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A6NMY6 (AXA2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Last modified April 16, 2014. Version 56. 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·Cross-refs·Entry info·DocumentsCustomize order

Names and origin

Protein namesRecommended name:
Putative annexin A2-like protein
Alternative name(s):
Annexin A2 pseudogene 2
Lipocortin II pseudogene
Gene names
Name:ANXA2P2
Synonyms:ANX2L2, ANX2P2, LPC2B
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 existenceUncertain

General annotation (Comments)

Function

Calcium-regulated membrane-binding protein whose affinity for calcium is greatly enhanced by anionic phospholipids By similarity. It binds two calcium ions with high affinity By similarity. May be involved in heat-stress response By similarity.

Subunit structure

Heterotetramer containing 2 light chains of S100A10/p11 and 2 heavy chains of ANXA2P2/p36 By similarity.

Subcellular location

Secretedextracellular spaceextracellular matrixbasement membrane By similarity. Melanosome By similarity. Note: In the lamina beneath the plasma membrane By similarity. In melanosome fractions from stage I to stage IV By similarity. Translocated from the cytoplasm to the cell surface through a Golgi-independent mechanism By similarity.

Domain

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

Miscellaneous

It may cross-link plasma membrane phospholipids with actin and the cytoskeleton and be involved with exocytosis By similarity.

Sequence similarities

Belongs to the annexin family.

Contains 4 annexin repeats.

Caution

Could be the product of a pseudogene. The existence of a transcript at this locus is supported by only one sequence submission (Ref.1).

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Initiator methionine11Removed By similarity
Chain2 – 339338Putative annexin A2-like protein
PRO_0000343940

Regions

Repeat37 – 10266Annexin 1
Repeat109 – 17466Annexin 2
Repeat193 – 25967Annexin 3
Repeat269 – 33466Annexin 4
Region2 – 2423S100A10-binding site Potential

Amino acid modifications

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

Experimental info

Sequence conflict721V → S in M62898. Ref.1
Sequence conflict3381D → A in M62898. Ref.1

Sequences

Sequence LengthMass (Da)Tools
A6NMY6 [UniParc].

Last modified January 15, 2008. Version 2.
Checksum: 6A05AB3E19392A15

FASTA33938,659
        10         20         30         40         50         60 
MSTVHEILCK LSLEGDHSTP PSAYGSVKAY TNFDAERDAL NIETAIKTKG VDEVTIVNIV 

        70         80         90        100        110        120 
TNRDNAQRQD IVFSYQRRTK KELASALKSA LSGHLETVIL GLLKTPAQYD ASELKASMKG 

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

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

       250        260        270        280        290        300 
LESIRKEVKG DLENAFLNLV QRIQNKPLYF ADQLYDSMKG KGTRDKVLIR IMVSRSEVDM 

       310        320        330 
LKIRSEFKRK YGKSLYYYIQ QDTKGDYQKA LLYLCGGDD 

« Hide

References

« Hide 'large scale' references
[1]"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].
[2]"DNA sequence and analysis of human chromosome 9."
Humphray S.J., Oliver K., Hunt A.R., Plumb R.W., Loveland J.E., Howe K.L., Andrews T.D., Searle S., Hunt S.E., Scott C.E., Jones M.C., Ainscough R., Almeida J.P., Ambrose K.D., Ashwell R.I.S., Babbage A.K., Babbage S., Bagguley C.L. expand/collapse author list , Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beasley H., Beasley O., Bird C.P., Bray-Allen S., Brown A.J., Brown J.Y., Burford D., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Chen Y., Clarke G., Clark S.Y., Clee C.M., Clegg S., Collier R.E., Corby N., Crosier M., Cummings A.T., Davies J., Dhami P., Dunn M., Dutta I., Dyer L.W., Earthrowl M.E., Faulkner L., Fleming C.J., Frankish A., Frankland J.A., French L., Fricker D.G., Garner P., Garnett J., Ghori J., Gilbert J.G.R., Glison C., Grafham D.V., Gribble S., Griffiths C., Griffiths-Jones S., Grocock R., Guy J., Hall R.E., Hammond S., Harley J.L., Harrison E.S.I., Hart E.A., Heath P.D., Henderson C.D., Hopkins B.L., Howard P.J., Howden P.J., Huckle E., Johnson C., Johnson D., Joy A.A., Kay M., Keenan S., Kershaw J.K., Kimberley A.M., King A., Knights A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C., Lloyd D.M., Lovell J., Martin S., Mashreghi-Mohammadi M., Matthews L., McLaren S., McLay K.E., McMurray A., Milne S., Nickerson T., Nisbett J., Nordsiek G., Pearce A.V., Peck A.I., Porter K.M., Pandian R., Pelan S., Phillimore B., Povey S., Ramsey Y., Rand V., Scharfe M., Sehra H.K., Shownkeen R., Sims S.K., Skuce C.D., Smith M., Steward C.A., Swarbreck D., Sycamore N., Tester J., Thorpe A., Tracey A., Tromans A., Thomas D.W., Wall M., Wallis J.M., West A.P., Whitehead S.L., Willey D.L., Williams S.A., Wilming L., Wray P.W., Young L., Ashurst J.L., Coulson A., Blocker H., Durbin R.M., Sulston J.E., Hubbard T., Jackson M.J., Bentley D.R., Beck S., Rogers J., Dunham I.
Nature 429:369-374(2004) [PubMed] [Europe PMC] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
+Additional computationally mapped references.

Cross-references

Sequence databases

EMBL
GenBank
DDBJ
M62898 mRNA. No translation available.
AL139008 Genomic DNA. No translation available.
UniGeneHs.534301.

3D structure databases

ProteinModelPortalA6NMY6.
SMRA6NMY6. Positions 2-339.
ModBaseSearch...
MobiDBSearch...

Protein-protein interaction databases

IntActA6NMY6. 5 interactions.

Proteomic databases

PRIDEA6NMY6.

Protocols and materials databases

StructuralBiologyKnowledgebaseSearch...

Genome annotation databases

UCSCuc010mjx.3. human.

Organism-specific databases

GeneCardsGC09P033780.
HGNCHGNC:539. ANXA2P2.
HPACAB004311.
neXtProtNX_A6NMY6.
GenAtlasSearch...

Phylogenomic databases

HOVERGENHBG061815.
InParanoidA6NMY6.
PhylomeDBA6NMY6.

Gene expression databases

GenevestigatorA6NMY6.

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 nameAXA2L_HUMAN
AccessionPrimary (citable) accession number: A6NMY6
Entry history
Integrated into UniProtKB/Swiss-Prot: July 22, 2008
Last sequence update: January 15, 2008
Last modified: April 16, 2014
This is version 56 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

Human chromosome 9

Human chromosome 9: entries, gene names and cross-references to MIM