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Mini-chromosome maintenance complex-binding protein (MCM-BP) (MCM-binding protein)

 MCMBP_HUMAN             Reviewed;         642 AA.
Q9BTE3; B3KSP7; Q6IA56; Q9BVT9; Q9H916;
19-JUL-2005, integrated into UniProtKB/Swiss-Prot.
19-JUL-2005, sequence version 2.
18-JUL-2018, entry version 132.
RecName: Full=Mini-chromosome maintenance complex-binding protein;
Short=MCM-BP;
Short=MCM-binding protein;
Name=MCMBP; Synonyms=C10orf119;
Homo sapiens (Human).
Eukaryota; Metazoa; Chordata; Craniata; Vertebrata; Euteleostomi;
Mammalia; Eutheria; Euarchontoglires; Primates; Haplorrhini;
Catarrhini; Hominidae; Homo.
NCBI_TaxID=9606;
[1]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 1).
TISSUE=Uterus;
PubMed=14702039; DOI=10.1038/ng1285;
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.;
"Complete sequencing and characterization of 21,243 full-length human
cDNAs.";
Nat. Genet. 36:40-45(2004).
[2]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2).
Ebert L., Schick M., Neubert P., Schatten R., Henze S., Korn B.;
"Cloning of human full open reading frames in Gateway(TM) system entry
vector (pDONR201).";
Submitted (JUN-2004) to the EMBL/GenBank/DDBJ databases.
[3]
NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
PubMed=15164054; DOI=10.1038/nature02462;
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.;
"The DNA sequence and comparative analysis of human chromosome 10.";
Nature 429:375-381(2004).
[4]
NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA] (ISOFORM 2), AND NUCLEOTIDE
SEQUENCE [LARGE SCALE MRNA] OF 340-642 (ISOFORMS 1/2).
TISSUE=Muscle, and Placenta;
PubMed=15489334; DOI=10.1101/gr.2596504;
The MGC Project Team;
"The status, quality, and expansion of the NIH full-length cDNA
project: the Mammalian Gene Collection (MGC).";
Genome Res. 14:2121-2127(2004).
[5]
SUBCELLULAR LOCATION, IDENTIFICATION BY MASS SPECTROMETRY, AND
INTERACTION WITH THE MCM COMPLEX.
PubMed=17296731; DOI=10.1128/MCB.02384-06;
Sakwe A.M., Nguyen T., Athanasopoulos V., Shire K., Frappier L.;
"Identification and characterization of a novel component of the human
minichromosome maintenance complex.";
Mol. Cell. Biol. 27:3044-3055(2007).
[6]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; THR-160 AND
SER-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=18669648; DOI=10.1073/pnas.0805139105;
Dephoure N., Zhou C., Villen J., Beausoleil S.A., Bakalarski C.E.,
Elledge S.J., Gygi S.P.;
"A quantitative atlas of mitotic phosphorylation.";
Proc. Natl. Acad. Sci. U.S.A. 105:10762-10767(2008).
[7]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19413330; DOI=10.1021/ac9004309;
Gauci S., Helbig A.O., Slijper M., Krijgsveld J., Heck A.J.,
Mohammed S.;
"Lys-N and trypsin cover complementary parts of the phosphoproteome in
a refined SCX-based approach.";
Anal. Chem. 81:4493-4501(2009).
[8]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=19608861; DOI=10.1126/science.1175371;
Choudhary C., Kumar C., Gnad F., Nielsen M.L., Rehman M.,
Walther T.C., Olsen J.V., Mann M.;
"Lysine acetylation targets protein complexes and co-regulates major
cellular functions.";
Science 325:834-840(2009).
[9]
INTERACTION WITH THE RPA COMPLEX.
PubMed=20679368; DOI=10.1093/jb/mvq085;
Nakaya R., Takaya J., Onuki T., Moritani M., Nozaki N., Ishimi Y.;
"Identification of proteins that may directly interact with human
RPA.";
J. Biochem. 148:539-547(2010).
[10]
FUNCTION.
PubMed=20090939; DOI=10.1371/journal.pgen.1000817;
Takahashi N., Quimbaya M., Schubert V., Lammens T., Vandepoele K.,
Schubert I., Matsui M., Inze D., Berx G., De Veylder L.;
"The MCM-binding protein ETG1 aids sister chromatid cohesion required
for postreplicative homologous recombination repair.";
PLoS Genet. 6:E1000817-E1000817(2010).
[11]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Cervix carcinoma;
PubMed=20068231; DOI=10.1126/scisignal.2000475;
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.;
"Quantitative phosphoproteomics reveals widespread full
phosphorylation site occupancy during mitosis.";
Sci. Signal. 3:RA3-RA3(2010).
[12]
IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21269460; DOI=10.1186/1752-0509-5-17;
Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P.,
Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.;
"Initial characterization of the human central proteome.";
BMC Syst. Biol. 5:17-17(2011).
[13]
FUNCTION.
PubMed=21196493; DOI=10.1101/gad.614411;
Nishiyama A., Frappier L., Mechali M.;
"MCM-BP regulates unloading of the MCM2-7 helicase in late S phase.";
Genes Dev. 25:165-175(2011).
[14]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
PubMed=21406692; DOI=10.1126/scisignal.2001570;
Rigbolt K.T., Prokhorova T.A., Akimov V., Henningsen J.,
Johansen P.T., Kratchmarova I., Kassem M., Mann M., Olsen J.V.,
Blagoev B.;
"System-wide temporal characterization of the proteome and
phosphoproteome of human embryonic stem cell differentiation.";
Sci. Signal. 4:RS3-RS3(2011).
[15]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154; SER-167 AND
SER-298, AND IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE
ANALYSIS].
TISSUE=Cervix carcinoma, and Erythroleukemia;
PubMed=23186163; DOI=10.1021/pr300630k;
Zhou H., Di Palma S., Preisinger C., Peng M., Polat A.N., Heck A.J.,
Mohammed S.;
"Toward a comprehensive characterization of a human cancer cell
phosphoproteome.";
J. Proteome Res. 12:260-271(2013).
[16]
PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-154, AND IDENTIFICATION
BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
TISSUE=Liver;
PubMed=24275569; DOI=10.1016/j.jprot.2013.11.014;
Bian Y., Song C., Cheng K., Dong M., Wang F., Huang J., Sun D.,
Wang L., Ye M., Zou H.;
"An enzyme assisted RP-RPLC approach for in-depth analysis of human
liver phosphoproteome.";
J. Proteomics 96:253-262(2014).
-!- 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.
{ECO:0000269|PubMed:20090939, ECO:0000269|PubMed:21196493}.
-!- SUBUNIT: 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.
{ECO:0000269|PubMed:17296731, ECO:0000269|PubMed:20679368}.
-!- INTERACTION:
P04424:ASL; NbExp=5; IntAct=EBI-9384556, EBI-750131;
O00311:CDC7; NbExp=2; IntAct=EBI-749378, EBI-374980;
Q13451:FKBP5; NbExp=3; IntAct=EBI-9384556, EBI-306914;
Q9Y248:GINS2; NbExp=2; IntAct=EBI-749378, EBI-747491;
Q9BRT9:GINS4; NbExp=2; IntAct=EBI-749378, EBI-747500;
P49736:MCM2; NbExp=4; IntAct=EBI-749378, EBI-374819;
P24279:MCM3 (xeno); NbExp=3; IntAct=EBI-9384556, EBI-10541;
P25205:MCM3; NbExp=11; IntAct=EBI-749378, EBI-355153;
P30665:MCM4 (xeno); NbExp=3; IntAct=EBI-9384556, EBI-4326;
P33991:MCM4; NbExp=14; IntAct=EBI-749378, EBI-374938;
P33992:MCM5; NbExp=13; IntAct=EBI-749378, EBI-359410;
Q14566:MCM6; NbExp=15; IntAct=EBI-749378, EBI-374900;
P33993:MCM7; NbExp=21; IntAct=EBI-749378, EBI-355924;
Q9UJA3:MCM8; NbExp=3; IntAct=EBI-749378, EBI-8756095;
Q9NRG1:PRTFDC1; NbExp=5; IntAct=EBI-9384556, EBI-739759;
Q9UQE7:SMC3; NbExp=6; IntAct=EBI-749378, EBI-80718;
-!- SUBCELLULAR LOCATION: Nucleus {ECO:0000269|PubMed:17296731}.
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.
-!- ALTERNATIVE PRODUCTS:
Event=Alternative splicing; Named isoforms=3;
Name=1;
IsoId=Q9BTE3-1; Sequence=Displayed;
Name=2;
IsoId=Q9BTE3-2; Sequence=VSP_014707;
Name=3;
IsoId=Q9BTE3-3; Sequence=VSP_040721, VSP_014707;
Note=No experimental confirmation available.;
-!- SIMILARITY: Belongs to the MCMBP family. {ECO:0000305}.
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EMBL; AK023143; BAB14427.1; -; mRNA.
EMBL; AK094075; BAG52809.1; -; mRNA.
EMBL; CR457299; CAG33580.1; -; mRNA.
EMBL; AC027672; -; NOT_ANNOTATED_CDS; Genomic_DNA.
EMBL; BC000935; AAH00935.1; -; mRNA.
EMBL; BC004183; AAH04183.1; -; mRNA.
EMBL; BC007219; AAH07219.1; -; mRNA.
CCDS; CCDS58099.1; -. [Q9BTE3-2]
CCDS; CCDS7617.1; -. [Q9BTE3-1]
RefSeq; NP_001243307.1; NM_001256378.1. [Q9BTE3-2]
RefSeq; NP_001243308.1; NM_001256379.1. [Q9BTE3-3]
RefSeq; NP_079110.1; NM_024834.3. [Q9BTE3-1]
UniGene; Hs.124246; -.
PDB; 4KG9; X-ray; 1.70 A; B=152-161.
PDBsum; 4KG9; -.
ProteinModelPortal; Q9BTE3; -.
SMR; Q9BTE3; -.
BioGrid; 122976; 56.
IntAct; Q9BTE3; 29.
MINT; Q9BTE3; -.
STRING; 9606.ENSP00000353098; -.
iPTMnet; Q9BTE3; -.
PhosphoSitePlus; Q9BTE3; -.
BioMuta; MCMBP; -.
DMDM; 71153001; -.
EPD; Q9BTE3; -.
MaxQB; Q9BTE3; -.
PaxDb; Q9BTE3; -.
PeptideAtlas; Q9BTE3; -.
PRIDE; Q9BTE3; -.
ProteomicsDB; 78982; -.
ProteomicsDB; 78983; -. [Q9BTE3-2]
ProteomicsDB; 78984; -. [Q9BTE3-3]
DNASU; 79892; -.
Ensembl; ENST00000360003; ENSP00000353098; ENSG00000197771. [Q9BTE3-1]
Ensembl; ENST00000369077; ENSP00000358073; ENSG00000197771. [Q9BTE3-2]
GeneID; 79892; -.
KEGG; hsa:79892; -.
UCSC; uc001leq.3; human. [Q9BTE3-1]
CTD; 79892; -.
DisGeNET; 79892; -.
EuPathDB; HostDB:ENSG00000197771.12; -.
GeneCards; MCMBP; -.
HGNC; HGNC:25782; MCMBP.
HPA; CAB013792; -.
HPA; HPA038481; -.
MIM; 610909; gene.
neXtProt; NX_Q9BTE3; -.
OpenTargets; ENSG00000197771; -.
PharmGKB; PA134862625; -.
eggNOG; KOG2545; Eukaryota.
eggNOG; ENOG410XNU0; LUCA.
GeneTree; ENSGT00390000017265; -.
HOGENOM; HOG000237536; -.
HOVERGEN; HBG059839; -.
InParanoid; Q9BTE3; -.
OMA; VDMRKAN; -.
OrthoDB; EOG091G09IO; -.
PhylomeDB; Q9BTE3; -.
TreeFam; TF324793; -.
ChiTaRS; MCMBP; human.
GenomeRNAi; 79892; -.
PRO; PR:Q9BTE3; -.
Proteomes; UP000005640; Chromosome 10.
Bgee; ENSG00000197771; -.
CleanEx; HS_C10orf119; -.
ExpressionAtlas; Q9BTE3; baseline and differential.
Genevisible; Q9BTE3; HS.
GO; GO:0005829; C:cytosol; IDA:HPA.
GO; GO:0000790; C:nuclear chromatin; IBA:GO_Central.
GO; GO:0005654; C:nucleoplasm; IDA:HPA.
GO; GO:0005634; C:nucleus; IDA:UniProtKB.
GO; GO:0005886; C:plasma membrane; IDA:HPA.
GO; GO:0003682; F:chromatin binding; IDA:UniProtKB.
GO; GO:0051301; P:cell division; IEA:UniProtKB-KW.
GO; GO:0006261; P:DNA-dependent DNA replication; IMP:UniProtKB.
GO; GO:0007062; P:sister chromatid cohesion; IMP:UniProtKB.
InterPro; IPR019140; MCM_complex-bd.
PANTHER; PTHR13489; PTHR13489; 1.
Pfam; PF09739; MCM_bind; 1.
1: Evidence at protein level;
3D-structure; Alternative splicing; Cell cycle; Cell division;
Complete proteome; DNA replication; Mitosis; Nucleus; Phosphoprotein;
Reference proteome.
CHAIN 1 642 Mini-chromosome maintenance complex-
binding protein.
/FTId=PRO_0000089827.
MOD_RES 154 154 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:20068231,
ECO:0000244|PubMed:21406692,
ECO:0000244|PubMed:23186163,
ECO:0000244|PubMed:24275569}.
MOD_RES 160 160 Phosphothreonine.
{ECO:0000244|PubMed:18669648}.
MOD_RES 167 167 Phosphoserine.
{ECO:0000244|PubMed:23186163}.
MOD_RES 298 298 Phosphoserine.
{ECO:0000244|PubMed:18669648,
ECO:0000244|PubMed:23186163}.
VAR_SEQ 1 173 Missing (in isoform 3). {ECO:0000305}.
/FTId=VSP_040721.
VAR_SEQ 334 335 Missing (in isoform 2 and isoform 3).
{ECO:0000303|PubMed:15489334,
ECO:0000303|Ref.2}.
/FTId=VSP_014707.
CONFLICT 164 164 H -> Y (in Ref. 2; CAG33580).
{ECO:0000305}.
CONFLICT 350 350 E -> V (in Ref. 2; CAG33580).
{ECO:0000305}.
CONFLICT 610 610 T -> A (in Ref. 1; BAG52809).
{ECO:0000305}.
SEQUENCE 642 AA; 72980 MW; D9EA81646F1D50E2 CRC64;
MPCGEDWLSH PLGIVQGFFA QNGVNPDWEK KVIEYFKEKL KENNAPKWVP SLNEVPLHYL
KPNSFVKFRC MIQDMFDPEF YMGVYETVNQ NTKAHVLHFG KYRDVAECGP QQELDLNSPR
NTTLERQTFY CVPVPGESTW VKEAYVNANQ ARVSPSTSYT PSRHKRSYED DDDMDLQPNK
QKDQHAGARQ AGSVGGLQWC GEPKRLETEA STGQQLNSLN LSSPFDLNFP LPGEKGPACL
VKVYEDWDCF KVNDILELYG ILSVDPVLSI LNNDERDASA LLDPMECTDT AEEQRVHSPP
ASLVPRIHVI LAQKLQHINP LLPACLNKEE SKTCKFVSSF MSELSPVRAE LLGFLTHALL
GDSLAAEYLI LHLISTVYTR RDVLPLGKFT VNLSGCPRNS TFTEHLYRII QHLVPASFRL
QMTIENMNHL KFIPHKDYTA NRLVSGLLQL PSNTSLVIDE TLLEQGQLDT PGVHNVTALS
NLITWQKVDY DFSYHQMEFP CNINVFITSE GRSLLPADCQ IHLQPQLIPP NMEEYMNSLL
SAVLPSVLNK FRIYLTLLRF LEYSISDEIT KAVEDDFVEM RKNDPQSITA DDLHQLLVVA
RCLSLSAGQT TLSRERWLRA KQLESLRRTR LQQQKCVNGN EL


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28-536 The protein encoded by MCM4 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-542 The protein encoded by MCM4 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-543 The protein encoded by MCM4 is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-540 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
28-544 MCM7 encodes a protein that is one of the highly conserved mini-chromosome maintenance proteins (MCM) that are essential for the initiation of eukaryotic genome replication. The hexameric protein comp 0.1 mg
EIAAB12528 CAP-binding protein complex-interacting protein 1,DJ-1-binding protein,DJBP,DJBP,EFCAB6,EF-hand calcium-binding domain-containing protein 6,Homo sapiens,Human,KIAA1672
18-003-43630 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
18-003-44214 Non-POU domain-containing octamer-binding protein - NonO protein; 54 kDa nuclear RNA- and DNA-binding protein; p54(nrb); p54nrb; 55 kDa nuclear protein; NMT55; DNA-binding p52_p100 complex. 52 kDa sub 0.1 mg Protein A
EIAAB43802 Mouse,Mus musculus,Prbp,PRM-1 RNA-binding protein,Protamine-1 RNA-binding protein,RISC-loading complex subunit TARBP2,TAR RNA-binding protein 2,Tarbp2
orb80983 Rat S100 Calcium Binding Protein G protein CABP9K (CALB3 or CABP1; mouse, rat, and human 79 aa; chromosome Xp; ~9 kDa) is cytosolic Ca-binding protein initially found in rat pancreas. It is also expre 1


 

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