Javascript is not enabled on this browser. This site will not work properly without Javascript.
PhosphoSitePlus Homepage Cell Signaling Technology
PhosphoSitePlus
HomeAbout PhosphoSiteUsing PhosphoSiteCuration ProcessContact
NIH-logos NIGMS Logo NIAAA Logo NCI Logo NIH Logo
Protein Page:
Geminin (human)
p Phosphorylation
a Acetylation
m Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
u Ubiquitination
s Sumoylation
n Neddylation
gl O-GlcNAc
ga O-GalNAc
h Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage

Overview
Geminin 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. Homotetramer. Interacts with CDT1; inhibits binding of the MCM complex to origins of replication. Interacts with IDAS; targets GMNN to the nucleus, prevents GMNN interaction with CDT1 and competes with IDAS homodimerization. Belongs to the geminin family. Note: This description may include information from UniProtKB.
Protein type: Cell cycle regulation; Motility/polarity/chemotaxis
Cellular Component: nucleoplasm; cytoplasm; nucleus; cytosol
Molecular Function: protein binding; histone deacetylase binding; transcription corepressor activity
Biological Process: organ morphogenesis; negative regulation of DNA replication; protein complex assembly; mitotic cell cycle; negative regulation of transcription, DNA-dependent; negative regulation of cell cycle
Reference #:  O75496 (UniProtKB)
Alt. Names/Synonyms: Gem; GEMI; Geminin; geminin, DNA replication inhibitor; GMNN; RP3-369A17.3
Gene Symbols: GMNN
Molecular weight: 23,565 Da
Basal Isoelectric point: 4.93  Predict pI for various phosphorylation states
Protein-Specific Antibodies or siRNAs from Cell Signaling Technology® Total Proteins
Select Structure to View Below

Geminin

Protein Structure Not Found.


STRING  |  Scansite  |  Phospho.ELM  |  NetworKIN  |  Pfam  |  RCSB PDB  |  Phospho3D  |  Source  |  GeneCards  |  UniProtKB  |  Entrez-Gene  |  GenPept  |  Ensembl Gene


Sites Implicated In
apoptosis, altered: S200‑p, S201‑p, S202‑p, T203‑p
molecular association, regulation: S184‑p

Modification Sites and Domains Show Modification Legend
Click here to view phosphorylation modifications only

Modification Sites in Parent Protein, Orthologs, and Isoforms Show Modification Legend
 

Show Multiple Sequence Alignment


 SS 

SS: The number of records in which this modification site was determined using site-specific methods. SS methods include amino acid sequencing, site-directed mutagenesis, modification site-specific antibodies, specific MS strategies, etc.


 MS 

MS: The number of records in which this modification site was assigned using ONLY proteomic discovery-mode mass spectrometry.


       human

 
0 1 S19 IKENIKNSSVPRRTL
0 1 K27-a SVPRRTLkMIQPSAs
0 1 S34-p kMIQPSAsGsLVGRE
0 2 S36-p IQPSAsGsLVGRENE
0 1 S49-p NELSAGLskRKHRND
0 2 K50-a ELSAGLskRKHRNDH
0 5 K50-u ELSAGLskRKHRNDH
0 1 S63-p DHLTSTTssPGVIVP
0 5 S64-p HLTSTTssPGVIVPE
0 1 S85-p LGGVTQEsFDLMIKE
0 1 K105-a YWKEVAEkRRKALYE
1 0 S184-p EEETVEDsLVEDSEI
1 0 S200-p TCAEGTVssstDAKP
1 0 S201-p CAEGTVssstDAKPC
1 0 S202-p AEGTVssstDAKPCI
1 0 T203-p EGTVssstDAKPCI_
  mouse

 
S19-p AQENVKNsPVPRRTL
K27 PVPRRTLKMIQPSAD
D34 KMIQPSADGSLVGRE
S36 IQPSADGSLVGRENE
F49 NELPKGLFKRKLWDD
K50 ELPKGLFKRKLWDDQ
K50 ELPKGLFKRKLWDDQ
S63 DQLASQTSSCGPEAN
S64 QLASQTSSCGPEANE
A82 VGDLTQEAFDLISKE
Q102 YWKEVAEQRRKALYE
S181 EEEAVEYSELEDSGA
S197 TCAEETVSSSTDARP
S198 CAEETVSSSTDARPC
S199 AEETVSSSTDARPCT
T200 EETVSSSTDARPCT_
  rat

 
S19-p AQENVKSsPVPRRTL
K27 PVPRRTLKMIQPSAA
A34 KMIQPSAAGSLVGRE
S36 IQPSAAGSLVGRENE
S49 NELPKGLSKRKLWDD
K50 ELPKGLSKRKLWDDQ
K50 ELPKGLSKRKLWDDQ
S63 DQLTSKISSCGPEAN
S64 QLTSKISSCGPEANE
A82 VGDLTQEACDLMTKE
Q102 YWKEVAEQRRKALYE
S181 EKETVEYSEPEDSDT
S197 TCAEETVSSSSDGTA
S198 CAEETVSSSSDGTAC
S199 AEETVSSSSDGTACT
S200 EETVSSSSDGTACT_
Home  |  Curator Login With enhanced literature mining using Linguamatics I2E I2E Logo Produced by 3rd Millennium  |  Design by Digizyme
©2003-2013 Cell Signaling Technology, Inc.