ID GEMI_HUMAN Reviewed; 209 AA. AC O75496; B3KMM8; Q9H1Z1; DT 02-MAY-2002, integrated into UniProtKB/Swiss-Prot. DT 01-NOV-1998, sequence version 1. DT 27-MAR-2024, entry version 189. DE RecName: Full=Geminin; GN Name=GMNN; OS Homo sapiens (Human). OC Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi; Mammalia; OC Eutheria; Euarchontoglires; Primates; Haplorrhini; Catarrhini; Hominidae; OC Homo. OX NCBI_TaxID=9606; RN [1] RP NUCLEOTIDE SEQUENCE [MRNA], FUNCTION, AND DEVELOPMENTAL STAGE. RX PubMed=9635433; DOI=10.1016/s0092-8674(00)81209-x; RA McGarry T.J., Kirschner M.W.; RT "Geminin, an inhibitor of DNA replication, is degraded during mitosis."; RL Cell 93:1043-1053(1998). RN [2] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA], AND VARIANT THR-18. RC TISSUE=Embryo; RX PubMed=14702039; DOI=10.1038/ng1285; RA Ota T., Suzuki Y., Nishikawa T., Otsuki T., Sugiyama T., Irie R., RA Wakamatsu A., Hayashi K., Sato H., Nagai K., Kimura K., Makita H., RA Sekine M., Obayashi M., Nishi T., Shibahara T., Tanaka T., Ishii S., RA Yamamoto J., Saito K., Kawai Y., Isono Y., Nakamura Y., Nagahari K., RA Murakami K., Yasuda T., Iwayanagi T., Wagatsuma M., Shiratori A., Sudo H., RA Hosoiri T., Kaku Y., Kodaira H., Kondo H., Sugawara M., Takahashi M., RA Kanda K., Yokoi T., Furuya T., Kikkawa E., Omura Y., Abe K., Kamihara K., RA Katsuta N., Sato K., Tanikawa M., Yamazaki M., Ninomiya K., Ishibashi T., RA Yamashita H., Murakawa K., Fujimori K., Tanai H., Kimata M., Watanabe M., RA Hiraoka S., Chiba Y., Ishida S., Ono Y., Takiguchi S., Watanabe S., RA Yosida M., Hotuta T., Kusano J., Kanehori K., Takahashi-Fujii A., Hara H., RA Tanase T.-O., Nomura Y., Togiya S., Komai F., Hara R., Takeuchi K., RA Arita M., Imose N., Musashino K., Yuuki H., Oshima A., Sasaki N., RA Aotsuka S., Yoshikawa Y., Matsunawa H., Ichihara T., Shiohata N., Sano S., RA Moriya S., Momiyama H., Satoh N., Takami S., Terashima Y., Suzuki O., RA Nakagawa S., Senoh A., Mizoguchi H., Goto Y., Shimizu F., Wakebe H., RA Hishigaki H., Watanabe T., Sugiyama A., Takemoto M., Kawakami B., RA Yamazaki M., Watanabe K., Kumagai A., Itakura S., Fukuzumi Y., Fujimori Y., RA Komiyama M., Tashiro H., Tanigami A., Fujiwara T., Ono T., Yamada K., RA Fujii Y., Ozaki K., Hirao M., Ohmori Y., Kawabata A., Hikiji T., RA Kobatake N., Inagaki H., Ikema Y., Okamoto S., Okitani R., Kawakami T., RA Noguchi S., Itoh T., Shigeta K., Senba T., Matsumura K., Nakajima Y., RA Mizuno T., Morinaga M., Sasaki M., Togashi T., Oyama M., Hata H., RA Watanabe M., Komatsu T., Mizushima-Sugano J., Satoh T., Shirai Y., RA Takahashi Y., Nakagawa K., Okumura K., Nagase T., Nomura N., Kikuchi H., RA Masuho Y., Yamashita R., Nakai K., Yada T., Nakamura Y., Ohara O., RA Isogai T., Sugano S.; RT "Complete sequencing and characterization of 21,243 full-length human RT cDNAs."; RL Nat. Genet. 36:40-45(2004). RN [3] RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]. RX PubMed=14574404; DOI=10.1038/nature02055; RA Mungall A.J., Palmer S.A., Sims S.K., Edwards C.A., Ashurst J.L., RA Wilming L., Jones M.C., Horton R., Hunt S.E., Scott C.E., Gilbert J.G.R., RA Clamp M.E., Bethel G., Milne S., Ainscough R., Almeida J.P., Ambrose K.D., RA Andrews T.D., Ashwell R.I.S., Babbage A.K., Bagguley C.L., Bailey J., RA Banerjee R., Barker D.J., Barlow K.F., Bates K., Beare D.M., Beasley H., RA Beasley O., Bird C.P., Blakey S.E., Bray-Allen S., Brook J., Brown A.J., RA Brown J.Y., Burford D.C., Burrill W., Burton J., Carder C., Carter N.P., RA Chapman J.C., Clark S.Y., Clark G., Clee C.M., Clegg S., Cobley V., RA Collier R.E., Collins J.E., Colman L.K., Corby N.R., Coville G.J., RA Culley K.M., Dhami P., Davies J., Dunn M., Earthrowl M.E., Ellington A.E., RA Evans K.A., Faulkner L., Francis M.D., Frankish A., Frankland J., RA French L., Garner P., Garnett J., Ghori M.J., Gilby L.M., Gillson C.J., RA Glithero R.J., Grafham D.V., Grant M., Gribble S., Griffiths C., RA Griffiths M.N.D., Hall R., Halls K.S., Hammond S., Harley J.L., Hart E.A., RA Heath P.D., Heathcott R., Holmes S.J., Howden P.J., Howe K.L., Howell G.R., RA Huckle E., Humphray S.J., Humphries M.D., Hunt A.R., Johnson C.M., RA Joy A.A., Kay M., Keenan S.J., Kimberley A.M., King A., Laird G.K., RA Langford C., Lawlor S., Leongamornlert D.A., Leversha M., Lloyd C.R., RA Lloyd D.M., Loveland J.E., Lovell J., Martin S., Mashreghi-Mohammadi M., RA Maslen G.L., Matthews L., McCann O.T., McLaren S.J., McLay K., McMurray A., RA Moore M.J.F., Mullikin J.C., Niblett D., Nickerson T., Novik K.L., RA Oliver K., Overton-Larty E.K., Parker A., Patel R., Pearce A.V., Peck A.I., RA Phillimore B.J.C.T., Phillips S., Plumb R.W., Porter K.M., Ramsey Y., RA Ranby S.A., Rice C.M., Ross M.T., Searle S.M., Sehra H.K., Sheridan E., RA Skuce C.D., Smith S., Smith M., Spraggon L., Squares S.L., Steward C.A., RA Sycamore N., Tamlyn-Hall G., Tester J., Theaker A.J., Thomas D.W., RA Thorpe A., Tracey A., Tromans A., Tubby B., Wall M., Wallis J.M., RA West A.P., White S.S., Whitehead S.L., Whittaker H., Wild A., Willey D.J., RA Wilmer T.E., Wood J.M., Wray P.W., Wyatt J.C., Young L., Younger R.M., RA Bentley D.R., Coulson A., Durbin R.M., Hubbard T., Sulston J.E., Dunham I., RA Rogers J., Beck S.; RT "The DNA sequence and analysis of human chromosome 6."; RL Nature 425:805-811(2003). RN [4] RP NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]. RC TISSUE=Lung, and Urinary bladder; RX PubMed=15489334; DOI=10.1101/gr.2596504; RG The MGC Project Team; RT "The status, quality, and expansion of the NIH full-length cDNA project: RT the Mammalian Gene Collection (MGC)."; RL Genome Res. 14:2121-2127(2004). RN [5] RP FUNCTION, AND INTERACTION WITH CDT1. RX PubMed=14993212; DOI=10.1074/jbc.m313175200; RA Sugimoto N., Tatsumi Y., Tsurumi T., Matsukage A., Kiyono T., Nishitani H., RA Fujita M.; RT "Cdt1 phosphorylation by cyclin A-dependent kinases negatively regulates RT its function without affecting geminin binding."; RL J. Biol. Chem. 279:19691-19697(2004). RN [6] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-64, AND RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=18669648; DOI=10.1073/pnas.0805139105; RA Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., RA Elledge S.J., Gygi S.P.; RT "A quantitative atlas of mitotic phosphorylation."; RL Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008). RN [7] RP ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, AND IDENTIFICATION BY MASS RP SPECTROMETRY [LARGE SCALE ANALYSIS]. RX PubMed=19608861; DOI=10.1126/science.1175371; RA Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., RA Olsen J.V., Mann M.; RT "Lysine acetylation targets protein complexes and co-regulates major RT cellular functions."; RL Science 325:834-840(2009). RN [8] RP FUNCTION. RX PubMed=20129055; DOI=10.1016/j.molcel.2009.12.012; RA Miotto B., Struhl K.; RT "HBO1 histone acetylase activity is essential for DNA replication licensing RT and inhibited by Geminin."; RL Mol. Cell 37:57-66(2010). RN [9] RP IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma; RX PubMed=20068231; DOI=10.1126/scisignal.2000475; RA Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., RA Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.; RT "Quantitative phosphoproteomics reveals widespread full phosphorylation RT site occupancy during mitosis."; RL Sci. Signal. 3:RA3-RA3(2010). RN [10] RP SUBCELLULAR LOCATION, AND INTERACTION WITH IDAS AND CDT1. RX PubMed=21543332; DOI=10.1074/jbc.m110.207688; RA Pefani D.E., Dimaki M., Spella M., Karantzelis N., Mitsiki E., Kyrousi C., RA Symeonidou I.E., Perrakis A., Taraviras S., Lygerou Z.; RT "Idas, a novel phylogenetically conserved geminin-related protein, binds to RT geminin and is required for cell cycle progression."; RL J. Biol. Chem. 286:23234-23246(2011). RN [11] RP INTERACTION WITH LRWD1 AND CDT1, AND PHOSPHORYLATION DURING MITOSIS. RX PubMed=22645314; DOI=10.1128/mcb.00362-12; RA Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V., RA Prasanth S.G.; RT "Dynamic association of ORCA with prereplicative complex components RT regulates DNA replication initiation."; RL Mol. Cell. Biol. 32:3107-3120(2012). RN [12] RP PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-34; SER-36; SER-49 AND RP SER-64, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. RC TISSUE=Cervix carcinoma, and Erythroleukemia; RX PubMed=23186163; DOI=10.1021/pr300630k; RA Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., RA Mohammed S.; RT "Toward a comprehensive characterization of a human cancer cell RT phosphoproteome."; RL J. Proteome Res. 12:260-271(2013). RN [13] RP INVOLVEMENT IN MGORS6, AND VARIANT MGORS6 ARG-17. RX PubMed=26637980; DOI=10.1016/j.ajhg.2015.11.006; RA Burrage L.C., Charng W.L., Eldomery M.K., Willer J.R., Davis E.E., RA Lugtenberg D., Zhu W., Leduc M.S., Akdemir Z.C., Azamian M., Zapata G., RA Hernandez P.P., Schoots J., de Munnik S.A., Roepman R., Pearring J.N., RA Jhangiani S., Katsanis N., Vissers L.E., Brunner H.G., Beaudet A.L., RA Rosenfeld J.A., Muzny D.M., Gibbs R.A., Eng C.M., Xia F., Lalani S.R., RA Lupski J.R., Bongers E.M., Yang Y.; RT "De Novo GMNN Mutations Cause Autosomal-Dominant Primordial Dwarfism RT Associated with Meier-Gorlin Syndrome."; RL Am. J. Hum. Genet. 97:904-913(2015). RN [14] RP X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 110-145, SUBUNIT, AND COILED-COIL RP DOMAIN. RX PubMed=15313623; DOI=10.1016/j.jmb.2004.06.065; RA Thepaut M., Maiorano D., Guichou J.-F., Auge M.-T., Dumas C., Mechali M., RA Padilla A.; RT "Crystal structure of the coiled-coil dimerization motif of geminin: RT structural and functional insights on DNA replication regulation."; RL J. Mol. Biol. 342:275-287(2004). RN [15] RP X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 70-152, SUBUNIT, INTERACTION WITH RP CDT1, AND COILED-COIL DOMAIN. RX PubMed=15260975; DOI=10.1016/j.molcel.2004.06.045; RA Saxena S., Yuan P., Dhar S.K., Senga T., Takeda D., Robinson H., RA Kornbluth S., Swaminathan K., Dutta A.; RT "A dimerized coiled-coil domain and an adjoining part of geminin interact RT with two sites on Cdt1 for replication inhibition."; RL Mol. Cell 15:245-258(2004). RN [16] RP ELECTRON MICROSCOPY (17.5 ANGSTROMS), SUBUNIT, AND COILED-COIL DOMAIN. RX PubMed=15378034; DOI=10.1038/nsmb835; RA Okorokov A.L., Orlova E.V., Kingsbury S.R., Bagneris C., Gohlke U., RA Williams G.H., Stoeber K.; RT "Molecular structure of human geminin."; RL Nat. Struct. Mol. Biol. 11:1021-1022(2004). RN [17] RP X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), AND SUBUNIT. RX PubMed=19906994; DOI=10.1073/pnas.0905281106; RA De Marco V., Gillespie P.J., Li A., Karantzelis N., Christodoulou E., RA Klompmaker R., van Gerwen S., Fish A., Petoukhov M.V., Iliou M.S., RA Lygerou Z., Medema R.H., Blow J.J., Svergun D.I., Taraviras S., RA Perrakis A.; RT "Quaternary structure of the human Cdt1-Geminin complex regulates DNA RT replication licensing."; RL Proc. Natl. Acad. Sci. U.S.A. 106:19807-19812(2009). RN [18] RP STRUCTURE BY NMR OF 171-190 IN COMPLEX WITH HOXC9, FUNCTION, AND RP PHOSPHORYLATION AT SER-184. RX PubMed=22615398; DOI=10.1073/pnas.1200874109; RA Zhou B., Liu C., Xu Z., Zhu G.; RT "Structural basis for homeodomain recognition by the cell-cycle regulator RT Geminin."; RL Proc. Natl. Acad. Sci. U.S.A. 109:8931-8936(2012). RN [19] RP X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 83-160 IN COMPLEX WITH MCIDAS, RP SUBUNIT, FUNCTION, AND COILED-COIL DOMAIN. RX PubMed=24064211; DOI=10.1074/jbc.m113.491928; RA Caillat C., Pefani E.D., Gillespie P.J., Taraviras S., Blow J.J., RA Lygerou Z., Perrakis A.; RT "The Geminin and Idas coiled coils preferentially form a heterodimer that RT inhibits Geminin function in DNA replication licensing."; RL J. Biol. Chem. 288:31624-31634(2013). CC -!- FUNCTION: Inhibits DNA replication by preventing the incorporation of CC MCM complex into pre-replication complex (pre-RC) (PubMed:9635433, CC PubMed:14993212, PubMed:20129055, PubMed:24064211). It is degraded CC during the mitotic phase of the cell cycle (PubMed:9635433, CC PubMed:14993212, PubMed:24064211). Its destruction at the metaphase- CC anaphase transition permits replication in the succeeding cell cycle CC (PubMed:9635433, PubMed:14993212, PubMed:24064211). Inhibits histone CC acetyltransferase activity of KAT7/HBO1 in a CDT1-dependent manner, CC inhibiting histone H4 acetylation and DNA replication licensing CC (PubMed:20129055). Inhibits the transcriptional activity of a subset of CC Hox proteins, enrolling them in cell proliferative control CC (PubMed:22615398). {ECO:0000269|PubMed:14993212, CC ECO:0000269|PubMed:20129055, ECO:0000269|PubMed:22615398, CC ECO:0000269|PubMed:24064211, ECO:0000269|PubMed:9635433}. CC -!- SUBUNIT: Homotetramer (PubMed:15313623, PubMed:15260975, CC PubMed:15378034, PubMed:19906994). Interacts with CDT1; this inhibits CC binding of the MCM complex to origins of replication (PubMed:14993212, CC PubMed:21543332, PubMed:15260975, PubMed:19906994). The complex with CC CDT1 exists in two forms, a 'permissive' heterotrimer and an CC 'inhibitory' heterohexamer (PubMed:14993212, PubMed:15260975, CC PubMed:19906994). Interacts (via coiled-coil domain) with IDAS (via CC coiled-coil domain); this targets GMNN to the nucleus CC (PubMed:21543332). The heterodimer formed by GMNN and MCIDAS has much CC lower affinity for CDT1 than the GMNN homodimer (PubMed:24064211). CC Interacts with a subset of Hox proteins, affinity increasing from CC anterior to posterior types, the strongest interaction being with CC HOXB1, HOXC9 and HOXD10 (PubMed:22615398). Interacts with LRWD1 from CC G1/S to mitosis (PubMed:22645314). {ECO:0000269|PubMed:14993212, CC ECO:0000269|PubMed:15260975, ECO:0000269|PubMed:15313623, CC ECO:0000269|PubMed:15378034, ECO:0000269|PubMed:19906994, CC ECO:0000269|PubMed:21543332, ECO:0000269|PubMed:22615398, CC ECO:0000269|PubMed:22645314, ECO:0000269|PubMed:24064211}. CC -!- INTERACTION: CC O75496; Q8IYE0: CCDC146; NbExp=4; IntAct=EBI-371669, EBI-10749669; CC O75496; Q8IYE0-2: CCDC146; NbExp=4; IntAct=EBI-371669, EBI-10247802; CC O75496; P42771: CDKN2A; NbExp=2; IntAct=EBI-371669, EBI-375053; CC O75496; Q9H211: CDT1; NbExp=21; IntAct=EBI-371669, EBI-456953; CC O75496; Q9BZE0: GLIS2; NbExp=3; IntAct=EBI-371669, EBI-7251368; CC O75496; P31274: HOXC9; NbExp=3; IntAct=EBI-371669, EBI-1779423; CC O75496; Q63ZY3: KANK2; NbExp=3; IntAct=EBI-371669, EBI-2556193; CC O75496; Q8TBB1: LNX1; NbExp=3; IntAct=EBI-371669, EBI-739832; CC O75496; D6RGH6: MCIDAS; NbExp=8; IntAct=EBI-371669, EBI-3954372; CC O75496; Q06124-2: PTPN11; NbExp=3; IntAct=EBI-371669, EBI-17635971; CC O75496; Q86UD0: SAPCD2; NbExp=3; IntAct=EBI-371669, EBI-2561646; CC O75496; P15622-3: ZNF250; NbExp=3; IntAct=EBI-371669, EBI-10177272; CC O75496; Q8NDP4: ZNF439; NbExp=7; IntAct=EBI-371669, EBI-747580; CC -!- SUBCELLULAR LOCATION: Cytoplasm {ECO:0000269|PubMed:21543332}. Nucleus CC {ECO:0000269|PubMed:21543332}. Note=Mainly cytoplasmic but can be CC relocalized to the nucleus. {ECO:0000269|PubMed:21543332}. CC -!- DEVELOPMENTAL STAGE: Absent during G1 phase, accumulates during S, G2, CC and M phases, and disappears at the time of the metaphase-anaphase CC transition. {ECO:0000269|PubMed:9635433}. CC -!- PTM: Phosphorylated during mitosis. Phosphorylation at Ser-184 by CK2 CC results in enhanced binding to Hox proteins and more potent inhibitory CC effect on Hox transcriptional activity. {ECO:0000269|PubMed:22615398, CC ECO:0000269|PubMed:22645314}. CC -!- DISEASE: Meier-Gorlin syndrome 6 (MGORS6) [MIM:616835]: A form of CC Meier-Gorlin syndrome, a syndrome characterized by bilateral microtia, CC aplasia/hypoplasia of the patellae, and severe intrauterine and CC postnatal growth retardation with short stature and poor weight gain. CC Additional clinical findings include anomalies of cranial sutures, CC microcephaly, apparently low-set and simple ears, microstomia, full CC lips, highly arched or cleft palate, micrognathia, genitourinary tract CC anomalies, and various skeletal anomalies. While almost all cases have CC primordial dwarfism with substantial prenatal and postnatal growth CC retardation, not all cases have microcephaly, and microtia and CC absent/hypoplastic patella are absent in some. Despite the presence of CC microcephaly, intellect is usually normal. CC {ECO:0000269|PubMed:26637980}. Note=The disease is caused by variants CC affecting the gene represented in this entry. CC -!- SIMILARITY: Belongs to the geminin family. {ECO:0000305}. CC --------------------------------------------------------------------------- CC Copyrighted by the UniProt Consortium, see https://www.uniprot.org/terms CC Distributed under the Creative Commons Attribution (CC BY 4.0) License CC --------------------------------------------------------------------------- DR EMBL; AF067855; AAC39787.1; -; mRNA. DR EMBL; AK021685; BAG51040.1; -; mRNA. DR EMBL; AL133264; -; NOT_ANNOTATED_CDS; Genomic_DNA. DR EMBL; BC005185; AAH05185.1; -; mRNA. DR EMBL; BC005389; AAH05389.1; -; mRNA. DR CCDS; CCDS4560.1; -. DR RefSeq; NP_001238918.1; NM_001251989.1. DR RefSeq; NP_001238919.1; NM_001251990.1. DR RefSeq; NP_001238920.1; NM_001251991.1. DR RefSeq; NP_056979.1; NM_015895.4. DR RefSeq; XP_005249216.1; XM_005249159.1. DR PDB; 1T6F; X-ray; 1.47 A; A/B=109-145. DR PDB; 1UII; X-ray; 2.00 A; A/B=70-152. DR PDB; 2LP0; NMR; -; B=171-190. DR PDB; 2WVR; X-ray; 3.30 A; A/B=1-209. DR PDB; 4BRY; X-ray; 2.89 A; A=83-160. DR PDB; 7KLZ; X-ray; 3.40 A; C/D=195-209. DR PDBsum; 1T6F; -. DR PDBsum; 1UII; -. DR PDBsum; 2LP0; -. DR PDBsum; 2WVR; -. DR PDBsum; 4BRY; -. DR PDBsum; 7KLZ; -. DR AlphaFoldDB; O75496; -. DR BMRB; O75496; -. DR SASBDB; O75496; -. DR SMR; O75496; -. DR BioGRID; 119246; 108. DR ComplexPortal; CPX-6094; HOXD10-Geminin transcriptional repressor complex. DR ComplexPortal; CPX-659; CDT1-Geminin complex. DR ComplexPortal; CPX-660; HOXC9-Geminin transcriptional repressor complex. DR ComplexPortal; CPX-661; IDAS-Geminin complex. DR CORUM; O75496; -. DR DIP; DIP-31088N; -. DR IntAct; O75496; 68. DR MINT; O75496; -. DR STRING; 9606.ENSP00000230056; -. DR ChEMBL; CHEMBL1293278; -. DR GlyGen; O75496; 4 sites, 1 O-linked glycan (4 sites). DR iPTMnet; O75496; -. DR MetOSite; O75496; -. DR PhosphoSitePlus; O75496; -. DR BioMuta; GMNN; -. DR EPD; O75496; -. DR jPOST; O75496; -. DR MassIVE; O75496; -. DR MaxQB; O75496; -. DR PaxDb; 9606-ENSP00000230056; -. DR PeptideAtlas; O75496; -. DR ProteomicsDB; 50053; -. DR Pumba; O75496; -. DR Antibodypedia; 25345; 495 antibodies from 35 providers. DR CPTC; O75496; 3 antibodies. DR DNASU; 51053; -. DR Ensembl; ENST00000230056.8; ENSP00000230056.3; ENSG00000112312.10. DR Ensembl; ENST00000356509.7; ENSP00000348902.3; ENSG00000112312.10. DR Ensembl; ENST00000620958.4; ENSP00000477506.1; ENSG00000112312.10. DR GeneID; 51053; -. DR KEGG; hsa:51053; -. DR MANE-Select; ENST00000230056.8; ENSP00000230056.3; NM_015895.5; NP_056979.1. DR UCSC; uc003nem.4; human. DR AGR; HGNC:17493; -. DR CTD; 51053; -. DR DisGeNET; 51053; -. DR GeneCards; GMNN; -. DR HGNC; HGNC:17493; GMNN. DR HPA; ENSG00000112312; Tissue enhanced (pancreas). DR MalaCards; GMNN; -. DR MIM; 602842; gene. DR MIM; 616835; phenotype. DR neXtProt; NX_O75496; -. DR OpenTargets; ENSG00000112312; -. DR Orphanet; 2554; Ear-patella-short stature syndrome. DR PharmGKB; PA38455; -. DR VEuPathDB; HostDB:ENSG00000112312; -. DR eggNOG; ENOG502SDC5; Eukaryota. DR GeneTree; ENSGT00940000153270; -. DR InParanoid; O75496; -. DR OMA; HWNDQLI; -. DR OrthoDB; 4119853at2759; -. DR PhylomeDB; O75496; -. DR TreeFam; TF101171; -. DR PathwayCommons; O75496; -. DR Reactome; R-HSA-68867; Assembly of the pre-replicative complex. DR Reactome; R-HSA-68962; Activation of the pre-replicative complex. DR Reactome; R-HSA-69052; Switching of origins to a post-replicative state. DR SignaLink; O75496; -. DR SIGNOR; O75496; -. DR BioGRID-ORCS; 51053; 342 hits in 1161 CRISPR screens. DR ChiTaRS; GMNN; human. DR EvolutionaryTrace; O75496; -. DR GeneWiki; Geminin; -. DR GenomeRNAi; 51053; -. DR Pharos; O75496; Tbio. DR PRO; PR:O75496; -. DR Proteomes; UP000005640; Chromosome 6. DR RNAct; O75496; Protein. DR Bgee; ENSG00000112312; Expressed in oocyte and 195 other cell types or tissues. DR ExpressionAtlas; O75496; baseline and differential. DR GO; GO:0005737; C:cytoplasm; IDA:UniProtKB. DR GO; GO:0005829; C:cytosol; IDA:HPA. DR GO; GO:0005654; C:nucleoplasm; IDA:HPA. DR GO; GO:0005634; C:nucleus; IDA:UniProtKB. DR GO; GO:0017053; C:transcription repressor complex; IPI:ComplexPortal. DR GO; GO:0003682; F:chromatin binding; IDA:CAFA. DR GO; GO:0140297; F:DNA-binding transcription factor binding; IEA:Ensembl. DR GO; GO:0042826; F:histone deacetylase binding; IPI:UniProtKB. DR GO; GO:0003714; F:transcription corepressor activity; IEA:Ensembl. DR GO; GO:0009887; P:animal organ morphogenesis; IEA:Ensembl. DR GO; GO:0071163; P:DNA replication preinitiation complex assembly; IDA:CAFA. DR GO; GO:0045786; P:negative regulation of cell cycle; IDA:UniProtKB. DR GO; GO:0008156; P:negative regulation of DNA replication; IDA:UniProtKB. DR GO; GO:2000104; P:negative regulation of DNA-templated DNA replication; IDA:CAFA. DR GO; GO:0045892; P:negative regulation of DNA-templated transcription; IDA:UniProtKB. DR GO; GO:0035563; P:positive regulation of chromatin binding; IDA:CAFA. DR GO; GO:0006275; P:regulation of DNA replication; IMP:UniProtKB. DR GO; GO:0030174; P:regulation of DNA-templated DNA replication initiation; IDA:ComplexPortal. DR GO; GO:0007346; P:regulation of mitotic cell cycle; IDA:ComplexPortal. DR CDD; cd22589; geminin_CC; 1. DR DisProt; DP00901; -. DR Gene3D; 1.20.5.1180; Geminin coiled-coil domain; 1. DR IDEAL; IID00409; -. DR InterPro; IPR022786; Geminin/Multicilin. DR PANTHER; PTHR13372; GEMININ; 1. DR PANTHER; PTHR13372:SF4; GEMININ; 1. DR Pfam; PF07412; Geminin; 1. DR SUPFAM; SSF111469; Geminin coiled-coil domain; 1. DR Genevisible; O75496; HS. PE 1: Evidence at protein level; KW 3D-structure; Acetylation; Cell cycle; Coiled coil; Cytoplasm; KW Disease variant; DNA replication inhibitor; Dwarfism; Nucleus; KW Phosphoprotein; Reference proteome. FT CHAIN 1..209 FT /note="Geminin" FT /id="PRO_0000148729" FT REGION 1..79 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 82..161 FT /note="Necessary and sufficient for interaction with IDAS FT and CDT1" FT /evidence="ECO:0000269|PubMed:21543332" FT REGION 164..209 FT /note="Disordered" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT REGION 170..190 FT /note="Homeodomain binding" FT COILED 94..144 FT /evidence="ECO:0000269|PubMed:15260975, FT ECO:0000269|PubMed:15313623, ECO:0000269|PubMed:15378034, FT ECO:0000269|PubMed:24064211" FT COMPBIAS 21..39 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 59..79 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 168..186 FT /note="Acidic residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT COMPBIAS 194..209 FT /note="Polar residues" FT /evidence="ECO:0000256|SAM:MobiDB-lite" FT MOD_RES 27 FT /note="N6-acetyllysine" FT /evidence="ECO:0007744|PubMed:19608861" FT MOD_RES 34 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 36 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 49 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:23186163" FT MOD_RES 63 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648" FT MOD_RES 64 FT /note="Phosphoserine" FT /evidence="ECO:0007744|PubMed:18669648, FT ECO:0007744|PubMed:23186163" FT MOD_RES 184 FT /note="Phosphoserine; by CK2" FT /evidence="ECO:0000269|PubMed:22615398" FT VARIANT 15 FT /note="N -> H (in dbSNP:rs34891389)" FT /id="VAR_033959" FT VARIANT 17 FT /note="K -> R (in MGORS6; dbSNP:rs864309488)" FT /evidence="ECO:0000269|PubMed:26637980" FT /id="VAR_076172" FT VARIANT 18 FT /note="N -> T (in dbSNP:rs1923185)" FT /evidence="ECO:0000269|PubMed:14702039" FT /id="VAR_024233" FT VARIANT 48 FT /note="L -> F (in dbSNP:rs2307307)" FT /id="VAR_033960" FT VARIANT 54 FT /note="R -> W (in dbSNP:rs2307306)" FT /id="VAR_033961" FT VARIANT 60 FT /note="S -> P (in dbSNP:rs2307302)" FT /id="VAR_053107" FT VARIANT 203 FT /note="T -> M (in dbSNP:rs2307303)" FT /id="VAR_053108" FT HELIX 110..142 FT /evidence="ECO:0007829|PDB:1T6F" FT TURN 177..179 FT /evidence="ECO:0007829|PDB:2LP0" SQ SEQUENCE 209 AA; 23565 MW; 0BABE60F6F5AC252 CRC64; MNPSMKQKQE EIKENIKNSS VPRRTLKMIQ PSASGSLVGR ENELSAGLSK RKHRNDHLTS TTSSPGVIVP ESSENKNLGG VTQESFDLMI KENPSSQYWK EVAEKRRKAL YEALKENEKL HKEIEQKDNE IARLKKENKE LAEVAEHVQY MAELIERLNG EPLDNFESLD NQEFDSEEET VEDSLVEDSE IGTCAEGTVS SSTDAKPCI //