UniProt Accession

 AXA2L_HUMAN; A6NMY6 

Genbank Protein ID

 M62898; AL139008 

Genbank Nucleotide ID

  

Protein Name

 Putative annexin A2-like protein 

Protein Synonyms/Alias

 Annexin A2 pseudogene 2; Lipocortin II pseudogene 

Gene Name

 ANXA2P2 

Gene Synonyms/Alias

 ANX2L2; ANX2P2; LPC2B 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
10	TVHEILCKLSLEGDH	acetylation	[1]
28	PSAYGSVKAYTNFDA	ubiquitination	[2, 3]
47	LNIETAIKTKGVDEV	acetylation	[1]
47	LNIETAIKTKGVDEV	ubiquitination	[2, 3]
49	IETAIKTKGVDEVTI	ubiquitination	[3]
81	SYQRRTKKELASALK	acetylation	[1]
104	TVILGLLKTPAQYDA	acetylation	[4]
104	TVILGLLKTPAQYDA	ubiquitination	[2, 3, 5, 6]
115	QYDASELKASMKGLG	acetylation	[1, 4, 7]
115	QYDASELKASMKGLG	ubiquitination	[2, 3]
119	SELKASMKGLGTDED	ubiquitination	[3]
148	QEINRVYKEMYKTDL	acetylation	[4, 7]
148	QEINRVYKEMYKTDL	ubiquitination	[2, 3, 8, 9]
152	RVYKEMYKTDLEKDI	acetylation	[4, 7]
152	RVYKEMYKTDLEKDI	ubiquitination	[2, 3]
157	MYKTDLEKDIISDTS	acetylation	[1, 4, 7, 10]
157	MYKTDLEKDIISDTS	ubiquitination	[2, 3, 5]
176	KLMVALAKGRRAEDG	acetylation	[1]
176	KLMVALAKGRRAEDG	ubiquitination	[3]
204	DLYDAGVKRKGTDVP	acetylation	[7]
204	DLYDAGVKRKGTDVP	ubiquitination	[3]
212	RKGTDVPKWISIMTE	acetylation	[1, 7]
212	RKGTDVPKWISIMTE	ubiquitination	[2, 3]
227	RSVPHLQKVFDRYKS	acetylation	[1, 4, 7]
227	RSVPHLQKVFDRYKS	ubiquitination	[3, 8]
233	QKVFDRYKSYSPYDM	ubiquitination	[3]
279	DQLYDSMKGKGTRDK	acetylation	[4, 7]
302	RSEVDMLKIRSEFKR	acetylation	[1, 4, 7]
302	RSEVDMLKIRSEFKR	ubiquitination	[2, 3]
313	EFKRKYGKSLYYYIQ	acetylation	[1, 4, 7]
313	EFKRKYGKSLYYYIQ	ubiquitination	[2, 3, 5, 8]
324	YYIQQDTKGDYQKAL	acetylation	[7]
324	YYIQQDTKGDYQKAL	ubiquitination	[2, 3, 5, 6]
329	DTKGDYQKALLYLCG	ubiquitination	[3, 6]

Reference

 [1] Proteomic investigations of lysine acetylation identify diverse substrates of mitochondrial deacetylase sirt3.
 Sol EM, Wagner SA, Weinert BT, Kumar A, Kim HS, Deng CX, Choudhary C.
 PLoS One. 2012;7(12):e50545. [PMID: 23236377]
 [2] Systematic and quantitative assessment of the ubiquitin-modified proteome.
 Kim W, Bennett EJ, Huttlin EL, Guo A, Li J, Possemato A, Sowa ME, Rad R, Rush J, Comb MJ, Harper JW, Gygi SP.
 Mol Cell. 2011 Oct 21;44(2):325-40. [PMID: 21906983]
 [3] Landscape of the PARKIN-dependent ubiquitylome in response to mitochondrial depolarization.
 Sarraf SA, Raman M, Guarani-Pereira V, Sowa ME, Huttlin EL, Gygi SP, Harper JW.
 Nature. 2013 Apr 18;496(7445):372-6. [PMID: 23503661]
 [4] Lysine acetylation targets protein complexes and co-regulates major cellular functions.
 Choudhary C, Kumar C, Gnad F, Nielsen ML, Rehman M, Walther TC, Olsen JV, Mann M.
 Science. 2009 Aug 14;325(5942):834-40. [PMID: 19608861]
 [5] Mass spectrometric analysis of lysine ubiquitylation reveals promiscuity at site level.
 Danielsen JM, Sylvestersen KB, Bekker-Jensen S, Szklarczyk D, Poulsen JW, Horn H, Jensen LJ, Mailand N, Nielsen ML.
 Mol Cell Proteomics. 2011 Mar;10(3):M110.003590. [PMID: 21139048]
 [6] Global identification of modular cullin-RING ligase substrates.
 Emanuele MJ, Elia AE, Xu Q, Thoma CR, Izhar L, Leng Y, Guo A, Chen YN, Rush J, Hsu PW, Yen HC, Elledge SJ.
 Cell. 2011 Oct 14;147(2):459-74. [PMID: 21963094]
 [7] Proteomic investigations reveal a role for RNA processing factor THRAP3 in the DNA damage response.
 Beli P, Lukashchuk N, Wagner SA, Weinert BT, Olsen JV, Baskcomb L, Mann M, Jackson SP, Choudhary C.
 Mol Cell. 2012 Apr 27;46(2):212-25. [PMID: 22424773]
 [8] A proteome-wide, quantitative survey of in vivo ubiquitylation sites reveals widespread regulatory roles.
 Wagner SA, Beli P, Weinert BT, Nielsen ML, Cox J, Mann M, Choudhary C.
 Mol Cell Proteomics. 2011 Oct;10(10):M111.013284. [PMID: 21890473]
 [9] Refined preparation and use of anti-diglycine remnant (K-ε-GG) antibody enables routine quantification of 10,000s of ubiquitination sites in single proteomics experiments.
 Udeshi ND, Svinkina T, Mertins P, Kuhn E, Mani DR, Qiao JW, Carr SA.
 Mol Cell Proteomics. 2013 Mar;12(3):825-31. [PMID: 23266961]
 [10] Regulation of cellular metabolism by protein lysine acetylation.
 Zhao S, Xu W, Jiang W, Yu W, Lin Y, Zhang T, Yao J, Zhou L, Zeng Y, Li H, Li Y, Shi J, An W, Hancock SM, He F, Qin L, Chin J, Yang P, Chen X, Lei Q, Xiong Y, Guan KL.
 Science. 2010 Feb 19;327(5968):1000-4. [PMID: 20167786] 

Functional Description

 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). 

Sequence Annotation

 REPEAT 37 102 Annexin 1.
 REPEAT 109 174 Annexin 2.
 REPEAT 193 259 Annexin 3.
 REPEAT 269 334 Annexin 4.
 REGION 2 24 S100A10-binding site (Potential).
 MOD_RES 2 2 N-acetylserine (By similarity).
 MOD_RES 24 24 Phosphotyrosine; by SRC (By similarity).
 MOD_RES 26 26 Phosphoserine (By similarity).  

Keyword

 Acetylation; Annexin; Basement membrane; Calcium; Calcium/phospholipid-binding; Complete proteome; Extracellular matrix; Phosphoprotein; Reference proteome; Repeat; Secreted. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 339 AA 

Protein Sequence

Gene Ontology

 GO:0005604; C:basement membrane; IEA:UniProtKB-SubCell.
 GO:0042470; C:melanosome; IEA:UniProtKB-SubCell.
 GO:0005509; F:calcium ion binding; IEA:InterPro.
 GO:0005544; F:calcium-dependent phospholipid binding; IEA:UniProtKB-KW.
 GO:0004859; F:phospholipase inhibitor activity; IEA:InterPro. 

Interpro

 IPR001464; Annexin.
 IPR018502; Annexin_repeat.
 IPR018252; Annexin_repeat_CS.
 IPR002389; AnnexinII. 

Pfam

 PF00191; Annexin 

SMART

 SM00335; ANX 

PROSITE

 PS00223; ANNEXIN 

PRINTS

 PR00196; ANNEXIN.
 PR00198; ANNEXINII.