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O75496

- GEMI_HUMAN

UniProt

O75496 - GEMI_HUMAN

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Protein

Geminin

Gene

GMNN

Organism
Homo sapiens (Human)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli

Functioni

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.
Inhibits the transcriptional activity of a subset of Hox proteins, enrolling them in cell proliferative control.

GO - Molecular functioni

  1. histone deacetylase binding Source: UniProtKB
  2. transcription corepressor activity Source: Ensembl

GO - Biological processi

  1. mitotic cell cycle Source: Reactome
  2. negative regulation of cell cycle Source: UniProtKB
  3. negative regulation of DNA replication Source: UniProtKB
  4. negative regulation of transcription, DNA-templated Source: UniProtKB
  5. organ morphogenesis Source: Ensembl
  6. protein complex assembly Source: Ensembl
Complete GO annotation...

Keywords - Molecular functioni

DNA replication inhibitor

Keywords - Biological processi

Cell cycle

Enzyme and pathway databases

ReactomeiREACT_1181. Association of licensing factors with the pre-replicative complex.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_207. Removal of licensing factors from origins.

Names & Taxonomyi

Protein namesi
Recommended name:
Geminin
Gene namesi
Name:GMNN
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:17493. GMNN.

Subcellular locationi

Cytoplasm. Nucleus
Note: Mainly cytoplasmic but can be relocalized to the nucleus.

GO - Cellular componenti

  1. cytoplasm Source: UniProtKB
  2. cytosol Source: Reactome
  3. nucleoplasm Source: Reactome
  4. nucleus Source: UniProtKB
Complete GO annotation...

Keywords - Cellular componenti

Cytoplasm, Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA38455.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 209209GemininPRO_0000148729Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei27 – 271N6-acetyllysine1 Publication
Modified residuei63 – 631Phosphoserine1 Publication
Modified residuei64 – 641Phosphoserine1 Publication
Modified residuei184 – 1841Phosphoserine; by CK21 Publication

Post-translational modificationi

Phosphorylated during mitosis. Phosphorylation at Ser-184 by CK2 results in enhanced binding to Hox proteins and more potent inhibitory effect on Hox transcriptional activity.3 Publications

Keywords - PTMi

Acetylation, Phosphoprotein

Proteomic databases

MaxQBiO75496.
PaxDbiO75496.
PRIDEiO75496.

PTM databases

PhosphoSiteiO75496.

Miscellaneous databases

PMAP-CutDBO75496.

Expressioni

Developmental stagei

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

Gene expression databases

BgeeiO75496.
CleanExiHS_GMNN.
ExpressionAtlasiO75496. baseline and differential.
GenevestigatoriO75496.

Organism-specific databases

HPAiCAB011458.
CAB047327.
CAB047328.
HPA049977.
HPA054597.

Interactioni

Subunit structurei

Homotetramer. Interacts with CDT1; this inhibits binding of the MCM complex to origins of replication. The complex with CDT1 exists in two forms, a "permissive" heterotrimer and an "inhibitory" heterohexamer. Interacts (via coiled-coil domain) with IDAS (via coiled-coil domain); this targets GMNN to the nucleus. The heterodimer formed by GMNN and MCIDAS has much lower affinity for CDT1 than the GMNN homodimer. Interacts with a subset of Hox proteins, affinity increasing from anterior to posterior types, the strongest interaction being with HOXB1, HOXC9 and HOXD10. Interacts with LRWD1 from G1/S to mitosis.9 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDT1Q9H21111EBI-371669,EBI-456953
MCIDASD6RGH67EBI-371669,EBI-3954372

Protein-protein interaction databases

BioGridi119246. 31 interactions.
DIPiDIP-31088N.
IntActiO75496. 9 interactions.
MINTiMINT-1201770.
STRINGi9606.ENSP00000230056.

Structurei

Secondary structure

1
209
Legend: HelixTurnBeta strand
Show more details
Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Helixi110 – 14233Combined sources
Turni177 – 1793Combined sources

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
EntryMethodResolution (Å)ChainPositionsPDBsum
1T6FX-ray1.47A/B109-145[»]
1UIIX-ray2.00A/B70-152[»]
2LP0NMR-B171-190[»]
2WVRX-ray3.30A/B1-209[»]
4BRYX-ray2.89A83-160[»]
ProteinModelPortaliO75496.
SMRiO75496. Positions 92-152.
ModBaseiSearch...
MobiDBiSearch...

Miscellaneous databases

EvolutionaryTraceiO75496.

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni82 – 16180Necessary and sufficient for interaction with IDAS and CDT1Add
BLAST
Regioni170 – 19021Homeodomain bindingAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili94 – 144514 PublicationsAdd
BLAST

Sequence similaritiesi

Belongs to the geminin family.Curated

Keywords - Domaini

Coiled coil

Phylogenomic databases

eggNOGiNOG39688.
GeneTreeiENSGT00390000016394.
HOGENOMiHOG000112711.
HOVERGENiHBG002965.
InParanoidiO75496.
KOiK10749.
OMAiVPEHSEN.
OrthoDBiEOG7RFTJX.
PhylomeDBiO75496.
TreeFamiTF101171.

Family and domain databases

InterProiIPR029697. Geminin.
IPR022786. Geminin/Multicilin.
[Graphical view]
PANTHERiPTHR13372:SF4. PTHR13372:SF4. 1 hit.
PfamiPF07412. Geminin. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

O75496-1 [UniParc]FASTAAdd to Basket

« Hide

        10         20         30         40         50
MNPSMKQKQE EIKENIKNSS VPRRTLKMIQ PSASGSLVGR ENELSAGLSK
60 70 80 90 100
RKHRNDHLTS TTSSPGVIVP ESSENKNLGG VTQESFDLMI KENPSSQYWK
110 120 130 140 150
EVAEKRRKAL YEALKENEKL HKEIEQKDNE IARLKKENKE LAEVAEHVQY
160 170 180 190 200
MAELIERLNG EPLDNFESLD NQEFDSEEET VEDSLVEDSE IGTCAEGTVS

SSTDAKPCI
Length:209
Mass (Da):23,565
Last modified:November 1, 1998 - v1
Checksum:i0BABE60F6F5AC252
GO

Sequence cautioni

The sequence CAC21511.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti15 – 151N → H.
Corresponds to variant rs34891389 [ dbSNP | Ensembl ].
VAR_033959
Natural varianti18 – 181N → T.1 Publication
Corresponds to variant rs1923185 [ dbSNP | Ensembl ].
VAR_024233
Natural varianti48 – 481L → F.
Corresponds to variant rs2307307 [ dbSNP | Ensembl ].
VAR_033960
Natural varianti54 – 541R → W.
Corresponds to variant rs2307306 [ dbSNP | Ensembl ].
VAR_033961
Natural varianti60 – 601S → P.
Corresponds to variant rs2307302 [ dbSNP | Ensembl ].
VAR_053107
Natural varianti203 – 2031T → M.
Corresponds to variant rs2307303 [ dbSNP | Ensembl ].
VAR_053108

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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.
CCDSiCCDS4560.1.
RefSeqiNP_001238918.1. NM_001251989.1.
NP_001238919.1. NM_001251990.1.
NP_001238920.1. NM_001251991.1.
NP_056979.1. NM_015895.4.
XP_005249216.1. XM_005249159.1.
UniGeneiHs.234896.

Genome annotation databases

EnsembliENST00000230056; ENSP00000230056; ENSG00000112312.
ENST00000356509; ENSP00000348902; ENSG00000112312.
ENST00000620958; ENSP00000477506; ENSG00000112312.
GeneIDi51053.
KEGGihsa:51053.
UCSCiuc003nem.3. human.

Keywords - Coding sequence diversityi

Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
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 .
CCDSi CCDS4560.1.
RefSeqi NP_001238918.1. NM_001251989.1.
NP_001238919.1. NM_001251990.1.
NP_001238920.1. NM_001251991.1.
NP_056979.1. NM_015895.4.
XP_005249216.1. XM_005249159.1.
UniGenei Hs.234896.

3D structure databases

Select the link destinations:
PDBei
RCSB PDBi
PDBji
Links Updated
Entry Method Resolution (Å) Chain Positions PDBsum
1T6F X-ray 1.47 A/B 109-145 [» ]
1UII X-ray 2.00 A/B 70-152 [» ]
2LP0 NMR - B 171-190 [» ]
2WVR X-ray 3.30 A/B 1-209 [» ]
4BRY X-ray 2.89 A 83-160 [» ]
ProteinModelPortali O75496.
SMRi O75496. Positions 92-152.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 119246. 31 interactions.
DIPi DIP-31088N.
IntActi O75496. 9 interactions.
MINTi MINT-1201770.
STRINGi 9606.ENSP00000230056.

Chemistry

ChEMBLi CHEMBL1293278.

PTM databases

PhosphoSitei O75496.

Proteomic databases

MaxQBi O75496.
PaxDbi O75496.
PRIDEi O75496.

Protocols and materials databases

DNASUi 51053.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000230056 ; ENSP00000230056 ; ENSG00000112312 .
ENST00000356509 ; ENSP00000348902 ; ENSG00000112312 .
ENST00000620958 ; ENSP00000477506 ; ENSG00000112312 .
GeneIDi 51053.
KEGGi hsa:51053.
UCSCi uc003nem.3. human.

Organism-specific databases

CTDi 51053.
GeneCardsi GC06P024779.
HGNCi HGNC:17493. GMNN.
HPAi CAB011458.
CAB047327.
CAB047328.
HPA049977.
HPA054597.
MIMi 602842. gene.
neXtProti NX_O75496.
PharmGKBi PA38455.
GenAtlasi Search...

Phylogenomic databases

eggNOGi NOG39688.
GeneTreei ENSGT00390000016394.
HOGENOMi HOG000112711.
HOVERGENi HBG002965.
InParanoidi O75496.
KOi K10749.
OMAi VPEHSEN.
OrthoDBi EOG7RFTJX.
PhylomeDBi O75496.
TreeFami TF101171.

Enzyme and pathway databases

Reactomei REACT_1181. Association of licensing factors with the pre-replicative complex.
REACT_1949. CDT1 association with the CDC6:ORC:origin complex.
REACT_207. Removal of licensing factors from origins.

Miscellaneous databases

ChiTaRSi GMNN. human.
EvolutionaryTracei O75496.
GeneWikii Geminin.
GenomeRNAii 51053.
NextBioi 53616.
PMAP-CutDB O75496.
PROi O75496.
SOURCEi Search...

Gene expression databases

Bgeei O75496.
CleanExi HS_GMNN.
ExpressionAtlasi O75496. baseline and differential.
Genevestigatori O75496.

Family and domain databases

InterProi IPR029697. Geminin.
IPR022786. Geminin/Multicilin.
[Graphical view ]
PANTHERi PTHR13372:SF4. PTHR13372:SF4. 1 hit.
Pfami PF07412. Geminin. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "Geminin, an inhibitor of DNA replication, is degraded during mitosis."
    McGarry T.J., Kirschner M.W.
    Cell 93:1043-1053(1998) [PubMed] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [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] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH CDT1.
  6. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-63 AND SER-64, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  7. "Lysine acetylation targets protein complexes and co-regulates major cellular functions."
    Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M., Walther T.C., Olsen J.V., Mann M.
    Science 325:834-840(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-27, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  8. "Quantitative phosphoproteomics reveals widespread full phosphorylation site occupancy during mitosis."
    Olsen J.V., Vermeulen M., Santamaria A., Kumar C., Miller M.L., Jensen L.J., Gnad F., Cox J., Jensen T.S., Nigg E.A., Brunak S., Mann M.
    Sci. Signal. 3:RA3-RA3(2010) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  9. "Idas, a novel phylogenetically conserved geminin-related protein, binds to geminin and is required for cell cycle progression."
    Pefani D.E., Dimaki M., Spella M., Karantzelis N., Mitsiki E., Kyrousi C., Symeonidou I.E., Perrakis A., Taraviras S., Lygerou Z.
    J. Biol. Chem. 286:23234-23246(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH IDAS AND CDT1.
  10. "Dynamic association of ORCA with prereplicative complex components regulates DNA replication initiation."
    Shen Z., Chakraborty A., Jain A., Giri S., Ha T., Prasanth K.V., Prasanth S.G.
    Mol. Cell. Biol. 32:3107-3120(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH LRWD1 AND CDT1, PHOSPHORYLATION DURING MITOSIS.
  11. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (1.47 ANGSTROMS) OF 110-145, SUBUNIT, COILED-COIL DOMAIN.
  12. "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] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.0 ANGSTROMS) OF 70-152, SUBUNIT, INTERACTION WITH CDT1, COILED-COIL DOMAIN.
  13. Cited for: ELECTRON MICROSCOPY (17.5 ANGSTROMS), SUBUNIT, COILED-COIL DOMAIN.
  14. Cited for: X-RAY CRYSTALLOGRAPHY (3.3 ANGSTROMS), SUBUNIT.
  15. "Structural basis for homeodomain recognition by the cell-cycle regulator Geminin."
    Zhou B., Liu C., Xu Z., Zhu G.
    Proc. Natl. Acad. Sci. U.S.A. 109:8931-8936(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: STRUCTURE BY NMR OF 171-190 IN COMPLEX WITH HOXC9, FUNCTION, PHOSPHORYLATION AT SER-184.
  16. "The Geminin and Idas coiled coils preferentially form a heterodimer that inhibits Geminin function in DNA replication licensing."
    Caillat C., Pefani E.D., Gillespie P.J., Taraviras S., Blow J.J., Lygerou Z., Perrakis A.
    J. Biol. Chem. 288:31624-31634(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: X-RAY CRYSTALLOGRAPHY (2.89 ANGSTROMS) OF 83-160 IN COMPLEX WITH MCIDAS, SUBUNIT, FUNCTION, COILED-COIL DOMAIN.

Entry informationi

Entry nameiGEMI_HUMAN
AccessioniPrimary (citable) accession number: O75496
Secondary accession number(s): B3KMM8, Q9H1Z1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 2, 2002
Last sequence update: November 1, 1998
Last modified: November 26, 2014
This is version 125 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program
DisclaimerAny medical or genetic information present in this entry is provided for research, educational and informational purposes only. It is not in any way intended to be used as a substitute for professional medical advice, diagnosis, treatment or care.

Miscellaneousi

Keywords - Technical termi

3D-structure, Complete proteome, Reference proteome

Documents

  1. Human chromosome 6
    Human chromosome 6: entries, gene names and cross-references to MIM
  2. Human entries with polymorphisms or disease mutations
    List of human entries with polymorphisms or disease mutations
  3. Human polymorphisms and disease mutations
    Index of human polymorphisms and disease mutations
  4. MIM cross-references
    Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
  5. PDB cross-references
    Index of Protein Data Bank (PDB) cross-references
  6. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3