P33993 (MCM7_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
DNA replication licensing factor MCM7
EC=3.6.4.12

Alternative name(s):
CDC47 homolog
P1.1-MCM3

Gene names

Name:	MCM7
Synonyms:	CDC47, MCM2

Organism

Homo sapiens (Human) [Reference proteome]

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

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

Protein attributes

Sequence length	719 AA.
Sequence status	Complete.
Sequence processing	The displayed sequence is further processed into a mature form.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	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. Ref.11 Ref.12 Ref.13
Catalytic activity	ATP + H2O = ADP + phosphate.
Subunit structure	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. Ref.11 Ref.12 Ref.13 Ref.14 Ref.15 Ref.16
Subcellular location	Nucleus By similarity.
Post-translational modification	O-glycosylated (O-GlcNAcylated), in a cell cycle-dependent manner. Ref.22
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.
Sequence similarities	Belongs to the MCM family. Contains 1 MCM domain.

Ontologies

Keywords
Biological process	Cell cycle DNA replication
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing Polymorphism
Ligand	ATP-binding DNA-binding Nucleotide-binding
Molecular function	Helicase Hydrolase
PTM	Acetylation Glycoprotein Phosphoprotein
Technical term	Complete proteome Direct protein sequencing Reference proteome
Gene Ontology (GO)
Biological_process	ATP catabolic process Inferred from direct assay Ref.11. Source: GOC DNA replication initiation Inferred from electronic annotation. Source: InterPro DNA strand elongation involved in DNA replication Traceable author statement. Source: Reactome DNA unwinding involved in DNA replication Inferred from electronic annotation. Source: Ensembl G1/S transition of mitotic cell cycle Traceable author statement. Source: Reactome cell proliferation Inferred from electronic annotation. Source: Ensembl cellular response to DNA damage stimulus Inferred from mutant phenotype Ref.12. Source: UniProtKB cellular response to epidermal growth factor stimulus Inferred from electronic annotation. Source: Ensembl regulation of phosphorylation Inferred from mutant phenotype Ref.12. Source: UniProtKB response to drug Inferred from electronic annotation. Source: Ensembl
Cellular_component	MCM complex Inferred from direct assay Ref.16. Source: UniProtKB chromatin Traceable author statement PubMed 8798650. Source: ProtInc cytosol Inferred from electronic annotation. Source: Ensembl nucleoplasm Traceable author statement. Source: Reactome
Molecular_function	ATP binding Inferred from electronic annotation. Source: UniProtKB-KW DNA helicase activity Inferred from electronic annotation. Source: Ensembl single-stranded DNA binding Inferred from electronic annotation. Source: Ensembl
Complete GO annotation...

Binary interactions

With	Entry	#Exp.	IntAct	Notes
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.
INTS6	Q9UL03	10	EBI-355924,EBI-1381827
LYN	P07948	4	EBI-355924,EBI-79452
LYN	P07948-1	5	EBI-355924,EBI-6895930
MCM2	P49736	21	EBI-355924,EBI-374819
MCM4	P33991	13	EBI-355924,EBI-374938
MCM5	P33992	8	EBI-355924,EBI-359410
MCM6	Q14566	5	EBI-355924,EBI-374900
MCMBP	Q9BTE3	12	EBI-355924,EBI-749378
MYC	P01106	6	EBI-355924,EBI-447544
PLK1	P53350	4	EBI-355924,EBI-476768
SMC1A	Q14683	8	EBI-355924,EBI-80690
UBB	P0CG47	2	EBI-355924,EBI-413034

Alternative products

This entry describes 3 isoforms produced by alternative splicing. [Align] [Select]

Isoform 1 (identifier: P33993-1)

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.

Isoform 2 (identifier: P33993-2)

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

Note: No experimental confirmation available.

Isoform 3 (identifier: P33993-3)

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

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Initiator methionine	1	1	Removed Ref.7
	Chain	2 – 719	718	DNA replication licensing factor MCM7		PRO_0000194119
Regions
	Domain	332 – 538	207	MCM
	Nucleotide binding	381 – 388	8	ATP Potential
	Region	521 – 564	44	Interaction with RAD17
	Region	577 – 719	143	Interaction with ATRIP
	Motif	513 – 516	4	Arginine finger
Amino acid modifications
	Modified residue	2	1	N-acetylalanine Ref.7
	Modified residue	121	1	Phosphoserine Ref.17 Ref.18 Ref.20
	Modified residue	365	1	Phosphoserine Ref.20
	Modified residue	500	1	Phosphoserine Ref.17 Ref.18 Ref.19 Ref.20
Natural variations
	Alternative sequence	1 – 176	176	Missing in isoform 3.		VSP_044310
	Alternative sequence	329 – 658	330	Missing in isoform 2.		VSP_003205
	Natural variant	114	1	R → Q. Corresponds to variant rs2307348 [ dbSNP | Ensembl ].		VAR_029243
	Natural variant	144	1	N → S. Ref.1 Corresponds to variant rs2070215 [ dbSNP | Ensembl ].		VAR_013297
	Natural variant	473	1	G → S. Corresponds to variant rs2307347 [ dbSNP | Ensembl ].		VAR_014817
Experimental info
	Sequence conflict	103	1	I → L in CAA52803. Ref.6

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified May 15, 2002. Version 4. Checksum: 330A1DEFAEFBFB88	FASTA	719	81,308
	10 20 30 40 50 60 MALKDYALEK EKVKKFLQEF YQDDELGKKQ FKYGNQLVRL AHREQVALYV DLDDVAEDDP 70 80 90 100 110 120 ELVDSICENA RRYAKLFADA VQELLPQYKE REVVNKDVLD VYIEHRLMME QRSRDPGMVR 130 140 150 160 170 180 SPQNQYPAEL MRRFELYFQG PSSNKPRVIR EVRADSVGKL VTVRGIVTRV SEVKPKMVVA 190 200 210 220 230 240 TYTCDQCGAE TYQPIQSPTF MPLIMCPSQE CQTNRSGGRL YLQTRGSRFI KFQEMKMQEH 250 260 270 280 290 300 SDQVPVGNIP RSITVLVEGE NTRIAQPGDH VSVTGIFLPI LRTGFRQVVQ GLLSETYLEA 310 320 330 340 350 360 HRIVKMNKSE DDESGAGELT REELRQIAEE DFYEKLAASI APEIYGHEDV KKALLLLLVG 370 380 390 400 410 420 GVDQSPRGMK IRGNINICLM GDPGVAKSQL LSYIDRLAPR SQYTTGRGSS GVGLTAAVLR 430 440 450 460 470 480 DSVSGELTLE GGALVLADQG VCCIDEFDKM AEADRTAIHE VMEQQTISIA KAGILTTLNA 490 500 510 520 530 540 RCSILAAANP AYGRYNPRRS LEQNIQLPAA LLSRFDLLWL IQDRPDRDND LRLAQHITYV 550 560 570 580 590 600 HQHSRQPPSQ FEPLDMKLMR RYIAMCREKQ PMVPESLADY ITAAYVEMRR EAWASKDATY 610 620 630 640 650 660 TSARTLLAIL RLSTALARLR MVDVVEKEDV NEAIRLMEMS KDSLLGDKGQ TARTQRPADV 670 680 690 700 710 IFATVRELVS GGRSVRFSEA EQRCVSRGFT PAQFQAALDE YEELNVWQVN ASRTRITFV
	Isoform 2 [UniParc]. Checksum: CCAA37CB2DA54063	FASTA	389	44,649
	10 20 30 40 50 60 MALKDYALEK EKVKKFLQEF YQDDELGKKQ FKYGNQLVRL AHREQVALYV DLDDVAEDDP 70 80 90 100 110 120 ELVDSICENA RRYAKLFADA VQELLPQYKE REVVNKDVLD VYIEHRLMME QRSRDPGMVR 130 140 150 160 170 180 SPQNQYPAEL MRRFELYFQG PSSNKPRVIR EVRADSVGKL VTVRGIVTRV SEVKPKMVVA 190 200 210 220 230 240 TYTCDQCGAE TYQPIQSPTF MPLIMCPSQE CQTNRSGGRL YLQTRGSRFI KFQEMKMQEH 250 260 270 280 290 300 SDQVPVGNIP RSITVLVEGE NTRIAQPGDH VSVTGIFLPI LRTGFRQVVQ GLLSETYLEA 310 320 330 340 350 360 HRIVKMNKSE DDESGAGELT REELRQIADV IFATVRELVS GGRSVRFSEA EQRCVSRGFT 370 380 PAQFQAALDE YEELNVWQVN ASRTRITFV
	Isoform 3 [UniParc]. Checksum: 4CAA41B4F392F50C	FASTA	543	60,643
	10 20 30 40 50 60 MVVATYTCDQ CGAETYQPIQ SPTFMPLIMC PSQECQTNRS GGRLYLQTRG SRFIKFQEMK 70 80 90 100 110 120 MQEHSDQVPV GNIPRSITVL VEGENTRIAQ PGDHVSVTGI FLPILRTGFR QVVQGLLSET 130 140 150 160 170 180 YLEAHRIVKM NKSEDDESGA GELTREELRQ IAEEDFYEKL AASIAPEIYG HEDVKKALLL 190 200 210 220 230 240 LLVGGVDQSP RGMKIRGNIN ICLMGDPGVA KSQLLSYIDR LAPRSQYTTG RGSSGVGLTA 250 260 270 280 290 300 AVLRDSVSGE LTLEGGALVL ADQGVCCIDE FDKMAEADRT AIHEVMEQQT ISIAKAGILT 310 320 330 340 350 360 TLNARCSILA AANPAYGRYN PRRSLEQNIQ LPAALLSRFD LLWLIQDRPD RDNDLRLAQH 370 380 390 400 410 420 ITYVHQHSRQ PPSQFEPLDM KLMRRYIAMC REKQPMVPES LADYITAAYV EMRREAWASK 430 440 450 460 470 480 DATYTSARTL LAILRLSTAL ARLRMVDVVE KEDVNEAIRL MEMSKDSLLG DKGQTARTQR 490 500 510 520 530 540 PADVIFATVR ELVSGGRSVR FSEAEQRCVS RGFTPAQFQA ALDEYEELNV WQVNASRTRI TFV

References

	« Hide 'large scale' referencesShow 'large scale' references »
[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]	Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H., Dew I., Miller J.R., Flanigan M.J., Edwards N.J., Bolanos R., Fasulo D., Halldorsson B.V., Hannenhalli S., Turner R. , Yooseph S., Lu F., Nusskern D.R., Shue B.C., Zheng X.H., Zhong F., Delcher A.L., Huson D.H., Kravitz S.A., Mouchard L., Reinert K., Remington K.A., Clark A.G., Waterman M.S., Eichler E.E., Adams M.D., Hunkapiller M.W., Myers E.W., Venter J.C. Submitted (SEP-2005) to the EMBL/GenBank/DDBJ databases 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, 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: MASS SPECTROMETRY, HELICASE ACTIVITY OF THE MCM2-3 COMPLEX, INTERACTION WITH MCMBP, IDENTIFICATION IN THE MCM2-7 COMPLEX.
[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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. 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, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[21]	"Initial characterization of the human central proteome." Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J. BMC Syst. Biol. 5:17-17(2011) [PubMed] [Europe PMC] [Abstract] 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.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	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.
PIR	S70583.
RefSeq	NP_001265524.1. NM_001278595.1. NP_005907.3. NM_005916.4. NP_877577.1. NM_182776.2. XP_005250406.1. XM_005250349.1.
UniGene	Hs.438720.
3D structure databases
ProteinModelPortal	P33993.
SMR	P33993. Positions 138-275.
ModBase	Search...
MobiDB	Search...
Protein-protein interaction databases
BioGrid	110344. 99 interactions.
DIP	DIP-27580N.
IntAct	P33993. 136 interactions.
MINT	MINT-5005969.
STRING	9606.ENSP00000307288.
Chemistry
DrugBank	DB01076. Atorvastatin.
PTM databases
PhosphoSite	P33993.
Polymorphism databases
DMDM	20981696.
Proteomic databases
PaxDb	P33993.
PRIDE	P33993.
Protocols and materials databases
DNASU	4176.
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000303887; ENSP00000307288; ENSG00000166508. ENST00000343023; ENSP00000344006; ENSG00000166508. ENST00000354230; ENSP00000346171; ENSG00000166508.
GeneID	4176.
KEGG	hsa:4176.
UCSC	uc003usv.1. human.
Organism-specific databases
CTD	4176.
GeneCards	GC07M099690.
HGNC	HGNC:6950. MCM7.
HPA	CAB002163. CAB016312. HPA003898.
MIM	600592. gene.
neXtProt	NX_P33993.
PharmGKB	PA30697.
GenAtlas	Search...
Phylogenomic databases
eggNOG	COG1241.
HOGENOM	HOG000224125.
HOVERGEN	HBG000741.
InParanoid	P33993.
KO	K02210.
OMA	DINICLM.
OrthoDB	EOG7N0C42.
PhylomeDB	P33993.
TreeFam	TF300400.
Enzyme and pathway databases
Reactome	REACT_115566. Cell Cycle. REACT_21300. Mitotic M-M/G1 phases. REACT_383. DNA Replication.
Gene expression databases
ArrayExpress	P33993.
Bgee	P33993.
CleanEx	HS_MCM2. HS_MCM7.
Genevestigator	P33993.
Family and domain databases
Gene3D	2.40.50.140. 2 hits.
InterPro	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]
PANTHER	PTHR11630:SF26. PTHR11630:SF26. 1 hit.
Pfam	PF00493. MCM. 1 hit. PF14551. MCM_N. 1 hit. [Graphical view]
PRINTS	PR01657. MCMFAMILY. PR01663. MCMPROTEIN7.
SMART	SM00382. AAA. 1 hit. SM00350. MCM. 1 hit. [Graphical view]
SUPFAM	SSF50249. SSF50249. 2 hits. SSF52540. SSF52540. 1 hit.
PROSITE	PS00847. MCM_1. 1 hit. PS50051. MCM_2. 1 hit. [Graphical view]
ProtoNet	Search...
Other
ChiTaRS	MCM7. human.
GeneWiki	MCM7.
GenomeRNAi	4176.
NextBio	16450.
PRO	P33993.
SOURCE	Search...

Entry information

Entry name

MCM7_HUMAN

Accession

Primary (citable) accession number: P33993
Secondary accession number(s): A4D2A1 , A4D2A2, E9PGN9, Q15076, Q96D34, Q96GL1

Entry history

Integrated into UniProtKB/Swiss-Prot:	February 1, 1994
Last sequence update:	May 15, 2002
Last modified:	February 19, 2014
This is version 151 of the entry and version 4 of the sequence. [Complete history]

Entry status

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.