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Protein

Protein MCM10 homolog

Gene

Mcm10

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score: Annotation score: 4 out of 5-Experimental evidence at protein leveli

Functioni

Acts as a replication initiation factor that brings together the MCM2-7 helicase and the DNA polymerase alpha/primase complex in order to initiate DNA replication. Additionally, plays a role in preventing DNA damage during replication. Key effector of the RBBP6 and ZBTB38-mediated regulation of DNA-replication and common fragile sites stability; acts as a direct target of transcriptional repression by ZBTB38 (By similarity).By similarity

GO - Molecular functioni

  • DNA binding Source: UniProtKB-KW
  • enzyme binding Source: BHF-UCL
  • identical protein binding Source: MGI
  • metal ion binding Source: UniProtKB-KW

GO - Biological processi

  • cell proliferation Source: MGI
  • cellular response to DNA damage stimulus Source: UniProtKB
  • DNA replication Source: UniProtKB-KW
Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA replication

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69300. Removal of licensing factors from origins.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein MCM10 homolog
Gene namesi
Name:Mcm10
OrganismiMus musculus (Mouse)
Taxonomic identifieri10090 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
Proteomesi
  • UP000000589 Componenti: Chromosome 2

Organism-specific databases

MGIiMGI:1917274. Mcm10.

Subcellular locationi

  • Nucleus By similarity

  • Note: Colocalizes with ORC2 in nuclei foci. Associated with chromatin in S phase (By similarity).By similarity

GO - Cellular componenti

Complete GO annotation...

Keywords - Cellular componenti

Nucleus

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 885885Protein MCM10 homologPRO_0000278321Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851PhosphothreonineCombined sources
Cross-linki639 – 639Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)By similarity
Modified residuei656 – 6561PhosphoserineCombined sources
Cross-linki772 – 772Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)By similarity

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ0VBD2.
MaxQBiQ0VBD2.
PaxDbiQ0VBD2.
PRIDEiQ0VBD2.

PTM databases

iPTMnetiQ0VBD2.
PhosphoSiteiQ0VBD2.

Expressioni

Gene expression databases

BgeeiQ0VBD2.
GenevisibleiQ0VBD2. MM.

Interactioni

Subunit structurei

Self-associates (By similarity). Interacts with ORC2. May interact with MCM2 and MCM6. Interacts with the DNA polymerase alpha subunit POLA1. Interacts with RECQL4; this interaction regulates RECQL4 unwinding activity. Interacts with WDHD1 (By similarity).By similarity

GO - Molecular functioni

  • enzyme binding Source: BHF-UCL
  • identical protein binding Source: MGI

Protein-protein interaction databases

BioGridi213824. 2 interactions.
STRINGi10090.ENSMUSP00000027980.

Structurei

3D structure databases

ProteinModelPortaliQ0VBD2.
SMRiQ0VBD2. Positions 260-432, 780-867.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 153153N-terminal domainBy similarityAdd
BLAST
Regioni251 – 405155OB-fold domainBy similarityAdd
BLAST
Regioni406 – 43126Zinc finger-like 1Add
BLAST
Regioni793 – 81220Zinc finger-like 2By similarityAdd
BLAST
Regioni826 – 84621Zinc finger-like 3By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili101 – 13939Sequence analysisAdd
BLAST

Domaini

Each zinc finger-like domain binds a zinc ion and is involved in both ssDNA and dsDNA binding, as is the OB-fold domain.By similarity
The N-terminal domain mediates homodimerization.By similarity

Sequence similaritiesi

Belongs to the MCM10 family.Curated

Keywords - Domaini

Coiled coil, Zinc-finger

Phylogenomic databases

eggNOGiKOG3056. Eukaryota.
ENOG41100ZT. LUCA.
GeneTreeiENSGT00390000007134.
HOGENOMiHOG000082481.
HOVERGENiHBG055312.
InParanoidiQ0VBD2.
KOiK10736.
OMAiKHCSNCG.
OrthoDBiEOG7D59N8.
PhylomeDBiQ0VBD2.
TreeFamiTF313330.

Family and domain databases

InterProiIPR015411. Rep_factor_Mcm10_C.
IPR015408. Znf_Mcm10/DnaG.
[Graphical view]
PfamiPF09332. Mcm10. 1 hit.
PF09329. zf-primase. 1 hit.
[Graphical view]
SMARTiSM01280. Mcm10. 1 hit.
[Graphical view]

Sequencei

Sequence statusi: Complete.

Q0VBD2-1 [UniParc]FASTAAdd to basket

« Hide

        10         20         30         40         50
MDVEEDDLCL LTSLLEENEA VLPCSSEKDK SLSLGDGDPD EFDELFDADG
60 70 80 90 100
DGESYTEEAG SGEEGKTGNQ EERLATLFGD VEDLTDDEVA TSKVGNSGPP
110 120 130 140 150
PAPSQEKTSE ELQDELKKLQ EQMKSLQEQL KAASIKQPPG TAPLQEPPDS
160 170 180 190 200
SLQPLLKEKR IRRIQESACF SAELDVPTLP KAKRVARKPK TPAESSSRMR
210 220 230 240 250
TPAQPLQVSS SFLEPNHSSS SRSSTPSPQA VPGNKCSRTI RNQNTVSPGN
260 270 280 290 300
SGDRPQQVSQ VSVEAFSGLR LRRPRVSSTE MSRKMAGRKL IRLPQIKEKM
310 320 330 340 350
ATENLEETDW VTFGVILRKV TPQSATSGQT FSIWKLNDLH DLTQCVSLFL
360 370 380 390 400
FGDVHKDLWK TEQGTVIGLL NANPMKPKDG LKEVCLSIDH PQKVLIMGEA
410 420 430 440 450
MDLGACKAKK KNGEPCTQTV NLHDCEYCQY HIQAQYKKLS AKRTDLQSTF
460 470 480 490 500
SGGRIPKKFR KGTSLKERLC QDGFYYGGVS SESFAASRAA AIAPKKKVQT
510 520 530 540 550
TLTNLVVRGT NSIIQETKQK LGIPQKSLSC SEEFRELMAL PTFGARNLQK
560 570 580 590 600
HLARAKASGS SKPAIQSISA SALLKQQKQQ MLEMRKRRSE DIQKRFLQSS
610 620 630 640 650
SEVQSPAVPS SSRQAAAQSP RTGAEFPRLE GTATPRMPKL GRGISEGDDV
660 670 680 690 700
LFFDDSPPPR PKLSAAAEAK KLAAIAKLRA KGQILTKVDP NNTVRKQMDG
710 720 730 740 750
RAMLGVKERV ENSNTVSPEE ELEPARKKRR EQLAYLESEE FQKILKAKSK
760 770 780 790 800
HTDILKEAEA ELQKSYFEPL VKKEQMEEKM RATREVKCRV VTCRTCTYTH
810 820 830 840 850
FKPLETCVSE QHNLHWHDGV KRFFKCPCGN RTISLDKLPN KHCRNCGLYK
860 870 880
WERDGMLKEK TGPKIGGETL LPRGEEHAKF LNSLK
Length:885
Mass (Da):98,406
Last modified:September 5, 2006 - v1
Checksum:iCF2F91AC0A8A18B1
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti50 – 501G → R in AAH94576 (PubMed:15489334).Curated
Sequence conflicti673 – 6731A → V in BAC27135 (PubMed:16141072).Curated
Sequence conflicti873 – 8731R → I in AAH94576 (PubMed:15489334).Curated

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK030780 mRNA. Translation: BAC27135.1.
AK041406 mRNA. Translation: BAC30933.1.
AL928662 Genomic DNA. Translation: CAM22575.1.
BC094576 mRNA. Translation: AAH94576.1.
BC120689 mRNA. Translation: AAI20690.1.
BC120687 mRNA. Translation: AAI20688.1.
CCDSiCCDS15662.1.
RefSeqiNP_001292188.1. NM_001305259.1.
NP_081566.2. NM_027290.3.
UniGeneiMm.23828.
Mm.447935.

Genome annotation databases

EnsembliENSMUST00000027980; ENSMUSP00000027980; ENSMUSG00000026669.
ENSMUST00000102985; ENSMUSP00000100050; ENSMUSG00000026669.
GeneIDi70024.
KEGGimmu:70024.
UCSCiuc008ifh.2. mouse.

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AK030780 mRNA. Translation: BAC27135.1.
AK041406 mRNA. Translation: BAC30933.1.
AL928662 Genomic DNA. Translation: CAM22575.1.
BC094576 mRNA. Translation: AAH94576.1.
BC120689 mRNA. Translation: AAI20690.1.
BC120687 mRNA. Translation: AAI20688.1.
CCDSiCCDS15662.1.
RefSeqiNP_001292188.1. NM_001305259.1.
NP_081566.2. NM_027290.3.
UniGeneiMm.23828.
Mm.447935.

3D structure databases

ProteinModelPortaliQ0VBD2.
SMRiQ0VBD2. Positions 260-432, 780-867.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi213824. 2 interactions.
STRINGi10090.ENSMUSP00000027980.

PTM databases

iPTMnetiQ0VBD2.
PhosphoSiteiQ0VBD2.

Proteomic databases

EPDiQ0VBD2.
MaxQBiQ0VBD2.
PaxDbiQ0VBD2.
PRIDEiQ0VBD2.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000027980; ENSMUSP00000027980; ENSMUSG00000026669.
ENSMUST00000102985; ENSMUSP00000100050; ENSMUSG00000026669.
GeneIDi70024.
KEGGimmu:70024.
UCSCiuc008ifh.2. mouse.

Organism-specific databases

CTDi55388.
MGIiMGI:1917274. Mcm10.

Phylogenomic databases

eggNOGiKOG3056. Eukaryota.
ENOG41100ZT. LUCA.
GeneTreeiENSGT00390000007134.
HOGENOMiHOG000082481.
HOVERGENiHBG055312.
InParanoidiQ0VBD2.
KOiK10736.
OMAiKHCSNCG.
OrthoDBiEOG7D59N8.
PhylomeDBiQ0VBD2.
TreeFamiTF313330.

Enzyme and pathway databases

ReactomeiR-MMU-176187. Activation of ATR in response to replication stress.
R-MMU-68962. Activation of the pre-replicative complex.
R-MMU-69300. Removal of licensing factors from origins.

Miscellaneous databases

NextBioi330845.
PROiQ0VBD2.
SOURCEiSearch...

Gene expression databases

BgeeiQ0VBD2.
GenevisibleiQ0VBD2. MM.

Family and domain databases

InterProiIPR015411. Rep_factor_Mcm10_C.
IPR015408. Znf_Mcm10/DnaG.
[Graphical view]
PfamiPF09332. Mcm10. 1 hit.
PF09329. zf-primase. 1 hit.
[Graphical view]
SMARTiSM01280. Mcm10. 1 hit.
[Graphical view]
ProtoNetiSearch...

Publicationsi

  1. "The transcriptional landscape of the mammalian genome."
    Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
    , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
    Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
    Strain: C57BL/6J.
    Tissue: Thymus.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
    Strain: C57BL/6J.
  3. "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].
    Strain: C57BL/6J.
    Tissue: Brain.
  4. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85 AND SER-656, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Lung, Spleen and Testis.

Entry informationi

Entry nameiMCM10_MOUSE
AccessioniPrimary (citable) accession number: Q0VBD2
Secondary accession number(s): Q505F3, Q8BMJ1, Q8BYA7
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: September 5, 2006
Last modified: May 11, 2016
This is version 84 of the entry and version 1 of the sequence. [Complete history]
Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

Miscellaneousi

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.