A6NMY6 (AXA2L_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Putative annexin A2-like protein

Alternative name(s):
Annexin A2 pseudogene 2
Lipocortin II pseudogene

Gene names

Name:	ANXA2P2
Synonyms:	ANX2L2, ANX2P2, LPC2B

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	339 AA.
Sequence status	Complete.
Protein existence	Uncertain

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	Secreted › extracellular space › extracellular matrix › basement 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).

Ontologies

Keywords
Cellular component	Basement membrane Extracellular matrix Secreted
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
PTM	Acetylation Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Cellular component	basement membrane Inferred from electronic annotation. Source: UniProtKB-SubCell melanosome Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Inferred from electronic annotation. Source: InterPro calcium-dependent phospholipid binding Inferred from electronic annotation. Source: UniProtKB-KW cytoskeletal protein binding Inferred from electronic annotation. Source: InterPro phospholipase inhibitor activity Inferred from electronic annotation. Source: InterPro
Complete GO annotation...

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	2 – 339	338	Putative annexin A2-like protein		PRO_0000343940
Regions
	Repeat	37 – 102	66	Annexin 1
	Repeat	109 – 174	66	Annexin 2
	Repeat	193 – 259	67	Annexin 3
	Repeat	269 – 334	66	Annexin 4
	Region	2 – 24	23	S100A10-binding site Potential
Amino acid modifications
	Modified residue	2	1	N-acetylserine By similarity
	Modified residue	18	1	Phosphoserine By similarity
	Modified residue	19	1	Phosphothreonine Ref.3
	Modified residue	24	1	Phosphotyrosine; by SRC Ref.4
	Modified residue	26	1	Phosphoserine Ref.3
	Modified residue	30	1	Phosphotyrosine Ref.4
	Modified residue	127	1	Phosphoserine Ref.3
	Modified residue	188	1	Phosphotyrosine Ref.4
	Modified residue	238	1	Phosphotyrosine Ref.4
	Modified residue	316	1	Phosphotyrosine Ref.4
	Modified residue	317	1	Phosphotyrosine Ref.4
	Modified residue	318	1	Phosphotyrosine Ref.4
Experimental info
	Sequence conflict	72	1	V → S in M62898. Ref.1
	Sequence conflict	338	1	D → A in M62898. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	A6NMY6 [UniParc]. Last modified January 15, 2008. Version 2. Checksum: 6A05AB3E19392A15	FASTA	339	38,659
	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

References

	« Hide 'large scale' referencesShow '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: 2174397] [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. , 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: 15164053] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[3]	"A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19; SER-26 AND SER-127, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[4]	"An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells." Heibeck T.H., Ding S.-J., Opresko L.K., Zhao R., Schepmoes A.A., Yang F., Tolmachev A.V., Monroe M.E., Camp D.G. II, Smith R.D., Wiley H.S., Qian W.-J. J. Proteome Res. 8:3852-3861(2009) [PubMed: 19534553] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-24; TYR-30; TYR-188; TYR-238; TYR-316; TYR-317 AND TYR-318, MASS SPECTROMETRY. Tissue: Mammary epithelium.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	M62898 mRNA. No translation available. AL139008 Genomic DNA. No translation available.
IPI	IPI00334627.
UniGene	Hs.534301.
3D structure databases
ProteinModelPortal	A6NMY6.
SMR	A6NMY6. Positions 32-339.
ModBase	Search...
Protein-protein interaction databases
IntAct	A6NMY6. 5 interactions.
STRING	A6NMY6.
Proteomic databases
PRIDE	A6NMY6.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000332680; ENSP00000346032; ENSG00000182718. ENST00000396024; ENSP00000379342; ENSG00000182718. ENST00000421017; ENSP00000411352; ENSG00000182718. ENST00000451270; ENSP00000387545; ENSG00000182718.
UCSC	uc010mjx.1. human.
Organism-specific databases
GeneCards	GC09P033627.
H-InvDB	HIX0034915.
HGNC	HGNC:539. ANXA2P2.
HPA	CAB004311.
neXtProt	NX_A6NMY6.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG09237.
HOVERGEN	HBG061815.
InParanoid	A6NMY6.
PhylomeDB	A6NMY6.
Gene expression databases
Bgee	A6NMY6.
Genevestigator	A6NMY6.
Family and domain databases
InterPro	IPR001464. Annexin. IPR018502. Annexin_repeat. IPR018252. Annexin_repeat_CS. IPR002389. AnnexinII. [Graphical view]
Gene3D	G3DSA:1.10.220.10. Annexin. 4 hits.
PANTHER	PTHR10502. Annexin. 1 hit. PTHR10502:SF18. AnnexinII. 1 hit.
Pfam	PF00191. Annexin. 4 hits. [Graphical view]
PRINTS	PR00196. ANNEXIN. PR00198. ANNEXINII.
SMART	SM00335. ANX. 4 hits. [Graphical view]
SUPFAM	SSF47874. Annexin. 1 hit.
PROSITE	PS00223. ANNEXIN. 4 hits. [Graphical view]
ProtoNet	Search...

Entry information

Entry name

AXA2L_HUMAN

Accession

Primary (citable) accession number: A6NMY6

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 22, 2008
Last sequence update:	January 15, 2008
Last modified:	January 25, 2012
This is version 38 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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.