UniProt Accession

 GEMI_HUMAN; O75496; B3KMM8; Q9H1Z1 

Genbank Protein ID

 AF067855; AK021685; AL133264; BC005185; BC005389 

Genbank Nucleotide ID

 AAC39787.1; BAG51040.1; CAC21511.1; AAH05185.1; AAH05389.1 

Protein Name

 Geminin 

Protein Synonyms/Alias

  

Gene Name

 GMNN 

Gene Synonyms/Alias

  

Created Date

 July 27, 2013 

Organism

 Homo sapiens (Human) 

NCBI Taxa ID

 9606 

Lysine Modification

Position	Peptide	Type	References
6	**MNPSMKQKQEEIK	ubiquitination	[1]
27	SVPRRTLKMIQPSAS	acetylation	[2]
50	ELSAGLSKRKHRNDH	ubiquitination	[1, 3]
105	YWKEVAEKRRKALYE	acetylation	[4]
127	LHKEIEQKDNEIARL	ubiquitination	[1]
139	ARLKKENKELAEVAE	ubiquitination	[5]

Reference

 [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] 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]
 [3] 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]
 [4] 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]
 [5] 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] 

Functional Description

 Inhibits DNA replication by preventing the incorporation of MCM complex into pre-replication complex (pre-RC). It is degraded during the mitotic phase of the cell cycle. Its destruction at the metaphase-anaphase transition permits replication in the succeeding cell cycle. 

Sequence Annotation

 REGION 82 161 Necessary and sufficient for interaction
 REGION 170 190 Homeodomain binding.
 MOD_RES 27 27 N6-acetyllysine.
 MOD_RES 63 63 Phosphoserine.
 MOD_RES 64 64 Phosphoserine.
 MOD_RES 184 184 Phosphoserine; by CK2.  

Keyword

 3D-structure; Acetylation; Cell cycle; Coiled coil; Complete proteome; Cytoplasm; DNA replication inhibitor; Nucleus; Phosphoprotein; Polymorphism; Reference proteome. 

Sequence Source

 UniProt (SWISSPROT/TrEMBL); GenBank; EMBL 

Protein Length

 209 AA 

Protein Sequence

Gene Ontology

 GO:0005829; C:cytosol; TAS:Reactome.
 GO:0005654; C:nucleoplasm; TAS:Reactome.
 GO:0003714; F:transcription corepressor activity; IEA:Compara.
 GO:0000278; P:mitotic cell cycle; TAS:Reactome.
 GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB.
 GO:0008156; P:negative regulation of DNA replication; IDA:UniProtKB.
 GO:0045892; P:negative regulation of transcription, DNA-dependent; IDA:UniProtKB.
 GO:0009887; P:organ morphogenesis; IEA:Compara.
 GO:0006461; P:protein complex assembly; IEA:Compara. 

Interpro

 IPR022786; Geminin_fam. 

Pfam

 PF07412; Geminin 

SMART

  

PROSITE

  

PRINTS