GEMI_HUMAN
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 03-AUG-2022, entry version 180.
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; 99.
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 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; O75496; -.
DR PeptideAtlas; O75496; -.
DR PRIDE; O75496; -.
DR ProteomicsDB; 50053; -.
DR Antibodypedia; 25345; 423 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 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; HYWKEVA; -.
DR OrthoDB; 1631696at2759; -.
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; 333 hits in 1082 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 193 other tissues.
DR ExpressionAtlas; O75496; baseline and differential.
DR Genevisible; O75496; HS.
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 transcription, DNA-templated; 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 DisProt; DP00901; -.
DR IDEAL; IID00409; -.
DR InterPro; IPR029697; Geminin.
DR InterPro; IPR022786; Geminin/Multicilin.
DR PANTHER; PTHR13372:SF4; PTHR13372:SF4; 1.
DR Pfam; PF07412; Geminin; 1.
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
