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Protein

Protein MCM10 homolog

Gene

MCM10

Organism
Homo sapiens (Human)
Status
Reviewed-Annotation score: Annotation score: 5 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 (PubMed:24726359).5 Publications

GO - Molecular functioni

GO - Biological processi

Complete GO annotation...

Keywords - Biological processi

DNA damage, DNA replication

Keywords - Ligandi

DNA-binding, Metal-binding, Zinc

Enzyme and pathway databases

ReactomeiR-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-68962. Activation of the pre-replicative complex.
R-HSA-69300. Removal of licensing factors from origins.
SIGNORiQ7L590.

Names & Taxonomyi

Protein namesi
Recommended name:
Protein MCM10 homolog
Short name:
HsMCM10
Gene namesi
Name:MCM10
ORF Names:PRO2249
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresPrimatesHaplorrhiniCatarrhiniHominidaeHomo
Proteomesi
  • UP000005640 Componenti: Chromosome 10

Organism-specific databases

HGNCiHGNC:18043. MCM10.

Subcellular locationi

  • Nucleus 2 Publications

  • Note: Colocalizes with ORC2 in nuclei foci. Associated with chromatin in S phase. From early to mid-S phase located in discrete nuclear foci. In early S phase, several hundred foci appeared throughout the nucleus. In mid-S phase, the foci appeared at the nuclear periphery and nucleolar regions. In the late S and G phases localized to nucleoli.

GO - Cellular componenti

  • cytoplasm Source: HPA
  • nucleolus Source: HPA
  • nucleoplasm Source: Reactome
  • nucleus Source: UniProtKB
  • replication fork protection complex Source: GO_Central
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30689.

Polymorphism and mutation databases

BioMutaiMCM10.
DMDMi126215746.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Chaini1 – 875875Protein MCM10 homologPRO_0000278320Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei85 – 851PhosphothreonineCombined sources
Modified residuei93 – 931PhosphoserineCombined sources
Cross-linki627 – 627Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in ubiquitin)1 Publication
Modified residuei644 – 6441PhosphoserineBy similarity
Cross-linki762 – 762Glycyl lysine isopeptide (Lys-Gly) (interchain with G-Cter in SUMO2)Combined sources

Keywords - PTMi

Isopeptide bond, Phosphoprotein, Ubl conjugation

Proteomic databases

EPDiQ7L590.
MaxQBiQ7L590.
PaxDbiQ7L590.
PRIDEiQ7L590.

PTM databases

iPTMnetiQ7L590.
PhosphoSiteiQ7L590.

Expressioni

Developmental stagei

Expression is cell cycle regulated. Expression increases at the G1/S-boundary. Expression decreases in late M phase, remains low during G1 phase, and starts to accumulate at the onset of S phase.2 Publications

Gene expression databases

BgeeiQ7L590.
CleanExiHS_MCM10.
ExpressionAtlasiQ7L590. baseline and differential.
GenevisibleiQ7L590. HS.

Organism-specific databases

HPAiHPA045899.

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 similarity3 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
itself2EBI-374912,EBI-374912
GOLGA2Q083793EBI-10233517,EBI-618309
MCM6Q145663EBI-10233517,EBI-374900
ORC2Q134165EBI-374912,EBI-374957

GO - Molecular functioni

  • identical protein binding Source: IntAct

Protein-protein interaction databases

BioGridi120654. 61 interactions.
IntActiQ7L590. 37 interactions.
MINTiMINT-1201365.
STRINGi9606.ENSP00000354945.

Structurei

3D structure databases

ProteinModelPortaliQ7L590.
SMRiQ7L590. Positions 247-416, 770-857.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni1 – 156156N-terminal domainBy similarityAdd
BLAST
Regioni238 – 389152OB-fold domainBy similarityAdd
BLAST
Regioni390 – 41526Zinc finger-like 1Add
BLAST
Regioni783 – 80220Zinc finger-like 2By similarityAdd
BLAST
Regioni816 – 83621Zinc finger-like 3By similarityAdd
BLAST

Coiled coil

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Coiled coili104 – 14239Sequence 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.
HOVERGENiHBG055312.
InParanoidiQ7L590.
KOiK10736.
OMAiKHCSNCG.
OrthoDBiEOG7D59N8.
PhylomeDBiQ7L590.
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]

Sequences (2)i

Sequence statusi: Complete.

This entry describes 2 isoformsi produced by alternative splicing. AlignAdd to basket

Isoform 1 (identifier: Q7L590-1) [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
MDEEEDNLSL LTALLEENES ALDCNSEENN FLTRENGEPD AFDELFDADG
60 70 80 90 100
DGESYTEEAD DGETGETRDE KENLATLFGD MEDLTDEEEV PASQSTENRV
110 120 130 140 150
LPAPAPRREK TNEELQEELR NLQEQMKALQ EQLKVTTIKQ TASPARLQKS
160 170 180 190 200
PVEKSPRPPL KERRVQRIQE STCFSAELDV PALPRTKRVA RTPKASPPDP
210 220 230 240 250
KSSSSRMTSA PSQPLQTISR NKPSGITRGQ IVGTPGSSGE TTQPICVEAF
260 270 280 290 300
SGLRLRRPRV SSTEMNKKMT GRKLIRLSQI KEKMAREKLE EIDWVTFGVI
310 320 330 340 350
LKKVTPQSVN SGKTFSIWKL NDLRDLTQCV SLFLFGEVHK ALWKTEQGTV
360 370 380 390 400
VGILNANPMK PKDGSEEVCL SIDHPQKVLI MGEALDLGTC KAKKKNGEPC
410 420 430 440 450
TQTVNLRDCE YCQYHVQAQY KKLSAKRADL QSTFSGGRIP KKFARRGTSL
460 470 480 490 500
KERLCQDGFY YGGVSSASYA ASIAAAVAPK KKIQTTLSNL VVKGTNLIIQ
510 520 530 540 550
ETRQKLGIPQ KSLSCSEEFK ELMDLPTCGA RNLKQHLAKA TASGIMGSPK
560 570 580 590 600
PAIKSISASA LLKQQKQRML EMRRRKSEEI QKRFLQSSSE VESPAVPSSS
610 620 630 640 650
RQPPAQPPRT GSEFPRLEGA PATMTPKLGR GVLEGDDVLF YDESPPPRPK
660 670 680 690 700
LSALAEAKKL AAITKLRAKG QVLTKTNPNS IKKKQKDPQD ILEVKERVEK
710 720 730 740 750
NTMFSSQAED ELEPARKKRR EQLAYLESEE FQKILKAKSK HTGILKEAEA
760 770 780 790 800
EMQERYFEPL VKKEQMEEKM RNIREVKCRV VTCKTCAYTH FKLLETCVSE
810 820 830 840 850
QHEYHWHDGV KRFFKCPCGN RSISLDRLPN KHCSNCGLYK WERDGMLKEK
860 870
TGPKIGGETL LPRGEEHAKF LNSLK
Length:875
Mass (Da):98,183
Last modified:February 20, 2007 - v2
Checksum:iDD87191FFF3729D4
GO
Isoform 2 (identifier: Q7L590-2) [UniParc]FASTAAdd to basket

The sequence of this isoform differs from the canonical sequence as follows:
     152-152: Missing.

Show »
Length:874
Mass (Da):98,084
Checksum:i50A89BAF82253B43
GO

Sequence cautioni

The sequence AAF69623.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally extended.Curated

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti303 – 3031K → R in BAB70988 (PubMed:14702039).Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti134 – 1341K → R.1 Publication
Corresponds to variant rs17152897 [ dbSNP | Ensembl ].
VAR_030771
Natural varianti195 – 1951A → P.2 Publications
Corresponds to variant rs34630110 [ dbSNP | Ensembl ].
VAR_053836
Natural varianti418 – 4181A → V.
Corresponds to variant rs35114749 [ dbSNP | Ensembl ].
VAR_053837
Natural varianti541 – 5411T → S.2 Publications
Corresponds to variant rs7905784 [ dbSNP | Ensembl ].
VAR_030772
Natural varianti669 – 6691K → R.1 Publication
Corresponds to variant rs2274110 [ dbSNP | Ensembl ].
VAR_030773

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei152 – 1521Missing in isoform 2. 3 PublicationsVSP_029951

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042719 mRNA. Translation: BAB18723.1.
AL136840 mRNA. Translation: CAB66774.2.
AK055695 mRNA. Translation: BAB70988.1.
AK292701 mRNA. Translation: BAF85390.1.
AL355355, AL138764 Genomic DNA. Translation: CAI16558.1.
AL138764, AL355355 Genomic DNA. Translation: CAI12913.1.
CH471072 Genomic DNA. Translation: EAW86297.1.
BC004876 mRNA. Translation: AAH04876.2.
BC101727 mRNA. Translation: AAI01728.1.
BC143490 mRNA. Translation: AAI43491.1.
AF119869 mRNA. Translation: AAF69623.1. Different initiation.
CCDSiCCDS7095.1. [Q7L590-2]
CCDS7096.1. [Q7L590-1]
RefSeqiNP_060988.3. NM_018518.4. [Q7L590-2]
NP_877428.1. NM_182751.2. [Q7L590-1]
XP_011517840.1. XM_011519538.1. [Q7L590-1]
UniGeneiHs.198363.

Genome annotation databases

EnsembliENST00000378714; ENSP00000367986; ENSG00000065328. [Q7L590-2]
ENST00000484800; ENSP00000418268; ENSG00000065328. [Q7L590-1]
GeneIDi55388.
KEGGihsa:55388.
UCSCiuc001ima.4. human. [Q7L590-1]

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AB042719 mRNA. Translation: BAB18723.1.
AL136840 mRNA. Translation: CAB66774.2.
AK055695 mRNA. Translation: BAB70988.1.
AK292701 mRNA. Translation: BAF85390.1.
AL355355, AL138764 Genomic DNA. Translation: CAI16558.1.
AL138764, AL355355 Genomic DNA. Translation: CAI12913.1.
CH471072 Genomic DNA. Translation: EAW86297.1.
BC004876 mRNA. Translation: AAH04876.2.
BC101727 mRNA. Translation: AAI01728.1.
BC143490 mRNA. Translation: AAI43491.1.
AF119869 mRNA. Translation: AAF69623.1. Different initiation.
CCDSiCCDS7095.1. [Q7L590-2]
CCDS7096.1. [Q7L590-1]
RefSeqiNP_060988.3. NM_018518.4. [Q7L590-2]
NP_877428.1. NM_182751.2. [Q7L590-1]
XP_011517840.1. XM_011519538.1. [Q7L590-1]
UniGeneiHs.198363.

3D structure databases

ProteinModelPortaliQ7L590.
SMRiQ7L590. Positions 247-416, 770-857.
ModBaseiSearch...
MobiDBiSearch...

Protein-protein interaction databases

BioGridi120654. 61 interactions.
IntActiQ7L590. 37 interactions.
MINTiMINT-1201365.
STRINGi9606.ENSP00000354945.

PTM databases

iPTMnetiQ7L590.
PhosphoSiteiQ7L590.

Polymorphism and mutation databases

BioMutaiMCM10.
DMDMi126215746.

Proteomic databases

EPDiQ7L590.
MaxQBiQ7L590.
PaxDbiQ7L590.
PRIDEiQ7L590.

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENST00000378714; ENSP00000367986; ENSG00000065328. [Q7L590-2]
ENST00000484800; ENSP00000418268; ENSG00000065328. [Q7L590-1]
GeneIDi55388.
KEGGihsa:55388.
UCSCiuc001ima.4. human. [Q7L590-1]

Organism-specific databases

CTDi55388.
GeneCardsiMCM10.
HGNCiHGNC:18043. MCM10.
HPAiHPA045899.
MIMi609357. gene.
neXtProtiNX_Q7L590.
PharmGKBiPA30689.
GenAtlasiSearch...

Phylogenomic databases

eggNOGiKOG3056. Eukaryota.
ENOG41100ZT. LUCA.
GeneTreeiENSGT00390000007134.
HOVERGENiHBG055312.
InParanoidiQ7L590.
KOiK10736.
OMAiKHCSNCG.
OrthoDBiEOG7D59N8.
PhylomeDBiQ7L590.
TreeFamiTF313330.

Enzyme and pathway databases

ReactomeiR-HSA-176187. Activation of ATR in response to replication stress.
R-HSA-68962. Activation of the pre-replicative complex.
R-HSA-69300. Removal of licensing factors from origins.
SIGNORiQ7L590.

Miscellaneous databases

GeneWikiiMCM10.
GenomeRNAii55388.
PROiQ7L590.
SOURCEiSearch...

Gene expression databases

BgeeiQ7L590.
CleanExiHS_MCM10.
ExpressionAtlasiQ7L590. baseline and differential.
GenevisibleiQ7L590. HS.

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

« Hide 'large scale' publications
  1. "The human homolog of Saccharomyces cerevisiae Mcm10 interacts with replication factors and dissociates from nuclease-resistant nuclear structures in G(2) phase."
    Izumi M., Yanagi K., Mizuno T., Yokoi M., Kawasaki Y., Moon K.Y., Hurwitz J., Yatagai F., Hanaoka F.
    Nucleic Acids Res. 28:4769-4777(2000) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 2), SUBCELLULAR LOCATION, FUNCTION, DEVELOPMENTAL STAGE, INTERACTION WITH ORC2; MCM2 AND MCM6.
  2. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), VARIANTS PRO-195 AND SER-541.
    Tissue: Testis.
  3. "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 1), VARIANTS ARG-134 AND PRO-195.
    Tissue: Thymus.
  4. "The DNA sequence and comparative analysis of human chromosome 10."
    Deloukas P., Earthrowl M.E., Grafham D.V., Rubenfield M., French L., Steward C.A., Sims S.K., Jones M.C., Searle S., Scott C., Howe K., Hunt S.E., Andrews T.D., Gilbert J.G.R., Swarbreck D., Ashurst J.L., Taylor A., Battles J.
    , Bird C.P., Ainscough R., Almeida J.P., Ashwell R.I.S., Ambrose K.D., Babbage A.K., Bagguley C.L., Bailey J., Banerjee R., Bates K., Beasley H., Bray-Allen S., Brown A.J., Brown J.Y., Burford D.C., Burrill W., Burton J., Cahill P., Camire D., Carter N.P., Chapman J.C., Clark S.Y., Clarke G., Clee C.M., Clegg S., Corby N., Coulson A., Dhami P., Dutta I., Dunn M., Faulkner L., Frankish A., Frankland J.A., Garner P., Garnett J., Gribble S., Griffiths C., Grocock R., Gustafson E., Hammond S., Harley J.L., Hart E., Heath P.D., Ho T.P., Hopkins B., Horne J., Howden P.J., Huckle E., Hynds C., Johnson C., Johnson D., Kana A., Kay M., Kimberley A.M., Kershaw J.K., Kokkinaki M., Laird G.K., Lawlor S., Lee H.M., Leongamornlert D.A., Laird G., Lloyd C., Lloyd D.M., Loveland J., Lovell J., McLaren S., McLay K.E., McMurray A., Mashreghi-Mohammadi M., Matthews L., Milne S., Nickerson T., Nguyen M., Overton-Larty E., Palmer S.A., Pearce A.V., Peck A.I., Pelan S., Phillimore B., Porter K., Rice C.M., Rogosin A., Ross M.T., Sarafidou T., Sehra H.K., Shownkeen R., Skuce C.D., Smith M., Standring L., Sycamore N., Tester J., Thorpe A., Torcasso W., Tracey A., Tromans A., Tsolas J., Wall M., Walsh J., Wang H., Weinstock K., West A.P., Willey D.L., Whitehead S.L., Wilming L., Wray P.W., Young L., Chen Y., Lovering R.C., Moschonas N.K., Siebert R., Fechtel K., Bentley D., Durbin R.M., Hubbard T., Doucette-Stamm L., Beck S., Smith D.R., Rogers J.
    Nature 429:375-381(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  5. Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  6. "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] (ISOFORMS 1 AND 2), VARIANTS SER-541 AND ARG-669.
    Tissue: Liver, Lymph and Placenta.
  7. Zhang C., Yu Y., Zhang S., Wei H., Zhang Y., Zhou G., Bi J., Liu M., He F.
    Submitted (JAN-1999) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 517-875.
    Tissue: Fetal liver.
  8. "Cell cycle-dependent proteolysis and phosphorylation of human Mcm10."
    Izumi M., Yatagai F., Hanaoka F.
    J. Biol. Chem. 276:48526-48531(2001) [PubMed] [Europe PMC] [Abstract]
    Cited for: DEVELOPMENTAL STAGE, PHOSPHORYLATION.
  9. "Localization of human Mcm10 is spatially and temporally regulated during the S phase."
    Izumi M., Yatagai F., Hanaoka F.
    J. Biol. Chem. 279:32569-32577(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, SUBCELLULAR LOCATION.
  10. "Mcm10 and And-1/CTF4 recruit DNA polymerase alpha to chromatin for initiation of DNA replication."
    Zhu W., Ukomadu C., Jha S., Senga T., Dhar S.K., Wohlschlegel J.A., Nutt L.K., Kornbluth S., Dutta A.
    Genes Dev. 21:2288-2299(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH POLA1 AND WDHD1.
  11. "Human Mcm10 regulates the catalytic subunit of DNA polymerase-alpha and prevents DNA damage during replication."
    Chattopadhyay S., Bielinsky A.K.
    Mol. Biol. Cell 18:4085-4095(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  12. "Tryptic digestion of ubiquitin standards reveals an improved strategy for identifying ubiquitinated proteins by mass spectrometry."
    Denis N.J., Vasilescu J., Lambert J.-P., Smith J.C., Figeys D.
    Proteomics 7:868-874(2007) [PubMed] [Europe PMC] [Abstract]
    Cited for: UBIQUITINATION [LARGE SCALE ANALYSIS] AT LYS-627.
    Tissue: Mammary cancer.
  13. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Embryonic kidney.
  14. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT THR-85 AND SER-93, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  15. "MCM10 mediates RECQ4 association with MCM2-7 helicase complex during DNA replication."
    Xu X., Rochette P.J., Feyissa E.A., Su T.V., Liu Y.
    EMBO J. 28:3005-3014(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH RECQL4.
  16. "Physical interactions between Mcm10, DNA, and DNA polymerase alpha."
    Warren E.M., Huang H., Fanning E., Chazin W.J., Eichman B.F.
    J. Biol. Chem. 284:24662-24672(2009) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  17. "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 THR-85, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  18. "The RBBP6/ZBTB38/MCM10 axis regulates DNA replication and common fragile site stability."
    Miotto B., Chibi M., Xie P., Koundrioukoff S., Moolman-Smook H., Pugh D., Debatisse M., He F., Zhang L., Defossez P.A.
    Cell Rep. 7:575-587(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION.
  19. "Uncovering global SUMOylation signaling networks in a site-specific manner."
    Hendriks I.A., D'Souza R.C., Yang B., Verlaan-de Vries M., Mann M., Vertegaal A.C.
    Nat. Struct. Mol. Biol. 21:927-936(2014) [PubMed] [Europe PMC] [Abstract]
    Cited for: SUMOYLATION [LARGE SCALE ANALYSIS] AT LYS-762, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Entry informationi

Entry nameiMCM10_HUMAN
AccessioniPrimary (citable) accession number: Q7L590
Secondary accession number(s): A8K9I6
, B7ZKZ8, Q3MIR3, Q7LD55, Q96GX4, Q96NB6, Q9H0D7, Q9H3P9, Q9P177
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 20, 2007
Last sequence update: February 20, 2007
Last modified: June 8, 2016
This is version 113 of the entry and version 2 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

Complete proteome, Reference proteome

Documents

  1. Human chromosome 10
    Human chromosome 10: 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

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.