CPLM-020156

Genbank Nucleotide ID

Mini-chromosome maintenance complex-binding protein

Protein Synonyms/Alias

MCM-BP; MCM-binding protein

Homo sapiens (Human)

Position	Peptide	Type	References
31	VNPDWEKKVIEYFKE	ubiquitination	[1, 2]
37	KKVIEYFKEKLKENN	ubiquitination	[1]
47	LKENNAPKWVPSLNE	ubiquitination	[3]
61	EVPLHYLKPNSFVKF	acetylation	[4, 5]
61	EVPLHYLKPNSFVKF	ubiquitination	[1, 2, 3, 6, 7, 8, 9]
67	LKPNSFVKFRCMIQD	ubiquitination	[1]
101	AHVLHFGKYRDVAEC	ubiquitination	[1]
142	PGESTWVKEAYVNAN	ubiquitination	[1, 2, 7, 8]
180	DMDLQPNKQKDQHAG	ubiquitination	[1, 2, 6, 7, 10]
182	DLQPNKQKDQHAGAR	ubiquitination	[1]
204	LQWCGEPKRLETEAS	ubiquitination	[1, 2, 6]
235	NFPLPGEKGPACLVK	ubiquitination	[1, 7]
242	KGPACLVKVYEDWDC	ubiquitination	[1, 2, 7]
314	IHVILAQKLQHINPL	ubiquitination	[1, 7]
328	LLPACLNKEESKTCK	acetylation	[2, 4, 5]
328	LLPACLNKEESKTCK	ubiquitination	[1, 2]
332	CLNKEESKTCKFVSS	ubiquitination	[1, 3, 6]
388	RDVLPLGKFTVNLSG	ubiquitination	[1, 2, 3, 7]
431	IENMNHLKFIPHKDY	ubiquitination	[1]
436	HLKFIPHKDYTANRL	ubiquitination	[1, 2]
582	DDFVEMRKNDPQSIT	ubiquitination	[1, 2, 6, 8, 10, 11, 12]
621	RERWLRAKQLESLRR	ubiquitination	[1]
635	RTRLQQQKCVNGNEL	ubiquitination	[1, 2, 6, 7, 8, 13]

[1] 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]
[2] 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]
[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] 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 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]
[6] 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]
[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] 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]
[9] 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]
[10] 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]
[11] A data set of human endogenous protein ubiquitination sites.
Shi Y, Chan DW, Jung SY, Malovannaya A, Wang Y, Qin J.
Mol Cell Proteomics. 2011 May;10(5):M110.002089. [PMID: 20972266]
[12] 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]
[13] 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]

Functional Description

Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion.

MOD_RES 154 154 Phosphoserine.
MOD_RES 160 160 Phosphothreonine.
MOD_RES 298 298 Phosphoserine.

Alternative splicing; Cell cycle; Cell division; Complete proteome; DNA replication; Mitosis; Nucleus; Phosphoprotein; Reference proteome.

UniProt (SWISSPROT/TrEMBL); GenBank; EMBL

GO:0005737; C:cytoplasm; IDA:HPA.
GO:0005634; C:nucleus; IDA:UniProtKB.
GO:0005886; C:plasma membrane; IDA:HPA.
GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO:0006261; P:DNA-dependent DNA replication; IMP:UniProtKB.
GO:0007067; P:mitosis; IEA:UniProtKB-KW.
GO:0000084; P:S phase of mitotic cell cycle; IMP:UniProtKB.
GO:0007062; P:sister chromatid cohesion; IMP:UniProtKB.

IPR019140; MCM_complex-bd.