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P97310

- MCM2_MOUSE

UniProt

P97310 - MCM2_MOUSE

Protein

DNA replication licensing factor MCM2

Gene

Mcm2

Organism
Mus musculus (Mouse)
Status
Reviewed - Annotation score: 5 out of 5- Experimental evidence at protein leveli
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    • History
      Entry version 139 (01 Oct 2014)
      Sequence version 3 (13 Apr 2004)
      Previous versions | rss
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    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 the entry in S phase and for cell division.

    Catalytic activityi

    ATP + H2O = ADP + phosphate.

    Regions

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri329 – 35527C4-typeSequence AnalysisAdd
    BLAST
    Nucleotide bindingi523 – 5308ATPSequence Analysis

    GO - Molecular functioni

    1. ATP binding Source: UniProtKB-KW
    2. DNA helicase activity Source: InterPro
    3. DNA replication origin binding Source: MGI
    4. histone binding Source: MGI
    5. metal ion binding Source: UniProtKB-KW

    GO - Biological processi

    1. cell cycle Source: UniProtKB-KW
    2. cellular response to interleukin-4 Source: MGI
    3. DNA replication initiation Source: MGI
    4. DNA unwinding involved in DNA replication Source: MGI
    5. nucleosome assembly Source: MGI

    Keywords - Molecular functioni

    Helicase, Hydrolase

    Keywords - Biological processi

    Cell cycle, DNA replication

    Keywords - Ligandi

    ATP-binding, DNA-binding, Metal-binding, Nucleotide-binding, Zinc

    Enzyme and pathway databases

    ReactomeiREACT_217374. Unwinding of DNA.

    Names & Taxonomyi

    Protein namesi
    Recommended name:
    DNA replication licensing factor MCM2 (EC:3.6.4.12)
    Alternative name(s):
    Minichromosome maintenance protein 2 homolog
    Nuclear protein BM28
    Gene namesi
    Name:Mcm2
    Synonyms:Bm28, Cdcl1, Kiaa0030, Mcmd2
    OrganismiMus musculus (Mouse)
    Taxonomic identifieri10090 [NCBI]
    Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaSciurognathiMuroideaMuridaeMurinaeMusMus
    ProteomesiUP000000589: Chromosome 6

    Organism-specific databases

    MGIiMGI:105380. Mcm2.

    Subcellular locationi

    Nucleus Curated

    GO - Cellular componenti

    1. chromatin Source: Ensembl
    2. MCM complex Source: UniProtKB
    3. nuclear origin of replication recognition complex Source: MGI
    4. nucleus Source: MGI

    Keywords - Cellular componenti

    Nucleus

    Pathology & Biotechi

    Mutagenesis

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Mutagenesisi237 – 2371L → P: Impairs interaction with KAT7. 1 Publication

    PTM / Processingi

    Molecule processing

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Initiator methioninei1 – 11Removed1 Publication
    Chaini2 – 904903DNA replication licensing factor MCM2PRO_0000194088Add
    BLAST

    Amino acid modifications

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Modified residuei2 – 21N-acetylalanine1 Publication
    Modified residuei12 – 121Phosphoserine1 Publication
    Modified residuei21 – 211Phosphoserine3 Publications
    Modified residuei26 – 261PhosphoserineBy similarity
    Modified residuei27 – 271Phosphoserine2 Publications
    Modified residuei39 – 391PhosphothreonineBy similarity
    Modified residuei40 – 401Phosphoserine; by CDC7By similarity
    Modified residuei41 – 411PhosphoserineBy similarity
    Modified residuei53 – 531Phosphoserine; by CDC7By similarity
    Modified residuei59 – 591PhosphothreonineBy similarity
    Modified residuei108 – 1081PhosphoserineBy similarity
    Modified residuei139 – 1391Phosphoserine2 Publications
    Modified residuei140 – 1401Phosphoserine2 Publications
    Modified residuei216 – 2161N6-acetyllysineBy similarity
    Modified residuei381 – 3811PhosphoserineBy similarity

    Post-translational modificationi

    Phosphorylated on Ser-108 by ATR in proliferating cells. Ser-108 proliferation is increased by genotoxic agents. Ser-40 is mediated by the CDC7-DBF4 and CDC7-DBF4B complexes, while Ser-53 phosphorylation is only mediated by the CDC7-DBF4 complex. Phosphorylation by the CDC7-DBF4 complex during G1/S phase is required for the initiation of DNA replication By similarity.By similarity

    Keywords - PTMi

    Acetylation, Phosphoprotein

    Proteomic databases

    MaxQBiP97310.
    PaxDbiP97310.
    PRIDEiP97310.

    PTM databases

    PhosphoSiteiP97310.

    Miscellaneous databases

    PMAP-CutDBP97310.

    Expressioni

    Gene expression databases

    ArrayExpressiP97310.
    BgeeiP97310.
    GenevestigatoriP97310.

    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. Interacts with KAT7 and DBF4. May interact with MCM10 By similarity.By similarity

    Protein-protein interaction databases

    BioGridi201346. 4 interactions.
    DIPiDIP-33057N.
    IntActiP97310. 7 interactions.
    MINTiMINT-4101561.

    Structurei

    3D structure databases

    ProteinModelPortaliP97310.
    SMRiP97310. Positions 199-798.
    ModBaseiSearch...
    MobiDBiSearch...

    Family & Domainsi

    Domains and Repeats

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Domaini473 – 680208MCMAdd
    BLAST

    Region

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Regioni2 – 257256Interaction with KAT7Add
    BLAST

    Motif

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Motifi655 – 6584Arginine finger

    Sequence similaritiesi

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

    Zinc finger

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Zinc fingeri329 – 35527C4-typeSequence AnalysisAdd
    BLAST

    Keywords - Domaini

    Zinc-finger

    Phylogenomic databases

    eggNOGiCOG1241.
    GeneTreeiENSGT00740000115337.
    HOVERGENiHBG106398.
    InParanoidiP97310.
    KOiK02540.
    OMAiNMEETVY.
    OrthoDBiEOG71VSRZ.
    PhylomeDBiP97310.
    TreeFamiTF300772.

    Family and domain databases

    Gene3Di2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProiIPR008045. MCM2.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view]
    PfamiPF00493. MCM. 1 hit.
    PF12619. MCM2_N. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view]
    PRINTSiPR01657. MCMFAMILY.
    PR01658. MCMPROTEIN2.
    SMARTiSM00350. MCM. 1 hit.
    [Graphical view]
    SUPFAMiSSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEiPS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view]

    Sequencei

    Sequence statusi: Complete.

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

    P97310-1 [UniParc]FASTAAdd to Basket

    « Hide

    MAESSESLSA SSPARQRRRI SDPLTSSPGR SSRRADALTS SPGRDLPPFE    50
    DESEGLLGTE GPMEEEEDGE ELIGDGMERD YRPIPELDVY EAEGLALDDE 100
    DVEELTASQR EAAERTMRQR DREAGRGLGR MRRGLLYDSS EEDEERPARK 150
    RRHVERATED GEEDEEMIES IENLEDLKGH SVREWVSMAG PRLEIHHRFK 200
    NFLRTHVDSH GHNVFKERIS DMCKENRESL VVNYEDLAAR EHVLAYFLPE 250
    APAELLQIFD EAALEVVLAM YPKYDRITNH IHVRISHLPL VEELRSLRQL 300
    HLNQLIRTSG VVTSCTGVLP QLSMVKYNCS KCNFVLGPFC QSQNQEVKPG 350
    SCPECQSAGP FEINMEETIY QNYQRIRIQE SPGKVAAGRL PRSKDAILLA 400
    DLVDSCKPGD EIELTGIYHN NYDGSLNTAN GFPVFATIIL ANHVAKKDNK 450
    VAVGELTDED VKMITGLSKD QQIGEKIFAS IAPSIYGHED IKRGLALALF 500
    GGEPKNPGGK HKVRGDINVL LCGDPGTAKS QFLKYIEKVS SRAIFTTGQG 550
    ASAVGLTAYV QRHPVSREWT LEAGALVLAD RGVCLIDEFD KMNDQDRTSI 600
    HEAMEQQSIS ISKAGIVTSL QARCTVIAAA NPIGGRYDPS LTFSENVDLT 650
    EPIISRFDVL CVVRDTVDPV QDEMLARFVV GSHVRHHPSN KKDEGLTNGG 700
    TLEPAMPNTY GVEPLPQEVL KKYIIYAKER VRPKLNQMDQ DKVARMYSDL 750
    RKESMATGSI PITVRHIESM IRMAEAHARM HLRDYVMEDD VNMAIRVMME 800
    SFIDTQKFSV MRSMRKTFAR YLSFRRDNND LLLFILKQLV AEQVTYQRNR 850
    FGAQQDTIEI PEKDLMDKAR QINIHNLSAF YDSDLFKFNK FSRDLKRKLI 900
    LQQF 904
    Length:904
    Mass (Da):102,078
    Last modified:April 13, 2004 - v3
    Checksum:i7B61C13DAD1CAC58
    GO

    Sequence cautioni

    The sequence BAC97849.1 differs from that shown. Reason: Erroneous initiation. Translation N-terminally shortened.

    Experimental Info

    Feature keyPosition(s)LengthDescriptionGraphical viewFeature identifierActions
    Sequence conflicti70 – 701E → G in AAC16250. (PubMed:9371513)Curated
    Sequence conflicti135 – 1351L → P in AAC16250. (PubMed:9371513)Curated
    Sequence conflicti185 – 1851W → R in BAA22148. (PubMed:9077461)Curated
    Sequence conflicti271 – 2711Y → H in AAC16250. (PubMed:9371513)Curated
    Sequence conflicti506 – 5061N → D in AAC36510. (PubMed:9798653)Curated
    Sequence conflicti521 – 5211L → S in AAC36510. (PubMed:9798653)Curated
    Sequence conflicti648 – 6481D → N in AAC36510. (PubMed:9798653)Curated
    Sequence conflicti822 – 8221L → I in AAC16250. (PubMed:9371513)Curated

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86725 mRNA. Translation: BAA22148.1.
    AF004105 mRNA. Translation: AAC16250.1.
    AK129039 mRNA. Translation: BAC97849.1. Different initiation.
    AK088156 mRNA. Translation: BAC40178.1.
    BC055318 mRNA. Translation: AAH55318.1.
    U89403 mRNA. Translation: AAC36510.1.
    CCDSiCCDS39554.1.
    PIRiT10067.
    RefSeqiNP_032590.2. NM_008564.2.
    UniGeneiMm.16711.

    Genome annotation databases

    EnsembliENSMUST00000058011; ENSMUSP00000061923; ENSMUSG00000002870.
    GeneIDi17216.
    KEGGimmu:17216.
    UCSCiuc009cvx.2. mouse.

    Cross-referencesi

    Sequence databases

    Select the link destinations:
    EMBL
    GenBank
    DDBJ
    Links Updated
    D86725 mRNA. Translation: BAA22148.1 .
    AF004105 mRNA. Translation: AAC16250.1 .
    AK129039 mRNA. Translation: BAC97849.1 . Different initiation.
    AK088156 mRNA. Translation: BAC40178.1 .
    BC055318 mRNA. Translation: AAH55318.1 .
    U89403 mRNA. Translation: AAC36510.1 .
    CCDSi CCDS39554.1.
    PIRi T10067.
    RefSeqi NP_032590.2. NM_008564.2.
    UniGenei Mm.16711.

    3D structure databases

    ProteinModelPortali P97310.
    SMRi P97310. Positions 199-798.
    ModBasei Search...
    MobiDBi Search...

    Protein-protein interaction databases

    BioGridi 201346. 4 interactions.
    DIPi DIP-33057N.
    IntActi P97310. 7 interactions.
    MINTi MINT-4101561.

    PTM databases

    PhosphoSitei P97310.

    Proteomic databases

    MaxQBi P97310.
    PaxDbi P97310.
    PRIDEi P97310.

    Protocols and materials databases

    Structural Biology Knowledgebase Search...

    Genome annotation databases

    Ensembli ENSMUST00000058011 ; ENSMUSP00000061923 ; ENSMUSG00000002870 .
    GeneIDi 17216.
    KEGGi mmu:17216.
    UCSCi uc009cvx.2. mouse.

    Organism-specific databases

    CTDi 4171.
    MGIi MGI:105380. Mcm2.
    Rougei Search...

    Phylogenomic databases

    eggNOGi COG1241.
    GeneTreei ENSGT00740000115337.
    HOVERGENi HBG106398.
    InParanoidi P97310.
    KOi K02540.
    OMAi NMEETVY.
    OrthoDBi EOG71VSRZ.
    PhylomeDBi P97310.
    TreeFami TF300772.

    Enzyme and pathway databases

    Reactomei REACT_217374. Unwinding of DNA.

    Miscellaneous databases

    ChiTaRSi MCM2. mouse.
    NextBioi 291606.
    PMAP-CutDB P97310.
    PROi P97310.
    SOURCEi Search...

    Gene expression databases

    ArrayExpressi P97310.
    Bgeei P97310.
    Genevestigatori P97310.

    Family and domain databases

    Gene3Di 2.40.50.140. 2 hits.
    3.40.50.300. 1 hit.
    InterProi IPR008045. MCM2.
    IPR018525. MCM_CS.
    IPR001208. MCM_DNA-dep_ATPase.
    IPR027925. MCM_N.
    IPR012340. NA-bd_OB-fold.
    IPR027417. P-loop_NTPase.
    [Graphical view ]
    Pfami PF00493. MCM. 1 hit.
    PF12619. MCM2_N. 1 hit.
    PF14551. MCM_N. 1 hit.
    [Graphical view ]
    PRINTSi PR01657. MCMFAMILY.
    PR01658. MCMPROTEIN2.
    SMARTi SM00350. MCM. 1 hit.
    [Graphical view ]
    SUPFAMi SSF50249. SSF50249. 1 hit.
    SSF52540. SSF52540. 1 hit.
    PROSITEi PS00847. MCM_1. 1 hit.
    PS50051. MCM_2. 1 hit.
    [Graphical view ]
    ProtoNeti Search...

    Publicationsi

    1. "Mouse MCM proteins: complex formation and transportation to the nucleus."
      Kimura H., Ohtomo T., Yamaguchi M., Ishii A., Sugimoto K.
      Genes Cells 1:977-993(1996) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 217-224; 376-384 AND 477-487.
    2. Kimura H.
      Submitted (AUG-1997) to the EMBL/GenBank/DDBJ databases
      Cited for: SEQUENCE REVISION.
    3. "Clone 10d/BM28 (CDCL1), an early S-phase protein, is an important growth regulator of melanoma."
      Spanjaard R.A., Lee P.J., Sarkar S., Goedegebuure P.S., Eberlein T.J.
      Cancer Res. 57:5122-5128(1997) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA].
      Tissue: Melanoma.
    4. "Prediction of the coding sequences of mouse homologues of KIAA gene: III. The complete nucleotide sequences of 500 mouse KIAA-homologous cDNAs identified by screening of terminal sequences of cDNA clones randomly sampled from size-fractionated libraries."
      Okazaki N., Kikuno R., Ohara R., Inamoto S., Koseki H., Hiraoka S., Saga Y., Nagase T., Ohara O., Koga H.
      DNA Res. 10:167-180(2003) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Tissue: Embryonic tail.
    5. "The transcriptional landscape of the mammalian genome."
      Carninci P., Kasukawa T., Katayama S., Gough J., Frith M.C., Maeda N., Oyama R., Ravasi T., Lenhard B., Wells C., Kodzius R., Shimokawa K., Bajic V.B., Brenner S.E., Batalov S., Forrest A.R., Zavolan M., Davis M.J.
      , Wilming L.G., Aidinis V., Allen J.E., Ambesi-Impiombato A., Apweiler R., Aturaliya R.N., Bailey T.L., Bansal M., Baxter L., Beisel K.W., Bersano T., Bono H., Chalk A.M., Chiu K.P., Choudhary V., Christoffels A., Clutterbuck D.R., Crowe M.L., Dalla E., Dalrymple B.P., de Bono B., Della Gatta G., di Bernardo D., Down T., Engstrom P., Fagiolini M., Faulkner G., Fletcher C.F., Fukushima T., Furuno M., Futaki S., Gariboldi M., Georgii-Hemming P., Gingeras T.R., Gojobori T., Green R.E., Gustincich S., Harbers M., Hayashi Y., Hensch T.K., Hirokawa N., Hill D., Huminiecki L., Iacono M., Ikeo K., Iwama A., Ishikawa T., Jakt M., Kanapin A., Katoh M., Kawasawa Y., Kelso J., Kitamura H., Kitano H., Kollias G., Krishnan S.P., Kruger A., Kummerfeld S.K., Kurochkin I.V., Lareau L.F., Lazarevic D., Lipovich L., Liu J., Liuni S., McWilliam S., Madan Babu M., Madera M., Marchionni L., Matsuda H., Matsuzawa S., Miki H., Mignone F., Miyake S., Morris K., Mottagui-Tabar S., Mulder N., Nakano N., Nakauchi H., Ng P., Nilsson R., Nishiguchi S., Nishikawa S., Nori F., Ohara O., Okazaki Y., Orlando V., Pang K.C., Pavan W.J., Pavesi G., Pesole G., Petrovsky N., Piazza S., Reed J., Reid J.F., Ring B.Z., Ringwald M., Rost B., Ruan Y., Salzberg S.L., Sandelin A., Schneider C., Schoenbach C., Sekiguchi K., Semple C.A., Seno S., Sessa L., Sheng Y., Shibata Y., Shimada H., Shimada K., Silva D., Sinclair B., Sperling S., Stupka E., Sugiura K., Sultana R., Takenaka Y., Taki K., Tammoja K., Tan S.L., Tang S., Taylor M.S., Tegner J., Teichmann S.A., Ueda H.R., van Nimwegen E., Verardo R., Wei C.L., Yagi K., Yamanishi H., Zabarovsky E., Zhu S., Zimmer A., Hide W., Bult C., Grimmond S.M., Teasdale R.D., Liu E.T., Brusic V., Quackenbush J., Wahlestedt C., Mattick J.S., Hume D.A., Kai C., Sasaki D., Tomaru Y., Fukuda S., Kanamori-Katayama M., Suzuki M., Aoki J., Arakawa T., Iida J., Imamura K., Itoh M., Kato T., Kawaji H., Kawagashira N., Kawashima T., Kojima M., Kondo S., Konno H., Nakano K., Ninomiya N., Nishio T., Okada M., Plessy C., Shibata K., Shiraki T., Suzuki S., Tagami M., Waki K., Watahiki A., Okamura-Oho Y., Suzuki H., Kawai J., Hayashizaki Y.
      Science 309:1559-1563(2005) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [LARGE SCALE MRNA].
      Strain: NOD.
      Tissue: Thymus.
    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].
      Strain: C57BL/6.
      Tissue: Brain.
    7. "Expressed genes in interleukin-4 treated B cells identified by cDNA representational difference analysis."
      Chu C.C., Paul W.E.
      Mol. Immunol. 35:487-502(1998) [PubMed] [Europe PMC] [Abstract]
      Cited for: NUCLEOTIDE SEQUENCE [MRNA] OF 477-668.
      Strain: BALB/c.
      Tissue: Spleen.
    8. "Identification, characterization and chromosomal localization of the cognate human and murine DBF4 genes."
      Lepke M., Puetter V., Staib C., Kneissl M., Berger C., Hoehn K., Nanda I., Schmid M., Grummt F.
      Mol. Gen. Genet. 262:220-229(1999) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH DBF4.
      Strain: C57BL/6J.
      Tissue: Egg and Embryo.
    9. "Replication factors MCM2 and ORC1 interact with the histone acetyltransferase HBO1."
      Burke T.W., Cook J.G., Asano M., Nevins J.R.
      J. Biol. Chem. 276:15397-15408(2001) [PubMed] [Europe PMC] [Abstract]
      Cited for: INTERACTION WITH KAT7, MUTAGENESIS OF LEU-237.
    10. Cited for: IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Embryonic brain.
    11. "A differential phosphoproteomic analysis of retinoic acid-treated P19 cells."
      Smith J.C., Duchesne M.A., Tozzi P., Ethier M., Figeys D.
      J. Proteome Res. 6:3174-3186(2007) [PubMed] [Europe PMC] [Abstract]
      Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Teratocarcinoma.
    12. Cited for: PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-21; SER-27; SER-139 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS].
      Tissue: Liver.
    13. "Large scale localization of protein phosphorylation by use of electron capture dissociation mass spectrometry."
      Sweet S.M., Bailey C.M., Cunningham D.L., Heath J.K., Cooper H.J.
      Mol. Cell. Proteomics 8:904-912(2009) [PubMed] [Europe PMC] [Abstract]
      Cited for: ACETYLATION [LARGE SCALE ANALYSIS] AT ALA-2, PHOSPHORYLATION [LARGE SCALE ANALYSIS] AT SER-12; SER-21; SER-27; SER-139 AND SER-140, IDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS], CLEAVAGE OF INITIATOR METHIONINE [LARGE SCALE ANALYSIS].
      Tissue: Embryonic fibroblast.

    Entry informationi

    Entry nameiMCM2_MOUSE
    AccessioniPrimary (citable) accession number: P97310
    Secondary accession number(s): O08971, O89057, Q8C2R0
    Entry historyi
    Integrated into UniProtKB/Swiss-Prot: November 1, 1997
    Last sequence update: April 13, 2004
    Last modified: October 1, 2014
    This is version 139 of the entry and version 3 of the sequence. [Complete history]
    Entry statusiReviewed (UniProtKB/Swiss-Prot)
    Annotation programChordata Protein Annotation Program

    Miscellaneousi

    Keywords - Technical termi

    Complete proteome, Direct protein sequencing, Reference proteome

    Documents

    1. MGD cross-references
      Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
    2. SIMILARITY comments
      Index of protein domains and families

    External Data

    Dasty 3