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1.A.31.1.3
Annexin A1 (McNeil et al., 2006)

Accession Number:P04083
Protein Name:Annexin A1
Length:346
Molecular Weight:38714.00
Species:Homo sapiens (Human) [9606]
Location1 / Topology2 / Orientation3: Nucleus1

Cross database links:

Genevestigator: P04083
eggNOG: prNOG18218
HEGENOM: HBG745057
RefSeq: NP_000691.1   
Entrez Gene ID: 301   
Pfam: PF00191   
Drugbank: Drugbank Link   
OMIM: 151690  gene
KEGG: hsa:301   

Gene Ontology

GO:0016323 C:basolateral plasma membrane
GO:0005929 C:cilium
GO:0001533 C:cornified envelope
GO:0005737 C:cytoplasm
GO:0005576 C:extracellular region
GO:0005634 C:nucleus
GO:0005509 F:calcium ion binding
GO:0005544 F:calcium-dependent phospholipid binding
GO:0019834 F:phospholipase A2 inhibitor activity
GO:0030674 F:protein binding, bridging
GO:0005102 F:receptor binding
GO:0005198 F:structural molecule activity
GO:0006916 P:anti-apoptosis
GO:0007166 P:cell surface receptor linked signaling pathway
GO:0006928 P:cellular component movement
GO:0006954 P:inflammatory response
GO:0030216 P:keratinocyte differentiation
GO:0006629 P:lipid metabolic process
GO:0018149 P:peptide cross-linking
GO:0031340 P:positive regulation of vesicle fusion
GO:0007165 P:signal transduction

References (15)

[1] “Cloning and expression of human lipocortin, a phospholipase A2 inhibitor with potential anti-inflammatory activity.”  Wallner B.P.et.al.   2936963
[2] “Correlation of gene and protein structure of rat and human lipocortin I.”  Kovacic R.T.et.al.   1832554
[3] “Structural characterization of a biologically active human lipocortin 1 expressed in Escherichia coli.”  Arcone R.et.al.   8425544
[4] “The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).”  The MGC Project Teamet.al.   15489334
[5] “Location of sites in human lipocortin I that are phosphorylated by protein tyrosine kinases and protein kinases A and C.”  Varticovski L.et.al.   2457390
[6] “Characterization by tandem mass spectrometry of structural modifications in proteins.”  Biemann K.et.al.   3303336
[7] “A dimeric form of lipocortin-1 in human placenta.”  Pepinsky R.B.et.al.   2532504
[8] “Phosphorylation of annexin I by TRPM7 channel-kinase.”  Dorovkov M.V.et.al.   15485879
[9] “Immunoaffinity profiling of tyrosine phosphorylation in cancer cells.”  Rush J.et.al.   15592455
[10] “Global, in vivo, and site-specific phosphorylation dynamics in signaling networks.”  Olsen J.V.et.al.   17081983
[11] “Global survey of phosphotyrosine signaling identifies oncogenic kinases in lung cancer.”  Rikova K.et.al.   18083107
[12] “An extensive survey of tyrosine phosphorylation revealing new sites in human mammary epithelial cells.”  Heibeck T.H.et.al.   19534553
[13] “Lysine acetylation targets protein complexes and co-regulates major cellular functions.”  Choudhary C.et.al.   19608861
[14] “Crystal structure of human annexin I at 2.5-A resolution.”  Weng X.et.al.   8453382
[15] “NMR solution structure of domain 1 of human annexin I shows an autonomous folding unit.”  Gao J.et.al.   9915835
Structure:
1AIN   1BO9   1QLS     

External Searches:

  • Search: DB with
  • BLAST ExPASy (Swiss Institute of Bioinformatics (SIB) BLAST)
  • CDD Search (Conserved Domain Database)
  • Search COGs (Clusters of Orthologous Groups of proteins)
  • 2° Structure (Network Protein Sequence Analysis)

Analyze:

Predict TMSs (Predict number of transmembrane segments)
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FASTA formatted sequence
1:	MAMVSEFLKQ AWFIENEEQE YVQTVKSSKG GPGSAVSPYP TFNPSSDVAA LHKAIMVKGV 
61:	DEATIIDILT KRNNAQRQQI KAAYLQETGK PLDETLKKAL TGHLEEVVLA LLKTPAQFDA 
121:	DELRAAMKGL GTDEDTLIEI LASRTNKEIR DINRVYREEL KRDLAKDITS DTSGDFRNAL 
181:	LSLAKGDRSE DFGVNEDLAD SDARALYEAG ERRKGTDVNV FNTILTTRSY PQLRRVFQKY 
241:	TKYSKHDMNK VLDLELKGDI EKCLTAIVKC ATSKPAFFAE KLHQAMKGVG TRHKALIRIM 
301:	VSRSEIDMND IKAFYQKMYG ISLCQAILDE TKGDYEKILV ALCGGN