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Protein Page:
Geminin (human)
p Phosphorylation
ac Acetylation
me Methylation
m1 Mono-methylation
m2 Di-methylation
m3 Tri-methylation
ub Ubiquitination
sm Sumoylation
ne Neddylation
gl O-GlcNAc
ga O-GalNAc
pa Palmitoylation
ad Adenylylation
sn S-Nitrosylation
ca Caspase cleavage
sc Succinylation

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: Motility/polarity/chemotaxis; Cell cycle regulation
Chromosomal Location of Human Ortholog: 6p22.3
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.


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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 2 S19 IKENIKNSSVPRRTL
0 1 K27-ac SVPRRTLkMIQPSAs
0 1 S34-p kMIQPSAsGsLVGRE
0 2 S36-p IQPSAsGsLVGRENE
0 1 S45-p VGRENELsAGLskRK
0 2 S49-p NELsAGLskRKHRND
0 2 K50-ac ELsAGLskRKHRNDH
0 5 K50-ub ELsAGLskRKHRNDH
0 1 T61-p RNDHLTStTssPGVI
0 1 S63-p DHLTStTssPGVIVP
0 5 S64-p HLTStTssPGVIVPE
0 1 S85-p LGGVTQEsFDLMIKE
0 1 S95-p LMIKENPssQyWKEV
0 1 S96-p MIKENPssQyWKEVA
1 1 Y98-p KENPssQyWKEVAEk
0 1 K105-ac yWKEVAEkRRKALYE
1 0 Y150-p EVAEHVQyMAELIER
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
P45 VGRENELPKGLFKRK
F49 NELPKGLFKRKLWDD
K50 ELPKGLFKRKLWDDQ
K50 ELPKGLFKRKLWDDQ
- gap
S63 DQLASQTSSCGPEAN
S64 QLASQTSSCGPEANE
A82 VGDLTQEAFDLISKE
S92 LISKENPSSQYWKEV
S93 ISKENPSSQYWKEVA
Y95 KENPSSQYWKEVAEQ
Q102 YWKEVAEQRRKALYE
Y147 EVAEHVQYMAEVIER
S181 EEEAVEYSELEDSGA
S197 TCAEETVSSSTDARP
S198 CAEETVSSSTDARPC
S199 AEETVSSSTDARPCT
T200 EETVSSSTDARPCT_
  rat

 
S19-p AQENVKSsPVPRRTL
K27-ac PVPRRTLkMIQPSAA
A34 kMIQPSAAGSLVGRE
S36 IQPSAAGSLVGRENE
P45 VGRENELPKGLSKRK
S49 NELPKGLSKRKLWDD
K50 ELPKGLSKRKLWDDQ
K50 ELPKGLSKRKLWDDQ
- gap
S63 DQLTSKISSCGPEAN
S64 QLTSKISSCGPEANE
A82 VGDLTQEACDLMTKE
S92 LMTKENPSSQYWKEV
S93 MTKENPSSQYWKEVA
Y95 KENPSSQYWKEVAEQ
Q102 YWKEVAEQRRKALYE
Y147 EVAEHVQYMAEVIER
S181 EKETVEYSEPEDSDT
S197 TCAEETVSSSSDGTA
S198 CAEETVSSSSDGTAC
S199 AEETVSSSSDGTACT
S200 EETVSSSSDGTACT_
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