Q9BTE3 (MCMBP_HUMAN) Reviewed, UniProtKB/Swiss-Prot

Names and origin

Protein names

Recommended name:
Mini-chromosome maintenance complex-binding protein
Short name=MCM-BP
Short name=MCM-binding protein

Gene names

Name:	MCMBP
Synonyms:	C10orf119

Organism

Homo sapiens (Human)

Taxonomic identifier

9606 [NCBI]

Taxonomic lineage

Eukaryota › Metazoa › Chordata › Craniata › Vertebrata › Euteleostomi › Mammalia › Eutheria › Euarchontoglires › Primates › Haplorrhini › Catarrhini › Hominidae › Homo

Protein attributes

Sequence length	642 AA.
Sequence status	Complete.
Protein existence	Evidence at protein level

General annotation (Comments)

Function	Associated component of the MCM complex that acts as a regulator of DNA replication. Binds to the MCM complex during late S phase and promotes the disassembly of the MCM complex from chromatin, thereby acting as a key regulator of pre-replication complex (pre-RC) unloading from replicated DNA. Can dissociate the MCM complex without addition of ATP; probably acts by destabilizing interactions of each individual subunits of the MCM complex. Required for sister chromatid cohesion. Ref.13 Ref.15
Subunit structure	Interacts with the MCM complex: associates with the MCM3-7 complex which lacks MCM2, while it does not interact with the MCM complex when MCM2 is present (MCM2-7 complex). Interacts with the RPA complex, when composed of all RPA1, RPA2 and RPA3 components, but not with RPA1 or RPA2 alone. Ref.6 Ref.12
Subcellular location	Nucleus. Note: Associates with chromatin. Highly associated with chromatin in G1/S and S phases, reduced binding to chromatin in G2, and further decreased binding in early M phase. It then reassociates with chromatin in late M phase. Dissociates from chromatin later than component of the MCM complex. Ref.6
Sequence similarities	Belongs to the MCMBP family.

Ontologies

Keywords
Biological process	Cell cycle Cell division DNA replication Mitosis
Cellular component	Nucleus
Coding sequence diversity	Alternative splicing
PTM	Phosphoprotein
Technical term	Complete proteome Reference proteome
Gene Ontology (GO)
Biological process	DNA-dependent DNA replication Inferred from mutant phenotype Ref.15. Source: UniProtKB S phase of mitotic cell cycle Inferred from mutant phenotype Ref.15. Source: UniProtKB cell division Inferred from electronic annotation. Source: UniProtKB-KW mitosis Inferred from electronic annotation. Source: UniProtKB-KW sister chromatid cohesion Inferred from mutant phenotype Ref.13. Source: UniProtKB
Cellular component	cytoplasm Inferred from direct assay. Source: HPA nucleus Inferred from direct assay Ref.6. Source: UniProtKB plasma membrane Inferred from direct assay. Source: HPA
Molecular function	chromatin binding Inferred from direct assay Ref.6. Source: UniProtKB
Complete GO annotation...

Alternative products

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

Isoform 1 (identifier: Q9BTE3-1)

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: Q9BTE3-2)

The sequence of this isoform differs from the canonical sequence as follows:
     334-335: Missing.

Isoform 3 (identifier: Q9BTE3-3)

The sequence of this isoform differs from the canonical sequence as follows:
     1-173: Missing.
     334-335: Missing.

Note: No experimental confirmation available.

Sequence annotation (Features)

	Feature key	Position(s)	Length	Description	Graphical view	Feature identifier
Molecule processing
	Chain	1 – 642	642	Mini-chromosome maintenance complex-binding protein		PRO_0000089827
Amino acid modifications
	Modified residue	154	1	Phosphoserine Ref.5 Ref.7 Ref.8 Ref.9 Ref.10 Ref.11
	Modified residue	160	1	Phosphothreonine Ref.5 Ref.7 Ref.8 Ref.9
	Modified residue	298	1	Phosphoserine Ref.8
Natural variations
	Alternative sequence	1 – 173	173	Missing in isoform 3.		VSP_040721
	Alternative sequence	334 – 335	2	Missing in isoform 2 and isoform 3.		VSP_014707
Experimental info
	Sequence conflict	164	1	H → Y in CAG33580. Ref.2
	Sequence conflict	350	1	E → V in CAG33580. Ref.2
	Sequence conflict	610	1	T → A in BAG52809. Ref.1

Sequences

	Sequence		Length	Mass (Da)
	Isoform 1 [UniParc]. Last modified July 19, 2005. Version 2. Checksum: D9EA81646F1D50E2	FASTA	642	72,980
	10 20 30 40 50 60 MPCGEDWLSH PLGIVQGFFA QNGVNPDWEK KVIEYFKEKL KENNAPKWVP SLNEVPLHYL 70 80 90 100 110 120 KPNSFVKFRC MIQDMFDPEF YMGVYETVNQ NTKAHVLHFG KYRDVAECGP QQELDLNSPR 130 140 150 160 170 180 NTTLERQTFY CVPVPGESTW VKEAYVNANQ ARVSPSTSYT PSRHKRSYED DDDMDLQPNK 190 200 210 220 230 240 QKDQHAGARQ AGSVGGLQWC GEPKRLETEA STGQQLNSLN LSSPFDLNFP LPGEKGPACL 250 260 270 280 290 300 VKVYEDWDCF KVNDILELYG ILSVDPVLSI LNNDERDASA LLDPMECTDT AEEQRVHSPP 310 320 330 340 350 360 ASLVPRIHVI LAQKLQHINP LLPACLNKEE SKTCKFVSSF MSELSPVRAE LLGFLTHALL 370 380 390 400 410 420 GDSLAAEYLI LHLISTVYTR RDVLPLGKFT VNLSGCPRNS TFTEHLYRII QHLVPASFRL 430 440 450 460 470 480 QMTIENMNHL KFIPHKDYTA NRLVSGLLQL PSNTSLVIDE TLLEQGQLDT PGVHNVTALS 490 500 510 520 530 540 NLITWQKVDY DFSYHQMEFP CNINVFITSE GRSLLPADCQ IHLQPQLIPP NMEEYMNSLL 550 560 570 580 590 600 SAVLPSVLNK FRIYLTLLRF LEYSISDEIT KAVEDDFVEM RKNDPQSITA DDLHQLLVVA 610 620 630 640 RCLSLSAGQT TLSRERWLRA KQLESLRRTR LQQQKCVNGN EL
	Isoform 2 [UniParc]. Checksum: F7B4B5237F033E09	FASTA	640	72,749
	10 20 30 40 50 60 MPCGEDWLSH PLGIVQGFFA QNGVNPDWEK KVIEYFKEKL KENNAPKWVP SLNEVPLHYL 70 80 90 100 110 120 KPNSFVKFRC MIQDMFDPEF YMGVYETVNQ NTKAHVLHFG KYRDVAECGP QQELDLNSPR 130 140 150 160 170 180 NTTLERQTFY CVPVPGESTW VKEAYVNANQ ARVSPSTSYT PSRHKRSYED DDDMDLQPNK 190 200 210 220 230 240 QKDQHAGARQ AGSVGGLQWC GEPKRLETEA STGQQLNSLN LSSPFDLNFP LPGEKGPACL 250 260 270 280 290 300 VKVYEDWDCF KVNDILELYG ILSVDPVLSI LNNDERDASA LLDPMECTDT AEEQRVHSPP 310 320 330 340 350 360 ASLVPRIHVI LAQKLQHINP LLPACLNKEE SKTFVSSFMS ELSPVRAELL GFLTHALLGD 370 380 390 400 410 420 SLAAEYLILH LISTVYTRRD VLPLGKFTVN LSGCPRNSTF TEHLYRIIQH LVPASFRLQM 430 440 450 460 470 480 TIENMNHLKF IPHKDYTANR LVSGLLQLPS NTSLVIDETL LEQGQLDTPG VHNVTALSNL 490 500 510 520 530 540 ITWQKVDYDF SYHQMEFPCN INVFITSEGR SLLPADCQIH LQPQLIPPNM EEYMNSLLSA 550 560 570 580 590 600 VLPSVLNKFR IYLTLLRFLE YSISDEITKA VEDDFVEMRK NDPQSITADD LHQLLVVARC 610 620 630 640 LSLSAGQTTL SRERWLRAKQ LESLRRTRLQ QQKCVNGNEL
	Isoform 3 [UniParc]. Checksum: 723B4CAC74EC4791	FASTA	467	52,652
	10 20 30 40 50 60 MDLQPNKQKD QHAGARQAGS VGGLQWCGEP KRLETEASTG QQLNSLNLSS PFDLNFPLPG 70 80 90 100 110 120 EKGPACLVKV YEDWDCFKVN DILELYGILS VDPVLSILNN DERDASALLD PMECTDTAEE 130 140 150 160 170 180 QRVHSPPASL VPRIHVILAQ KLQHINPLLP ACLNKEESKT FVSSFMSELS PVRAELLGFL 190 200 210 220 230 240 THALLGDSLA AEYLILHLIS TVYTRRDVLP LGKFTVNLSG CPRNSTFTEH LYRIIQHLVP 250 260 270 280 290 300 ASFRLQMTIE NMNHLKFIPH KDYTANRLVS GLLQLPSNTS LVIDETLLEQ GQLDTPGVHN 310 320 330 340 350 360 VTALSNLITW QKVDYDFSYH QMEFPCNINV FITSEGRSLL PADCQIHLQP QLIPPNMEEY 370 380 390 400 410 420 MNSLLSAVLP SVLNKFRIYL TLLRFLEYSI SDEITKAVED DFVEMRKNDP QSITADDLHQ 430 440 450 460 LLVVARCLSL SAGQTTLSRE RWLRAKQLES LRRTRLQQQK CVNGNEL

References

	« Hide 'large scale' referencesShow 'large scale' references »
[1]	"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: 14702039] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1). Tissue: Uterus.
[2]	"Cloning of human full open reading frames in Gateway(TM) system entry vector (pDONR201)." Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B. Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
[3]	"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: 15164054] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
[4]	"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: 15489334] [Abstract] Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] OF 340-642 (ISOFORMS 1/2). Tissue: Muscle and Placenta.
[5]	"A probability-based approach for high-throughput protein phosphorylation analysis and site localization." Beausoleil S.A., Villen J., Gerber S.A., Rush J., Gygi S.P. Nat. Biotechnol. 24:1285-1292(2006) [PubMed: 16964243] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND THR-160, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[6]	"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: 17296731] [Abstract] Cited for: SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, INTERACTION WITH THE MCM COMPLEX.
[7]	"Combining protein-based IMAC, peptide-based IMAC, and MudPIT for efficient phosphoproteomic analysis." Cantin G.T., Yi W., Lu B., Park S.K., Xu T., Lee J.-D., Yates J.R. III J. Proteome Res. 7:1346-1351(2008) [PubMed: 18220336] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND THR-160, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[8]	"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: 18669648] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; THR-160 AND SER-298, MASS SPECTROMETRY. Tissue: Cervix carcinoma.
[9]	"Lys-N and trypsin cover complementary parts of the phosphoproteome in a refined SCX-based approach." Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J., Mohammed S. Anal. Chem. 81:4493-4501(2009) [PubMed: 19413330] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154 AND THR-160, MASS SPECTROMETRY. Tissue: Embryonic kidney.
[10]	"Large-scale proteomics analysis of the human kinome." Oppermann F.S., Gnad F., Olsen J.V., Hornberger R., Greff Z., Keri G., Mann M., Daub H. Mol. Cell. Proteomics 8:1751-1764(2009) [PubMed: 19369195] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, MASS SPECTROMETRY.
[11]	"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: 19690332] [Abstract] Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, MASS SPECTROMETRY. Tissue: Leukemic T-cell.
[12]	"Identification of proteins that may directly interact with human RPA." Nakaya R., Takaya J., Onuki T., Moritani M., Nozaki N., Ishimi Y. J. Biochem. 148:539-547(2010) [PubMed: 20679368] [Abstract] Cited for: INTERACTION WITH THE RPA COMPLEX.
[13]	"The MCM-binding protein ETG1 aids sister chromatid cohesion required for postreplicative homologous recombination repair." Takahashi N., Quimbaya M., Schubert V., Lammens T., Vandepoele K., Schubert I., Matsui M., Inze D., Berx G., De Veylder L. PLoS Genet. 6:E1000817-E1000817(2010) [PubMed: 20090939] [Abstract] Cited for: FUNCTION.
[14]	"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: 21269460] [Abstract] Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
[15]	"MCM-BP regulates unloading of the MCM2-7 helicase in late S phase." Nishiyama A., Frappier L., Mechali M. Genes Dev. 25:165-175(2011) [PubMed: 21196493] [Abstract] Cited for: FUNCTION.
+	Additional computationally mapped references.

Cross-references

Sequence databases
EMBL GenBank DDBJ	AK023143 mRNA. Translation: BAB14427.1. AK094075 mRNA. Translation: BAG52809.1. CR457299 mRNA. Translation: CAG33580.1. AC027672 Genomic DNA. No translation available. BC000935 mRNA. Translation: AAH00935.1. BC004183 mRNA. Translation: AAH04183.1. BC007219 mRNA. Translation: AAH07219.1.
IPI	IPI00478758. IPI00552546. IPI00979721.
RefSeq	NP_079110.1. NM_024834.2.
UniGene	Hs.124246.
3D structure databases
ProteinModelPortal	Q9BTE3.
ModBase	Search...
Protein-protein interaction databases
IntAct	Q9BTE3. 9 interactions.
MINT	MINT-1465513.
STRING	Q9BTE3.
PTM databases
PhosphoSite	Q9BTE3.
Polymorphism databases
DMDM	71153001.
Proteomic databases
PRIDE	Q9BTE3.
Protocols and materials databases
StructuralBiologyKnowledgebase	Search...
Genome annotation databases
Ensembl	ENST00000360003; ENSP00000353098; ENSG00000197771. ENST00000369077; ENSP00000358073; ENSG00000197771.
GeneID	79892.
KEGG	hsa:79892.
UCSC	uc001leq.1. human. uc001ler.2. human.
Organism-specific databases
CTD	79892.
GeneCards	GC10M121588.
HGNC	HGNC:25782. MCMBP.
HPA	CAB013792. HPA038481.
MIM	610909. gene.
neXtProt	NX_Q9BTE3.
PharmGKB	PA134862625.
GenAtlas	Search...
Phylogenomic databases
eggNOG	prNOG07154.
GeneTree	ENSGT00390000017265.
HOGENOM	HBG591977.
HOVERGEN	HBG059839.
InParanoid	Q9BTE3.
OMA	NNAPKWV.
OrthoDB	EOG4WM4T5.
PhylomeDB	Q9BTE3.
Gene expression databases
ArrayExpress	Q9BTE3.
Bgee	Q9BTE3.
CleanEx	HS_C10orf119.
Genevestigator	Q9BTE3.
GermOnline	ENSG00000197771. Homo sapiens.
Family and domain databases
InterPro	IPR019140. MCM_complex-bd. [Graphical view]
PANTHER	PTHR13489. PTHR13489. 1 hit.
Pfam	PF09739. DUF2044. 1 hit. [Graphical view]
ProtoNet	Search...
Other
NextBio	69714.
SOURCE	Search...

Entry information

Entry name

MCMBP_HUMAN

Accession

Primary (citable) accession number: Q9BTE3
Secondary accession number(s): B3KSP7 , Q6IA56, Q9BVT9, Q9H916

Entry history

Integrated into UniProtKB/Swiss-Prot:	July 19, 2005
Last sequence update:	July 19, 2005
Last modified:	January 25, 2012
This is version 75 of the entry and version 2 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.