UniProt Accession

 S10AD_HUMAN; Q99584; Q52PI9; Q6FGF8 

Genbank Protein ID

 X99920; CR542149; BT006724; BX470102; BC000632; BC068064; BC070291; AY987392 

Genbank Nucleotide ID

 CAA68188.1; CAG46946.1; AAP35370.1; CAI14760.1; AAH00632.1; AAH68064.1; AAH70291.1; AAX89402.1 

Protein Name

 Protein S100-A13 

Protein Synonyms/Alias

 S100 calcium-binding protein A13 

Gene Name

 S100A13 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
61	GSLDEKMKSLDVNQD	ubiquitination	[1, 2, 3, 4, 5, 6]

Reference

 [1] 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]
 [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] 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]
 [4] 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]
 [5] 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]
 [6] hCKSAAP_UbSite: improved prediction of human ubiquitination sites by exploiting amino acid pattern and properties.
 Chen Z, Zhou Y, Song J, Zhang Z.
 Biochim Biophys Acta. 2013 Aug;1834(8):1461-7. [PMID: 23603789] 

Functional Description

 Plays a role in the export of proteins that lack a signal peptide and are secreted by an alternative pathway. Binds two calcium ions per subunit. Binds one copper ion. Binding of one copper ion does not interfere with calcium binding. Required for the copper-dependent stress-induced export of IL1A and FGF1. The calcium-free protein binds to lipid vesicles containing phosphatidylserine, but not to vesicles containing phosphatidylcholine (By similarity). 

Sequence Annotation

 DOMAIN 18 53 EF-hand.
 MOD_RES 32 32 Phosphoserine (By similarity).  

Keyword

 3D-structure; Calcium; Complete proteome; Copper; Cytoplasm; Lipid-binding; Metal-binding; Phosphoprotein; Protein transport; Reference proteome; Repeat; Secreted; Transport. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 98 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; IDA:UniProtKB.
 GO:0005615; C:extracellular space; IDA:UniProtKB.
 GO:0005634; C:nucleus; IDA:UniProtKB.
 GO:0048471; C:perinuclear region of cytoplasm; IDA:UniProtKB.
 GO:0005509; F:calcium ion binding; IDA:UniProtKB.
 GO:0005507; F:copper ion binding; IDA:UniProtKB.
 GO:0008289; F:lipid binding; IEA:UniProtKB-KW.
 GO:0008270; F:zinc ion binding; IDA:UniProtKB.
 GO:0050703; P:interleukin-1 alpha secretion; IDA:UniProtKB.
 GO:0043303; P:mast cell degranulation; NAS:UniProtKB.
 GO:0008284; P:positive regulation of cell proliferation; IEA:Compara.
 GO:0043123; P:positive regulation of I-kappaB kinase/NF-kappaB cascade; IDA:UniProtKB.
 GO:0008360; P:regulation of cell shape; IEA:Compara.
 GO:0046688; P:response to copper ion; IEA:Compara.
 GO:0051602; P:response to electrical stimulus; IEA:Compara. 

Interpro

 IPR011992; EF-hand-like_dom.
 IPR013787; S100_Ca-bd_sub. 

Pfam

 PF01023; S_100 

SMART

  

PROSITE

 PS00018; EF_HAND_1
 PS50222; EF_HAND_2
 PS00303; S100_CABP 

PRINTS