Reviewed, UniProtKB/Swiss-Prot O75496 (GEMI_HUMAN)

Names and origin

Protein names

Recommended name:
    Geminin

Gene names

Name:

GMNN

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	209 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is not processed.
Protein existence	Evidence 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 process	Cell cycle
Coding sequence diversity	Polymorphism
Domain	Coiled coil
Molecular function	DNA replication inhibitor
PTM	Phosphoprotein
Technical term	3D-structure
Gene Ontology (GO)
Biological process	cell 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 component	nucleoplasm Inferred from Experiment. Source: Reactome
Molecular function	protein binding Inferred from physical interaction. Source: IntAct
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
CDKN1A	P38936	1	EBI-371669,EBI-375077
CDKN2A	P42771	1	EBI-371669,EBI-375053
CDT1	Q9H211	5	EBI-371669,EBI-456953
MCM6	Q14566	1	EBI-371669,EBI-374900

Sequence annotation (Features)

Feature key

Position(s)

Length

Description

Graphical view

Feature identifier

Molecule processing

Chain

1 – 209

209

Geminin

PRO_0000148729

Regions

Coiled coil

94 – 144

51

Amino acid modifications

Modified residue

63

1

Phosphoserine Ref.7

Modified residue

64

1

Phosphoserine Ref.7 Ref.6

Natural variations

Natural variant

15

1

N → H: dbSNP rs34891389.

VAR_033959

Natural variant

18

1

N → T: dbSNP rs1923185. Ref.2

VAR_024233

Natural variant

48

1

L → F: dbSNP rs2307307.

VAR_033960

Natural variant

54

1

R → W: dbSNP rs2307306.

VAR_033961

Natural variant

60

1

S → P: dbSNP rs2307302.

VAR_053107

Natural variant

203

1

T → M: dbSNP rs2307303.

VAR_053108

Secondary structure

1

.

.

.

209

Helix Strand Turn

Details...

Helix

94 – 151

58

Sequences

	Sequence		Length	Mass (Da)
	O75496-1 [UniParc]. Last modified November 1, 1998. Version 1. Checksum: 0BABE60F6F5AC252	FASTA	209	23,565
	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

References

	« Hide 'large scale' referencesShow '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. , 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. , 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

EMBLGenBankDDBJ

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.

IPI

IPI00026309.

RefSeq

NP_056979.1.

UniGene

Hs.234896

3D structure databases

PDBPDBe

Entry	Method	Resolution (Å)	Chain	Positions	PDBsum
1T6F	X-ray	1.47	A/B	110-145	[»]
1UII	X-ray	2.00	A/B	70-152	[»]

SMR

O75496. Positions 82-159.

ModBase

Search...

Protein-protein interaction databases

IntAct

O75496. 4 interactions.

PTM databases

PhosphoSite

O75496.

Proteomic databases

PRIDE

O75496.

Genome annotation databases

Ensembl

ENSG00000112312. Homo sapiens. [Contig view]

GeneID

51053.

KEGG

hsa:51053.

Organism-specific databases

GeneCards

GC06P024883.

H-InvDB

HIX0005629.

HGNC

HGNC:17493. GMNN.

HPA

CAB011458.

MIM

602842. gene.

PharmGKB

PA38455.

GenAtlas

Search...

Phylogenomic databases

HOGENOM

O75496.

HOVERGEN

O75496.

OMA

O75496. ENPSSQY.

Enzyme and pathway databases

Reactome

REACT_152. Cell Cycle, Mitotic.
REACT_383. DNA Replication.

Gene expression databases

ArrayExpress

O75496.

Bgee

O75496.

CleanEx

HS_GMNN.

GermOnline

ENSG00000112312. Homo sapiens.

Family and domain databases

InterPro

IPR009984. Geminin.
[Graphical view]

PANTHER

PTHR13372. Geminin. 1 hit.

Pfam

PF07412. Geminin. 1 hit.
[Graphical view]

ProtoNet

Search...

Other Resources

NextBio

53616.

PMAP-CutDB

O75496.

SOURCE

Search...

Entry information

Entry name

GEMI_HUMAN

Accession

Primary (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 status

Reviewed (UniProtKB/Swiss-Prot)

Annotation project

HPI (Human Proteome Initiative)