MCM7

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 key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Nucleotide bindingⁱ	381 – 388	8	ATPSequence analysis

Enzyme and pathway databases

Reactomeⁱ	R-HSA-176187. Activation of ATR in response to replication stress. R-HSA-176974. Unwinding of DNA. R-HSA-68867. Assembly of the pre-replicative complex. R-HSA-68949. Orc1 removal from chromatin. R-HSA-68962. Activation of the pre-replicative complex. R-HSA-69052. Switching of origins to a post-replicative state. R-HSA-69300. Removal of licensing factors from origins.
SIGNORⁱ	P33993.

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
Organismⁱ	Homo sapiens (Human)
Taxonomic identifierⁱ	9606 [NCBI]
Taxonomic lineageⁱ	cellular organisms › Eukaryota › Opisthokonta › Metazoa › Eumetazoa › Bilateria › Deuterostomia › Chordata › Craniata › Vertebrata › Gnathostomata › Teleostomi › Euteleostomi › Sarcopterygii › Dipnotetrapodomorpha › Tetrapoda › Amniota › Mammalia › Theria › Eutheria › Boreoeutheria › Euarchontoglires › Primates › Haplorrhini › Simiiformes › Catarrhini › Hominoidea › Hominidae › Homininae › Homo
Proteomesⁱ	UP000005640 Componentⁱ: Chromosome 7

Organism-specific databases

HGNCⁱ	HGNC:6950. MCM7.

HGNCⁱ

HGNC:6950. MCM7.

Subcellular locationⁱ

Nucleus By similarity

GO - Cellular componentⁱ

chromatin
Source: ProtInc
Traceable author statementⁱ
- 8798650
cytoplasm Source: HPA
cytosol Source: Ensembl
MCM complex
Source: UniProtKB
Inferred from direct assayⁱ
- 17296731
membrane
Source: UniProtKB
Inferred from direct assayⁱ
- 19946888
nuclear chromosome, telomeric region
Source: BHF-UCL
Inferred from direct assayⁱ
- 19135898
nucleoplasm Source: HPA

Complete GO annotation...

Keywords - Cellular componentⁱ

Nucleus

Pathology & Biotechⁱ

Organism-specific databases

PharmGKBⁱ	PA30697.

PharmGKBⁱ

PA30697.

Polymorphism and mutation databases

DMDMⁱ	20981696.

DMDMⁱ

20981696.

PTM / Processingⁱ

Molecule processing

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Initiator methionineⁱ			RemovedCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Chainⁱ	2 – 719	718	DNA replication licensing factor MCM7		PRO_0000194119	Add BLAST

Amino acid modifications

Feature key	Position(s)	Length	Description
Modified residueⁱ	2 – 2	1	N-acetylalanineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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, CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS], IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. 1 Publication Manual assertion based on experiment inⁱ Ref.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.
Modified residueⁱ	121 – 121	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.18 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.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]. Ref.25 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-314; SER-500 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	314 – 314	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.25 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-314; SER-500 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	365 – 365	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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].
Modified residueⁱ	500 – 500	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.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]. Ref.18 "A quantitative atlas of mitotic phosphorylation." Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E., Elledge S.J., Gygi S.P. Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121 AND SER-500, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]. Ref.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]. Ref.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]. Ref.25 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-314; SER-500 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
Modified residueⁱ	678 – 678	1	PhosphoserineCombined sources Manual assertion inferred from combination of experimental and computational evidenceⁱ Ref.25 "Toward a comprehensive characterization of a human cancer cell phosphoproteome." Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J., Mohammed S. J. Proteome Res. 12:260-271(2013) [PubMed] [Europe PMC] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-121; SER-314; SER-500 AND SER-678, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].

Post-translational modificationⁱ

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

Keywords - PTMⁱ

Acetylation, Glycoprotein, Phosphoprotein

Proteomic databases

EPDⁱ	P33993.
MaxQBⁱ	P33993.
PaxDbⁱ	P33993.
PeptideAtlasⁱ	P33993.
PRIDEⁱ	P33993.

PTM databases

iPTMnetⁱ	P33993.
PhosphoSiteⁱ	P33993.
SwissPalmⁱ	P33993.

Expressionⁱ

Gene expression databases

Bgeeⁱ	ENSG00000166508.
CleanExⁱ	HS_MCM2. HS_MCM7.
ExpressionAtlasⁱ	P33993. baseline and differential.
Genevisibleⁱ	P33993. HS.

Organism-specific databases

HPAⁱ	CAB002163. 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 (Probable). Interacts with the ATR-ATRIP complex and with RAD17. Interacts with TIPIN. Interacts with MCMBP. Interacts with ANKRD17.Curated7 Publications

Binary interactionsⁱ

With	Entry	#Exp.	IntAct	Notes
AK8	Q96MA6	3	EBI-355924,EBI-8466265
CCDC102B	A1A4H1	3	EBI-355924,EBI-10171570
CDC6	Q99741	2	EBI-355924,EBI-374862
CDKN1B	P46527	2	EBI-355924,EBI-519280
CDKN1C	P49918	2	EBI-355924,EBI-519256
E6	P03126	2	EBI-355924,EBI-1177242	From a different organism.
E6	P06462	2	EBI-355924,EBI-7069993	From a different organism.
E6	P06463	2	EBI-355924,EBI-1186926	From a different organism.
GOLGA2	Q08379	3	EBI-355924,EBI-618309
INTS6	Q9UL03	10	EBI-355924,EBI-1381827
KIFC3	Q9BVG8	3	EBI-355924,EBI-2125614
LYN	P07948	4	EBI-355924,EBI-79452
LYN	P07948-1	5	EBI-355924,EBI-6895930
MBIP	Q9NS73-5	3	EBI-355924,EBI-10182361
MCM2	P49736	21	EBI-355924,EBI-374819
MCM4	P33991	14	EBI-355924,EBI-374938
MCM5	P33992	8	EBI-355924,EBI-359410
MCM6	Q14566	6	EBI-355924,EBI-374900
MCMBP	Q9BTE3	21	EBI-355924,EBI-749378
MIPOL1	Q8TD10	3	EBI-355924,EBI-2548751
MYC	P01106	6	EBI-355924,EBI-447544
NAB2	Q15742	3	EBI-355924,EBI-8641936
PLK1	P53350	4	EBI-355924,EBI-476768
PNMA1	Q8ND90	3	EBI-355924,EBI-302345
SMC1A	Q14683	8	EBI-355924,EBI-80690
SP2	Q02086	3	EBI-355924,EBI-8651703
TRIM27	P14373	3	EBI-355924,EBI-719493
TRIM54	Q9BYV2	3	EBI-355924,EBI-2130429
UBB	P0CG47	2	EBI-355924,EBI-413034
UBQLN1	Q9UMX0-2	3	EBI-355924,EBI-10173939
USHBP1	Q8N6Y0	3	EBI-355924,EBI-739895

With

Entry

#Exp.

IntAct

Notes

AK8

Q96MA6

3

EBI-355924,EBI-8466265

CCDC102B

A1A4H1

3

EBI-355924,EBI-10171570

CDC6

Q99741

2

EBI-355924,EBI-374862

CDKN1B

P46527

2

EBI-355924,EBI-519280

CDKN1C

P49918

2

EBI-355924,EBI-519256

E6

P03126

2

EBI-355924,EBI-1177242

From a different organism.

E6

P06462

2

EBI-355924,EBI-7069993

From a different organism.

E6

P06463

2

EBI-355924,EBI-1186926

From a different organism.

GOLGA2

Q08379

3

EBI-355924,EBI-618309

INTS6

Q9UL03

10

EBI-355924,EBI-1381827

KIFC3

Q9BVG8

3

EBI-355924,EBI-2125614

LYN

P07948

4

EBI-355924,EBI-79452

LYN

P07948-1

5

EBI-355924,EBI-6895930

MBIP

Q9NS73-5

3

EBI-355924,EBI-10182361

MCM2

P49736

21

EBI-355924,EBI-374819

MCM4

P33991

14

EBI-355924,EBI-374938

MCM5

P33992

8

EBI-355924,EBI-359410

MCM6

Q14566

6

EBI-355924,EBI-374900

MCMBP

Q9BTE3

21

EBI-355924,EBI-749378

MIPOL1

Q8TD10

3

EBI-355924,EBI-2548751

MYC

P01106

6

EBI-355924,EBI-447544

NAB2

Q15742

3

EBI-355924,EBI-8641936

PLK1

P53350

4

EBI-355924,EBI-476768

PNMA1

Q8ND90

3

EBI-355924,EBI-302345

SMC1A

Q14683

8

EBI-355924,EBI-80690

SP2

Q02086

3

EBI-355924,EBI-8651703

TRIM27

P14373

3

EBI-355924,EBI-719493

TRIM54

Q9BYV2

3

EBI-355924,EBI-2130429

UBB

P0CG47

2

EBI-355924,EBI-413034

UBQLN1

Q9UMX0-2

3

EBI-355924,EBI-10173939

USHBP1

Q8N6Y0

3

EBI-355924,EBI-739895

Protein-protein interaction databases

BioGridⁱ	110344. 160 interactions.
DIPⁱ	DIP-27580N.
IntActⁱ	P33993. 176 interactions.
MINTⁱ	MINT-5005969.
STRINGⁱ	9606.ENSP00000307288.

Structureⁱ

3D structure databases

ProteinModelPortalⁱ	P33993.
SMRⁱ	P33993. Positions 11-640.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Family & Domainsⁱ

Domains and Repeats

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Domainⁱ	332 – 538	207	MCM			Add BLAST

Region

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Regionⁱ	521 – 564	44	Interaction with RAD17			Add BLAST
Regionⁱ	577 – 719	143	Interaction with ATRIP			Add BLAST

Motif

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Motifⁱ	513 – 516	4	Arginine finger

Sequence similaritiesⁱ

Belongs to the MCM family.Curated

Contains 1 MCM domain.Curated

Phylogenomic databases

eggNOGⁱ	KOG0482. Eukaryota. COG1241. LUCA.
GeneTreeⁱ	ENSGT00670000098113.
HOGENOMⁱ	HOG000224125.
HOVERGENⁱ	HBG000741.
InParanoidⁱ	P33993.
KOⁱ	K02210.
OMAⁱ	QEFYQDD.
OrthoDBⁱ	EOG091G02LB.
PhylomeDBⁱ	P33993.
TreeFamⁱ	TF300400.

Family and domain databases

Gene3Dⁱ	2.40.50.140. 2 hits. 3.40.50.300. 1 hit.
InterProⁱ	IPR003593. AAA+_ATPase. IPR031327. MCM. IPR008050. MCM7. IPR018525. MCM_CS. IPR001208. MCM_dom. IPR027925. MCM_N. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase. [Graphical view]
PANTHERⁱ	PTHR11630:SF26. PTHR11630:SF26. 2 hits.
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]

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 Add to basket Added to basket

Isoform 1 (identifier: P33993-1) [UniParc]FASTA Add 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]FASTA Add to basket

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

« 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 REELRQIADV IFATVRELVS GGRSVRFSEA 
       360        370        380 
EQRCVSRGFT PAQFQAALDE YEELNVWQVN ASRTRITFV

Note: No experimental confirmation available.

Show »

Length:389

Mass (Da):44,649

Checksum:ⁱCCAA37CB2DA54063

GO

Isoform 3 (identifier: P33993-3) [UniParc]FASTA Add to basket

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

« Hide

        10         20         30         40         50
MVVATYTCDQ CGAETYQPIQ SPTFMPLIMC PSQECQTNRS GGRLYLQTRG 
        60         70         80         90        100
SRFIKFQEMK MQEHSDQVPV GNIPRSITVL VEGENTRIAQ PGDHVSVTGI 
       110        120        130        140        150
FLPILRTGFR QVVQGLLSET YLEAHRIVKM NKSEDDESGA GELTREELRQ 
       160        170        180        190        200
IAEEDFYEKL AASIAPEIYG HEDVKKALLL LLVGGVDQSP RGMKIRGNIN 
       210        220        230        240        250
ICLMGDPGVA KSQLLSYIDR LAPRSQYTTG RGSSGVGLTA AVLRDSVSGE 
       260        270        280        290        300
LTLEGGALVL ADQGVCCIDE FDKMAEADRT AIHEVMEQQT ISIAKAGILT 
       310        320        330        340        350
TLNARCSILA AANPAYGRYN PRRSLEQNIQ LPAALLSRFD LLWLIQDRPD 
       360        370        380        390        400
RDNDLRLAQH ITYVHQHSRQ PPSQFEPLDM KLMRRYIAMC REKQPMVPES 
       410        420        430        440        450
LADYITAAYV EMRREAWASK DATYTSARTL LAILRLSTAL ARLRMVDVVE 
       460        470        480        490        500
KEDVNEAIRL MEMSKDSLLG DKGQTARTQR PADVIFATVR ELVSGGRSVR 
       510        520        530        540 
FSEAEQRCVS RGFTPAQFQA ALDEYEELNV WQVNASRTRI TFV

Show »

Length:543

Mass (Da):60,643

Checksum:ⁱ4CAA41B4F392F50C

GO

Experimental Info

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Sequence conflictⁱ	103 – 103	1	I → L in CAA52803 (PubMed:15489334).Curated

Natural variant

Feature key	Position(s)	Length	Description	Feature identifier
Natural variantⁱ	114 – 114	1	R → Q. Corresponds to variant rs2307348 [ dbSNP \| Ensembl ].	VAR_029243
Natural variantⁱ	144 – 144	1	N → S.1 Publication Manual assertion based on experiment inⁱ Ref.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. Corresponds to variant rs2070215 [ dbSNP \| Ensembl ].	VAR_013297
Natural variantⁱ	473 – 473	1	G → S. Corresponds to variant rs2307347 [ dbSNP \| Ensembl ].	VAR_014817

Alternative sequence

Feature key	Position(s)	Length	Description	Graphical view	Feature identifier	Actions
Alternative sequenceⁱ	1 – 176	176	Missing in isoform 3. 1 Publication Manual assertion based on opinion inⁱ Ref.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. Sugano S. Nat. Genet. 36:40-45(2004) [PubMed] [Europe PMC] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 3).		VSP_044310	Add BLAST
Alternative sequenceⁱ	329 – 658	330	Missing in isoform 2. 1 Publication Manual assertion based on opinion inⁱ Ref.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).		VSP_003205	Add 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.
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.

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.3. human. [P33993-1]

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 11-640.
ModBaseⁱ	Search...
MobiDBⁱ	Search...

Protein-protein interaction databases

BioGridⁱ	110344. 160 interactions.
DIPⁱ	DIP-27580N.
IntActⁱ	P33993. 176 interactions.
MINTⁱ	MINT-5005969.
STRINGⁱ	9606.ENSP00000307288.

PTM databases

iPTMnetⁱ	P33993.
PhosphoSiteⁱ	P33993.
SwissPalmⁱ	P33993.

Polymorphism and mutation databases

DMDMⁱ	20981696.

DMDMⁱ

20981696.

Proteomic databases

EPDⁱ	P33993.
MaxQBⁱ	P33993.
PaxDbⁱ	P33993.
PeptideAtlasⁱ	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.3. human. [P33993-1]

Organism-specific databases

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

Phylogenomic databases

eggNOGⁱ	KOG0482. Eukaryota. COG1241. LUCA.
GeneTreeⁱ	ENSGT00670000098113.
HOGENOMⁱ	HOG000224125.
HOVERGENⁱ	HBG000741.
InParanoidⁱ	P33993.
KOⁱ	K02210.
OMAⁱ	QEFYQDD.
OrthoDBⁱ	EOG091G02LB.
PhylomeDBⁱ	P33993.
TreeFamⁱ	TF300400.

Enzyme and pathway databases

Reactomeⁱ	R-HSA-176187. Activation of ATR in response to replication stress. R-HSA-176974. Unwinding of DNA. R-HSA-68867. Assembly of the pre-replicative complex. R-HSA-68949. Orc1 removal from chromatin. R-HSA-68962. Activation of the pre-replicative complex. R-HSA-69052. Switching of origins to a post-replicative state. R-HSA-69300. Removal of licensing factors from origins.
SIGNORⁱ	P33993.

Miscellaneous databases

ChiTaRSⁱ	MCM7. human.
GeneWikiⁱ	MCM7.
GenomeRNAiⁱ	4176.
PROⁱ	P33993.
SOURCEⁱ	Search...

Gene expression databases

Bgeeⁱ	ENSG00000166508.
CleanExⁱ	HS_MCM2. HS_MCM7.
ExpressionAtlasⁱ	P33993. baseline and differential.
Genevisibleⁱ	P33993. HS.

Family and domain databases

Gene3Dⁱ	2.40.50.140. 2 hits. 3.40.50.300. 1 hit.
InterProⁱ	IPR003593. AAA+_ATPase. IPR031327. MCM. IPR008050. MCM7. IPR018525. MCM_CS. IPR001208. MCM_dom. IPR027925. MCM_N. IPR012340. NA-bd_OB-fold. IPR027417. P-loop_NTPase. [Graphical view]
PANTHERⁱ	PTHR11630:SF26. PTHR11630:SF26. 2 hits.
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...

Entry informationⁱ

Entry nameⁱ

MCM7_HUMAN

Accessionⁱ

Primary (citable) accession number: P33993
Secondary accession number(s): A4D2A1

Q96GL1

Entry historyⁱ

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 15, 2002
Last modified:	September 7, 2016
This is version 178 of the entry and version 4 of the sequence. [Complete history]

Entry statusⁱ

Reviewed (UniProtKB/Swiss-Prot)

Annotation program

Chordata Protein Annotation Program

Disclaimer

Any 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

Human chromosome 7
Human chromosome 7: entries, gene names and cross-references to MIM
Human entries with polymorphisms or disease mutations
List of human entries with polymorphisms or disease mutations
Human polymorphisms and disease mutations
Index of human polymorphisms and disease mutations
MIM cross-references
Online Mendelian Inheritance in Man (MIM) cross-references in UniProtKB/Swiss-Prot
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.

UniProtKB

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UniRef

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Supporting data

UniProtKB - P33993 (MCM7_HUMAN)

UniProt

P33993 - MCM7_HUMAN

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DNA replication licensing factor MCM7

Select a section on the left to see content.

<p>Provides any useful information about the protein, mostly biological knowledge.</p><p><a href='../manual/function_section' target='_top'>More...</a></p>Functioni

Regions

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Biological processi

Enzyme and pathway databases

<p>Provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.</p><p><a href='../manual/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

Organism-specific databases

<p>Provides information on the location and the topology of the mature protein in the cell.</p><p><a href='../manual/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:</p><p><a href='../manual/gene_ontology' target='_top'>More...</a></p>GO - Cellular componenti

<p>Provides information on the disease(s) and phenotype(s) associated with a protein.</p><p><a href='../manual/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

Organism-specific databases

Polymorphism and mutation databases

<p>Describes post-translational modifications (PTMs) and/or processing events.</p><p><a href='../manual/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Amino acid modifications

Proteomic databases

PTM databases

<p>Provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.</p><p><a href='../manual/expression_section' target='_top'>More...</a></p>Expressioni

Gene expression databases

Organism-specific databases

<p>Provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.</p><p><a href='../manual/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

<p>Provides information on the tertiary and secondary structure of a protein.</p><p><a href='../manual/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

<p>Provides information on sequence similarities with other proteins and the domain(s) present in a protein.</p><p><a href='../manual/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Domains and Repeats

Region

Motif

<p>Provides information about the sequence similarity with other proteins.</p><p><a href='../manual/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Phylogenomic databases

Family and domain databases

<p>Displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including length and molecular weight.</p><p><a href='../manual/sequences_section' target='_top'>More...</a></p>Sequences (3)i

Experimental Info

Natural variant

Alternative sequence

Sequence databases

Genome annotation databases

<p>Is used to point to information related to entries and found in data collections other than UniProtKB.</p><p><a href='../manual/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

3D structure databases

Protein-protein interaction databases

PTM databases

Polymorphism and mutation databases

Proteomic databases

Protocols and materials databases

Genome annotation databases

Organism-specific databases

Phylogenomic databases

Enzyme and pathway databases

Miscellaneous databases

Gene expression databases

Family and domain databases

<p>Provides general information on the entry.</p><p><a href='../manual/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>Contains any relevant information that doesn’t fit in any other defined sections</p><p><a href='../manual/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Miscellaneous

Documents

Functionⁱ

GO - Molecular functionⁱ

GO - Biological processⁱ

Names & Taxonomyⁱ

Subcellular locationⁱ

GO - Cellular componentⁱ

Pathology & Biotechⁱ

PTM / Processingⁱ

Expressionⁱ

Interactionⁱ

Structureⁱ

Family & Domainsⁱ

Sequence similaritiesⁱ

Sequences (3)ⁱ

Cross-referencesⁱ

Entry informationⁱ

Miscellaneousⁱ