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geminin (human)

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 Cellular Component: nucleoplasm; cytoplasm; cytosol; nucleus Molecular Function: protein binding; histone deacetylase binding; transcription corepressor activity Biological Process: organ morphogenesis; M/G1 transition of mitotic cell cycle; 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®

Select Structure to View Below geminin 1T6F - A/B=110-145 (human) 1UII - A/B=70-152 (human) 2LP0 - B=171-190 (human) 2WVR - A/B=1-209 (human) 1WLQ - A/B/D/E=79-157 (mouse) 2ZXX - A/D/E/B=79-157 (mouse)

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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

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		S36-p	IQPSASGsLVGRENE
0	5		K50-u	ELSAGLSkRKHRNDH
0	2		K50-a	ELSAGLSkRKHRNDH
0	1		S63-p	DHLTSTTssPGVIVP
0	4		S64-p	HLTSTTssPGVIVPE
0	1		S95-p	LMIKENPssQyWKEV
0	1		S96-p	MIKENPssQyWKEVA
0	1		Y98-p	KENPssQyWKEVAEk
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	AQENVKNSPVPRRTL
K27	PVPRRTLKMIQPSAD
S36	IQPSADGSLVGRENE
K50	ELPKGLFKRKLWDDQ
K50	ELPKGLFKRKLWDDQ
S63	DQLASQTSSCGPEAN
S64	QLASQTSSCGPEANE
S92	LISKENPSSQYWKEV
S93	ISKENPSSQYWKEVA
Y95	KENPSSQYWKEVAEQ
Q102	YWKEVAEQRRKALYE
S181	EEEAVEYSELEDSGA
S197	TCAEETVSSSTDARP
S198	CAEETVSSSTDARPC
S199	AEETVSSSTDARPCT
T200	EETVSSSTDARPCT_

	rat
S19-p	AQENVKSsPVPRRTL
K27	PVPRRTLKMIQPSAA
S36	IQPSAAGSLVGRENE
K50	ELPKGLSKRKLWDDQ
K50	ELPKGLSKRKLWDDQ
S63	DQLTSKISSCGPEAN
S64	QLTSKISSCGPEANE
S92	LMTKENPSSQYWKEV
S93	MTKENPSSQYWKEVA
Y95	KENPSSQYWKEVAEQ
Q102	YWKEVAEQRRKALYE
S181	EKETVEYSEPEDSDT
S197	TCAEETVSSSSDGTA
S198	CAEETVSSSSDGTAC
S199	AEETVSSSSDGTACT
S200	EETVSSSSDGTACT_

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