Annexin A1 - Homo sapiens (Human)

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Reviewed, UniProtKB/Swiss-Prot P04083 (ANXA1_HUMAN)

Last modified February 9, 2010. Version 141. History...

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

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Names and origin

Protein names

Recommended name:
    Annexin A1
Alternative name(s):
    Annexin-1
    Annexin I
    Lipocortin I
    Calpactin II
    Chromobindin-9
    p35
    Phospholipase A2 inhibitory protein

Gene names

Name:	ANXA1
Synonyms:	ANX1, LPC1

Organism

Homo sapiens (Human) [Complete proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

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Protein attributes

Sequence length	346 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level.

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General annotation (Comments)

Function	Calcium/phospholipid-binding protein which promotes membrane fusion and is involved in exocytosis. This protein regulates phospholipase A2 activity. It seems to bind from two to four calcium ions with high affinity.
Subunit structure	Homodimer in placenta (20%); linked by transglutamylation. Interacts with DYSF By similarity. Ref.7
Subcellular location	Nucleus By similarity. Cytoplasm By similarity. Cell projection › cilium By similarity. Basolateral cell membrane By similarity. Note: Found in the cilium, nucleus and basolateral cell membrane of ciliated cells in the tracheal endothelium By similarity. Found in the cytoplasm of type II pneumocytes and alveolar macrophages By similarity.
Domain	A pair of annexin repeats may form one binding site for calcium and phospholipid.
Post-translational modification	Phosphorylated by protein kinase C, epidermal growth factor receptor/kinase and TRPM7. Phosphorylation results in loss of the inhibitory activity. Ref.5 Ref.8 Ref.9 Ref.10 Ref.11 Ref.13
Sequence similarities	Belongs to the annexin family. Contains 4 annexin repeats.

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Ontologies

Keywords
Cellular component	Cell membrane Cell projection Cilium Cytoplasm Membrane Nucleus
Domain	Annexin Repeat
Ligand	Calcium Calcium/phospholipid-binding
Molecular function	Phospholipase A2 inhibitor
PTM	Acetylation Isopeptide bond Phosphoprotein
Technical term	3D-structure Complete proteome Direct protein sequencing
Gene Ontology (GO)
Biological process	anti-apoptosis Traceable author statement. Source: UniProtKB cell surface receptor linked signal transduction Traceable author statement. Source: ProtInc cellular component movement Traceable author statement. Source: ProtInc inflammatory response Traceable author statement. Source: ProtInc keratinocyte differentiation Inferred from direct assay. Source: UniProtKB lipid metabolic process Ref.1 Traceable author statement. Source: ProtInc peptide cross-linking Inferred from direct assay. Source: UniProtKB
Cellular component	basolateral plasma membrane Inferred from electronic annotation. Source: UniProtKB-SubCell cilium Inferred from electronic annotation. Source: UniProtKB-SubCell cornified envelope Inferred from direct assay. Source: UniProtKB cytoplasm Traceable author statement. Source: UniProtKB extracellular region Inferred from Experiment. Source: Reactome nucleus Inferred from electronic annotation. Source: UniProtKB-SubCell
Molecular function	calcium ion binding Traceable author statement. Source: ProtInc calcium-dependent phospholipid binding Inferred from electronic annotation. Source: UniProtKB-KW phospholipase A2 inhibitor activity Inferred from electronic annotation. Source: UniProtKB-KW protein binding, bridging Inferred from direct assay. Source: UniProtKB receptor binding Traceable author statement. Source: ProtInc structural molecule activity Inferred from direct assay. Source: UniProtKB
Complete GO annotation...

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Binary interactions

With	Entry	#Exp.	IntAct	Notes
DLG3	Q92796	1	EBI-354007,EBI-80440
PPM1B	O75688	1	EBI-354007,EBI-1047039

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Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Initiator methionine

Removed

Chain

2 – 346

345

Annexin A1

PRO_0000067460

Regions

Repeat

51 – 111

Annexin 1

Repeat

123 – 183

Annexin 2

Repeat

207 – 267

Annexin 3

Repeat

282 – 342

Annexin 4

Amino acid modifications

Modified residue

N-acetylalanine Ref.6

Modified residue

Phosphoserine; by TRPM7 Ref.8

Modified residue

Phosphotyrosine; by EGFR Ref.5 Ref.10

Modified residue

Phosphothreonine

Modified residue

Phosphoserine; by PKC Ref.5

Modified residue

Phosphotyrosine Ref.11 Ref.13

Modified residue

161

N6-acetyllysine Ref.14

Modified residue

207

Phosphotyrosine Ref.9 Ref.11 Ref.13

Modified residue

239

N6-acetyllysine Ref.14

Modified residue

250

N6-acetyllysine Ref.14

Modified residue

281

N6-acetyllysine Ref.14

Modified residue

312

N6-acetyllysine Ref.14

Cross-link

Isoglutamyl lysine isopeptide (Gln-Lys) (interchain with K-?)

Secondary structure

346

Helix Strand Turn

Details...

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Sequences

Sequence

Length

Mass (Da)

Tools

P04083-1 [UniParc].

Last modified January 23, 2007. Version 2.
Checksum: 14B42E1FA4178EC0
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FASTA

346

38,714

        10         20         30         40         50         60 
MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV 

        70         80         90        100        110        120 
DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA LLKTPAQFDA 

       130        140        150        160        170        180 
DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL 

       190        200        210        220        230        240 
LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY 

       250        260        270        280        290        300 
TKYSKHDMNK VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM 

       310        320        330        340 
VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN

« Hide

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References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential anti-inflammatory activity." Wallner B.P., Mattaliano R.J., Hession C., Cate R.L., Tizard R., Sinclair L.K., Foeller C., Chow E.P., Browning J.L., Ramachandran K.L., Pepinsky R.B. Nature 320:77-81(1986) [PubMed: 2936963] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[2]	"Correlation of gene and protein structure of rat and human lipocortin I." Kovacic R.T., Tizard R., Cate R.L., Frey A.Z., Wallner B.P. Biochemistry 30:9015-9021(1991) [PubMed: 1832554] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA].
[3]	"Structural characterization of a biologically active human lipocortin 1 expressed in Escherichia coli." Arcone R., Arpaia G., Ruoppolo M., Malorni A., Pucci P., Marino G., Ialenti A., di Rosa M., Ciliberto G. Eur. J. Biochem. 211:347-355(1993) [PubMed: 8425544] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [MRNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. Tissue: Cervix and Lung.
[5]	"Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C." Varticovski L., Chahwala S.B., Whitman M., Cantley L., Schindler D., Chow E.P., Sinclair L.K., Pepinsky R.B. Biochemistry 27:3682-3690(1988) [PubMed: 2457390] [Abstract] Cited for: PARTIAL PROTEIN SEQUENCE, PHOSPHORYLATION AT TYR-21 AND SER-27.
[6]	"Characterization by tandem mass spectrometry of structural modifications in proteins." Biemann K., Scoble H.A. Science 237:992-998(1987) [PubMed: 3303336] [Abstract] Cited for: ACETYLATION AT ALA-2, MASS SPECTROMETRY.
[7]	"A dimeric form of lipocortin-1 in human placenta." Pepinsky R.B., Sinclair L.K., Chow E.P., O'Brine-Greco B. Biochem. J. 263:97-103(1989) [PubMed: 2532504] [Abstract] Cited for: DIMERIZATION.
[8]	"Phosphorylation of annexin I by TRPM7 channel-kinase." Dorovkov M.V., Ryazanov A.G. J. Biol. Chem. 279:50643-50646(2004) [PubMed: 15485879] [Abstract] Cited for: PHOSPHORYLATION AT SER-5 BY TRPM7.
[9]	"Immunoaffinity profiling of tyrosine phosphorylation in cancer cells." Rush J., Moritz A., Lee K.A., Guo A., Goss V.L., Spek E.J., Zhang H., Zha X.-M., Polakiewicz R.D., Comb M.J. Nat. Biotechnol. 23:94-101(2005) [PubMed: 15592455] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-207, MASS SPECTROMETRY.
[10]	"Global, in vivo, and site-specific phosphorylation dynamics in signaling networks." Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M. Cell 127:635-648(2006) [PubMed: 17081983] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-21, MASS SPECTROMETRY. Tissue: Epithelium.
[11]	"Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer." Rikova K., Guo A., Zeng Q., Possemato A., Yu J., Haack H., Nardone J., Lee K., Reeves C., Li Y., Hu Y., Tan Z., Stokes M., Sullivan L., Mitchell J., Wetzel R., Macneill J., Ren J.M. Comb M.J. Cell 131:1190-1203(2007) [PubMed: 18083107] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT TYR-39 AND TYR-207, MASS SPECTROMETRY.
[12]	Colinge J., Superti-Furga G., Bennett K.L. Submitted (OCT-2008) to UniProtKB Cited for: IDENTIFICATION [LARGE SCALE ANALYSIS], MASS SPECTROMETRY.
[13]	"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-39 AND TYR-207, MASS SPECTROMETRY. Tissue: Mammary epithelium.
[14]	"Lysine acetylation targets protein complexes and co-regulates major cellular functions." Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T., Olsen J.V., Mann M. Science 325:834-840(2009) [PubMed: 19608861] [Abstract] Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-161; LYS-239; LYS-250; LYS-281 AND LYS-312, MASS SPECTROMETRY.
[15]	"Crystal structure of human annexin I at 2.5-A resolution." Weng X., Luecke H., Song I.S., Kang D.S., Kim S.-H., Huber R. Protein Sci. 2:448-458(1993) [PubMed: 8453382] [Abstract] Cited for: X-RAY CRYSTALLOGRAPHY (2.5 ANGSTROMS).
[16]	"NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit." Gao J., Li Y., Yan H. J. Biol. Chem. 274:2971-2977(1999) [PubMed: 9915835] [Abstract] Cited for: STRUCTURE BY NMR OF 41-113.
+	Additional computationally mapped references.

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Cross-references

Sequence databases

EMBL
GenBank
DDBJ

X05908 mRNA. Translation: CAA29338.1.
BC001275 mRNA. Translation: AAH01275.1.
BC035993 mRNA. Translation: AAH35993.1.

IPI

IPI00218918.

PIR

LUHU. A03080.

RefSeq

NP_000691.1.

UniGene

Hs.494173

3D structure databases

PDBe
RCSB PDB
PDBj

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1AIN	X-ray	2.50	A	33-346	[»]
1BO9	NMR	-	A	41-113	[»]
1QLS	X-ray	2.30	D	2-12	[»]

SMR

P04083. Positions 2-344.

ModBase

Search...

Protein-protein interaction databases

IntAct

P04083. 5 interactions.

STRING

P04083.

Protein family/group databases

TCDB

1.A.31.1.3. annexin family.

PTM databases

PhosphoSite

P04083.

2-D gel databases

DOSAC-COBS-2DPAGE

P04083.

PHCI-2DPAGE

P04083.

REPRODUCTION-2DPAGE

IPI00218918.
P04083.

Proteomic databases

PeptideAtlas

P04083.

PRIDE

P04083.

Genome annotation databases

Ensembl

ENST00000257497; ENSP00000257497; ENSG00000135046; Homo sapiens. [Genome view]
ENST00000376911; ENSP00000366109; ENSG00000135046; Homo sapiens. [Genome view]

GeneID

301.

KEGG

hsa:301.

UCSC

uc004ajf.1. human.

Organism-specific databases

CTD

301.

GeneCards

GC09P074956.

H-InvDB

HIX0008100.

HGNC

HGNC:533. ANXA1.

HPA

CAB013023.
HPA011271.
HPA011272.

MIM

151690. gene.

PharmGKB

PA24823.

GenAtlas

Search...

Phylogenomic databases

eggNOG

prNOG18218.

HOGENOM

HBG745057.

HOVERGEN

P04083.

InParanoid

P04083.

OMA

DIENCLT.

OrthoDB

EOG9BK7PB.

PhylomeDB

P04083.

Enzyme and pathway databases

Reactome

REACT_14797. Signaling by GPCR.

Gene expression databases

ArrayExpress

P04083.

Bgee

P04083.

CleanEx

HS_ANXA1.

Genevestigator

P04083.

GermOnline

ENSG00000135046. Homo sapiens.

Family and domain databases

InterPro

IPR001464. Annexin.
IPR018502. Annexin_repeat.
IPR018252. Annexin_repeat_CS.
IPR002388. AnnexinI.
[Graphical view]

Gene3D

G3DSA:1.10.220.10. Annexin. 4 hits.

PANTHER

PTHR10502. Annexin. 1 hit.

Pfam

PF00191. Annexin. 4 hits.
[Graphical view]

PRINTS

PR00196. ANNEXIN.
PR00197. ANNEXINI.

SMART

SM00335. ANX. 4 hits.
[Graphical view]

PROSITE

PS00223. ANNEXIN. 4 hits.
[Graphical view]

ProtoNet

Search...

Other Resources

DrugBank

DB00240. Alclometasone.
DB00288. Amcinonide.
DB00394. Beclomethasone.
DB00443. Betamethasone.
DB01013. Clobetasol.
DB00838. Clocortolone.
DB01260. Desonide.
DB00547. Desoximetasone.
DB01234. Dexamethasone.
DB00223. Diflorasone.
DB00663. Flumethasone Pivalate.
DB00596. Halobetasol Propionate.
DB00769. Hydrocortamate.
DB00741. Hydrocortisone.
DB00873. Loteprednol Etabonate.
DB00959. Methylprednisolone.
DB00764. Mometasone.
DB01130. Prednicarbate.
DB00635. Prednisone.
DB00896. Rimexolone.
DB00620. Triamcinolone.

NextBio

1213.

SOURCE

Search...

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Entry information

Entry name

ANXA1_HUMAN

Accession

Primary (citable) accession number: P04083

Entry history

Integrated into UniProtKB/Swiss-Prot:	November 1, 1986
Last sequence update:	January 23, 2007
Last modified:	February 9, 2010
This is version 141 of the entry and version 2 of the sequence. [Complete history]

Entry status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)

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.

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Relevant documents

Human chromosome 9

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

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin

Protein attributes

General annotation (Comments)

Ontologies

Binary interactions

With

Entry

#Exp.

IntAct

Notes

Sequence annotation (Features)

Molecule processing

Regions

Amino acid modifications

Secondary structure

Sequences

References

Cross-references

Sequence databases

3D structure databases

Protein-protein interaction databases

Protein family/group databases

PTM databases

2-D gel databases

Proteomic databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Gene expression databases

Family and domain databases

Other Resources

Entry information

Relevant documents