UniProt Accession

 S10A6_HUMAN; P06703; D3DV39; Q5RHS4 

Genbank Protein ID

 M14300; J02763; M18981; AY034480; BT006965; BX470102; CH471121; CH471121; CH471121; CH471121; CH471121; CH471121; CH471121; CH471121; BC001431; BC009017 

Genbank Nucleotide ID

 AAA35886.1; AAA51905.1; AAA51906.1; AAK59702.1; AAP35611.1; CAI14752.1; EAW53318.1; EAW53320.1; EAW53321.1; EAW53322.1; EAW53323.1; EAW53324.1; EAW53325.1; EAW53326.1; AAH01431.1; AAH09017.1 

Protein Name

 Protein S100-A6 

Protein Synonyms/Alias

 Calcyclin; Growth factor-inducible protein 2A9; MLN 4; Prolactin receptor-associated protein; PRA; S100 calcium-binding protein A6 

Gene Name

 S100A6 

Gene Synonyms/Alias

 CACY 

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
31	GDKHTLSKKELKELI	ubiquitination	[1, 2]
35	TLSKKELKELIQKEL	acetylation	[3]
35	TLSKKELKELIQKEL	ubiquitination	[1]
40	ELKELIQKELTIGSK	acetylation	[4, 5]
40	ELKELIQKELTIGSK	ubiquitination	[1, 2]
47	KELTIGSKLQDAEIA	acetylation	[3, 6]
47	KELTIGSKLQDAEIA	ubiquitination	[1, 2, 7, 8, 9]

Reference

 [1] 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]
 [2] 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]
 [3] 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]
 [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] 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]
 [6] Spermidine and resveratrol induce autophagy by distinct pathways converging on the acetylproteome.
 Morselli E, Mariño G, Bennetzen MV, Eisenberg T, Megalou E, Schroeder S, Cabrera S, Bénit P, Rustin P, Criollo A, Kepp O, Galluzzi L, Shen S, Malik SA, Maiuri MC, Horio Y, López-Otín C, Andersen JS, Tavernarakis N, Madeo F, Kroemer G.
 J Cell Biol. 2011 Feb 21;192(4):615-29. [PMID: 21339330]
 [7] 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]
 [8] Ubiquitin ligase substrate identification through quantitative proteomics at both the protein and peptide levels.
 Lee KA, Hammerle LP, Andrews PS, Stokes MP, Mustelin T, Silva JC, Black RA, Doedens JR.
 J Biol Chem. 2011 Dec 2;286(48):41530-8. [PMID: 21987572]
 [9] Systems-wide analysis of ubiquitylation dynamics reveals a key role for PAF15 ubiquitylation in DNA-damage bypass.
 Povlsen LK, Beli P, Wagner SA, Poulsen SL, Sylvestersen KB, Poulsen JW, Nielsen ML, Bekker-Jensen S, Mailand N, Choudhary C.
 Nat Cell Biol. 2012 Oct;14(10):1089-98. [PMID: 23000965] 

Functional Description

 May function as calcium sensor and contribute to cellular calcium signaling (Potential). May function by interacting with other proteins and indirectly play a role in the reorganization of the actin cytoskeleton and in cell motility. Binds 2 calcium ions. Calcium binding is cooperative. 

Sequence Annotation

 DOMAIN 12 47 EF-hand 1.
 DOMAIN 48 83 EF-hand 2.
 MOD_RES 40 40 N6-acetyllysine.  

Keyword

 3D-structure; Acetylation; Calcium; Cell membrane; Complete proteome; Cytoplasm; Direct protein sequencing; Membrane; Metal-binding; Nucleus; Polymorphism; Reference proteome; Repeat. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 90 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0031234; C:extrinsic to internal side of plasma membrane; IDA:UniProtKB.
 GO:0005635; C:nuclear envelope; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0001726; C:ruffle; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IDA:UniProtKB.
 GO:0048306; F:calcium-dependent protein binding; IDA:UniProtKB.
 GO:0015075; F:ion transmembrane transporter activity; IEA:Compara.
 GO:0042803; F:protein homodimerization activity; IDA:UniProtKB.
 GO:0005523; F:tropomyosin binding; IDA:UniProtKB.
 GO:0008270; F:zinc ion binding; IEA:Compara.
 GO:0007409; P:axonogenesis; NAS:UniProtKB.
 GO:0048146; P:positive regulation of fibroblast proliferation; NAS:UniProtKB.
 GO:0007165; P:signal transduction; TAS:UniProtKB. 

Interpro

 IPR011992; EF-hand-like_dom.
 IPR018247; EF_Hand_1_Ca_BS.
 IPR002048; EF_hand_dom.
 IPR001751; S100/CaBP-9k_CS.
 IPR013787; S100_Ca-bd_sub. 

Pfam

 PF01023; S_100 

SMART

  

PROSITE

 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS00303; S100_CABP 

PRINTS