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P25205

- MCM3_HUMAN

UniProt

P25205 - MCM3_HUMAN

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Protein

DNA replication licensing factor MCM3

Gene

MCM3

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

Functioni

Acts as component of the MCM2-7 complex (MCM complex) which is the putative replicative helicase essential for 'once per cell cycle' DNA replication initiation and elongation in eukaryotic cells. The active ATPase sites in the MCM2-7 ring are formed through the interaction surfaces of two neighboring subunits such that a critical structure of a conserved arginine finger motif is provided in trans relative to the ATP-binding site of the Walker A box of the adjacent subunit. The six ATPase active sites, however, are likely to contribute differentially to the complex helicase activity. Required for DNA replication and cell proliferation.

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi345 – 3528ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA binding Source: ProtInc
  3. DNA helicase activity Source: InterPro

GO - Biological processi

  1. DNA replication Source: Reactome
  2. DNA replication initiation Source: ProtInc
  3. DNA strand elongation involved in DNA replication Source: Reactome
  4. G1/S transition of mitotic cell cycle Source: Reactome
  5. mitotic cell cycle Source: Reactome
Complete GO annotation...

Keywords - Molecular functioni

Helicase, Hydrolase

Keywords - Biological processi

Cell cycle, DNA replication

Keywords - Ligandi

ATP-binding, DNA-binding, Nucleotide-binding

Enzyme and pathway databases

ReactomeiREACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_207. Removal of licensing factors from origins.
REACT_2148. Switching of origins to a post-replicative state.
REACT_2243. Assembly of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6776. Unwinding of DNA.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM3 (EC:3.6.4.12)
Alternative name(s):
DNA polymerase alpha holoenzyme-associated protein P1
P1-MCM3
RLF subunit beta
p102
Gene namesi
Name:MCM3
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
ProteomesiUP000005640: Chromosome 6

Organism-specific databases

HGNCiHGNC:6945. MCM3.

Subcellular locationi

GO - Cellular componenti

  1. alpha DNA polymerase:primase complex Source: ProtInc
  2. centrosome Source: HPA
  3. intracellular membrane-bounded organelle Source: HPA
  4. MCM complex Source: UniProtKB
  5. membrane Source: UniProtKB
  6. nucleoplasm Source: Reactome
  7. nucleus Source: BHF-UCL
  8. perinuclear region of cytoplasm Source: BHF-UCL
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Mutagenesis

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Mutagenesisi535 – 5351S → A: 50% reduction in phosphorylation by ATM or ATR. 1 Publication

Organism-specific databases

PharmGKBiPA30691.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed4 Publications
Chaini2 – 808807DNA replication licensing factor MCM3PRO_0000194093Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine4 Publications
Modified residuei160 – 1601Phosphoserine2 Publications
Modified residuei293 – 2931N6-acetyllysineBy similarity
Modified residuei535 – 5351Phosphoserine; by ATM1 Publication
Modified residuei547 – 5471N6-acetyllysineBy similarity
Modified residuei668 – 6681Phosphoserine2 Publications
Modified residuei672 – 6721Phosphoserine5 Publications
Modified residuei674 – 6741Phosphothreonine4 Publications
Modified residuei681 – 6811Phosphoserine1 Publication
Modified residuei708 – 7081Phosphotyrosine1 Publication
Modified residuei711 – 7111Phosphoserine4 Publications
Modified residuei713 – 7131Phosphothreonine2 Publications
Modified residuei722 – 7221Phosphothreonine7 Publications
Modified residuei725 – 7251Phosphothreonine1 Publication

Post-translational modificationi

O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner.1 Publication

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP25205.
PaxDbiP25205.
PeptideAtlasiP25205.
PRIDEiP25205.

PTM databases

PhosphoSiteiP25205.

Miscellaneous databases

PMAP-CutDBP25205.

Expressioni

Gene expression databases

BgeeiP25205.
CleanExiHS_MCM3.
ExpressionAtlasiP25205. baseline and differential.
GenevestigatoriP25205.

Organism-specific databases

HPAiCAB002162.
HPA004789.
HPA004790.

Interactioni

Subunit structurei

Component of the MCM2-7 complex. The complex forms a toroidal hexameric ring with the proposed subunit order MCM2-MCM6-MCM4-MCM7-MCM3-MCM5 (By simililarity). Associated with the replication-specific DNA polymerase alpha. Interacts with MCMBP.2 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
HIST2H4BP628052EBI-355153,EBI-302023
MCM2P497365EBI-355153,EBI-374819
MCM5P339924EBI-355153,EBI-359410
MCM6Q145662EBI-355153,EBI-374900
MCMBPQ9BTE311EBI-355153,EBI-749378
ORC2Q134162EBI-355153,EBI-374957

Protein-protein interaction databases

BioGridi110340. 90 interactions.
DIPiDIP-31726N.
IntActiP25205. 38 interactions.
MINTiMINT-1201900.
STRINGi9606.ENSP00000229854.

Structurei

3D structure databases

ProteinModelPortaliP25205.
SMRiP25205. Positions 10-650.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini295 – 502208MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi477 – 4804Arginine finger

Sequence similaritiesi

Belongs to the MCM family.Curated
Contains 1 MCM domain.Curated

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00550000075022.
HOGENOMiHOG000224126.
HOVERGENiHBG104962.
InParanoidiP25205.
KOiK02541.
PhylomeDBiP25205.
TreeFamiTF106459.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008046. Mcm3.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01659. MCMPROTEIN3.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequences (2)i

Sequence statusi: Complete.

Sequence processingi: The displayed sequence is further processed into a mature form.

This entry describes 2 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P25205-1) [UniParc]FASTAAdd to Basket

This isoform has been chosen as the 'canonical' sequence. All positional information in this entry refers to it. This is also the sequence that appears in the downloadable versions of the entry.

« Hide

        10         20         30         40         50
MAGTVVLDDV ELREAQRDYL DFLDDEEDQG IYQSKVRELI SDNQYRLIVN
60 70 80 90 100
VNDLRRKNEK RANRLLNNAF EELVAFQRAL KDFVASIDAT YAKQYEEFYV
110 120 130 140 150
GLEGSFGSKH VSPRTLTSCF LSCVVCVEGI VTKCSLVRPK VVRSVHYCPA
160 170 180 190 200
TKKTIERRYS DLTTLVAFPS SSVYPTKDEE NNPLETEYGL SVYKDHQTIT
210 220 230 240 250
IQEMPEKAPA GQLPRSVDVI LDDDLVDKAK PGDRVQVVGT YRCLPGKKGG
260 270 280 290 300
YTSGTFRTVL IACNVKQMSK DAQPSFSAED IAKIKKFSKT RSKDIFDQLA
310 320 330 340 350
KSLAPSIHGH DYVKKAILCL LLGGVERDLE NGSHIRGDIN ILLIGDPSVA
360 370 380 390 400
KSQLLRYVLC TAPRAIPTTG RGSSGVGLTA AVTTDQETGE RRLEAGAMVL
410 420 430 440 450
ADRGVVCIDE FDKMSDMDRT AIHEVMEQGR VTIAKAGIHA RLNARCSVLA
460 470 480 490 500
AANPVYGRYD QYKTPMENIG LQDSLLSRFD LLFIMLDQMD PEQDREISDH
510 520 530 540 550
VLRMHRYRAP GEQDGDAMPL GSAVDILATD DPNFSQEDQQ DTQIYEKHDN
560 570 580 590 600
LLHGTKKKKE KMVSAAFMKK YIHVAKIIKP VLTQESATYI AEEYSRLRSQ
610 620 630 640 650
DSMSSDTART SPVTARTLET LIRLATAHAK ARMSKTVDLQ DAEEAVELVQ
660 670 680 690 700
YAYFKKVLEK EKKRKKRSED ESETEDEEEK SQEDQEQKRK RRKTRQPDAK
710 720 730 740 750
DGDSYDPYDF SDTEEEMPQV HTPKTADSQE TKESQKVELS ESRLKAFKVA
760 770 780 790 800
LLDVFREAHA QSIGMNRLTE SINRDSEEPF SSVEIQAALS KMQDDNQVMV

SEGIIFLI
Length:808
Mass (Da):90,981
Last modified:August 14, 2001 - v3
Checksum:iC967C068B7090558
GO
Isoform 2 (identifier: P25205-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-1: M → MLPRSPPLPRGNLWWREEFGSFRAGVESSWEPPRDFGGGSSLAAGM

Note: No experimental confirmation available

Show »
Length:853
Mass (Da):95,908
Checksum:iE3EFA82D0E088CF1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti230 – 2312KP → NA in BAA07267. (PubMed:7758114)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti105 – 1051S → G.
Corresponds to variant rs2307332 [ dbSNP | Ensembl ].
VAR_014810
Natural varianti280 – 2801D → V.1 Publication
Corresponds to variant rs2307329 [ dbSNP | Ensembl ].
VAR_014811
Natural varianti287 – 2871F → L.1 Publication
Corresponds to variant rs2307328 [ dbSNP | Ensembl ].
VAR_014812
Natural varianti590 – 5901I → L.1 Publication
Corresponds to variant rs17240063 [ dbSNP | Ensembl ].
VAR_020516
Natural varianti774 – 7741R → W.1 Publication
Corresponds to variant rs2230239 [ dbSNP | Ensembl ].
VAR_020517
Natural varianti777 – 7771E → K.1 Publication
Corresponds to variant rs2230240 [ dbSNP | Ensembl ].
VAR_020427

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 11M → MLPRSPPLPRGNLWWREEFG SFRAGVESSWEPPRDFGGGS SLAAGM in isoform 2. 1 PublicationVSP_057050

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X62153 mRNA. Translation: CAA44078.2.
D38073 mRNA. Translation: BAA07267.1.
AK301704 mRNA. Translation: BAG63176.1.
AY621074 Genomic DNA. Translation: AAT27321.1.
AL034343 Genomic DNA. Translation: CAB75298.1.
CH471081 Genomic DNA. Translation: EAX04367.1.
BC001626 mRNA. Translation: AAH01626.1.
BC003509 mRNA. Translation: AAH03509.2.
PIRiS62594.
RefSeqiNP_001257401.1. NM_001270472.1.
NP_002379.3. NM_002388.4.
UniGeneiHs.179565.

Genome annotation databases

EnsembliENST00000229854; ENSP00000229854; ENSG00000112118.
GeneIDi4172.
KEGGihsa:4172.

Polymorphism databases

DMDMi19857543.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Web resourcesi

NIEHS-SNPs

Sequence databases

Select the link destinations:
EMBL
GenBank
DDBJ
Links Updated
X62153 mRNA. Translation: CAA44078.2 .
D38073 mRNA. Translation: BAA07267.1 .
AK301704 mRNA. Translation: BAG63176.1 .
AY621074 Genomic DNA. Translation: AAT27321.1 .
AL034343 Genomic DNA. Translation: CAB75298.1 .
CH471081 Genomic DNA. Translation: EAX04367.1 .
BC001626 mRNA. Translation: AAH01626.1 .
BC003509 mRNA. Translation: AAH03509.2 .
PIRi S62594.
RefSeqi NP_001257401.1. NM_001270472.1.
NP_002379.3. NM_002388.4.
UniGenei Hs.179565.

3D structure databases

ProteinModelPortali P25205.
SMRi P25205. Positions 10-650.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110340. 90 interactions.
DIPi DIP-31726N.
IntActi P25205. 38 interactions.
MINTi MINT-1201900.
STRINGi 9606.ENSP00000229854.

PTM databases

PhosphoSitei P25205.

Polymorphism databases

DMDMi 19857543.

Proteomic databases

MaxQBi P25205.
PaxDbi P25205.
PeptideAtlasi P25205.
PRIDEi P25205.

Protocols and materials databases

DNASUi 4172.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000229854 ; ENSP00000229854 ; ENSG00000112118 .
GeneIDi 4172.
KEGGi hsa:4172.

Organism-specific databases

CTDi 4172.
GeneCardsi GC06M052128.
HGNCi HGNC:6945. MCM3.
HPAi CAB002162.
HPA004789.
HPA004790.
MIMi 602693. gene.
neXtProti NX_P25205.
PharmGKBi PA30691.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1241.
GeneTreei ENSGT00550000075022.
HOGENOMi HOG000224126.
HOVERGENi HBG104962.
InParanoidi P25205.
KOi K02541.
PhylomeDBi P25205.
TreeFami TF106459.

Enzyme and pathway databases

Reactomei REACT_1095. Activation of the pre-replicative complex.
REACT_1156. Orc1 removal from chromatin.
REACT_207. Removal of licensing factors from origins.
REACT_2148. Switching of origins to a post-replicative state.
REACT_2243. Assembly of the pre-replicative complex.
REACT_6769. Activation of ATR in response to replication stress.
REACT_6776. Unwinding of DNA.

Miscellaneous databases

ChiTaRSi MCM3. human.
GeneWikii MCM3.
GenomeRNAii 4172.
NextBioi 13605303.
PMAP-CutDB P25205.
PROi P25205.
SOURCEi Search...

Gene expression databases

Bgeei P25205.
CleanExi HS_MCM3.
ExpressionAtlasi P25205. baseline and differential.
Genevestigatori P25205.

Family and domain databases

Gene3Di 2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR008046. Mcm3.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view ]
Pfami PF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view ]
PRINTSi PR01657. MCMFAMILY.
PR01659. MCMPROTEIN3.
SMARTi SM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 2 hits.
PROSITEi PS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "The P1 family: a new class of nuclear mammalian proteins related to the yeast Mcm replication proteins."
    Hu B., Burkhart R., Schulte D., Musahl C., Knippers R.
    Nucleic Acids Res. 21:5289-5293(1993) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cervix.
  2. Goehring F., Jehnichen P., Hemmer W.H.
    Submitted (AUG-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: SEQUENCE REVISION.
  3. "Identification of the yeast MCM3-related protein as a component of Xenopus DNA replication licensing factor."
    Kubota Y., Mimura S., Nishimoto S., Takisawa H., Nojima H.
    Cell 81:601-609(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1).
    Tissue: Cervix.
  4. "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] (ISOFORM 2).
    Tissue: Testis.
  5. NIEHS SNPs program
    Submitted (MAY-2004) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [GENOMIC DNA], VARIANTS VAL-280; LEU-287; LEU-590; TRP-774 AND LYS-777.
  6. "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].
  7. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  8. "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] (ISOFORM 1).
    Tissue: Lymph and Pancreas.
  9. Bienvenut W.V., Glen H., Brunton V.G., Frame M.C.
    Submitted (JUL-2007) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-13; 47-55; 337-351 AND 749-756, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Osteosarcoma.
  10. "Properties of the nuclear P1 protein, a mammalian homologue of the yeast Mcm3 replication protein."
    Thoemmes P., Fett R., Schray B., Burkhart R., Barnes M., Kennedy C., Brown N.C., Knippers R.
    Nucleic Acids Res. 20:1069-1074(1992) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 563-808 (ISOFORM 1).
  11. "Minichromosome maintenance proteins are direct targets of the ATM and ATR checkpoint kinases."
    Cortez D., Glick G., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 101:10078-10083(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION AT SER-535, MUTAGENESIS OF SER-535.
  12. "Global, in vivo, and site-specific phosphorylation dynamics in signaling networks."
    Olsen J.V., Blagoev B., Gnad F., Macek B., Kumar C., Mortensen P., Mann M.
    Cell 127:635-648(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  13. "Essential role of phosphorylation of MCM2 by Cdc7/Dbf4 in the initiation of DNA replication in mammalian cells."
    Tsuji T., Ficarro S.B., Jiang W.
    Mol. Biol. Cell 17:4459-4472(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, ATPASE ACTIVITY OF THE MCM2-7 COMPLEX.
  14. "A probability-based approach for high-throughput protein phosphorylation analysis and site localization."
    Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P.
    Nat. Biotechnol. 24:1285-1292(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672 AND THR-674, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "Toward a global characterization of the phosphoproteome in prostate cancer cells: identification of phosphoproteins in the LNCaP cell line."
    Giorgianni F., Zhao Y., Desiderio D.M., Beranova-Giorgianni S.
    Electrophoresis 28:2027-2034(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Prostate cancer.
  16. "Identification and characterization of a novel component of the human minichromosome maintenance complex."
    Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.
    Mol. Cell. Biol. 27:3044-3055(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION BY MASS SPECTROMETRY.
  17. "Kinase-selective enrichment enables quantitative phosphoproteomics of the kinome across the cell cycle."
    Daub H., Olsen J.V., Bairlein M., Gnad F., Oppermann F.S., Korner R., Greff Z., Keri G., Stemmann O., Mann M.
    Mol. Cell 31:438-448(2008) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-668; SER-672; THR-674; SER-681; SER-711; THR-713 AND THR-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach."
    Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S.
    Anal. Chem. 81:4493-4501(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  20. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  21. "Quantitative phosphoproteomic analysis of T cell receptor signaling reveals system-wide modulation of protein-protein interactions."
    Mayya V., Lundgren D.H., Hwang S.-I., Rezaul K., Wu L., Eng J.K., Rodionov V., Han D.K.
    Sci. Signal. 2:RA46-RA46(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-672; THR-674; TYR-708; SER-711; THR-713; THR-722 AND THR-725, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  22. "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: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-668; SER-672; SER-711 AND THR-722, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  23. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  24. "System-wide temporal characterization of the proteome and phosphoproteome of human embryonic stem cell differentiation."
    Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J., Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V., Blagoev B.
    Sci. Signal. 4:RS3-RS3(2011) [PubMed] [Europe PMC] [Abstract]
    Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-160; SER-672; THR-674 AND SER-711, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  25. "Characterization of O-GlcNAc cycling and proteomic identification of differentially O-GlcNAcylated proteins during G1/S transition."
    Drougat L., Olivier-Van Stichelen S., Mortuaire M., Foulquier F., Lacoste A.S., Michalski J.C., Lefebvre T., Vercoutter-Edouart A.S.
    Biochim. Biophys. Acta 1820:1839-1848(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: GLYCOSYLATION.
  26. "Comparative large-scale characterisation of plant vs. mammal proteins reveals similar and idiosyncratic N-alpha acetylation features."
    Bienvenut W.V., Sumpton D., Martinez A., Lilla S., Espagne C., Meinnel T., Giglione C.
    Mol. Cell. Proteomics 11:M111.015131-M111.015131(2012) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  27. Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCM3_HUMAN
AccessioniPrimary (citable) accession number: P25205
Secondary accession number(s): B4DWW4
, Q92660, Q9BTR3, Q9NUE7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: May 1, 1992
Last sequence update: August 14, 2001
Last modified: October 29, 2014
This is version 170 of the entry and version 3 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

Miscellaneous

Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. The MCM2-7 hexamer is the proposed physiological active complex.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, 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. SIMILARITY comments
    Index of protein domains and families

External Data

Dasty 3