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Reviewed, UniProtKB/Swiss-Prot O75496 (GEMI_HUMAN)

Last modified June 16, 2009. Version 65. Feed History...

Clusters with 100%, 90%, 50% identity | Documents (6) | Third-party data | Customize display text xml rdf/xml gff fasta
Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents

Names and origin

Protein namesRecommended name:
    Geminin
Gene names
Name: GMNN
OrganismHomo sapiens (Human)
Taxonomic identifier9606 [NCBI]
Taxonomic lineageEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo

Protein attributes

Sequence length209 AA.
Sequence statusComplete.
Sequence processingThe displayed sequence is not processed.
Protein existenceEvidence at protein level.

General annotation (Comments)

Function

Inhibits DNA replication by preventing the incorporation of MCM complex into prereplication 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. Ref.1 Ref.5

Subunit structure

Homotetramer. Interaction with CDT1 inhibits binding of the MCM complex to origins of replication. Ref.8 Ref.9 Ref.10

Developmental stage

Absent during G1 phase, accumulates during S, G2, and M phases, and disappears at the time of the metaphase-anaphase transition. Ref.1

Sequence similarities

Belongs to the geminin family.

Ontologies

Keywords
   Biological processCell cycle
   Coding sequence diversityPolymorphism
   DomainCoiled coil
   Molecular functionDNA replication inhibitor
   PTMPhosphoprotein
   Technical term3D-structure
Gene Ontology (GO)
   Biological processcell cycle

Inferred from electronic annotation. Source: UniProtKB-KW

negative regulation of DNA replication Ref.1

Inferred from direct assay. Source: UniProtKB

negative regulation of cell cycle Ref.1

Inferred from direct assay. Source: UniProtKB

   Cellular componentnucleoplasm

Inferred from Experiment. Source: Reactome

   Molecular functionprotein binding

Inferred from physical interaction. Source: IntAct

Complete GO annotation...

Sequence annotation (Features)

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifier

Molecule processing

Chain1 – 209209Geminin
PRO_0000148729

Regions

Coiled coil94 – 14451

Amino acid modifications

Modified residue631Phosphoserine Ref.7
Modified residue641Phosphoserine Ref.7 Ref.6

Natural variations

Natural variant151N → H: dbSNP rs34891389.
VAR_033959
Natural variant181N → T: dbSNP rs1923185. Ref.2
VAR_024233
Natural variant481L → F: dbSNP rs2307307.
VAR_033960
Natural variant541R → W: dbSNP rs2307306.
VAR_033961
Natural variant601S → P: dbSNP rs2307302.
VAR_053107
Natural variant2031T → M: dbSNP rs2307303.
VAR_053108

Secondary structure

... 209
Helix Strand Turn

Details...

Sequences

Sequence LengthMass (Da)Tools
O75496-1 [UniParc].

Last modified November 1, 1998. Version 1.
Checksum: 0BABE60F6F5AC252

FASTA20923,565
        10         20         30         40         50         60 
MNPSMKQKQE EIKENIKNSS VPRRTLKMIQ PSASGSLVGR ENELSAGLSK RKHRNDHLTS 

        70         80         90        100        110        120 
TTSSPGVIVP ESSENKNLGG VTQESFDLMI KENPSSQYWK EVAEKRRKAL YEALKENEKL 

       130        140        150        160        170        180 
HKEIEQKDNE IARLKKENKE LAEVAEHVQY MAELIERLNG EPLDNFESLD NQEFDSEEET 

       190        200 
VEDSLVEDSE IGTCAEGTVS SSTDAKPCI 

« Hide

References

« Hide 'large scale' references
[1]"Geminin, an inhibitor of DNA replication, is degraded during mitosis."
McGarry T.J., Kirschner M.W.
Cell 93:1043-1053(1998) [PubMed: 9635433] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, DEVELOPMENTAL STAGE.
[2]"Complete sequencing and characterization of 21,243 full-length human cDNAs."
Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S. expand/collapse author list , Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., Isogai T., Sugano S.
Nat. Genet. 36:40-45(2004) [PubMed: 14702039] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], VARIANT THR-18.
Tissue: Embryo.
[3]"The DNA sequence and analysis of human chromosome 6."
Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., Andrews T.D. expand/collapse author list , Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., Rogers J., Beck S.
Nature 425:805-811(2003) [PubMed: 14574404] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]"The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)."
The MGC Project Team
Genome Res. 14:2121-2127(2004) [PubMed: 15489334] [Abstract]
Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
Tissue: Lung and Urinary bladder.
[5]"Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates its function without affecting geminin binding."
Sugimoto N., Tatsumi Y., Tsurumi T., Matsukage A., Kiyono T., Nishitani H., Fujita M.
J. Biol. Chem. 279:19691-19697(2004) [PubMed: 14993212] [Abstract]
Cited for: FUNCTION, INTERACTION WITH CDT1.
[6]"Global proteomic profiling of phosphopeptides using electron transfer dissociation tandem mass spectrometry."
Molina H., Horn D.M., Tang N., Mathivanan S., Pandey A.
Proc. Natl. Acad. Sci. U.S.A. 104:2199-2204(2007) [PubMed: 17287340] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-64, MASS SPECTROMETRY.
[7]"A quantitative atlas of mitotic phosphorylation."
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P.
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed: 18669648] [Abstract]
Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-64, MASS SPECTROMETRY.
[8]"Crystal structure of the coiled-coil dimerization motif of geminin: structural and functional insights on DNA replication regulation."
Thepaut M., Maiorano D., Guichou J.-F., Auge M.-T., Dumas C., Mechali M., Padilla A.
J. Mol. Biol. 342:275-287(2004) [PubMed: 15313623] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 110-145, SUBUNIT, COILED-COIL.
[9]"A dimerized coiled-coil domain and an adjoining part of geminin interact with two sites on Cdt1 for replication inhibition."
Saxena S., Yuan P., Dhar S.K., Senga T., Takeda D., Robinson H., Kornbluth S., Swaminathan K., Dutta A.
Mol. Cell 15:245-258(2004) [PubMed: 15260975] [Abstract]
Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 70-152, SUBUNIT, INTERACTION WITH CDT1, COILED-COIL.
[10]"Molecular structure of human geminin."
Okorokov A.L., Orlova E.V., Kingsbury S.R., Bagneris C., Gohlke U., Williams G.H., Stoeber K.
Nat. Struct. Mol. Biol. 11:1021-1022(2004) [PubMed: 15378034] [Abstract]
Cited for: ELECTRON MICROSCOPY (17.5 ANGSTROMS), SUBUNIT, COILED-COIL.
+Additional computationally mapped references.

Cross-references

Sequence databases

AF067855 mRNA. Translation: AAC39787.1.
AK021685 mRNA. Translation: BAG51040.1.
AL133264 Genomic DNA. Translation: CAC21511.1. Different initiation.
BC005185 mRNA. Translation: AAH05185.1.
BC005389 mRNA. Translation: AAH05389.1.
IPIIPI00026309.
RefSeqNP_056979.1.
UniGeneHs.234896

3D structure databases

EntryMethodResolution (Å)ChainPositionsPDBsum
1T6FX-ray1.47A/B110-145[»]
1UIIX-ray2.00A/B70-152[»]
SMRO75496. Positions 82-159.
ModBaseSearch...

Protein-protein interaction databases

IntActO75496. 4 interactions.

PTM databases

PhosphoSiteO75496.

Proteomic databases

PRIDEO75496.

Genome annotation databases

EnsemblENSG00000112312. Homo sapiens. [Contig view]
GeneID51053.
KEGGhsa:51053.

Organism-specific databases

GeneCardsGC06P024883.
H-InvDBHIX0005629.
HGNCHGNC:17493. GMNN.
HPACAB011458.
MIM602842. gene.
PharmGKBPA38455.
GenAtlasSearch...

Phylogenomic databases

HOGENOMO75496.
HOVERGENO75496.
OMAO75496. ENPSSQY.

Enzyme and pathway databases

ReactomeREACT_152. Cell Cycle, Mitotic.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpressO75496.
BgeeO75496.
CleanExHS_GMNN.
GermOnlineENSG00000112312. Homo sapiens.

Family and domain databases

InterProIPR009984. Geminin.
[Graphical view]
PANTHERPTHR13372. Geminin. 1 hit.
PfamPF07412. Geminin. 1 hit.
[Graphical view]
ProtoNetSearch...

Other Resources

NextBio53616.
PMAP-CutDBO75496.
SOURCESearch...

Entry information

Entry nameGEMI_HUMAN
AccessionPrimary (citable) accession number: O75496
Secondary accession number(s): B3KMM8, Q9H1Z1
Entry history
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1998
Last modified: June 16, 2009
This is version 65 of the entry and version 1 of the sequence. [Complete history]
Entry statusReviewed (UniProtKB/Swiss-Prot)
Annotation projectHPI (Human Proteome Initiative)

Relevant documents

Human chromosome 6

Human chromosome 6: entries, gene names and cross-references to MIM

Human entries with polymorphisms or disease mutations

List of human entries with polymorphisms or disease mutations

Human polymorphisms and disease mutations

Index of human polymorphisms and disease mutations

MIM cross-references

Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot

PDB cross-references

Index of Protein Data Bank (PDB) cross-references

SIMILARITY comments

Index of protein domains and families

Names and origin · Protein attributes · General annotation (Comments) · Ontologies · Binary interactions · Sequence annotation (Features) · Sequences · References · Cross-references · Entry information · Relevant documents