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Protein

DNA replication licensing factor MCM4

Gene

Mcm4

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: 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.By similarity

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi509 – 5168ATPSequence analysis

GO - Molecular functioni

  • ATP binding Source: UniProtKB-KW
  • ATP-dependent DNA helicase activity Source: Ensembl
  • single-stranded DNA binding Source: MGI

GO - Biological processi

  • cell cycle Source: UniProtKB-KW
  • DNA replication initiation Source: InterPro
  • DNA unwinding involved in DNA replication Source: MGI
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

ReactomeiR-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-68867. Assembly of the pre-replicative complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69052. Switching of origins to a post-replicative state.
R-MMU-69300. Removal of licensing factors from origins.

Names & Taxonomyi

Protein namesi
Recommended name:
DNA replication licensing factor MCM4 (EC:3.6.4.12)
Alternative name(s):
CDC21 homolog
P1-CDC21
Gene namesi
Name:Mcm4
Synonyms:Cdc21, Mcmd4
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 16

Organism-specific databases

MGIiMGI:103199. Mcm4.

Subcellular locationi

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methionineiRemovedBy similarity
Chaini2 – 862861DNA replication licensing factor MCM4PRO_0000194102Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylserineBy similarity
Modified residuei19 – 191PhosphothreonineCombined sources
Modified residuei26 – 261PhosphoserineBy similarity
Modified residuei31 – 311PhosphoserineBy similarity
Modified residuei32 – 321PhosphoserineBy similarity
Modified residuei119 – 1191PhosphoserineBy similarity
Modified residuei130 – 1301PhosphoserineCombined sources
Modified residuei141 – 1411PhosphoserineBy similarity
Modified residuei144 – 1441PhosphoserineBy similarity
Modified residuei219 – 2191N6-acetyllysineBy similarity
Modified residuei449 – 4491N6-acetyllysineBy similarity
Modified residuei857 – 8571N6-acetyllysineCombined sources

Post-translational modificationi

Sumoylated; SUMO2 modified in response to stress caused by inhibition of proteasome activity (in vitro).1 Publication

Keywords - PTMi

Acetylation, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiP49717.
PaxDbiP49717.
PRIDEiP49717.

PTM databases

iPTMnetiP49717.
PhosphoSiteiP49717.

Expressioni

Gene expression databases

BgeeiP49717.
ExpressionAtlasiP49717. baseline and differential.
GenevisibleiP49717. MM.

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. Interacts with MCMBP.By similarity

Protein-protein interaction databases

BioGridi201347. 3 interactions.
IntActiP49717. 3 interactions.
MINTiMINT-1867081.
STRINGi10090.ENSMUSP00000023353.

Structurei

3D structure databases

ProteinModelPortaliP49717.
SMRiP49717. Positions 155-768.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini457 – 666210MCMAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi641 – 6444Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiKOG0478. Eukaryota.
COG1241. LUCA.
HOGENOMiHOG000224127.
HOVERGENiHBG102781.
InParanoidiP49717.
KOiK02212.
OMAiKNTIRIC.
OrthoDBiEOG78D7JF.
PhylomeDBiP49717.
TreeFamiTF300463.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008047. MCM_4.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01660. MCMPROTEIN4.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

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

P49717-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MSSPASTPSR RSSRRGRVTP TQSLRSEESR SSPNRRRRGE DSSTGELLPM
60 70 80 90 100
PTSPGADLQS PPAQNALFSS PPQMHSLAIP LDFDVSSPLT YGTPSSRVEG
110 120 130 140 150
TPRSGVRGTP VRQRPDLGSA RKGLQVDLQS DGAAAEDIVP SEQSLGQKLV
160 170 180 190 200
IWGTDVNVAT CKENFQRFLQ CFTDPLAKEE ENVGIDITQP LYMQQLGEIN
210 220 230 240 250
ITGEPFLNVN CEHIKSFSKN LYRQLISYPQ EVIPTFDMAV NEIFFDRYPD
260 270 280 290 300
SILEHQIQVR PFNALKTKSM RNLNPEDIDQ LITISGMVIR TSQLIPEMQE
310 320 330 340 350
AFFQCQVCAH TTRVEIDRGR IAEPCSCVHC HTTHSMALIH NRSFFSDKQM
360 370 380 390 400
IKLQESPEDM PAGQTPHTIV LFAHNDLVDK VQPGDRVNVT GIYRAVPIRV
410 420 430 440 450
NPRVSNVKSV YKTHIDVIHY RKTDAKRLHG LDEEAEQKLF SEKRVKLLKE
460 470 480 490 500
LSRKPDIYER LASALAPSIY EHEDIKKGIL LQLFGGTRKD FSHTGRGKFR
510 520 530 540 550
AEINILLCGD PGTSKSQLLQ YVYNLVPRGQ YTSGKGSSAV GLTAYVMKDP
560 570 580 590 600
ETRQLVLQTG ALVLSDNGIC CIDEFDKMNE STRSVLHEVM EQQTLSIAKA
610 620 630 640 650
GIICQLNART SVLAAANPIE SQWNPKKTTI ENIQLPHTLL SRFDLIFLML
660 670 680 690 700
DPQDEAYDRR LAHHLVSLYY QSEEQVEEEF LDMAVLKDYI AYAHSTIMPR
710 720 730 740 750
LSEEASQALI EAYVNMRKIG SSRGMVSAYP RQLESLIRLA EAHAKVRFSN
760 770 780 790 800
KVEAIDVEEA KRLHREALKQ SATDPRTGIV DISILTTGMS ATSRKRKEEL
810 820 830 840 850
AEALRKLILS KGKTPALKYQ QLFEDIRGQS DTAITKDMFE EALRALADDD
860
FLTVTGKTVR LL
Length:862
Mass (Da):96,736
Last modified:October 1, 1996 - v1
Checksum:i516ACC1A3C6FB16E
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti530 – 5301Q → R in AAC36509 (PubMed:9798653).Curated
Sequence conflicti572 – 5721I → T in AAC36509 (PubMed:9798653).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26089 mRNA. Translation: BAA05082.1.
U89402 mRNA. Translation: AAC36509.1.
CCDSiCCDS27977.1.
PIRiS56766.
RefSeqiNP_032591.3. NM_008565.3.
UniGeneiMm.1500.

Genome annotation databases

EnsembliENSMUST00000023353; ENSMUSP00000023353; ENSMUSG00000022673.
GeneIDi17217.
KEGGimmu:17217.
UCSCiuc007yhr.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D26089 mRNA. Translation: BAA05082.1.
U89402 mRNA. Translation: AAC36509.1.
CCDSiCCDS27977.1.
PIRiS56766.
RefSeqiNP_032591.3. NM_008565.3.
UniGeneiMm.1500.

3D structure databases

ProteinModelPortaliP49717.
SMRiP49717. Positions 155-768.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi201347. 3 interactions.
IntActiP49717. 3 interactions.
MINTiMINT-1867081.
STRINGi10090.ENSMUSP00000023353.

PTM databases

iPTMnetiP49717.
PhosphoSiteiP49717.

Proteomic databases

EPDiP49717.
PaxDbiP49717.
PRIDEiP49717.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000023353; ENSMUSP00000023353; ENSMUSG00000022673.
GeneIDi17217.
KEGGimmu:17217.
UCSCiuc007yhr.2. mouse.

Organism-specific databases

CTDi4173.
MGIiMGI:103199. Mcm4.

Phylogenomic databases

eggNOGiKOG0478. Eukaryota.
COG1241. LUCA.
HOGENOMiHOG000224127.
HOVERGENiHBG102781.
InParanoidiP49717.
KOiK02212.
OMAiKNTIRIC.
OrthoDBiEOG78D7JF.
PhylomeDBiP49717.
TreeFamiTF300463.

Enzyme and pathway databases

ReactomeiR-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-68867. Assembly of the pre-replicative complex.
R-MMU-68949. Orc1 removal from chromatin.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69052. Switching of origins to a post-replicative state.
R-MMU-69300. Removal of licensing factors from origins.

Miscellaneous databases

ChiTaRSiMcm4. mouse.
NextBioi291610.
PROiP49717.
SOURCEiSearch...

Gene expression databases

BgeeiP49717.
ExpressionAtlasiP49717. baseline and differential.
GenevisibleiP49717. MM.

Family and domain databases

Gene3Di2.20.28.10. 1 hit.
2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR031327. MCM.
IPR008047. MCM_4.
IPR018525. MCM_CS.
IPR001208. MCM_dom.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
IPR004039. Rubredoxin-type_fold.
[Graphical view]
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01660. MCMPROTEIN4.
SMARTiSM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 1 hit.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

« Hide 'large scale' publications
  1. "Molecular cloning of cDNA encoding mouse Cdc21 and CDC46 homologs and characterization of the products: physical interaction between P1(MCM3) and CDC46 proteins."
    Kimura H., Takizawa N., Nozaki N., Sugimoto K.
    Nucleic Acids Res. 23:2097-2104(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA].
  2. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
    Chu C.C., Paul W.E.
    Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 503-602.
    Strain: BALB/cJ.
    Tissue: Spleen.
  3. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-19 AND SER-130, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Heart, Kidney, Liver, Lung, Pancreas, Spleen and Testis.
  4. "SIRT5-mediated lysine desuccinylation impacts diverse metabolic pathways."
    Park J., Chen Y., Tishkoff D.X., Peng C., Tan M., Dai L., Xie Z., Zhang Y., Zwaans B.M., Skinner M.E., Lombard D.B., Zhao Y.
    Mol. Cell 50:919-930(2013) [PubMed] [Europe PMC] [Abstract]
    Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT LYS-857, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic fibroblast.
  5. Cited for: SUMOYLATION.

Entry informationi

Entry nameiMCM4_MOUSE
AccessioniPrimary (citable) accession number: P49717
Secondary accession number(s): O89056
Entry historyi
Integrated into UniProtKB/Swiss-Prot: October 1, 1996
Last sequence update: October 1, 1996
Last modified: May 11, 2016
This is version 133 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

Miscellaneous

Early fractionation of eukaryotic MCM proteins yielded a variety of dimeric, trimeric and tetrameric complexes with unclear biological significance. Specifically a MCM467 subcomplex is shown to have in vitro helicase activity which is inhibited by the MCM2 subunit. The MCM2-7 hexamer is the proposed physiological active complex.By similarity

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  2. SIMILARITY comments
    Index of protein domains and families

Similar proteinsi

Links to similar proteins from the UniProt Reference Clusters (UniRef) at 100%, 90% and 50% sequence identity:
100%UniRef100 combines identical sequences and sub-fragments with 11 or more residues from any organism into one UniRef entry.
90%UniRef90 is built by clustering UniRef100 sequences that have at least 90% sequence identity to, and 80% overlap with, the longest sequence (a.k.a seed sequence).
50%UniRef50 is built by clustering UniRef90 seed sequences that have at least 50% sequence identity to, and 80% overlap with, the longest sequence in the cluster.