November 24, 2009. Version 39. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (2) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Sequence annotation (Features) · Sequences · References · Web resources · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Annexin A2
Alternative name(s):
    Annexin-2
Gene names
Name: ANXA2
Synonyms: ANX2
OrganismPongo abelii (Sumatran orangutan)
Taxonomic identifier9601 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaePongo

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.

Subcellular location

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

Domain

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

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_0000288686

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 residue181Phosphoserine By similarity
Modified residue191Phosphothreonine By similarity
Modified residue241Phosphotyrosine; by SRC By similarity
Modified residue261Phosphoserine; by PKC By similarity
Modified residue301Phosphotyrosine By similarity
Modified residue1041N6-acetyllysine By similarity
Modified residue1151N6-acetyllysine By similarity
Modified residue1481N6-acetyllysine By similarity
Modified residue1521N6-acetyllysine By similarity
Modified residue1571N6-acetyllysine By similarity
Modified residue1881Phosphotyrosine By similarity
Modified residue1991Phosphotyrosine By similarity
Modified residue2271N6-acetyllysine By similarity
Modified residue2381Phosphotyrosine By similarity
Modified residue2751Phosphotyrosine By similarity
Modified residue2791N6-acetyllysine By similarity
Modified residue3021N6-acetyllysine By similarity
Modified residue3131N6-acetyllysine By similarity
Modified residue3161Phosphotyrosine By similarity
Modified residue3171Phosphotyrosine By similarity
Modified residue3181Phosphotyrosine By similarity

Sequences

Sequence LengthMass (Da)Tools
Q5R5A0-1 [UniParc].

Last modified December 21, 2004. Version 1.
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

References

[1]The German cDNA consortium
Submitted (NOV-2004) to the EMBL/GenBank/DDBJ databases
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Kidney.

Web resources

Protein Spotlight

Red velvet - Issue 86 of September 2007

Cross-references

Sequence databases

CR860964 mRNA. Translation: CAH93066.1.
RefSeqNP_001126816.1.
UniGenePab.8142

3D structure databases

HSSPHSSP built from PDB template 1W7B based on UniProtKB P07355.
SMRQ5R5A0. Positions 21-339.
ModBaseSearch...

Genome annotation databases

GeneID100173821.

Organism-specific databases

CTD100173821.

Phylogenomic databases

HOVERGENQ5R5A0.
OMACHLQKVF

Family and domain databases

InterProIPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002389. AnnexinII.
[Graphical view]
Gene3DG3DSA:1.10.220.10. Annexin. 4 hits.
PANTHERPTHR10502. Annexin. 1 hit.
PTHR10502:SF18. AnnexinII. 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_PONAB
AccessionPrimary (citable) accession number: Q5R5A0
Entry history
Integrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: December 21, 2004
Last modified: November 24, 2009
This is version 39 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Protein Spotlight

Protein Spotlight articles and cited UniProtKB/Swiss-Prot entries

SIMILARITY comments

Index of protein domains and families

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