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P33993

- MCM7_HUMAN

UniProt

P33993 - MCM7_HUMAN

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Protein

DNA replication licensing factor MCM7

Gene

MCM7

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

Display
All None

  • Function
  • Names & Taxonomy
  • Subcellular locationSubcell. location
  • Pathology & BiotechPathol./Biotech
  • PTM / Processing
  • Expression
  • Interaction
  • Structure
  • Family & Domains
  • Sequences (3)
  • Cross-references
  • Publications
  • Entry information
  • Miscellaneous
  • Similar proteins
Top

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 S-phase checkpoint activation upon UV-induced damage.3 Publications

Catalytic activityi

ATP + H2O = ADP + phosphate.

Regions

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Nucleotide bindingi381 – 3888ATPSequence Analysis

GO - Molecular functioni

  1. ATP binding Source: UniProtKB-KW
  2. DNA helicase activity Source: Ensembl
  3. single-stranded DNA binding Source: Ensembl

GO - Biological processi

  1. cell proliferation Source: Ensembl
  2. cellular response to DNA damage stimulus Source: UniProtKB
  3. cellular response to epidermal growth factor stimulus Source: Ensembl
  4. DNA replication Source: Reactome
  5. DNA replication initiation Source: InterPro
  6. DNA strand elongation involved in DNA replication Source: Reactome
  7. DNA unwinding involved in DNA replication Source: Ensembl
  8. G1/S transition of mitotic cell cycle Source: Reactome
  9. mitotic cell cycle Source: Reactome
  10. regulation of phosphorylation Source: UniProtKB
  11. response to drug Source: Ensembl
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 MCM7 (EC:3.6.4.12)
Alternative name(s):
CDC47 homolog
P1.1-MCM3
Gene namesi
Name:MCM7
Synonyms:CDC47, MCM2
OrganismiHomo sapiens (Human)
Taxonomic identifieri9606 [NCBI]
Taxonomic lineageiEukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo
ProteomesiUP000005640: Chromosome 7

Organism-specific databases

HGNCiHGNC:6950. MCM7.

Subcellular locationi

Nucleus By similarity

GO - Cellular componenti

  1. chromatin Source: ProtInc
  2. cytoplasm Source: HPA
  3. cytosol Source: Ensembl
  4. MCM complex Source: UniProtKB
  5. membrane Source: UniProtKB
  6. nucleoplasm Source: Reactome
  7. nucleus Source: HPA
Complete GO annotation...

Keywords - Cellular componenti

Nucleus

Pathology & Biotechi

Organism-specific databases

PharmGKBiPA30697.

PTM / Processingi

Molecule processing

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Initiator methioninei1 – 11Removed2 Publications
Chaini2 – 719718DNA replication licensing factor MCM7PRO_0000194119Add
BLAST

Amino acid modifications

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Modified residuei2 – 21N-acetylalanine2 Publications
Modified residuei121 – 1211Phosphoserine3 Publications
Modified residuei365 – 3651Phosphoserine1 Publication
Modified residuei500 – 5001Phosphoserine4 Publications

Post-translational modificationi

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

Keywords - PTMi

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

MaxQBiP33993.
PaxDbiP33993.
PRIDEiP33993.

PTM databases

PhosphoSiteiP33993.

Expressioni

Gene expression databases

BgeeiP33993.
CleanExiHS_MCM2.
HS_MCM7.
ExpressionAtlasiP33993. baseline and differential.
GenevestigatoriP33993.

Organism-specific databases

HPAiCAB002163.
CAB016312.
HPA003898.

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). Interacts with the ATR-ATRIP complex and with RAD17. Interacts with TIPIN. Interacts with MCMBP.6 Publications

Binary interactionsi

WithEntry#Exp.IntActNotes
CDC6Q997412EBI-355924,EBI-374862
CDKN1BP465272EBI-355924,EBI-519280
CDKN1CP499182EBI-355924,EBI-519256
E6P031262EBI-355924,EBI-1177242From a different organism.
E6P064622EBI-355924,EBI-7069993From a different organism.
E6P064632EBI-355924,EBI-1186926From a different organism.
INTS6Q9UL0310EBI-355924,EBI-1381827
LYNP079484EBI-355924,EBI-79452
LYNP07948-15EBI-355924,EBI-6895930
MCM2P4973621EBI-355924,EBI-374819
MCM4P3399114EBI-355924,EBI-374938
MCM5P339928EBI-355924,EBI-359410
MCM6Q145665EBI-355924,EBI-374900
MCMBPQ9BTE316EBI-355924,EBI-749378
MYCP011066EBI-355924,EBI-447544
PLK1P533504EBI-355924,EBI-476768
SMC1AQ146838EBI-355924,EBI-80690
UBBP0CG472EBI-355924,EBI-413034

Protein-protein interaction databases

BioGridi110344. 125 interactions.
DIPiDIP-27580N.
IntActiP33993. 146 interactions.
MINTiMINT-5005969.
STRINGi9606.ENSP00000307288.

Structurei

3D structure databases

ProteinModelPortaliP33993.
SMRiP33993. Positions 11-281.
ModBaseiSearch...
MobiDBiSearch...

Family & Domainsi

Domains and Repeats

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Domaini332 – 538207MCMAdd
BLAST

Region

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Regioni521 – 56444Interaction with RAD17Add
BLAST
Regioni577 – 719143Interaction with ATRIPAdd
BLAST

Motif

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Motifi513 – 5164Arginine finger

Sequence similaritiesi

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

Phylogenomic databases

eggNOGiCOG1241.
GeneTreeiENSGT00670000098113.
HOGENOMiHOG000224125.
HOVERGENiHBG000741.
InParanoidiP33993.
KOiK02210.
OMAiPTPYTGF.
OrthoDBiEOG7N0C42.
PhylomeDBiP33993.
TreeFamiTF300400.

Family and domain databases

Gene3Di2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProiIPR003593. AAA+_ATPase.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view]
PANTHERiPTHR11630:SF26. PTHR11630:SF26. 1 hit.
PfamiPF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view]
PRINTSiPR01657. MCMFAMILY.
PR01663. MCMPROTEIN7.
SMARTiSM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view]
SUPFAMiSSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEiPS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view]

Sequences (3)i

Sequence statusi: Complete.

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

This entry describes 3 isoformsi produced by alternative splicing. Align

Isoform 1 (identifier: P33993-1) [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
MALKDYALEK EKVKKFLQEF YQDDELGKKQ FKYGNQLVRL AHREQVALYV 
        60         70         80         90        100
DLDDVAEDDP ELVDSICENA RRYAKLFADA VQELLPQYKE REVVNKDVLD 
       110        120        130        140        150
VYIEHRLMME QRSRDPGMVR SPQNQYPAEL MRRFELYFQG PSSNKPRVIR 
       160        170        180        190        200
EVRADSVGKL VTVRGIVTRV SEVKPKMVVA TYTCDQCGAE TYQPIQSPTF 
       210        220        230        240        250
MPLIMCPSQE CQTNRSGGRL YLQTRGSRFI KFQEMKMQEH SDQVPVGNIP 
       260        270        280        290        300
RSITVLVEGE NTRIAQPGDH VSVTGIFLPI LRTGFRQVVQ GLLSETYLEA 
       310        320        330        340        350
HRIVKMNKSE DDESGAGELT REELRQIAEE DFYEKLAASI APEIYGHEDV 
       360        370        380        390        400
KKALLLLLVG GVDQSPRGMK IRGNINICLM GDPGVAKSQL LSYIDRLAPR 
       410        420        430        440        450
SQYTTGRGSS GVGLTAAVLR DSVSGELTLE GGALVLADQG VCCIDEFDKM 
       460        470        480        490        500
AEADRTAIHE VMEQQTISIA KAGILTTLNA RCSILAAANP AYGRYNPRRS 
       510        520        530        540        550
LEQNIQLPAA LLSRFDLLWL IQDRPDRDND LRLAQHITYV HQHSRQPPSQ 
       560        570        580        590        600
FEPLDMKLMR RYIAMCREKQ PMVPESLADY ITAAYVEMRR EAWASKDATY 
       610        620        630        640        650
TSARTLLAIL RLSTALARLR MVDVVEKEDV NEAIRLMEMS KDSLLGDKGQ 
       660        670        680        690        700
TARTQRPADV IFATVRELVS GGRSVRFSEA EQRCVSRGFT PAQFQAALDE 
       710 
YEELNVWQVN ASRTRITFV
Length:719
Mass (Da):81,308
Last modified:May 15, 2002 - v4
Checksum:i330A1DEFAEFBFB88
GO
Isoform 2 (identifier: P33993-2) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     329-658: Missing.

Note: No experimental confirmation available.

Show »
Length:389
Mass (Da):44,649
Checksum:iCCAA37CB2DA54063
GO
Isoform 3 (identifier: P33993-3) [UniParc]FASTAAdd to Basket

The sequence of this isoform differs from the canonical sequence as follows:
     1-176: Missing.

Show »
Length:543
Mass (Da):60,643
Checksum:i4CAA41B4F392F50C
GO

Experimental Info

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Sequence conflicti103 – 1031I → L in CAA52803. (PubMed:15489334)Curated

Natural variant

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Natural varianti114 – 1141R → Q.
Corresponds to variant rs2307348 [ dbSNP | Ensembl ].		VAR_029243
Natural varianti144 – 1441N → S.1 Publication
Corresponds to variant rs2070215 [ dbSNP | Ensembl ].		VAR_013297
Natural varianti473 – 4731G → S.
Corresponds to variant rs2307347 [ dbSNP | Ensembl ].		VAR_014817

Alternative sequence

Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
Alternative sequencei1 – 176176Missing in isoform 3. 1 PublicationVSP_044310Add
BLAST
Alternative sequencei329 – 658330Missing in isoform 2. 1 PublicationVSP_003205Add
BLAST

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
D55716 mRNA. Translation: BAA09534.1.
AK055379 mRNA. Translation: BAG51508.1.
AC073842 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23855.1.
CH236956 Genomic DNA. Translation: EAL23856.1.
CH471091 Genomic DNA. Translation: EAW76598.1.
CH471091 Genomic DNA. Translation: EAW76599.1.
BC009398 mRNA. Translation: AAH09398.1.
BC013375 mRNA. Translation: AAH13375.1.
X74796 mRNA. Translation: CAA52803.1.
D28480 mRNA. Translation: BAA05839.1.
CCDSiCCDS5683.1. [P33993-1]
CCDS5684.1. [P33993-3]
PIRiS70583.
RefSeqiNP_001265524.1. NM_001278595.1. [P33993-3]
NP_005907.3. NM_005916.4. [P33993-1]
NP_877577.1. NM_182776.2. [P33993-3]
UniGeneiHs.438720.

Genome annotation databases

EnsembliENST00000303887; ENSP00000307288; ENSG00000166508. [P33993-1]
ENST00000343023; ENSP00000344006; ENSG00000166508. [P33993-2]
ENST00000354230; ENSP00000346171; ENSG00000166508. [P33993-3]
ENST00000621318; ENSP00000483795; ENSG00000166508. [P33993-3]
GeneIDi4176.
KEGGihsa:4176.
UCSCiuc003usv.1. human. [P33993-1]

Polymorphism databases

DMDMi20981696.

Keywords - Coding sequence diversityi

Alternative splicing, Polymorphism

Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
 D55716 mRNA. Translation: BAA09534.1 .
AK055379 mRNA. Translation: BAG51508.1 .
AC073842 Genomic DNA. No translation available.
CH236956 Genomic DNA. Translation: EAL23855.1 .
CH236956 Genomic DNA. Translation: EAL23856.1 .
CH471091 Genomic DNA. Translation: EAW76598.1 .
CH471091 Genomic DNA. Translation: EAW76599.1 .
BC009398 mRNA. Translation: AAH09398.1 .
BC013375 mRNA. Translation: AAH13375.1 .
X74796 mRNA. Translation: CAA52803.1 .
D28480 mRNA. Translation: BAA05839.1 .
CCDSi CCDS5683.1. [P33993-1 ]
CCDS5684.1. [P33993-3 ]
PIRi S70583.
RefSeqi NP_001265524.1. NM_001278595.1. [P33993-3 ]
NP_005907.3. NM_005916.4. [P33993-1 ]
NP_877577.1. NM_182776.2. [P33993-3 ]
UniGenei Hs.438720.

3D structure databases

ProteinModelPortali P33993.
SMRi P33993. Positions 11-281.
ModBasei Search...
MobiDBi Search...

Protein-protein interaction databases

BioGridi 110344. 125 interactions.
DIPi DIP-27580N.
IntActi P33993. 146 interactions.
MINTi MINT-5005969.
STRINGi 9606.ENSP00000307288.

PTM databases

PhosphoSitei P33993.

Polymorphism databases

DMDMi 20981696.

Proteomic databases

MaxQBi P33993.
PaxDbi P33993.
PRIDEi P33993.

Protocols and materials databases

DNASUi 4176.
Structural Biology Knowledgebase Search...

Genome annotation databases

Ensembli ENST00000303887 ; ENSP00000307288 ; ENSG00000166508 . [P33993-1 ]
ENST00000343023 ; ENSP00000344006 ; ENSG00000166508 . [P33993-2 ]
ENST00000354230 ; ENSP00000346171 ; ENSG00000166508 . [P33993-3 ]
ENST00000621318 ; ENSP00000483795 ; ENSG00000166508 . [P33993-3 ]
GeneIDi 4176.
KEGGi hsa:4176.
UCSCi uc003usv.1. human. [P33993-1 ]

Organism-specific databases

CTDi 4176.
GeneCardsi GC07M099690.
HGNCi HGNC:6950. MCM7.
HPAi CAB002163.
CAB016312.
HPA003898.
MIMi 600592. gene.
neXtProti NX_P33993.
PharmGKBi PA30697.
GenAtlasi Search...

Phylogenomic databases

eggNOGi COG1241.
GeneTreei ENSGT00670000098113.
HOGENOMi HOG000224125.
HOVERGENi HBG000741.
InParanoidi P33993.
KOi K02210.
OMAi PTPYTGF.
OrthoDBi EOG7N0C42.
PhylomeDBi P33993.
TreeFami TF300400.

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 MCM7. human.
GeneWikii MCM7.
GenomeRNAii 4176.
NextBioi 16450.
PROi P33993.
SOURCEi Search...

Gene expression databases

Bgeei P33993.
CleanExi HS_MCM2.
HS_MCM7.
ExpressionAtlasi P33993. baseline and differential.
Genevestigatori P33993.

Family and domain databases

Gene3Di 2.40.50.140. 2 hits.
3.40.50.300. 1 hit.
InterProi IPR003593. AAA+_ATPase.
IPR008050. MCM7.
IPR018525. MCM_CS.
IPR001208. MCM_DNA-dep_ATPase.
IPR027925. MCM_N.
IPR012340. NA-bd_OB-fold.
IPR027417. P-loop_NTPase.
[Graphical view ]
PANTHERi PTHR11630:SF26. PTHR11630:SF26. 1 hit.
Pfami PF00493. MCM. 1 hit.
PF14551. MCM_N. 1 hit.
[Graphical view ]
PRINTSi PR01657. MCMFAMILY.
PR01663. MCMPROTEIN7.
SMARTi SM00382. AAA. 1 hit.
SM00350. MCM. 1 hit.
[Graphical view ]
SUPFAMi SSF50249. SSF50249. 2 hits.
SSF52540. SSF52540. 1 hit.
PROSITEi PS00847. MCM_1. 1 hit.
PS50051. MCM_2. 1 hit.
[Graphical view ]
ProtoNeti Search...

Publicationsi

« Hide 'large scale' publications
  1. "hCDC47, a human member of the MCM family. Dissociation of the nucleus-bound form during S phase."
    Fujita M., Kiyono T., Hayashi Y., Ishibashi M.
    J. Biol. Chem. 271:4349-4354(1996) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] (ISOFORM 1), VARIANT SER-144.
  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] (ISOFORM 3).
    Tissue: Brain.
  3. "Human chromosome 7: DNA sequence and biology."
    Scherer S.W., Cheung J., MacDonald J.R., Osborne L.R., Nakabayashi K., Herbrick J.-A., Carson A.R., Parker-Katiraee L., Skaug J., Khaja R., Zhang J., Hudek A.K., Li M., Haddad M., Duggan G.E., Fernandez B.A., Kanematsu E., Gentles S.
    , Christopoulos C.C., Choufani S., Kwasnicka D., Zheng X.H., Lai Z., Nusskern D.R., Zhang Q., Gu Z., Lu F., Zeesman S., Nowaczyk M.J., Teshima I., Chitayat D., Shuman C., Weksberg R., Zackai E.H., Grebe T.A., Cox S.R., Kirkpatrick S.J., Rahman N., Friedman J.M., Heng H.H.Q., Pelicci P.G., Lo-Coco F., Belloni E., Shaffer L.G., Pober B., Morton C.C., Gusella J.F., Bruns G.A.P., Korf B.R., Quade B.J., Ligon A.H., Ferguson H., Higgins A.W., Leach N.T., Herrick S.R., Lemyre E., Farra C.G., Kim H.-G., Summers A.M., Gripp K.W., Roberts W., Szatmari P., Winsor E.J.T., Grzeschik K.-H., Teebi A., Minassian B.A., Kere J., Armengol L., Pujana M.A., Estivill X., Wilson M.D., Koop B.F., Tosi S., Moore G.E., Boright A.P., Zlotorynski E., Kerem B., Kroisel P.M., Petek E., Oscier D.G., Mould S.J., Doehner H., Doehner K., Rommens J.M., Vincent J.B., Venter J.C., Li P.W., Mural R.J., Adams M.D., Tsui L.-C.
    Science 300:767-772(2003) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
  4. "The DNA sequence of human chromosome 7."
    Hillier L.W., Fulton R.S., Fulton L.A., Graves T.A., Pepin K.H., Wagner-McPherson C., Layman D., Maas J., Jaeger S., Walker R., Wylie K., Sekhon M., Becker M.C., O'Laughlin M.D., Schaller M.E., Fewell G.A., Delehaunty K.D., Miner T.L.
    , Nash W.E., Cordes M., Du H., Sun H., Edwards J., Bradshaw-Cordum H., Ali J., Andrews S., Isak A., Vanbrunt A., Nguyen C., Du F., Lamar B., Courtney L., Kalicki J., Ozersky P., Bielicki L., Scott K., Holmes A., Harkins R., Harris A., Strong C.M., Hou S., Tomlinson C., Dauphin-Kohlberg S., Kozlowicz-Reilly A., Leonard S., Rohlfing T., Rock S.M., Tin-Wollam A.-M., Abbott A., Minx P., Maupin R., Strowmatt C., Latreille P., Miller N., Johnson D., Murray J., Woessner J.P., Wendl M.C., Yang S.-P., Schultz B.R., Wallis J.W., Spieth J., Bieri T.A., Nelson J.O., Berkowicz N., Wohldmann P.E., Cook L.L., Hickenbotham M.T., Eldred J., Williams D., Bedell J.A., Mardis E.R., Clifton S.W., Chissoe S.L., Marra M.A., Raymond C., Haugen E., Gillett W., Zhou Y., James R., Phelps K., Iadanoto S., Bubb K., Simms E., Levy R., Clendenning J., Kaul R., Kent W.J., Furey T.S., Baertsch R.A., Brent M.R., Keibler E., Flicek P., Bork P., Suyama M., Bailey J.A., Portnoy M.E., Torrents D., Chinwalla A.T., Gish W.R., Eddy S.R., McPherson J.D., Olson M.V., Eichler E.E., Green E.D., Waterston R.H., Wilson R.K.
    Nature 424:157-164(2003) [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).
    Tissue: Brain and Lung.
  7. Bienvenut W.V., von Kriegsheim A., Kolch W.
    Submitted (DEC-2008) to UniProtKB
    Cited for: PROTEIN SEQUENCE OF 2-12; 16-29; 33-39; 76-106; 134-147; 252-282; 472-481; 500-514 AND 605-611, CLEAVAGE OF INITIATOR METHIONINE, ACETYLATION AT ALA-2, IDENTIFICATION BY MASS SPECTROMETRY.
    Tissue: Chronic myeloid leukemia cell.
  8. Hu B.
    Submitted (FEB-1995) to the EMBL/GenBank/DDBJ databases
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 103-719.
  9. "Isolation and mapping of a human gene (MCM2) encoding a product homologous to yeast proteins involved in DNA replication."
    Nakatsuru S., Sudo K., Nakamura Y.
    Cytogenet. Cell Genet. 68:226-230(1995) [PubMed] [Europe PMC] [Abstract]
    Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 177-719.
    Tissue: Lung.
  10. "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] OF 261-557.
    Tissue: Cervix.
  11. "A DNA helicase activity is associated with an MCM4, -6, and -7 protein complex."
    Ishimi Y.
    J. Biol. Chem. 272:24508-24513(1997) [PubMed] [Europe PMC] [Abstract]
    Cited for: IDENTIFICATION IN THE MCM2-7 COMPLEX, FUNCTION.
  12. "Interaction between human MCM7 and Rad17 proteins is required for replication checkpoint signaling."
    Tsao C.-C., Geisen C., Abraham R.T.
    EMBO J. 23:4660-4669(2004) [PubMed] [Europe PMC] [Abstract]
    Cited for: FUNCTION, INTERACTION WITH ATR; ATRIP AND RAD17.
  13. "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: INTERACTION WITH ATRIP, FUNCTION.
  14. "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.
  15. "Tipin and Timeless form a mutually protective complex required for genotoxic stress resistance and checkpoint function."
    Chou D.M., Elledge S.J.
    Proc. Natl. Acad. Sci. U.S.A. 103:18143-18147(2006) [PubMed] [Europe PMC] [Abstract]
    Cited for: INTERACTION WITH TIPIN.
  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: HELICASE ACTIVITY OF THE MCM2-3 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX, 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 SER-121 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  18. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  19. "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-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Leukemic T-cell.
  20. "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-121; SER-365 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
    Tissue: Cervix carcinoma.
  21. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
  22. "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.
  23. "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].
+Additional computationally mapped references.

Entry informationi

Entry nameiMCM7_HUMAN
AccessioniPrimary (citable) accession number: P33993
Secondary accession number(s): A4D2A1
, A4D2A2, E9PGN9, Q15076, Q96D34, Q96GL1
Entry historyi
Integrated into UniProtKB/Swiss-Prot: February 1, 1994
Last sequence update: May 15, 2002
Last modified: January 7, 2015
This is version 160 of the entry and version 4 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. 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.

Keywords - Technical termi

Complete proteome, Direct protein sequencing, Reference proteome

Documents

  1. Human chromosome 7
    Human chromosome 7: 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

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 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.
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