CPLM-021602

Genbank Nucleotide ID

Calcyclin-binding protein

Protein Synonyms/Alias

CacyBP; hCacyBP; S100A6-binding protein; Siah-interacting protein

S100A6BP; SIP; PNAS-107

Homo sapiens (Human)

Position	Peptide	Type	References
8	MASEELQKDLEEVKV	acetylation	[1]
8	MASEELQKDLEEVKV	ubiquitination	[2]
14	QKDLEEVKVLLEKAT	ubiquitination	[2, 3]
19	EVKVLLEKATRKRVR	acetylation	[1]
19	EVKVLLEKATRKRVR	ubiquitination	[2]
33	RDALTAEKSKIETEI	ubiquitination	[4]
41	SKIETEIKNKMQQKS	ubiquitination	[2]
43	IETEIKNKMQQKSQK	ubiquitination	[2]
51	MQQKSQKKAELLDNE	ubiquitination	[2]
59	AELLDNEKPAAVVAP	acetylation	[5]
59	AELLDNEKPAAVVAP	ubiquitination	[2, 5]
85	YGWDQSDKFVKIYIT	acetylation	[1, 5, 6]
85	YGWDQSDKFVKIYIT	ubiquitination	[2, 3, 5]
118	RSFDLLVKNLNGKSY	acetylation	[1]
118	RSFDLLVKNLNGKSY	ubiquitination	[2, 3, 5, 7, 8, 9]
123	LVKNLNGKSYSMIVN	ubiquitination	[2, 3, 8, 10]
134	MIVNNLLKPISVEGS	acetylation	[1]
143	ISVEGSSKKVKTDTV	ubiquitination	[5, 7, 8, 9, 11]
144	SVEGSSKKVKTDTVL	ubiquitination	[2, 8]
146	EGSSKKVKTDTVLIL	ubiquitination	[2, 4, 5, 8]
171	DYLTQVEKECKEKEK	acetylation	[5]
171	DYLTQVEKECKEKEK	ubiquitination	[2, 5]
178	KECKEKEKPSYDTET	ubiquitination	[2, 4, 7, 8, 9]
196	EGLMNVLKKIYEDGD	ubiquitination	[2, 7]
197	GLMNVLKKIYEDGDD	ubiquitination	[2, 5, 7, 10]
207	EDGDDDMKRTINKAW	ubiquitination	[2, 5, 7, 8, 9, 10]
212	DMKRTINKAWVESRE	ubiquitination	[2, 3, 5, 7, 9, 10]
223	ESREKQAKGDTEF**	ubiquitination	[5]

[1] 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]
[2] 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]
[3] 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]
[4] Proteome-wide identification of ubiquitylation sites by conjugation of engineered lysine-less ubiquitin.
Oshikawa K, Matsumoto M, Oyamada K, Nakayama KI.
J Proteome Res. 2012 Feb 3;11(2):796-807. [PMID: 22053931]
[5] Integrated proteomic analysis of post-translational modifications by serial enrichment.
Mertins P, Qiao JW, Patel J, Udeshi ND, Clauser KR, Mani DR, Burgess MW, Gillette MA, Jaffe JD, Carr SA.
Nat Methods. 2013 Jul;10(7):634-7. [PMID: 23749302]
[6] 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]
[7] 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]
[8] 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]
[9] 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]
[10] Methods for quantification of in vivo changes in protein ubiquitination following proteasome and deubiquitinase inhibition.
Udeshi ND, Mani DR, Eisenhaure T, Mertins P, Jaffe JD, Clauser KR, Hacohen N, Carr SA.
Mol Cell Proteomics. 2012 May;11(5):148-59. [PMID: 22505724]
[11] 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]

Functional Description

May be involved in calcium-dependent ubiquitination and subsequent proteasomal degradation of target proteins. Probably serves as a molecular bridge in ubiquitin E3 complexes. Participates in the ubiquitin-mediated degradation of beta-catenin (CTNNB1).

DOMAIN 73 167 CS.
DOMAIN 168 228 SGS.
REGION 2 80 Interaction with SIAH1.
REGION 73 228 Interaction with SKP1.
REGION 154 228 Interaction with S100A6 (By similarity).
MOD_RES 2 2 N-acetylalanine.
MOD_RES 8 8 N6-acetyllysine.
MOD_RES 19 19 N6-acetyllysine.
MOD_RES 85 85 N6-acetyllysine.
MOD_RES 118 118 N6-acetyllysine.

3D-structure; Acetylation; Alternative splicing; Complete proteome; Cytoplasm; Direct protein sequencing; Nucleus; Phosphoprotein; Reference proteome; Ubl conjugation pathway.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0030877; C:beta-catenin destruction complex; IDA:UniProtKB.
GO:0044297; C:cell body; IEA:Compara.
GO:0043005; C:neuron projection; IEA:Compara.
GO:0005641; C:nuclear envelope lumen; IEA:Compara.
GO:0007568; P:aging; IEA:Compara.
GO:0055007; P:cardiac muscle cell differentiation; IEA:Compara.
GO:0071277; P:cellular response to calcium ion; IEA:Compara.
GO:0060548; P:negative regulation of cell death; IEA:Compara.
GO:0045740; P:positive regulation of DNA replication; IEA:Compara.
GO:0060416; P:response to growth hormone stimulus; IEA:Compara.

IPR007052; CS-like_domain.
IPR017447; CS_domain.
IPR008978; HSP20-like_chaperone.
IPR007699; SGS.
IPR015120; Siah-Interact_N.

PF04969; CS
PF05002; SGS
PF09032; Siah-Interact_N

PS51203; CS
PS51048; SGS